|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
9-558 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 928.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 9 EFVWFQEYPPSVPRTIDTGAVPSLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMM 88
Cdd:PRK08974 2 EKVWLNRYPADVPAEINPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALMM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 89 PNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAPFPKR 168
Cdd:PRK08974 82 PNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDQLSTAKG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 169 AIVNFVVKRVKKMVPAWSLPGTTGFRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAW 248
Cdd:PRK08974 162 TLVNFVVKYIKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 249 IGPFLDEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAE 328
Cdd:PRK08974 242 YGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 329 LDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPP 408
Cdd:PRK08974 322 LDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 409 GQPGELCVKGPQVMQGYWQKPEESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGV 488
Cdd:PRK08974 402 GEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKV 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 489 LEVACIGVPDEKSGEVPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK08974 481 LEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
9-559 |
0e+00 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 898.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 9 EFVWFQEYPPSVPRTIDTGAVPSLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMM 88
Cdd:PRK07059 2 EKIWLKSYPPGVPAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQS-RGLAKGARVAIMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 89 PNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAPFpKR 168
Cdd:PRK07059 81 PNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDLLGF-KG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 169 AIVNFVVKRVKKMVPAWSLPGTTGFRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAW 248
Cdd:PRK07059 160 HIVNFVVRRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 249 IGPFLDEGKEV----IITALPLYHIFALVVNCLLFLRHGCRNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAP 324
Cdd:PRK07059 240 LQPAFEKKPRPdqlnFVCALPLYHIFALTVCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 325 GFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEEN 404
Cdd:PRK07059 320 DFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 405 EVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQ 484
Cdd:PRK07059 400 DLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVAS 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522138377 485 HPGVLEVACIGVPDEKSGEVPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELRG 559
Cdd:PRK07059 480 HPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
12-558 |
0e+00 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 780.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 12 WFQEYPPSVPRTIDTGAVPSLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNL 91
Cdd:PRK08751 7 WLQSYPAGVAAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 92 LQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAPFPKRAIV 171
Cdd:PRK08751 87 LQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGFPKAALV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 172 NFVVKRVKKMVPAWSLPGTTGFRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGP 251
Cdd:PRK08751 167 NFVVKYVKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 252 --FLDEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAEL 329
Cdd:PRK08751 247 tgKLEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 330 DFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPG 409
Cdd:PRK08751 327 DFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 410 QPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVL 489
Cdd:PRK08751 407 EIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522138377 490 EVACIGVPDEKSGEVPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK08751 487 EVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
12-558 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 766.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 12 WFQEYPPSVPRTIDTGAVPSLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNL 91
Cdd:PRK05677 6 WKDKYPAGIAAEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 92 LQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAPFPKRAIV 171
Cdd:PRK05677 86 LQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIVTEVADMLPPLKRLLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 172 NFVVKRVKKMVPAWSLPGTTGFRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGP 251
Cdd:PRK05677 166 NAVVKHVKKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 252 FLDEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDF 331
Cdd:PRK05677 246 NLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 332 SRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLSVPQWnGTIGVPLPSTLVSLRDEEENEVPPGQP 411
Cdd:PRK05677 326 SALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQV-GTIGIPVPSTLCKVIDDDGNELPLGEV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 412 GELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEV 491
Cdd:PRK05677 405 GELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQC 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522138377 492 ACIGVPDEKSGEVPKVFVV-KKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK05677 485 AAIGVPDEKSGEAIKVFVVvKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
12-558 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 712.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 12 WFQEYPPSVPRTIDTGAVPSLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNL 91
Cdd:PRK12492 6 WNDKRPAGVPSTIDLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 92 LQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAPFPKRAIV 171
Cdd:PRK12492 86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLLPAAKGWLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 172 NFVVKRVKKMVPAWSLPGTTGFRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIG- 250
Cdd:PRK12492 166 NTVVDKVKKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSq 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 251 ------PFLDEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAP 324
Cdd:PRK12492 246 lgpdgqPLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 325 GFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEEN 404
Cdd:PRK12492 326 GFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 405 EVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQ 484
Cdd:PRK12492 406 ELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMA 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522138377 485 HPGVLEVACIGVPDEKSGEVPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK12492 486 HPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
32-558 |
0e+00 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 687.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 32 LVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNV 111
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 112 NPLYTPRELEHQLRDSGAKAIVIVENFCTtlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgtt 191
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVSFTD--------------------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 192 gfraALAKGRAqPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPfLDEGKEVIITALPLYHIFA 271
Cdd:cd05936 109 ----LLAAGAP-LGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLED-LLEGDDVVLAALPLFHVFG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 272 LVVNCLLFLRHGCRNVLITNPRDMAAFcVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEK 351
Cdd:cd05936 183 LTVALLLPLALGATIVLIPRFRPIGVL-KEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 352 WQKVTGVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEE 431
Cdd:cd05936 262 FEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 432 SAKVFTkDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVK 511
Cdd:cd05936 342 TAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 522138377 512 KDPA-LTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05936 421 KEGAsLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
32-558 |
0e+00 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 551.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 32 LVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNV 111
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRA-LGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 112 NPLYTPRELEHQLRDSGAKAIVIvenfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgtt 191
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 192 gfraalakgraqpyarvqlgpddiAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGkEVIITALPLYHIFA 271
Cdd:COG0318 103 ------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG--LTPG-DVVLVALPLFHVFG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 272 LVVNCLLFLRHGCRNVLITNpRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEK 351
Cdd:COG0318 156 LTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLER 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 352 WQKVTGVGLTEGYGLTECSPVVSFSPLSV-PQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPE 430
Cdd:COG0318 235 FEERFGVRIVEGYGLTETSPVVTVNPEDPgERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 431 ESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV 510
Cdd:COG0318 315 ATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVV 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 522138377 511 KKDPA-LTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:COG0318 394 LRPGAeLDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALR 442
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
12-558 |
4.01e-164 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 478.73 E-value: 4.01e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 12 WFQEYPPSVPRTIDTGAvPSLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQnVLGLQRGDRVALMMPNL 91
Cdd:PRK05605 15 WLQSYAPWTPHDLDYGD-TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNC 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 92 LQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAPFPKRAIV 171
Cdd:PRK05605 93 PQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVSVNMIAAMPLLQRLAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 172 NFVVKRVKKMVPAWS--LPGTTGFRAALAKGRAQPYARVQL---GPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVS 246
Cdd:PRK05605 173 RLPIPALRKARAALTgpAPGTVPWETLVDAAIGGDGSDVSHprpTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 247 AWIgPFLDEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLITNPrDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGF 326
Cdd:PRK05605 253 AWV-PGLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAP-DIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 327 AELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEE--N 404
Cdd:PRK05605 331 RGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDpdE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 405 EVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTkDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQ 484
Cdd:PRK05605 411 TMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLRE 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522138377 485 HPGVLEVACIGVPDEKSGE-VPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK05605 490 HPGVEDAAVVGLPREDGSEeVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVR 564
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
31-560 |
2.09e-157 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 459.37 E-value: 2.09e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 31 SLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVN 110
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAA-LGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 111 VNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTP-IQHVITTQIGDLAPFPkraivnfvvkrvkkmvpawslPG 189
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPaLEHVVICETEEDDPHT---------------------EK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 190 TTGFRAALAKGrAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIItALPLYHI 269
Cdd:PRK07656 144 MKTFTDFLAAG-DPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLG--LTEGDRYLA-ANPFFHV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 270 FALVVNCLLFLRHGCrNVLItnprdMAAFCVE-----LKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAV 344
Cdd:PRK07656 220 FGYKAGVNAPLMRGA-TILP-----LPVFDPDevfrlIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 345 QQAVAEKWQKVTGVG-LTEGYGLTECSPVVSFSPL--SVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQV 421
Cdd:PRK07656 294 PVALLERFESELGVDiVLTGYGLSEASGVTTFNRLddDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 422 MQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKS 501
Cdd:PRK07656 374 MKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERL 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 502 GEVPKVFVVKKDPA-LTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELRGK 560
Cdd:PRK07656 454 GEVGKAYVVLKPGAeLTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
31-558 |
2.58e-143 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 423.83 E-value: 2.58e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 31 SLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVN 110
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 111 VNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTP-IQHVITTQIGDLAPFPKRAIvnfvvkrvkkmvpawslpg 189
Cdd:PRK06187 86 INIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPtVRTVIVEGDGPAAPLAPEVG------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 190 ttGFRAALAkgrAQP--YARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEgKEVIITALPLY 267
Cdd:PRK06187 147 --EYEELLA---AASdtFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLK--LSR-DDVYLVIVPMF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 268 HIFALVVnCLLFLRHGCRNVLitnPR----DMAAFCVELKRsgFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTA 343
Cdd:PRK06187 219 HVHAWGL-PYLALMAGAKQVI---PRrfdpENLLDLIETER--VTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 344 VQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLS---VPQWN--GTIGVPLPstLVSLR--DEEENEVPP--GQPGEL 414
Cdd:PRK06187 293 LPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEdqlPGQWTkrRSAGRPLP--GVEARivDDDGDELPPdgGEVGEI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 415 CVKGPQVMQGYWQKPEESAKVFTkDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACI 494
Cdd:PRK06187 371 IVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVI 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522138377 495 GVPDEKSGEVPKVFVV-KKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK06187 450 GVPDEKWGERPVAVVVlKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
12-557 |
1.34e-138 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 413.27 E-value: 1.34e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 12 WFQEYPPSVPRTIDTGAVPsLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNL 91
Cdd:PRK06710 7 WLKSYPEEIPSTISYDIQP-LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQK-LGVEKGDRVAIMLPNC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 92 LQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAPFPKRAIV 171
Cdd:PRK06710 85 PQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPKNLLY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 172 NFVVKRVKKMVPAWSLPGTTGFRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGP 251
Cdd:PRK06710 165 PFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 252 FLdEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLItnPR-DMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELD 330
Cdd:PRK06710 245 CK-EGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI--PKfDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 331 FSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEV-PPG 409
Cdd:PRK06710 322 ISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEAlPPG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 410 QPGELCVKGPQVMQGYWQKPEESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVL 489
Cdd:PRK06710 402 EIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQ 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522138377 490 EVACIGVPDEKSGEVPKVFVV-KKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK06710 481 EVVTIGVPDPYRGETVKAFVVlKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
36-554 |
1.04e-137 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 406.23 E-value: 1.04e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 36 FEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLY 115
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRA-LGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 116 TPRELEHQLRDSGAKAIVivenfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfra 195
Cdd:cd17631 80 TPPEVAYILADSGAKVLF-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 196 alakgraqpyarvqlgpDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQqvsAWIGPFLDEGKEVIITALPLYHIFALVVN 275
Cdd:cd17631 98 -----------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAV---NALAALDLGPDDVLLVVAPLFHIGGLGVF 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 276 CLLFLRHGCRNVLITNPrDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQkV 355
Cdd:cd17631 158 TLPTLLRGGTVVILRKF-DPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQ-A 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 356 TGVGLTEGYGLTECSPVVSF-SPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAK 434
Cdd:cd17631 236 RGVKFVQGYGMTETSPGVTFlSPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 435 VFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDP 514
Cdd:cd17631 316 AF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG 394
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 522138377 515 A-LTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLR 554
Cdd:cd17631 395 AeLDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
36-469 |
5.46e-136 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 401.31 E-value: 5.46e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 36 FEQSCARFGDQIAYECM-GQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPL 114
Cdd:pfam00501 1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRA-LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 115 YTPRELEHQLRDSGAKAIVIVENFctTLQQVIANTP-IQHVITTQIGDLAPFPKRAIVNFVVKRVKKmvpawslpgttgf 193
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDAL--KLEELLEALGkLEVVKLVLVLDRDPVLKEEPLPEEAKPADV------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 194 raalakgraQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEG-KEVIITALPLYHIFAL 272
Cdd:pfam00501 145 ---------PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpDDRVLSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 273 VVNCLLFLRHGCRNVLI--TNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAE 350
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPpgFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 351 KWQKVTGVGLTEGYGLTECSPVVSFSPLSVPQWN--GTIGVPLPSTLVSLRDEEE-NEVPPGQPGELCVKGPQVMQGYWQ 427
Cdd:pfam00501 296 RFRELFGGALVNGYGLTETTGVVTTPLPLDEDLRslGSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 522138377 428 KPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVS 469
Cdd:pfam00501 376 DPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
53-553 |
7.99e-128 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 383.10 E-value: 7.99e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRK-LGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIVENFCTTLQQVIAN-TPIQHVITTqigDLAPFPKRAIVNFVvkRVKKMVPAWSLPgttgfraalakgraqpyARVQLG 211
Cdd:cd05911 87 FTDPDGLEKVKEAAKElGPKDKIIVL---DDKPDGVLSIEDLL--SPTLGEEDEDLP-----------------PPLKDG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 PDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAwIGPFLDEGKEVIITALPLYHIFAL--VVNCLLFlrhGCRnVLI 289
Cdd:cd05911 145 KDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQT-FLYGNDGSNDVILGFLPLYHIYGLftTLASLLN---GAT-VII 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 290 TNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKV-TGVGLTEGYGLTE 368
Cdd:cd05911 220 MPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRfPNATIKQGYGMTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 369 CSPVVSFSPLSvPQWNGTIGVPLPSTLVSLRDEEENE-VPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDV 447
Cdd:cd05911 300 TGGILTVNPDG-DDKPGSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 448 AVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKD-PALTEAELRAYCH 526
Cdd:cd05911 379 GYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPgEKLTEKEVKDYVA 458
|
490 500
....*....|....*....|....*...
gi 522138377 527 ENLTGYK-MPKYITFLPELPKSNVGKVL 553
Cdd:cd05911 459 KKVASYKqLRGGVVFVDEIPKSASGKIL 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
20-557 |
1.01e-125 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 379.69 E-value: 1.01e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 20 VPRTIDTGAVpSLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNLLQYPVSLF 99
Cdd:PRK08314 1 LPKSLTLPET-SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 100 GVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGD-LAPFPKRAIVNFVVKRV 178
Cdd:PRK08314 80 AILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDyLPAEPEIAVPAWLRAEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 179 KkmVPAWSLPGTTGFRAALAKGRAQPYARVqlGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpflDEGKE 258
Cdd:PRK08314 160 P--LQALAPGGVVAWKEALAAGLAPPPHTA--GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSN---STPES 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 259 VIITALPLYHIFALV--VNCLLFLrhGCRNVLITN-PRDMAAFCVElkRSGFTAITGVNTLFNGLLHAPGFAELDFSRFK 335
Cdd:PRK08314 233 VVLAVLPLFHVTGMVhsMNAPIYA--GATVVLMPRwDREAAARLIE--RYRVTHWTNIPTMVVDFLASPGLAERDLSSLR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 336 LAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLSVPQwNGTIGVPL---------PSTLvslrdeeeNEV 406
Cdd:PRK08314 309 YIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPK-LQCLGIPTfgvdarvidPETL--------EEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 407 PPGQPGELCVKGPQVMQGYWQKPEESAKVF-TKDG--WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVA 483
Cdd:PRK08314 380 PPGEVGEIVVHGPQVFKGYWNRPEATAEAFiEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLY 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522138377 484 QHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA---LTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK08314 460 KHPAIQEACVIATPDPRRGETVKAVVVLRPEArgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
214-553 |
2.86e-116 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 347.74 E-value: 2.86e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 DIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGkEVIITALPLYHIFALVVNcLLFLRHGCRNVLITnPR 293
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG--LTEG-DVFLSTLPLFHIGGLFGL-LGALLAGGTVVLLP-KF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 294 DMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVV 373
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 374 SFS-PLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFtKDGWLKTGDVAVFEP 452
Cdd:cd04433 156 ATGpPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-EDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 453 NGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA-LTEAELRAYCHENLTG 531
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 522138377 532 YKMPKYITFLPELPKSNVGKVL 553
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| pimA |
TIGR03205 |
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found ... |
14-558 |
7.41e-112 |
|
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found in a characteristic operon pimFABCDE for the metabolism of pimelate and related compounds. It is found, so far, in Bradyrhizobium japonicum and several strains of Rhodopseudomonas palustris. PimA from R. palustris was shown to be active as a CoA ligase for C(7) to C(14) dicarboxylates and fatty acids.
Pssm-ID: 132249 [Multi-domain] Cd Length: 541 Bit Score: 343.87 E-value: 7.41e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 14 QEYPPSV--PRTIDTGAVPSLVAmfeQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNVlGLQRGDRVALMMPNL 91
Cdd:TIGR03205 6 QFYPEGVrwDATIARGTLPDLLS---KAAADYGPRPALEFRDRPITYTELEAMAETAAAALLRA-GYGKDASVALYLGNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 92 LQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIvivenfcttlqqviantpiqhvITTQIGDLAPFPKRAIV 171
Cdd:TIGR03205 82 PDHPINFFGALKAGARVVHLSPLDGERALSHKLSDSGARLL----------------------ITSDLAALLPMALKFLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 172 NFVVKRV---------KKMVPAWSLPGTTGF--RAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTA 240
Cdd:TIGR03205 140 KGLLDRLivceddnwgKVGTPQAPIPADPRIvtYADFVKGAAAPAEWPAVTPDDVALLQYTGGTTGLPKGAMLTHGNLTS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 241 NVQQVSAWIGPFLDE--GKEVIITALPLYHIFALVVNCLLFLRHGcrNVLITNPR-DMAAFC--VELKRSgfTAITGVNT 315
Cdd:TIGR03205 220 AVSIYDVWGKPSRATrgDVERVICVLPLFHIYALTVILLRSLRRG--DLISLHQRfDVAAVFrdIEEKRA--TVFPGVPT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 316 LFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTE-CSPVVSfSPLSVPQWNGTIGVPLPST 394
Cdd:TIGR03205 296 MWIALANDPSLEKRDLSSLATIGSGGAPLPVEVANFFERKTGLKLKSGWGMTEtCSPGTG-HPPEGPDKPGSIGLMLPGI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 395 ---LVSLrDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLkTGDVAVFEPNGYLRIVDRKKDMILVSGF 471
Cdd:TIGR03205 375 eldVVSL-DDPTKVLPPGEVGELRIRGPNVTRGYWNRPEESAEAFVGDRFL-TGDIGYMDTDGYFFLVDRKKDMIISGGF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 472 NVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA--LTEAELRAYCHENLTGYKMPKYITFLPELPKSNV 549
Cdd:TIGR03205 453 NVYPQMIEQAIYEHPGVQEVIVIGIPDQYRGEAAKAFVKLRPGAkpFSLDELRAFLAGKLGKHELPVAVEFVDELPRTPV 532
|
....*....
gi 522138377 550 GKVLRKELR 558
Cdd:TIGR03205 533 GKLSRHELR 541
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
12-557 |
2.29e-105 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 327.77 E-value: 2.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 12 WFQEYPPSVPRTID--TGAVPsLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMP 89
Cdd:PRK06178 14 QQAAWPAGIPREPEypHGERP-LTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQ-RGVGAGDRVAVFLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 90 NLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAPFPKRA 169
Cdd:PRK06178 92 NCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVLPAEPTL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 170 IVNFVVKrvkkmVPAWSLPGTTGFRAAL-AKGRAQPYARVQLgpDDIAFLQYTGGTTGLSKGAVLTHGNV---TANVQQV 245
Cdd:PRK06178 172 PLPDSLR-----APRLAAAGAIDLLPALrACTAPVPLPPPAL--DALAALNYTGGTTGMPKGCEHTQRDMvytAAAAYAV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 246 SAWIGPfldegKEVIITALPLYHIfALVVNCLLF-LRHGCRNVLITnpR-DMAAFCVELKRSGFTAITGVNTLFNGLLHA 323
Cdd:PRK06178 245 AVVGGE-----DSVFLSFLPEFWI-AGENFGLLFpLFSGATLVLLA--RwDAVAFMAAVERYRVTRTVMLVDNAVELMDH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 324 PGFAELDFSRFKlAVGGGTAVQQ---AVAEKWQKVTGVGLTEG-YGLTECSPVVSFSP---------LSVPQWngtIGVP 390
Cdd:PRK06178 317 PRFAEYDLSSLR-QVRVVSFVKKlnpDYRQRWRALTGSVLAEAaWGMTETHTCDTFTAgfqdddfdlLSQPVF---VGLP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 391 LPSTLVSLRDEEENE-VPPGQPGELCVKGPQVMQGYWQKPEESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVS 469
Cdd:PRK06178 393 VPGTEFKICDFETGElLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 470 GFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-KKDPALTEAELRAYCHENLTGYKMPKyITFLPELPKSN 548
Cdd:PRK06178 472 GMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQlKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTA 550
|
....*....
gi 522138377 549 VGKVLRKEL 557
Cdd:PRK06178 551 TGKVRKQDL 559
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
53-557 |
6.69e-104 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 321.88 E-value: 6.69e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNVLGLQrGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:cd05904 30 GRALTYAELERRVRRLAAGLAKRGGRK-GDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VivenfctTLQQVIANTPiQHVITTQIGDLAPFpkraivnfvvkrvkkmvpawslpGTTGFRAALAKGRAQPYARVQLGP 212
Cdd:cd05904 109 F-------TTAELAEKLA-SLALPVVLLDSAEF-----------------------DSLSFSDLLFEADEAEPPVVVIKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPfLDEGKEVIITALPLYHIFALVVNCLLFLRHGcrNVLITNP 292
Cdd:cd05904 158 DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGS-NSDSEDVFLCVLPMFHIYGLSSFALGLLRLG--ATVVVMP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 293 R-DMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKW-QKVTGVGLTEGYGLTECS 370
Cdd:cd05904 235 RfDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFrAKFPNVDLGQGYGMTEST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 371 PVVS--FSPLSVPQWNGTIGVPLPSTLVSLRDEEENEV-PPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDV 447
Cdd:cd05904 315 GVVAmcFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESlPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 448 AVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKK-DPALTEAELRAYCH 526
Cdd:cd05904 395 CYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKpGSSLTEDEIMDFVA 474
|
490 500 510
....*....|....*....|....*....|.
gi 522138377 527 ENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd05904 475 KQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
34-558 |
6.49e-102 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 318.68 E-value: 6.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 34 AMFEQSCARFGDQIA--YECMGQTLSFAELDRLTQDFASYLQnVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNV 111
Cdd:PRK08315 20 QLLDRTAARYPDREAlvYRDQGLRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 112 NPLYTPRELEHQLRDSGAKAIVIVENFCTT-----LQQVIANTPiqhviTTQIGDL--APFPKraivnfvVKRVKKMVPA 184
Cdd:PRK08315 99 NPAYRLSELEYALNQSGCKALIAADGFKDSdyvamLYELAPELA-----TCEPGQLqsARLPE-------LRRVIFLGDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 185 wSLPGTTGFRAALAKGRAQPYARV-----QLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANvqqvSAWIGP---FLDEG 256
Cdd:PRK08315 167 -KHPGMLNFDELLALGRAVDDAELaarqaTLDPDDPINIQYTSGTTGFPKGATLTHRNILNN----GYFIGEamkLTEED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 257 KEVIitALPLYHIFALVVNCLLFLRHGCRNVLITNPRD----MAAfcVELKRSgfTAITGVNTLFNGLLHAPGFAELDFS 332
Cdd:PRK08315 242 RLCI--PVPLYHCFGMVLGNLACVTHGATMVYPGEGFDplatLAA--VEEERC--TALYGVPTMFIAELDHPDFARFDLS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 333 RFKLAVGGGTA----VQQAVAEKwqkvtgVGLTE---GYGLTECSPVvSF-----SPLS--VpqwnGTIGVPLPSTLVSL 398
Cdd:PRK08315 316 SLRTGIMAGSPcpieVMKRVIDK------MHMSEvtiAYGMTETSPV-STqtrtdDPLEkrV----TTVGRALPHLEVKI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 399 RDEEENE-VPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNE 477
Cdd:PRK08315 385 VDPETGEtVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPRE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 478 IEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA-LTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKE 556
Cdd:PRK08315 465 IEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGAtLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFK 544
|
..
gi 522138377 557 LR 558
Cdd:PRK08315 545 MR 546
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
56-557 |
1.88e-99 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 307.87 E-value: 1.88e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIV 135
Cdd:cd05935 2 LTYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 136 ENFcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqpyarvqlgpDDI 215
Cdd:cd05935 81 SEL--------------------------------------------------------------------------DDL 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 216 AFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDeGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLITN-PRD 294
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTG--LT-PSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARwDRE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 295 MAAFCVElkRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVS 374
Cdd:cd05935 164 TALELIE--KYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTH 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 375 FSPLSVPQWNgTIGVPLPSTLVSLRDEEEN-EVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDG---WLKTGDVAVF 450
Cdd:cd05935 242 TNPPLRPKLQ-CLGIP*FGVDARVIDIETGrELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYM 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 451 EPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKdPAL----TEAELRAYCH 526
Cdd:cd05935 321 DEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLR-PEYrgkvTEEDIIEWAR 399
|
490 500 510
....*....|....*....|....*....|.
gi 522138377 527 ENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd05935 400 EQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
35-558 |
3.23e-99 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 310.33 E-value: 3.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 35 MFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPL 114
Cdd:PRK08316 16 ILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLD-LGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 115 YTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAPFPKraivnfvvkrvkkmvpawslpGTTGFr 194
Cdd:PRK08316 95 LTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPG---------------------GWLDF- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 195 AALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTAnvQQVSAWIGPFLDEGkEVIITALPLYHIFALVV 274
Cdd:PRK08316 153 ADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIA--EYVSCIVAGDMSAD-DIPLHALPLYHCAQLDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 275 NCLLFLRHGCRNVLITNPRdmAAFCVEL-KRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAV-AEKW 352
Cdd:PRK08316 230 FLGPYLYVGATNVILDAPD--PELILRTiEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVlKELR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 353 QKVTGVGLTEGYGLTECSPVVS-FSP---LSVPqwnGTIGvpLPSTLVSLR--DEEENEVPPGQPGELCVKGPQVMQGYW 426
Cdd:PRK08316 308 ERLPGLRFYNCYGQTEIAPLATvLGPeehLRRP---GSAG--RPVLNVETRvvDDDGNDVAPGEVGEIVHRSPQLMLGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 427 QKPEESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGE-VP 505
Cdd:PRK08316 383 DDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEaVT 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 522138377 506 KVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK08316 462 AVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELR 514
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
44-558 |
3.90e-98 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 308.96 E-value: 3.90e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 44 GDQIAYECMG-----QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPR 118
Cdd:COG0365 23 GDKVALIWEGedgeeRTLTYAELRREVNRFANALRA-LGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 119 ELEHQLRDSGAKAiVIVENFCTTLQQVIANTPIqhviTTQIGDLAPFPKRAIVnfvvkrVKKMVPAWSLPGTTGFRAALA 198
Cdd:COG0365 102 ALADRIEDAEAKV-LITADGGLRGGKVIDLKEK----VDEALEELPSLEHVIV------VGRTGADVPMEGDLDWDELLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 199 kGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIgpfLD--EGkEVIITALPLYHIFALVvNC 276
Cdd:COG0365 171 -AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV---LDlkPG-DVFWCTADIGWATGHS-YI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 277 LLF-LRHGCRNVL---ITNPRDMAAFCVELKRSGFTAITGVNTLFNGLL-HAPGFAE-LDFSRFKLAVGGGTAVQQAVAE 350
Cdd:COG0365 245 VYGpLLNGATVVLyegRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMkAGDEPLKkYDLSSLRLLGSAGEPLNPEVWE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 351 KWQKVTGVGLTEGYGLTE-CSPVVSFSPLsVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQ--VMQGYWQ 427
Cdd:COG0365 325 WWYEAVGVPIVDGWGQTEtGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 428 KPEESAKVF--TKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVP 505
Cdd:COG0365 404 DPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVV 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 522138377 506 KVFVV-KKDPALTEA---ELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:COG0365 484 KAFVVlKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLR 540
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
25-558 |
2.66e-96 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 306.11 E-value: 2.66e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 25 DTGAVPSLVAMFEQSCARFGDQIAYEC--------MGQTLSFAEL-DRLTQdfASYLQNVLGLQRGDRVALMMPNLLQYP 95
Cdd:PRK07529 20 ARDLPASTYELLSRAAARHPDAPALSFlldadpldRPETWTYAELlADVTR--TANLLHSLGVGPGDVVAFLLPNLPETH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 96 VSLFGVLRAGlVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTT-----LQQVIANTP-IQHVITTQIGDLAPFPKRA 169
Cdd:PRK07529 98 FALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTdiwqkVAEVLAALPeLRTVVEVDLARYLPGPKRL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 170 IVNFVVKRVKKMVpawslpgtTGFRAALAKGRA-QPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANvqqvsAW 248
Cdd:PRK07529 177 AVPLIRRKAHARI--------LDFDAELARQPGdRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN-----AW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 249 IGP---FLDEGKeVIITALPLYHIFALVVNCLLFLRHGCRNVLIT-----NPRDMAAFCVELKRSGFTAITGVNTLFNGL 320
Cdd:PRK07529 244 LGAlllGLGPGD-TVFCGLPLFHVNALLVTGLAPLARGAHVVLATpqgyrGPGVIANFWKIVERYRINFLSGVPTVYAAL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 321 LHAPgFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSL-- 398
Cdd:PRK07529 323 LQVP-VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVvi 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 399 RDEE---ENEVPPGQPGELCVKGPQVMQGYWQkPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYP 475
Cdd:PRK07529 402 LDDAgryLRDCAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 476 NEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFV-VKKDPALTEAELRAYC----HENLTgykMPKYITFLPELPKSNVG 550
Cdd:PRK07529 481 AAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVqLKPGASATEAELLAFArdhiAERAA---VPKHVRILDALPKTAVG 557
|
....*...
gi 522138377 551 KVLRKELR 558
Cdd:PRK07529 558 KIFKPALR 565
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
34-558 |
4.35e-96 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 303.62 E-value: 4.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 34 AMFEQSCARFGDQ--IAYECMGQTLSFAELDRLTQDFASYLQnVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNV 111
Cdd:PRK12583 22 DAFDATVARFPDReaLVVRHQALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 112 NPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAP--FPKraivnfvVKRVKKMVPAwSLPG 189
Cdd:PRK12583 101 NPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAEGQPGALACerLPE-------LRGVVSLAPA-PPPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 190 TTGFRAALAKGRAQPYARV-----QLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEgKEVIITAL 264
Cdd:PRK12583 173 FLAWHELQARGETVSREALaerqaSLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLG--LTE-HDRLCVPV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 265 PLYHIFALVVNCLLFLRHGCRNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAV 344
Cdd:PRK12583 250 PLYHCFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPC 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 345 QQAVAEKWQKVTGVG-LTEGYGLTECSPVVSFSPL--SVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQV 421
Cdd:PRK12583 330 PIEVMRRVMDEMHMAeVQIAYGMTETSPVSLQTTAadDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 422 MQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKS 501
Cdd:PRK12583 410 MKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 522138377 502 GEVPKVFVV-KKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK12583 490 GEEIVAWVRlHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
212-558 |
6.30e-96 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 296.11 E-value: 6.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 PDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpflDEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLITN 291
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLG---LTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 292 PRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGV-GLTEGYGLTECS 370
Cdd:cd05917 78 SFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 371 PVV--SFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPP-GQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDV 447
Cdd:cd05917 158 PVStqTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 448 AVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFV-VKKDPALTEAELRAYCH 526
Cdd:cd05917 238 AVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIrLKEGAELTEEDIKAYCK 317
|
330 340 350
....*....|....*....|....*....|..
gi 522138377 527 ENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05917 318 GKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
56-558 |
3.50e-94 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 296.53 E-value: 3.50e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIv 135
Cdd:cd05926 15 LTYADLAELVDDLARQLAA-LGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 136 enfcttlqQVIANTPIQhvittqigDLAPFPKRAIVN--FVVKRVKKMVPAWSLPGTTgfrAALAKGRAQPYARvqlgPD 213
Cdd:cd05926 93 --------PKGELGPAS--------RAASKLGLAILElaLDVGVLIRAPSAESLSNLL---ADKKNAKSEGVPL----PD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 DIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAwiGPFLDEGKEVIITaLPLYHIFALVVNCLLFLRHGCrNVLITNPR 293
Cdd:cd05926 150 DLALILHTSGTTGRPKGVPLTHRNLAASATNITN--TYKLTPDDRTLVV-MPLFHVHGLVASLLSTLAAGG-SVVLPPRF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 294 DMAAFCVELKRSGFTAITGVNTLFNGLL-HAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPV 372
Cdd:cd05926 226 SASTFWPDVRDYNATWYTAVPTIHQILLnRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 373 VSFSPL-SVPQWNGTIGVPLpSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFE 451
Cdd:cd05926 306 MTSNPLpPGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 452 PNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-KKDPALTEAELRAYCHENLT 530
Cdd:cd05926 385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVlREGASVTEEELRAFCRKHLA 464
|
490 500
....*....|....*....|....*...
gi 522138377 531 GYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05926 465 AFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
45-558 |
4.25e-94 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 294.58 E-value: 4.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQL 124
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 125 RDSGAKAIVivenfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqp 204
Cdd:cd05941 81 TDSEPSLVL----------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 205 yarvqlgpdDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQ-VSAWigPFLDEgkEVIITALPLYHIFALVVNCLLFLRHG 283
Cdd:cd05941 90 ---------DPALILYTSGTTGRPKGVVLTHANLAANVRAlVDAW--RWTED--DVLLHVLPLHHVHGLVNALLCPLFAG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 284 CRNVLITNPRDMAAFCVELKRSgFTAITGVNTLFNGLLHAPGFAELD--------FSRFKLAVGGGTAVQQAVAEKWQKV 355
Cdd:cd05941 157 ASVEFLPKFDPKEVAISRLMPS-ITVFMGVPTIYTRLLQYYEAHFTDpqfaraaaAERLRLMVSGSAALPVPTLEEWEAI 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 356 TGVGLTEGYGLTECSPVVSfSPLSVPQWNGTIGVPLPSTLVSLRDEEENE-VPPGQPGELCVKGPQVMQGYWQKPEESAK 434
Cdd:cd05941 236 TGHTLLERYGMTEIGMALS-NPLDGERRPGTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVRGPSVFKEYWNKPEATKE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 435 VFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVS-GFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKD 513
Cdd:cd05941 315 EFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSgGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRA 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 522138377 514 --PALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05941 395 gaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELR 441
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
45-557 |
6.02e-93 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 293.30 E-value: 6.02e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQL 124
Cdd:PRK06839 17 DRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 125 RDSGAKAIVIVENFCTTLQQVIANTPIQHVIttQIGDLAPFPKRAIVNFVVKrvkkmvpawslpgttgfraalakgraqp 204
Cdd:PRK06839 97 KDSGTTVLFVEKTFQNMALSMQKVSYVQRVI--SITSLKEIEDRKIDNFVEK---------------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 205 yarvqlGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEgkeVIITALPLYHIFALVVNCLLFLRHGC 284
Cdd:PRK06839 147 ------NESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHD---RSIVLLPLFHIGGIGLFAFPTLFAGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 285 RNVLitnPR----DMAAFCVELKRsgFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKvTGVGL 360
Cdd:PRK06839 218 VIIV---PRkfepTKALSMIEKHK--VTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFID-RGFLF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 361 TEGYGLTECSPVV-SFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFtKD 439
Cdd:PRK06839 292 GQGFGMTETSPTVfMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 440 GWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA-LTE 518
Cdd:PRK06839 371 GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSvLIE 450
|
490 500 510
....*....|....*....|....*....|....*....
gi 522138377 519 AELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK06839 451 KDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
34-558 |
4.53e-92 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 292.05 E-value: 4.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 34 AMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNP 113
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLA-LGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFALP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 114 LYTPRELEHQLRDSGAKAIVIVE-----NFCTTLQQVIANTP-IQHVITtqIGDLAPFpkraivnfvvkrvkkmvpawsl 187
Cdd:COG1021 108 AHRRAEISHFAEQSEAVAYIIPDrhrgfDYRALARELQAEVPsLRHVLV--VGDAGEF---------------------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 188 pgtTGFRAALAKGRAQPYARVQlgPDDIAFLQYTGGTTGLSKGAVLTHG----NVTANVQQVSawigpfLDEGkEVIITA 263
Cdd:COG1021 164 ---TSLDALLAAPADLSEPRPD--PDDVAFFQLSGGTTGLPKLIPRTHDdylySVRASAEICG------LDAD-TVYLAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 264 LPLYHIFALVVNCLL-FLRHGCRNVLITNPRDMAAFcvEL-KRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGG 341
Cdd:COG1021 232 LPAAHNFPLSSPGVLgVLYAGGTVVLAPDPSPDTAF--PLiERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 342 TAVQQAVAEKWQKVTGVGLTEGYGLTEcsPVVSFSPLSVPQW--NGTIGVPL-PSTLVSLRDEEENEVPPGQPGELCVKG 418
Cdd:COG1021 310 AKLSPELARRVRPALGCTLQQVFGMAE--GLVNYTRLDDPEEviLTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 419 PQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPD 498
Cdd:COG1021 388 PYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPD 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522138377 499 EKSGEVPKVFVVKKDPALTEAELRAYCHE-NLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:COG1021 468 EYLGERSCAFVVPRGEPLTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKALR 528
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
25-495 |
5.28e-92 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 293.93 E-value: 5.28e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 25 DTGAVPSLVAMFEQSCARFGDQIAYECMG----QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFG 100
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLA-LGVKPGDRVAILSDNRPEWVIADLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 101 VLRAGLVVVnvnPLY---TPRELEHQLRDSGAKaIVIVENF--CTTLQQVIANTP-IQHVITtqIGDLAPfpkraivnfv 174
Cdd:COG1022 85 ILAAGAVTV---PIYptsSAEEVAYILNDSGAK-VLFVEDQeqLDKLLEVRDELPsLRHIVV--LDPRGL---------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 175 vkrvkkmvpaWSLPGTTGFRAALAKGRAQPY------ARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAW 248
Cdd:COG1022 149 ----------RDDPRLLSLDELLALGREVADpaeleaRRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 249 IGpfLDEGkEVIITALPLYHIFALVVnCLLFLRHGCRNVLITNPRDMAAfcvELKRSGFTAITGV--------NTLFNGL 320
Cdd:COG1022 219 LP--LGPG-DRTLSFLPLAHVFERTV-SYYALAAGATVAFAESPDTLAE---DLREVKPTFMLAVprvwekvyAGIQAKA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 321 LHAPGFAELDFSRF-KLA------------VGGGTAVQQAVAE-----KWQKVTG-----------------------VG 359
Cdd:COG1022 292 EEAGGLKRKLFRWAlAVGrryararlagksPSLLLRLKHALADklvfsKLREALGgrlrfavsggaalgpelarffraLG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 360 LT--EGYGLTECSPVVSFSPlsvPQWN--GTIGVPLPSTLVSLrdeeenevppGQPGELCVKGPQVMQGYWQKPEESAKV 435
Cdd:COG1022 372 IPvlEGYGLTETSPVITVNR---PGDNriGTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEA 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522138377 436 FTKDGWLKTGDVAVFEPNGYLRIVDRKKDMI-LVSGFNVYPNEIEGVVAQHPGVLEVACIG 495
Cdd:COG1022 439 FDADGWLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
53-558 |
8.40e-90 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 282.64 E-value: 8.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAA-LGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIvenfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqpyarvqlgp 212
Cdd:cd05934 80 VV------------------------------------------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 dDIAFLQYTGGTTGLSKGAVLTHGNVTaNVQQVSAWIGPFLDEgkEVIITALPLYHIFALVVNCLLFLRHGCRNVLItnP 292
Cdd:cd05934 82 -DPASILYTSGTTGPPKGVVITHANLT-FAGYYSARRFGLGED--DVYLTVLPLFHINAQAVSVLAALSVGATLVLL--P 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 293 RDMA-AFCVELKRSGFTAITGVNTLFNGLLHAPgfAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTEcSP 371
Cdd:cd05934 156 RFSAsRFWSDVRRYGATVTNYLGAMLSYLLAQP--PSPDDRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTE-TI 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 372 VVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVK---GPQVMQGYWQKPEESAKVFtKDGWLKTGDVA 448
Cdd:cd05934 233 VGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 449 VFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA-LTEAELRAYCHE 527
Cdd:cd05934 312 YRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGEtLDPEELFAFCEG 391
|
490 500 510
....*....|....*....|....*....|.
gi 522138377 528 NLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05934 392 QLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
41-560 |
1.46e-89 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 285.34 E-value: 1.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 41 ARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPREL 120
Cdd:PRK06188 23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEA-LGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 121 EHQLRDSGAKAIVIvenfcttlqqviantpiqhvittqigDLAPFPKRAIVNFV-VKRVKKMVPAWSLPGTTGFRAALAK 199
Cdd:PRK06188 102 AYVLEDAGISTLIV--------------------------DPAPFVERALALLArVPSLKHVLTLGPVPDGVDLLAAAAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 200 GRAQPYARVQLgPDDIAFLQYTGGTTGLSKGAVLTH-GNVTANVQQVSAWIGPfldEGKEVIITAlPLYHIFALVVNCLL 278
Cdd:PRK06188 156 FGPAPLVAAAL-PPDIAGLAYTGGTTGKPKGVMGTHrSIATMAQIQLAEWEWP---ADPRFLMCT-PLSHAGGAFFLPTL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 279 fLRHGCrnVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGV 358
Cdd:PRK06188 231 -LRGGT--VIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 359 GLTEGYGLTECSPVVSFSP-----LSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESA 433
Cdd:PRK06188 308 IFAQYYGQTEAPMVITYLRkrdhdPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 434 KVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-KK 512
Cdd:PRK06188 388 EAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVlRP 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 522138377 513 DPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELRGK 560
Cdd:PRK06188 467 GAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
44-558 |
1.81e-89 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 284.65 E-value: 1.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 44 GDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQ 123
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 124 LRDSGAKAIVIVENFCTTLQQVI--ANTPIQHVITTQigdlapfpkraivnfvvkrvkkmvPAWSLPGTTGFRAALAKGR 201
Cdd:cd05959 97 LEDSRARVVVVSGELAPVLAAALtkSEHTLVVLIVSG------------------------GAGPEAGALLLAELVAAEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 202 AQ-PYARVQlgPDDIAFLQYTGGTTGLSKGAVLTHGN--VTAN--VQQVSAwigpfLDEGkEVIITALPLYHIFALVvNC 276
Cdd:cd05959 153 EQlKPAATH--ADDPAFWLYSSGSTGRPKGVVHLHADiyWTAElyARNVLG-----IRED-DVCFSAAKLFFAYGLG-NS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 277 LLF-LRHGCRNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKV 355
Cdd:cd05959 224 LTFpLSVGATTVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 356 TGVGLTEGYGLTECSPV-VSFSPLSVPQwnGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAK 434
Cdd:cd05959 304 FGLDILDGIGSTEMLHIfLSNRPGRVRY--GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 435 VFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKK-- 512
Cdd:cd05959 382 TF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRpg 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 522138377 513 --DPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05959 461 yeDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
53-558 |
5.10e-88 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 280.61 E-value: 5.10e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMM----PNLLQYpvslFGVLRAGLVVVNVNPLYTPRELEHQLRDSG 128
Cdd:PRK07514 26 GLRYTYGDLDAASARLANLLVA-LGVKPGDRVAVQVekspEALALY----LATLRAGAVFLPLNTAYTLAELDYFIGDAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 129 AKAIVIVENFCTTLQQVIANTPIQHVITtqIGDLApfpkraivnfvvkrvkkmvpawslpgtTGFRAALAKGRAQPYARV 208
Cdd:PRK07514 101 PALVVCDPANFAWLSKIAAAAGAPHVET--LDADG---------------------------TGSLLEAAAAAPDDFETV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 209 QLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQ-VSAW-IGPfldegKEVIITALPLYHIFALVV--NCLLFlrHGC 284
Cdd:PRK07514 152 PRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTlVDYWrFTP-----DDVLIHALPIFHTHGLFVatNVALL--AGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 285 RnvLITNPR-DMAAFCVELKRSgfTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEG 363
Cdd:PRK07514 225 S--MIFLPKfDPDAVLALMPRA--TVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILER 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 364 YGLTECSPVVSfSPLSVPQWNGTIGVPLPStlVSLR--DEEEN-EVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDG 440
Cdd:PRK07514 301 YGMTETNMNTS-NPYDGERRAGTVGFPLPG--VSLRvtDPETGaELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 441 WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGE-VPKVFVVKKDPALTEA 519
Cdd:PRK07514 378 FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEgVTAVVVPKPGAALDEA 457
|
490 500 510
....*....|....*....|....*....|....*....
gi 522138377 520 ELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK07514 458 AILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
56-559 |
4.54e-81 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 260.35 E-value: 4.54e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIV 135
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 136 EnfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqpyarvqlgpDDI 215
Cdd:cd05972 80 A----------------------------------------------------------------------------EDP 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 216 AFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIITALP--LYHIFALVVNCLLflrHGCRNVLITNPR 293
Cdd:cd05972 84 ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLG--LRPDDIHWNIADPgwAKGAWSSFFGPWL---LGATVFVYEGPR 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 294 DMAAFCVE-LKRSGFTAITGVNTLFNgLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPV 372
Cdd:cd05972 159 FDAERILElLERYGVTSFCGPPTAYR-MLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 373 VSFSPlSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVK--GPQVMQGYWQKPEESAKVFtKDGWLKTGDVAVF 450
Cdd:cd05972 238 VGNFP-DMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYR 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 451 EPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKD-----PALTEaELRAYC 525
Cdd:cd05972 316 DEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSgyepsEELAE-ELQGHV 394
|
490 500 510
....*....|....*....|....*....|....
gi 522138377 526 HENLTGYKMPKYITFLPELPKSNVGKVLRKELRG 559
Cdd:cd05972 395 KKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
53-560 |
1.45e-79 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 259.53 E-value: 1.45e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:PLN02246 48 GRVYTYADVELLSRRVAAGLHK-LGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIVENFCTTLQQVIANTPIQHVITTQIGDlapfpkraivnfvvkrvkKMVPAWSLpgTTGFRAALAKgraqpyarVQLGP 212
Cdd:PLN02246 127 ITQSCYVDKLKGLAEDDGVTVVTIDDPPE------------------GCLHFSEL--TQADENELPE--------VEISP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTH-GNVTANVQQVSAWIGPFLDEGKEVIITALPLYHIFALvvNCLLF--LRHGCrNVLI 289
Cdd:PLN02246 179 DDVVALPYSSGTTGLPKGVMLTHkGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYSL--NSVLLcgLRVGA-AILI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 290 TNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGG----GTAVQQAVAEKwqkVTGVGLTEGYG 365
Cdd:PLN02246 256 MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGaaplGKELEDAFRAK---LPNAVLGQGYG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 366 LTECSPVVSFS------PLSV-PQWNGTI------GVPLPSTLVSLrdeeenevPPGQPGELCVKGPQVMQGYWQKPEES 432
Cdd:PLN02246 333 MTEAGPVLAMClafakePFPVkSGSCGTVvrnaelKIVDPETGASL--------PRNQPGEICIRGPQIMKGYLNDPEAT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 433 AKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVK- 511
Cdd:PLN02246 405 ANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRs 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 522138377 512 KDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELRGK 560
Cdd:PLN02246 485 NGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
55-559 |
1.56e-79 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 255.73 E-value: 1.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 55 TLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAivi 134
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAA-LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 135 venfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqpyarvqlgpDD 214
Cdd:cd05912 77 ------------------------------------------------------------------------------DD 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 215 IAFLQYTGGTTGLSKGAVLTHGNVTANVqqvsawIGPFLDEG---KEVIITALPLYHIFALVVncllFLR---HGCRNVL 288
Cdd:cd05912 79 IATIMYTSGTTGKPKGVQQTFGNHWWSA------IGSALNLGlteDDNWLCALPLFHISGLSI----LMRsviYGMTVYL 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 289 itnprdMAAFCVE-----LKRSGFTAITGVNTLFNGLL--HAPGFAElDFSRFKLavGGGTAVQQAVAEKWQKvtGVGLT 361
Cdd:cd05912 149 ------VDKFDAEqvlhlINSGKVTIISVVPTMLQRLLeiLGEGYPN-NLRCILL--GGGPAPKPLLEQCKEK--GIPVY 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 362 EGYGLTE-CSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDeeeNEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFtKDG 440
Cdd:cd05912 218 QSYGMTEtCSQIVTLSPEDALNKIGSAGKPLFPVELKIED---DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 441 WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPaLTEAE 520
Cdd:cd05912 294 WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP-ISEEE 372
|
490 500 510
....*....|....*....|....*....|....*....
gi 522138377 521 LRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELRG 559
Cdd:cd05912 373 LIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
29-558 |
3.12e-79 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 258.43 E-value: 3.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 29 VPSLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVV 108
Cdd:PRK07470 6 VMNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAA-RGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 109 VNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTP-IQHVITtqIGdlapfpkraivnfvvkrvkkmvpawSL 187
Cdd:PRK07470 85 VPTNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPdLTHVVA--IG-------------------------GA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 188 PGTTGFRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEGKEVIITAlPLY 267
Cdd:PRK07470 138 RAGLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMAFVITNHLADLMPGTTEQDASLVVA-PLS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 268 HifALVVNCLLFLRHGCRNVLITNPR-DMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQ 346
Cdd:PRK07470 217 H--GAGIHQLCQVARGAATVLLPSERfDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 347 AVAEKWQKVTGVGLTEGYGLTECS------PVVSFSPLSVPQWN-GTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGP 419
Cdd:PRK07470 295 ADQKRALAKLGKVLVQYFGLGEVTgnitvlPPALHDAEDGPDARiGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 420 QVMQGYWQKPEESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDE 499
Cdd:PRK07470 375 AVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDP 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 500 KSGEVPKVFVVKKDPA-LTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK07470 454 VWGEVGVAVCVARDGApVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
45-558 |
6.72e-78 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 253.73 E-value: 6.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQypvsLFGVLRA----GLVVVNVNPLYTPREL 120
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAA-LGVKKGDRVALLMKNGME----MILVIHAlqqlGAVAVLLNTRLSREEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 121 EHQLRDSGAKAIVIVENFCTtlqqviantpiQHVITTQIgDLAPFPKRAivnfvvKRVKKMVPAWSLpgttgfraalakg 200
Cdd:PRK03640 92 LWQLDDAEVKCLITDDDFEA-----------KLIPGISV-KFAELMNGP------KEEAEIQEEFDL------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 201 raqpyarvqlgpDDIAFLQYTGGTTGLSKGAVLTHGNVTAnvqqvSAwIGPFLDEG---KEVIITALPLYHI--FALVVN 275
Cdd:PRK03640 141 ------------DEVATIMYTSGTTGKPKGVIQTYGNHWW-----SA-VGSALNLGlteDDCWLAAVPIFHIsgLSILMR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 276 CLLFlrhGCRNVLitnprdMAAFCVE-----LKRSGFTAITGVNTLFNGLLhapgfAELDFSRFK-----LAVGGGTAVQ 345
Cdd:PRK03640 203 SVIY---GMRVVL------VEKFDAEkinklLQTGGVTIISVVSTMLQRLL-----ERLGEGTYPssfrcMLLGGGPAPK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 346 QAVAEKWQKvtGVGLTEGYGLTE-CSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEeNEVPPGQPGELCVKGPQVMQG 424
Cdd:PRK03640 269 PLLEQCKEK--GIPVYQSYGMTEtASQIVTLSPEDALTKLGSAGKPLFPCELKIEKDG-VVVPPFEEGEIVVKGPNVTKG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 425 YWQKPEESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEV 504
Cdd:PRK03640 346 YLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQV 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 522138377 505 PKVFVVkKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK03640 425 PVAFVV-KSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELK 477
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
57-558 |
7.64e-76 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 249.47 E-value: 7.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 57 SFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVE 136
Cdd:cd12119 27 TYAEVAERARRLANALRR-LGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 137 NFCTTLQQVIANTP-IQHVITTQIGDLAPFPkraivnfvvkrvkkmvpawSLPGTTGFRAALAKGRAqPYARVQLGPDDI 215
Cdd:cd12119 106 DFLPLLEAIAPRLPtVEHVVVMTDDAAMPEP-------------------AGVGVLAYEELLAAESP-EYDWPDFDENTA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 216 AFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEGkEVIITALPLYHIFA--LVVNCLLFlrhGCRNVLiTNPR 293
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSES-DVVLPVVPMFHVNAwgLPYAAAMV---GAKLVL-PGPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 294 DMAAFCVEL-KRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVtGVGLTEGYGLTECSPV 372
Cdd:cd12119 241 LDPASLAELiEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 373 VSFSPLSVPQWNG----------TIGVPLPSTLVSLRDEEENEVP--PGQPGELCVKGPQVMQGYWQKPEESAKvFTKDG 440
Cdd:cd12119 320 GTVARPPSEHSNLsedeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDEESEA-LTEDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 441 WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA-LTEA 519
Cdd:cd12119 399 WLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGAtVTAE 478
|
490 500 510
....*....|....*....|....*....|....*....
gi 522138377 520 ELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd12119 479 ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
12-558 |
3.66e-74 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 245.44 E-value: 3.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 12 WFQEYPPSVPRTIDtGAVPS---LVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQnVLGLQRGDRVALMM 88
Cdd:PRK06155 1 GEPLGAGLAARAVD-PLPPSertLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALA-AAGVKRGDRVALMC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 89 PNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIAntpiqhvittqiGDLaPFPKR 168
Cdd:PRK06155 79 GNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADP------------GDL-PLPAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 169 AIVNfvvkrvkkMVPAWSLPgtTGFRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGnvtanvQQVsaW 248
Cdd:PRK06155 146 WLLD--------APASVSVP--AGWSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHA------QFY--W 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 249 IGPFLDE-----GKEVIITALPLYHIFAL--VVNCLLflrHGCRNVLitNPRDMAA-FCVELKRSGFTAITGVNTLFNGL 320
Cdd:PRK06155 208 WGRNSAEdleigADDVLYTTLPLFHTNALnaFFQALL---AGATYVL--EPRFSASgFWPAVRRHGATVTYLLGAMVSIL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 321 LHAPGFAELDFSRFKLAVGGGTAVQQAVAekWQKVTGVGLTEGYGLTECSPVVSFSPLSvpQWNGTIGVPLPSTLVSLRD 400
Cdd:PRK06155 283 LSQPARESDRAHRVRVALGPGVPAALHAA--FRERFGVDLLDGYGSTETNFVIAVTHGS--QRPGSMGRLAPGFEARVVD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 401 EEENEVPPGQPGELCVKGPQ---VMQGYWQKPEESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNE 477
Cdd:PRK06155 359 EHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 478 IEGVVAQHPGVLEVACIGVPDEKSG-EVPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKE 556
Cdd:PRK06155 438 VEQVLLSHPAVAAAAVFPVPSELGEdEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFV 517
|
..
gi 522138377 557 LR 558
Cdd:PRK06155 518 LR 519
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
54-495 |
7.23e-74 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 242.12 E-value: 7.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVnvnPLY---TPRELEHQLRDSGAK 130
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIA-LGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYptsSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 131 AIvIVENfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqpyarvql 210
Cdd:cd05907 80 AL-FVED------------------------------------------------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 211 gPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPfldEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLIT 290
Cdd:cd05907 86 -PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA---TEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 291 NPRDMAAfcvELKRSGFTAITGV----NTLFNGLLHA--PG-----FAELDFSRFKLAVGGGTAVQQAVAEKWQKVtGVG 359
Cdd:cd05907 162 SAETLLD---DLSEVRPTVFLAVprvwEKVYAAIKVKavPGlkrklFDLAVGGRLRFAASGGAPLPAELLHFFRAL-GIP 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 360 LTEGYGLTECSPVVSFSPLSVPQwNGTIGVPLPSTLVSLRDEeenevppgqpGELCVKGPQVMQGYWQKPEESAKVFTKD 439
Cdd:cd05907 238 VYEGYGLTETSAVVTLNPPGDNR-IGTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDAD 306
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 522138377 440 GWLKTGDVAVFEPNGYLRIVDRKKDMILVS-GFNVYPNEIEGVVAQHPGVLEVACIG 495
Cdd:cd05907 307 GWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVIG 363
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
55-558 |
7.77e-74 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 241.52 E-value: 7.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 55 TLSFAELDRLTQDFASYLqNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVI 134
Cdd:cd05903 1 RLTYSELDTRADRLAAGL-AALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 135 VENFcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvKKMVPAwslpgttgfraalakgrAQPyarvqlgpDD 214
Cdd:cd05903 80 PERF----------------------------------------RQFDPA-----------------AMP--------DA 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 215 IAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGkEVIITALPLYHIFALVVNCLLFLRHGCRNVL--ITNP 292
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG--LGPG-DVFLVASPMAHQTGFVYGFTLPLLLGAPVVLqdIWDP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 293 RDmaafCVELKRS-GFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTEC-S 370
Cdd:cd05903 172 DK----ALALMREhGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECpG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 371 PVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEeSAKVFTKDGWLKTGDVAVF 450
Cdd:cd05903 248 AVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPD-LTADAAPEGWFRTGDLARL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 451 EPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA-LTEAELRAYC-HEN 528
Cdd:cd05903 327 DEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGAlLTFDELVAYLdRQG 406
|
490 500 510
....*....|....*....|....*....|
gi 522138377 529 LTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05903 407 VAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
214-554 |
1.05e-73 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 237.78 E-value: 1.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 DIAFLQYTGGTTGLSKGAVLTHgnvTANVQQVSAW--IGPFLDEGKEVIITalPLYHIFALVVNCLLFLRHGCrNVLITN 291
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAH---RQTLRAAAAWadCADLTEDDRYLIIN--PFFHTFGYKAGIVACLLTGA-TVVPVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 292 PRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQK-------VTGVGLTEGY 364
Cdd:cd17638 75 VFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSelgfetvLTAYGLTEAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 365 GLTECSPVVSFSPLSVpqwngTIGVPLPSTLVSLRDeeenevppgqPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKT 444
Cdd:cd17638 155 VATMCRPGDDAETVAT-----TCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 445 GDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDP-ALTEAELRA 523
Cdd:cd17638 220 GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGvTLTEEDVIA 299
|
330 340 350
....*....|....*....|....*....|.
gi 522138377 524 YCHENLTGYKMPKYITFLPELPKSNVGKVLR 554
Cdd:cd17638 300 WCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
46-558 |
1.74e-73 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 240.83 E-value: 1.74e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 46 QIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLR 125
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRN-LGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 126 DSGAKAIVIVEnfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqpy 205
Cdd:cd05919 80 DCEARLVVTSA--------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 206 arvqlgpDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQqvsAWIGPFL--DEGKEVIITAlPLYHIFALVvNCLLF-LRH 282
Cdd:cd05919 91 -------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFAD---AMAREALglTPGDRVFSSA-KMFFGYGLG-NSLWFpLAV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 283 GCRNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTE 362
Cdd:cd05919 159 GASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILD 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 363 GYGLTECSPVvsFSPLSVPQWN-GTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFtKDGW 441
Cdd:cd05919 239 GIGATEVGHI--FLSNRPGAWRlGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGW 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 442 LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPALTEA-- 519
Cdd:cd05919 316 YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEsl 395
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 522138377 520 --ELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05919 396 arDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
53-558 |
1.42e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 240.09 E-value: 1.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:PRK09088 20 GRRWTYAELDALVGRLAAVLRR-RGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VivenfcttlqqviantpiqhvittqiGDLAPFPKRAIVNFVvkrvkkmvpawslpgtTGFRAALAKgrAQPYARVQLGP 212
Cdd:PRK09088 99 L--------------------------GDDAVAAGRTDVEDL----------------AAFIASADA--LEPADTPSIPP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTHgnvtANVQQVSAWIGPFLDEGKE-VIITALPLYHIFALVVNCLLFLRHGcRNVLITN 291
Cdd:PRK09088 135 ERVSLILFTSGTSGQPKGVMLSE----RNLQQTAHNFGVLGRVDAHsSFLCDAPMFHIIGLITSVRPVLAVG-GSILVSN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 292 PRDMAAfcvELKRS-----GFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGtAVQQAVAEKWQKVTGVGLTEGYGL 366
Cdd:PRK09088 210 GFEPKR---TLGRLgdpalGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGG-APHAAEDILGWLDDGIPMVDGFGM 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 367 TECSPV--VSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKT 444
Cdd:PRK09088 286 SEAGTVfgMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 445 GDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPALTE-AELRA 523
Cdd:PRK09088 366 GDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDlERIRS 445
|
490 500 510
....*....|....*....|....*....|....*
gi 522138377 524 YCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK09088 446 HLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
31-557 |
3.69e-72 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 238.77 E-value: 3.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 31 SLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVN 110
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRG-LGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 111 VNPLYTPRELEHQLRDSGAKAIVIvenfcttlqqviantPIQHvittqigdlAPFPKRAIvnfvvkrvkkmvpawslpgt 190
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIV---------------PDRH---------AGFDHRAL-------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 191 tgFRAALAKGRaqpyarvqlgpdDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEgKEVIITALPLYHIF 270
Cdd:cd05920 131 --ARELAESIP------------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCG--LDQ-DTVYLAVLPAAHNF 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 271 AL----VVNCLLFlrhGCRNVLITNPRDMAAFCVeLKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQ 346
Cdd:cd05920 194 PLacpgVLGTLLA---GGRVVLAPDPSPDAAFPL-IEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 347 AVAEKWQKVTGVGLTEGYGLTEcsPVVSFSPLSVP--QWNGTIGVPL-PSTLVSLRDEEENEVPPGQPGELCVKGPQVMQ 423
Cdd:cd05920 270 ALARRVPPVLGCTLQQVFGMAE--GLLNYTRLDDPdeVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 424 GYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGE 503
Cdd:cd05920 348 GYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGE 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 522138377 504 VPKVFVVKKDPALTEAELRAYCHE-NLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd05920 428 RSCAFVVLRDPPPSAAQLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
45-558 |
1.06e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 238.91 E-value: 1.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLqNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQL 124
Cdd:PRK07786 32 DAPALRFLGNTTTWRELDDRVAALAGAL-SRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 125 RDSGAKAIVIvenfcttlQQVIANtpiqhvITTQIGDLAPFPKRAIVnfvvkrvkkmVPAWSLPGTTGFRAALAKGRAqP 204
Cdd:PRK07786 111 SDCGAHVVVT--------EAALAP------VATAVRDIVPLLSTVVV----------AGGSSDDSVLGYEDLLAEAGP-A 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 205 YARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTAnvQQVSAWIGPFLDEGKEVIITALPLYHIfALVVNCLLFLRHGC 284
Cdd:PRK07786 166 HAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTG--QAMTCLRTNGADINSDVGFVGVPLFHI-AGIGSMLPGLLLGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 285 RNVLI-TNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEG 363
Cdd:PRK07786 243 PTVIYpLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQILAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 364 YGLTECSPVV-------SFSPLsvpqwnGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVF 436
Cdd:PRK07786 323 FGQTEMSPVTcmllgedAIRKL------GSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 437 tKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA- 515
Cdd:PRK07786 397 -AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDa 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 522138377 516 -LTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK07786 476 aLTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
57-557 |
1.58e-71 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 235.42 E-value: 1.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 57 SFAELDRLTQDFASYLQnVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSgakaivive 136
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALK-AQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDL--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 137 nfcttlqqviantPIQHVITTQigdlaPFPKRAIVnfvvkrvkkmvpAWSLPGTTgfraalAKGRAQPYARVQLGPDDIA 216
Cdd:TIGR01923 71 -------------DVQLLLTDS-----LLEEKDFQ------------ADSLDRIE------AAGRYETSLSASFNMDQIA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 217 FLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIItALPLYHI--FALVVNCLLflrhGCRNVLITNPrd 294
Cdd:TIGR01923 115 TLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLG--FTEDDNWLL-SLPLYHIsgLSILFRWLI----EGATLRIVDK-- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 295 MAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAEldfsRFKLAVGGGTAVQQAVAEKWQKvTGVGLTEGYGLTE-CSPVV 373
Cdd:TIGR01923 186 FNQLLEMIANERVTHISLVPTQLNRLLDEGGHNE----NLRKILLGGSAIPAPLIEEAQQ-YGLPIYLSYGMTEtCSQVT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 374 SFSPLSVPQwNGTIGVPLPSTLVSLRDEEENEVppgqpGELCVKGPQVMQGYWQkPEESAKVFTKDGWLKTGDVAVFEPN 453
Cdd:TIGR01923 261 TATPEMLHA-RPDVGRPLAGREIKIKVDNKEGH-----GEIMVKGANLMKGYLY-QGELTPAFEQQGWFNTGDIGELDGE 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 454 GYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPaLTEAELRAYCHENLTGYK 533
Cdd:TIGR01923 334 GFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESD-ISQAKLIAYLTEKLAKYK 412
|
490 500
....*....|....*....|....
gi 522138377 534 MPKYITFLPELPKSNVGKVLRKEL 557
Cdd:TIGR01923 413 VPIAFEKLDELPYNASGKILRNQL 436
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
53-558 |
3.17e-70 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 235.51 E-value: 3.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRD-SGAKA 131
Cdd:PLN02574 64 GFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDcSVGLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 132 IVIVENFCTtLQQViaNTPIQHVITTqigdlapfpkraiVNFVVKRVKKMVPAWslpgttgfraaLAKGRAQPYARVQLG 211
Cdd:PLN02574 144 FTSPENVEK-LSPL--GVPVIGVPEN-------------YDFDSKRIEFPKFYE-----------LIKEDFDFVPKPVIK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 PDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQ-----QVSAWIGPFLDEgkeVIITALPLYHIFALVVNCLLFLRHGcRN 286
Cdd:PLN02574 197 QDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrfEASQYEYPGSDN---VYLAALPMFHIYGLSLFVVGLLSLG-ST 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 287 VLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLH-APGFAELDFSRFKL-AVGGGTAVQQAVAEKWQKVTGVGLTEGY 364
Cdd:PLN02574 273 IVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKkAKGVCGEVLKSLKQvSCGAAPLSGKFIQDFVQTLPHVDFIQGY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 365 GLTEcSPVVSFSPLSVPQWN--GTIGVPLPSTLVSLRDEEENE-VPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGW 441
Cdd:PLN02574 353 GMTE-STAVGTRGFNTEKLSkySSVGLLAPNMQAKVVDWSTGClLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 442 LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKK-DPALTEAE 520
Cdd:PLN02574 432 LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRqGSTLSQEA 511
|
490 500 510
....*....|....*....|....*....|....*...
gi 522138377 521 LRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PLN02574 512 VINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
53-559 |
1.39e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 223.71 E-value: 1.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASylqnvlGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAi 132
Cdd:PRK07787 23 GRVLSRSDLAGAATAVAE------RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 vivenfcttlqqVIANTPiqhvittqiGDLAPFPkraivnfvVKRVKKMVPAWSLPgttgfraalakgrAQPyarvqlGP 212
Cdd:PRK07787 96 ------------WLGPAP---------DDPAGLP--------HVPVRLHARSWHRY-------------PEP------DP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTHGNVTANVQ---QVSAWigpfldEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLI 289
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVLSRRAIAADLDalaEAWQW------TADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 290 TNPRDmAAFCVELKRSGfTAITGVNTLFNGLLHAPGFAELdFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTEc 369
Cdd:PRK07787 202 GRPTP-EAYAQALSEGG-TLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTE- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 370 spvvSFSPLSV----PQWNGTIGVPLPSTLVSLRDEEENEVP--PGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLK 443
Cdd:PRK07787 278 ----TLITLSTradgERRPGWVGLPLAGVETRLVDEDGGPVPhdGETVGELQVRGPTLFDGYLNRPDATAAAFTADGWFR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 444 TGDVAVFEPNGYLRIVDRKK-DMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPAlTEAELR 522
Cdd:PRK07787 354 TGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV-AADELI 432
|
490 500 510
....*....|....*....|....*....|....*..
gi 522138377 523 AYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELRG 559
Cdd:PRK07787 433 DFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
53-558 |
1.59e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 224.40 E-value: 1.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRA-LGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIVENFCTTLQQVIANTPiqhvittqigdlAPFPKRAIVnfvvkrvkkmvpAWSLPGTTGFRAALAKGRAQPYARVQLGP 212
Cdd:PRK08276 88 IVSAALADTAAELAAELP------------AGVPLLLVV------------AGPVPGFRSYEEALAAQPDTPIADETAGA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DdiafLQYTGGTTGLSKGAV--LTHGNVTANVQQVSAWIGPFLDEGKE-VIITALPLYHIfALVVNCLLFLRHGCRNVLi 289
Cdd:PRK08276 144 D----MLYSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDsVYLSPAPLYHT-APLRFGMSALALGGTVVV- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 290 tnprdMAAFCVE-----LKRSGFTAITGVNTLFNGLLHAPGF--AELDFSRFKLAVGGGT----AVQQAVAEKWQKV--- 355
Cdd:PRK08276 218 -----MEKFDAEealalIERYRVTHSQLVPTMFVRMLKLPEEvrARYDVSSLRVAIHAAApcpvEVKRAMIDWWGPIihe 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 356 --TGvglTEGYGLTECSPVvsfsplsvpQW---NGTIGVPLPSTLVSLrDEEENEVPPGQPGELCVKGPQVMQGYWQKPE 430
Cdd:PRK08276 293 yyAS---SEGGGVTVITSE---------DWlahPGSVGKAVLGEVRIL-DEDGNELPPGEIGTVYFEMDGYPFEYHNDPE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 431 ESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFV- 509
Cdd:PRK08276 360 KTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVq 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 522138377 510 ----VKKDPALtEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK08276 440 padgADAGDAL-AAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
38-527 |
1.81e-66 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 225.20 E-value: 1.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 38 QSCARFGDQIAY------ECMGQTLSFAELDRLTQDFASYLQNVLGlqRGDRVALMMPNLLQYPVSLFGVLRAGLVVVnv 111
Cdd:cd05931 1 RRAAARPDRPAYtflddeGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 112 nPLYTPRELEHQLRdsgakaivivenfcttLQQVIANTPIQHVITTQiGDLApfpkrAIVNFVVKRVKKMVPAWSLPgtt 191
Cdd:cd05931 77 -PLPPPTPGRHAER----------------LAAILADAGPRVVLTTA-AALA-----AVRAFAASRPAAGTPRLLVV--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 192 gfrAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAwiGPFLDEGkEVIITALPLYHIFA 271
Cdd:cd05931 131 ---DLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR--AYGLDPG-DVVVSWLPLYHDMG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 272 LVVNCLLFLRHGCRNVLITnPrdmAAFcveLKR--------SGFTA-ITGvntlfngllhAPGFA--------------E 328
Cdd:cd05931 205 LIGGLLTPLYSGGPSVLMS-P---AAF---LRRplrwlrliSRYRAtISA----------APNFAydlcvrrvrdedleG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 329 LDFSRFKLAVGGGTAVQQAVAEKW-QKVTGVGLTE-----GYGLTECSPVVSFSPLSVP---------QWNGTI------ 387
Cdd:cd05931 268 LDLSSWRVALNGAEPVRPATLRRFaEAFAPFGFRPeafrpSYGLAEATLFVSGGPPGTGpvvlrvdrdALAGRAvavaad 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 388 ----------GVPLPSTLVSLRDEEEN-EVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTK------DGWLKTGDVAVF 450
Cdd:cd05931 348 dpaarelvscGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPSVASGYWGRPEATAETFGAlaatdeGGWLRTGDLGFL 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 451 EpNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLE---VACIGVPDEksGEVPKVFVVKKDPALTEAELRAYCHE 527
Cdd:cd05931 428 H-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDD--GEERLVVVAEVERGADPADLAAIAAA 504
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
5-560 |
1.11e-65 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 223.32 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 5 TAAGEFVWFQEYPP-SVPrtiDTGAVPSLVAmfeQSCARFGDQIAY--ECMGQTLSFAELDRLTQDFASYLQNvLGLQRG 81
Cdd:PLN02330 8 QEDNEHIFRSRYPSvPVP---DKLTLPDFVL---QDAELYADKVAFveAVTGKAVTYGEVVRDTRRFAKALRS-LGLRKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 82 DRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIvenfcttlqqviantpiqhvittqigD 161
Cdd:PLN02330 81 QVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT--------------------------N 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 162 LAPFPKRAIVNFVVKRVKKMVPAWSLPGTTGFRAALAKGRAQPYARVQlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTAN 241
Cdd:PLN02330 135 DTNYGKVKGLGLPVIVLGEEKIEGAVNWKELLEAADRAGDTSDNEEIL--QTDLCALPFSSGTTGISKGVMLTHRNLVAN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 242 VQQVSAWIGPFLdEGKEVIITALPLYHIFALVVNCLLFLRHGCRnVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLL 321
Cdd:PLN02330 213 LCSSLFSVGPEM-IGQVVTLGLIPFFHIYGITGICCATLRNKGK-VVVMSRFELRTFLNALITQEVSFAPIVPPIILNLV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 322 HAPGFAELDFSRFKLavgggTAVQQAVA----------EKwqKVTGVGLTEGYGLTE--CSPVVSFSP---LSVPQWNgT 386
Cdd:PLN02330 291 KNPIVEEFDLSKLKL-----QAIMTAAAplapelltafEA--KFPGVQVQEAYGLTEhsCITLTHGDPekgHGIAKKN-S 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 387 IGVPLPSTLVSLRDEEENE-VPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDM 465
Cdd:PLN02330 363 VGFILPNLEVKFIDPDTGRsLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKEL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 466 ILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-KKDPALTEAELRAYCHENLTGYKMPKYITFLPEL 544
Cdd:PLN02330 443 IKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVViNPKAKESEEDILNFVAANVAHYKKVRVVQFVDSI 522
|
570
....*....|....*.
gi 522138377 545 PKSNVGKVLRKELRGK 560
Cdd:PLN02330 523 PKSLSGKIMRRLLKEK 538
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
69-558 |
2.06e-65 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 220.00 E-value: 2.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 69 ASYLQNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAG----LVVVNVNPLYTPRELEHQLRDSGAKaIVIVENFCTTlqq 144
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGR-IVLADAGAAD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 145 viantpiqhvittqigdlapfpkraivnfvvkRVKKMVPAWSLPGTTgFRAALAKGRAQPYARVQLGPDDIAFLQYTGGT 224
Cdd:cd05922 82 --------------------------------RLRDALPASPDPGTV-LDADGIRAARASAPAHEVSHEDLALLLYTSGS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 225 TGLSKGAVLTHGNVTANVQQVSAWIGpflDEGKEVIITALPLYHIFALVVNCLLFLRHGcrnVLITNPRDM--AAFCVEL 302
Cdd:cd05922 129 TGSPKLVRLSHQNLLANARSIAEYLG---ITADDRALTVLPLSYDYGLSVLNTHLLRGA---TLVLTNDGVldDAFWEDL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 303 KRSGFTAITGVNTLFnGLLHAPGF--AELDFSRFkLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSP--- 377
Cdd:cd05922 203 REHGATGLAGVPSTY-AMLTRLGFdpAKLPSLRY-LTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPper 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 378 -LSVPqwnGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYL 456
Cdd:cd05922 281 iLEKP---GSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 457 RIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEkSGEVPKVFVVKKDpALTEAELRAYCHENLTGYKMPK 536
Cdd:cd05922 358 FIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPD-KIDPKDVLRSLAERLPPYKVPA 435
|
490 500
....*....|....*....|..
gi 522138377 537 YITFLPELPKSNVGKVLRKELR 558
Cdd:cd05922 436 TVRVVDELPLTASGKVDYAALR 457
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
45-557 |
3.12e-65 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 219.32 E-value: 3.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYtPRE-LEHQ 123
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRE-RGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY-PAErLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 124 LRDSGAKaivivenfcttlqqviantpiqHVITTqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraq 203
Cdd:cd05930 80 LEDSGAK----------------------LVLTD---------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 204 pyarvqlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQqvSAWIGPFLDEGKEVIITALP-----LYHIFALVVN--C 276
Cdd:cd05930 92 --------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL--WMQEAYPLTPGDRVLQFTSFsfdvsVWEIFGALLAgaT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 277 LLFLRHGCRnvliTNPRDMAAFCVElkrSGFTAITGVNTLFNGLLHAPGFAelDFSRFKLAVGGGTAVQQAVAEKWQKV- 355
Cdd:cd05930 162 LVVLPEEVR----KDPEALADLLAE---EGITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELl 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 356 TGVGLTEGYGLTECSPVVSFSPLSVPQWNG---TIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEES 432
Cdd:cd05930 233 PGARLVNLYGPTEATVDATYYRVPPDDEEDgrvPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 433 AKVFTKDGWL------KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPK 506
Cdd:cd05930 313 AERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLV 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 522138377 507 VFVV-KKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd05930 393 AYVVpDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
31-558 |
7.33e-65 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 221.16 E-value: 7.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 31 SLVAMFEQSCARFGDQIAY-ECMGQTLSFAELDRLTQDFASYLQNVlGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVV 109
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVvDNHGASYTYSALDHAASRLANWLLAK-GIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 110 NVNPLYTPRELEHQLRDSGAKAIvivenFCTTLQQVIANTPIQHVITTQIGDLAPfpkraivnfvVKRVKKMVPAWSLPg 189
Cdd:PRK06087 103 PLLPSWREAELVWVLNKCQAKMF-----FAPTLFKQTRPVDLILPLQNQLPQLQQ----------IVGVDKLAPATSSL- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 190 ttgfraALAK--GRAQPYAR-VQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEgkeVIITALPL 266
Cdd:PRK06087 167 ------SLSQiiADYEPLTTaITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQD---VFMMPAPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 267 YHIFALVVNCLLFLRHGCRNVL--ITNPrdmaAFCVEL-KRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTA 343
Cdd:PRK06087 238 GHATGFLHGVTAPFLIGARSVLldIFTP----DACLALlEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 344 VQQAVAEKWQKvTGVGLTEGYGLTECSPVVsFSPLSVP-QWNG-TIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQV 421
Cdd:PRK06087 314 IPKKVARECQQ-RGIKLLSVYGSTESSPHA-VVNLDDPlSRFMhTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 422 MQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKS 501
Cdd:PRK06087 392 FMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERL 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 502 GEVPKVFVVKKDP--ALTEAELRAY-CHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK06087 472 GERSCAYVVLKAPhhSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLR 531
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
57-558 |
1.16e-64 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 217.69 E-value: 1.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 57 SFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIve 136
Cdd:cd05971 8 TFKELKTASNRFANVLKE-IGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 137 nfcttlqqviantpiqhvittqigDlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqpyarvqlGPDDIA 216
Cdd:cd05971 85 ------------------------D-------------------------------------------------GSDDPA 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 217 FLQYTGGTTGLSKGAVLTHGNVTANVQQVS-------------------AWIGPFLDegkeVIITAlpLYHIFALVVN-- 275
Cdd:cd05971 92 LIIYTSGTTGPPKGALHAHRVLLGHLPGVQfpfnlfprdgdlywtpadwAWIGGLLD----VLLPS--LYFGVPVLAHrm 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 276 --------CLLFLRHGCRNVLI--TNPRDMAAFCVELKRsgftaiTGVNTLfngllhapgfaeldfsrfKLAVGGGTAVQ 345
Cdd:cd05971 166 tkfdpkaaLDLMSRYGVTTAFLppTALKMMRQQGEQLKH------AQVKLR------------------AIATGGESLGE 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 346 QAVAekWQKVT-GVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQ--VM 422
Cdd:cd05971 222 ELLG--WAREQfGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAF 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 423 QGYWQKPEESAKVFTKDgWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSG 502
Cdd:cd05971 300 LGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRG 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 503 EVPKVFVVKKDPALTE----AELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05971 379 EIVKAFVVLNPGETPSdalaREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
220-554 |
1.90e-64 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 213.67 E-value: 1.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 220 YTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKeVIITALPLYHIFALVVNcLLFLRHGCRNVLItnPRDMAAFC 299
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMG--LTEAD-VYLNMLPLFHIAGLNLA-LATFHAGGANVVM--EKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 300 VELKRS-GFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAvqqAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPL 378
Cdd:cd17637 81 LELIEEeKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGATFWSLYGQTETSGLVTLSPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 379 SvpQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFtKDGWLKTGDVAVFEPNGYLRI 458
Cdd:cd17637 158 R--ERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 459 VDRK--KDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPK-VFVVKKDPALTEAELRAYCHENLTGYKMP 535
Cdd:cd17637 235 AGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKaVCVLKPGATLTADELIEFVGSRIARYKKP 314
|
330
....*....|....*....
gi 522138377 536 KYITFLPELPKSNVGKVLR 554
Cdd:cd17637 315 RYVVFVEALPKTADGSIDR 333
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
212-558 |
1.96e-64 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 214.65 E-value: 1.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 PDDIAFLQYTGGTTGLSKGAVLTHGNVTANvqqvsAWIGPFLDEGKE--VIITALPLYHIFALVVNCLLFLRHGCRNVLI 289
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN-----AWMLALNSLFDPddVLLCGLPLFHVNGSVVTLLTPLASGAHVVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 290 T-----NPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAelDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGY 364
Cdd:cd05944 76 GpagyrNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNA--DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 365 GLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEE-----ENEVPPGQPGELCVKGPQVMQGYWQKpEESAKVFTKD 439
Cdd:cd05944 154 GLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDgvgrlLRDCAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 440 GWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFV-VKKDPALTE 518
Cdd:cd05944 233 GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqLKPGAVVEE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 522138377 519 AEL----RAYCHENLTgykMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05944 313 EELlawaRDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
53-558 |
3.68e-64 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 216.19 E-value: 3.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIVenfcttlqqviantpiqHVITTQigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqpyarvqlgp 212
Cdd:cd05958 88 LCA-----------------HALTAS------------------------------------------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWI-GPfldEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLI-- 289
Cdd:cd05958 97 DDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVlRL---REDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLee 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 290 TNPRDMAAFcveLKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTEC 369
Cdd:cd05958 174 ATPDLLLSA---IARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEM 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 370 SPV-VSFSPLSV-PqwnGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQvmqGYWQKPEESAKVFTKDGWLKTGDV 447
Cdd:cd05958 251 FHIfISARPGDArP---GATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 448 AVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKK-----DPALTEaELR 522
Cdd:cd05958 325 YSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpgvipGPVLAR-ELQ 403
|
490 500 510
....*....|....*....|....*....|....*.
gi 522138377 523 AYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05958 404 DHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
35-558 |
1.21e-63 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 216.86 E-value: 1.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 35 MFEQSCARFGDQIA--YE-CMGQTLSF------AELDRLTQDFASylqnvLGLQRGDRVALMMPNLLQYPVSLFGVLRAG 105
Cdd:PRK08008 12 MWDDLADVYGHKTAliFEsSGGVVRRYsylelnEEINRTANLFYS-----LGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 106 LVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIAN--TPIQHVITTQIGDLApfpkraivnfvvkrvkkmvp 183
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEdaTPLRHICLTRVALPA-------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 184 awsLPGTTGFRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHgnvtANVQ---QVSAWIGPFLDegKEVI 260
Cdd:PRK08008 147 ---DDGVSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITH----YNLRfagYYSAWQCALRD--DDVY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 261 ITALPLYHIFALVVNCLLFLRHGCRNVLITNpRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFA-----ELDFSRFK 335
Cdd:PRK08008 218 LTVMPAFHIDCQCTAAMAAFSAGATFVLLEK-YSARAFWGQVCKYRATITECIPMMIRTLMVQPPSAndrqhCLREVMFY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 336 LAVGggTAVQQAVAEKWqkvtGVGLTEGYGLTEC-SPVVSFSPLSVPQWNgTIGVPLPSTLVSLRDEEENEVPPGQPGEL 414
Cdd:PRK08008 297 LNLS--DQEKDAFEERF----GVRLLTSYGMTETiVGIIGDRPGDKRRWP-SIGRPGFCYEAEIRDDHNRPLPAGEIGEI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 415 CVKG---PQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEV 491
Cdd:PRK08008 370 CIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDI 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522138377 492 ACIGVPDEKSGEVPKVFVVKKDPA-LTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK08008 450 VVVGIKDSIRDEAIKAFVVLNEGEtLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
53-558 |
1.01e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 213.98 E-value: 1.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNVlGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:PRK06145 25 DQEISYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIVENFcttlqqviantpiqhvittqigdlapfpkRAIVNFVVKRVkkMVPAWSLPGTTgfraALAKGRAQPYARVQLGP 212
Cdd:PRK06145 104 LVDEEF-----------------------------DAIVALETPKI--VIDAAAQADSR----RLAQGGLEIPPQAAVAP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTHGNVT-ANVQQVSAwIGPFLDEGkevIITALPLYHIFALVVNCLLFLRHGcRNVLITN 291
Cdd:PRK06145 149 TDLVRLMYTSGTTDRPKGVMHSYGNLHwKSIDHVIA-LGLTASER---LLVVGPLYHVGAFDLPGIAVLWVG-GTLRIHR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 292 PRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAV-QQAVAEKWQKVTGVGLTEGYGLTE-C 369
Cdd:PRK06145 224 EFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTpESRIRDFTRVFTRARYIDAYGLTEtC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 370 SPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTkDGWLKTGDVAV 449
Cdd:PRK06145 304 SGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 450 FEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA-LTEAELRAYCHEN 528
Cdd:PRK06145 383 LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGAtLTLEALDRHCRQR 462
|
490 500 510
....*....|....*....|....*....|
gi 522138377 529 LTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK06145 463 LASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
53-554 |
3.62e-61 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 208.84 E-value: 3.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQnVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 vivenFCTTlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqpyarvqlgP 212
Cdd:cd05914 84 -----FVSD----------------------------------------------------------------------E 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAwIGPfLDEGkEVIITALPLYHIFALVVNCLLFLRHGCRNVLITNP 292
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKE-VVL-LGKG-DKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 293 -------------RDMAAFCVEL---KRSGFTAITGVN-TLFNGLLHAP----GFAELDFS--------RFKLAVGGGTA 343
Cdd:cd05914 166 psakiialafaqvTPTLGVPVPLvieKIFKMDIIPKLTlKKFKFKLAKKinnrKIRKLAFKkvheafggNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 344 VQQAVAEKWQKVtGVGLTEGYGLTECSPVVSFSPlsvpqWN----GTIGVPLPSTLVSLRDEEenevPPGQPGELCVKGP 419
Cdd:cd05914 246 INPDVEEFLRTI-GFPYTIGYGMTETAPIISYSP-----PNrirlGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGP 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 420 QVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILV-SGFNVYPNEIEGVVAQHPGVLEvACIGVPD 498
Cdd:cd05914 316 NVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLE-SLVVVQE 394
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522138377 499 EKSgevpkVFVVKKDPALTEA--------------ELRAYCHENLTGY-KMPKYITFLPELPKSNVGKVLR 554
Cdd:cd05914 395 KKL-----VALAYIDPDFLDVkalkqrniidaikwEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
68-558 |
2.57e-60 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 207.15 E-value: 2.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 68 FASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFcttlqqvia 147
Cdd:cd12118 42 LASALAA-LGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREF--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 148 ntpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttGFRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGL 227
Cdd:cd12118 112 --------------------------------------------EYEDLLAEGDPDFEWIPPADEWDPIALNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 228 SKGAVLTHG----NVTANVQqvsAWIGPfldeGKEVIITALPLYH---------IFAL--VVNCLlflrhgcRNVlitnp 292
Cdd:cd12118 148 PKGVVYHHRgaylNALANIL---EWEMK----QHPVYLWTLPMFHcngwcfpwtVAAVggTNVCL-------RKV----- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 293 rDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVtGVGLTEGYGLTECSPV 372
Cdd:cd12118 209 -DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEEL-GFDVTHVYGLTETYGP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 373 VSFSPLSvPQWNGTI-----------GVPLPSTL-VSLRDEEENEVPPG---QPGELCVKGPQVMQGYWQKPEESAKVFt 437
Cdd:cd12118 287 ATVCAWK-PEWDELPteerarlkarqGVRYVGLEeVDVLDPETMKPVPRdgkTIGEIVFRGNIVMKGYLKNPEATAEAF- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 438 KDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA-L 516
Cdd:cd12118 365 RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAkV 444
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 522138377 517 TEAELRAYCHENLTGYKMPKYITFLPeLPKSNVGKVLRKELR 558
Cdd:cd12118 445 TEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLR 485
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
41-558 |
5.04e-60 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 207.76 E-value: 5.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 41 ARFGDQIAY--ECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPR 118
Cdd:cd17642 28 ASVPGTIAFtdAHTGVNYSYAEYLEMSVRLAEALKK-YGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 119 ELEHQLRDSGAKAIvivenFCT--TLQQVI----ANTPIQH-VITTQIGDLAPFpkRAIVNFVvkrvkkmvpawSLPGTT 191
Cdd:cd17642 107 ELDHSLNISKPTIV-----FCSkkGLQKVLnvqkKLKIIKTiIILDSKEDYKGY--QCLYTFI-----------TQNLPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 192 GFRAALAKGRAqpYARvqlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANV-QQVSAWIGPFLDEGKeVIITALPLYHIF 270
Cdd:cd17642 169 GFNEYDFKPPS--FDR----DEQVALIMNSSGSTGLPKGVQLTHKNIVARFsHARDPIFGNQIIPDT-AILTVIPFHHGF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 271 ALVVNcLLFLRHGCRNVLITNpRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAE 350
Cdd:cd17642 242 GMFTT-LGYLICGFRVVLMYK-FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 351 KWQKVTGV-GLTEGYGLTECSPVVSFSPLSVPQwNGTIGVPLPSTLVSLRDEEENE-VPPGQPGELCVKGPQVMQGYWQK 428
Cdd:cd17642 320 AVAKRFKLpGIRQGYGLTETTSAILITPEGDDK-PGAVGKVVPFFYAKVVDLDTGKtLGPNERGELCVKGPMIMKGYVNN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 429 PEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVF 508
Cdd:cd17642 399 PEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAV 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 522138377 509 VVKK-DPALTEAELRAYCHENLTGYK-MPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd17642 479 VVLEaGKTMTEKEVMDYVASQVSTAKrLRGGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
34-557 |
7.40e-60 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 205.90 E-value: 7.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 34 AMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNP 113
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRA-AGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 114 LYTPRELEHQLRDSGAKAIVIvenfCTTLQQVIANTPiqhviTTQIGDLAPFPkraivnfvvkrvkkmvpawslpgttgf 193
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLT----DRSLAGRAGGLE-----VAVVIDEALDA--------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 194 raalakgRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSaWIGpfLDEGKEVIITAlPL------Y 267
Cdd:cd12117 124 -------GPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTN-YVT--LGPDDRVLQTS-PLafdastF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 268 HIFAlvvnCLLflrHGCRNVLIT--NPRDMAAFCVELKRSGFTAITGVNTLFNGLlhapgfAELDFSRF----KLAVGGG 341
Cdd:cd12117 193 EIWG----ALL---NGARLVLAPkgTLLDPDALGALIAEEGVTVLWLTAALFNQL------ADEDPECFaglrELLTGGE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 342 TAVQQAVAEKWQKVTGVGLTEGYGLTE-----CSPVV---SFSPLSVPqwngtIGVPLPSTLVSLRDEEENEVPPGQPGE 413
Cdd:cd12117 260 VVSPPHVRRVLAACPGLRLVNGYGPTEnttftTSHVVtelDEVAGSIP-----IGRPIANTRVYVLDEDGRPVPPGVPGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 414 LCVKGPQVMQGYWQKPEESAKVFTKDGWL------KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPG 487
Cdd:cd12117 335 LYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPG 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 488 VLEvACIGVPDEKSGEVPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd12117 415 VRE-AVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
53-560 |
4.26e-59 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 204.54 E-value: 4.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:PRK13391 22 GEVVTYRELDERSNRLAHLFRS-LGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIvenfcTTLQQVIANTPIQHVittqigdlapfPKraivnfVVKRVKKMVPAwSLPGTTGFRAALAKGRAQPYARVQLGP 212
Cdd:PRK13391 101 IT-----SAAKLDVARALLKQC-----------PG------VRHRLVLDGDG-ELEGFVGYAEAVAGLPATPIADESLGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DdiafLQYTGGTTGLSKG--AVLTHGNVtanVQQVSawIGPFL------DEGKEVIITAlPLYHIfALVVNCLLFLRHGC 284
Cdd:PRK13391 158 D----MLYSSGTTGRPKGikRPLPEQPP---DTPLP--LTAFLqrlwgfRSDMVYLSPA-PLYHS-APQRAVMLVIRLGG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 285 RNVLitnprdMAAFCVE-----LKRSGFTAITGVNTLFNGLLHAPGFAEL--DFSRFKLAVGGGTA----VQQAVAEKWQ 353
Cdd:PRK13391 227 TVIV------MEHFDAEqylalIEEYGVTHTQLVPTMFSRMLKLPEEVRDkyDLSSLEVAIHAAAPcppqVKEQMIDWWG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 354 KVTG--VGLTEGYGLTECSPvvsfsplsvPQW---NGTIGVPLPSTLVsLRDEEENEVPPGQPGELCVKGPQVMQgYWQK 428
Cdd:PRK13391 301 PIIHeyYAATEGLGFTACDS---------EEWlahPGTVGRAMFGDLH-ILDDDGAELPPGEPGTIWFEGGRPFE-YLND 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 429 PEESAKVFTKDG-WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKV 507
Cdd:PRK13391 370 PAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKA 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 522138377 508 FV-----VKKDPALtEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELRGK 560
Cdd:PRK13391 450 VVqpvdgVDPGPAL-AAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
55-559 |
5.60e-59 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 205.29 E-value: 5.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 55 TLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVI 134
Cdd:PRK13295 55 RFTYRELAALVDRVAVGLAR-LGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 135 VENF--------CTTLQQVIANtpIQHVITTQIGDLAPFPKRAIvnfvvkrvkkmVPAWSlpgttgfraaLAKGRAQPYA 206
Cdd:PRK13295 134 PKTFrgfdhaamARRLRPELPA--LRHVVVVGGDGADSFEALLI-----------TPAWE----------QEPDAPAILA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 207 RVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGkEVIITALPLYHIFALVVNCLLFLRHGCRN 286
Cdd:PRK13295 191 RLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLG--LGAD-DVILMASPMAHQTGFMYGLMMPVMLGATA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 287 VL--ITNPRDMAAFcveLKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGY 364
Cdd:PRK13295 268 VLqdIWDPARAAEL---IRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAW 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 365 GLTECSPVVSFSPLSVPQ-WNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFtkDGWLK 443
Cdd:PRK13295 345 GMTENGAVTLTKLDDPDErASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 444 TGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-KKDPALTEAELR 522
Cdd:PRK13295 423 TGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVpRPGQSLDFEEMV 502
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 522138377 523 AYCHEN-LTGYKMPKYITFLPELPKSNVGKV----LRKELRG 559
Cdd:PRK13295 503 EFLKAQkVAKQYIPERLVVRDALPRTPSGKIqkfrLREMLRG 544
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
55-559 |
1.62e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 204.01 E-value: 1.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 55 TLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVI 134
Cdd:PRK07788 74 TLTYAELDEQSNALARGLLA-LGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 135 VENFCTTLQQVIANTPIQHVITTQIGDLAPFPKRAIV--NFVVKRVKKMVPAWSLPGttgfraalakgraqpyarvqlgp 212
Cdd:PRK07788 153 DDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETldDLIAGSSTAPLPKPPKPG----------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 ddiAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIgPFldEGKEVIITALPLYHIFALVvNCLLFLRHGCRNVLitnP 292
Cdd:PRK07788 210 ---GIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRV-PF--RAGETTLLPAPMFHATGWA-HLTLAMALGSTVVL---R 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 293 RDM-AAFCVE-LKRSGFTAITGVNTLFNGLLHAPG--FAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTE 368
Cdd:PRK07788 280 RRFdPEATLEdIAKHKATALVVVPVMLSRILDLGPevLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 369 CSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESakvfTKDGWLKTGDVA 448
Cdd:PRK07788 360 VAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQ----IIDGLLSSGDVG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 449 VFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA-LTEAELRAYCHE 527
Cdd:PRK07788 436 YFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAaLDEDAIKDYVRD 515
|
490 500 510
....*....|....*....|....*....|..
gi 522138377 528 NLTGYKMPKYITFLPELPKSNVGKVLRKELRG 559
Cdd:PRK07788 516 NLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
53-558 |
1.80e-58 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 202.56 E-value: 1.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNvlGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:cd05909 5 GTSLTYRKLLTGAIALARKLAK--MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIVENFcttlqqviantpIQHVITTQIGDLAPFPKraIVnfVVKRVKKMVPAWSlpgttGFRAALAKGRAQPYARVQLG- 211
Cdd:cd05909 83 LTSKQF------------IEKLKLHHLFDVEYDAR--IV--YLEDLRAKISKAD-----KCKAFLAGKFPPKWLLRIFGv 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 ----PDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEgkeVIITALPLYHIFALVVNCLLFLRHGCRNV 287
Cdd:cd05909 142 apvqPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPED---VVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 288 LITNPRDmAAFCVEL-KRSGFTAITGVNTLFNGLLHAPgfAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGL 366
Cdd:cd05909 219 FHPNPLD-YKKIPELiYDKKATILLGTPTFLRGYARAA--HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 367 TECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEE-ENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFtKDGWLKTG 445
Cdd:cd05909 296 TECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 446 DVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQH-PGVLEVACIGVPDEKSGEvpKVFVVKKDPALTEAELRAY 524
Cdd:cd05909 375 DIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGE--KIVLLTTTTDTDPSSLNDI 452
|
490 500 510
....*....|....*....|....*....|....*...
gi 522138377 525 CHE----NLTgykMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05909 453 LKNagisNLA---KPSYIHQVEEIPLLGTGKPDYVTLK 487
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
56-558 |
2.52e-58 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 202.62 E-value: 2.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIV 135
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAA-LGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 136 ENFCTTLQQVI-ANTPIQHVittqigdlaPFPKRAIVNFVVKRVKKMVPawslPGTTGFRAALAKGraQPYARVQL-GPd 213
Cdd:PRK12406 91 ADLLHGLASALpAGVTVLSV---------PTPPEIAAAYRISPALLTPP----AGAIDWEGWLAQQ--EPYDGPPVpQP- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 diAFLQYTGGTTGLSKG---AVLTHGNVTANVQQVSAWIGpfLDEGKEVIITAlPLYH----IFALVVncllfLRHGcrN 286
Cdd:PRK12406 155 --QSMIYTSGTTGHPKGvrrAAPTPEQAAAAEQMRALIYG--LKPGIRALLTG-PLYHsapnAYGLRA-----GRLG--G 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 287 VLITNPR-DMAAFCVELKRSGFTAITGVNTLFNGLLHAPGF--AELDFSRFKLAVGGG----TAVQQAVAEKWQKVtgvg 359
Cdd:PRK12406 223 VLVLQPRfDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEvrAKYDVSSLRHVIHAAapcpADVKRAMIEWWGPV---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 360 LTEGYGLTECSPVVSFSP---LSVPqwnGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQ-GYWQKPEESAKV 435
Cdd:PRK12406 299 IYEYYGSTESGAVTFATSedaLSHP---GTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 436 fTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVpKVFVVKKDP- 514
Cdd:PRK12406 376 -DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEA-LMAVVEPQPg 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 522138377 515 -ALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK12406 454 aTLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
57-560 |
1.03e-56 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 198.87 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 57 SFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVive 136
Cdd:cd05970 49 TFAELADYSDKTANFFKA-MGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIV--- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 137 nfcttlqqVIANTPIQHVITTQIGDLAPFPKRAIVNFVVkrvkkmvpawsLPGTTGFRAALAKGRA---QPYARVQLGPD 213
Cdd:cd05970 125 --------AIAEDNIPEEIEKAAPECPSKPKLVWVGDPV-----------PEGWIDFRKLIKNASPdfeRPTANSYPCGE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 DIAFLQYTGGTTGLSKgaVLTHGNVTANVQQVSAWIGPFLDEGKEVIITALP---------LYHIFalVVNCLLFLRhgc 284
Cdd:cd05970 186 DILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTgwgkavwgkIYGQW--IAGAAVFVY--- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 285 rnvlitnprDMAAFCVE-----LKRSGFTAITGVNTLFNGLLHApGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVG 359
Cdd:cd05970 259 ---------DYDKFDPKallekLSKYGVTTFCAPPTIYRFLIRE-DLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 360 LTEGYGLTECSPVVSFSPLSVPQwNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCV---KGPQV--MQGYWQKPEESAK 434
Cdd:cd05970 329 LMEGFGQTETTLTIATFPWMEPK-PGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVglFGGYYKDAEKTAE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 435 VFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-KKD 513
Cdd:cd05970 408 VW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVlAKG 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 522138377 514 PALTEA---ELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELRGK 560
Cdd:cd05970 487 YEPSEElkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
57-492 |
2.09e-56 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 194.79 E-value: 2.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 57 SFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIvive 136
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 137 nfcttlqqviantpiqhVITTQIGDLAPFPKRAIVNFvvkrvkkmvpawslpgTTGFRAALAKGRAQPYARVQLGPDDIA 216
Cdd:TIGR01733 77 -----------------LTDSALASRLAGLVLPVILL----------------DPLELAALDDAPAPPPPDAPSGPDDLA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 217 FLQYTGGTTGLSKGAVLTHGNVTANVqqvsAWIGPFLDEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLITNP--RD 294
Cdd:TIGR01733 124 YVIYTSGSTGRPKGVVVTHRSLVNLL----AWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDeeRD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 295 MAAFCVELKRSGF-TAITGVNTLFNGLLHApgfAELDFSRFKLAVGGGTAVQQAVAEKWQ-KVTGVGLTEGYGLTECSPV 372
Cdd:TIGR01733 200 DAALLAALIAEHPvTVLNLTPSLLALLAAA---LPPALASLRLVILGGEALTPALVDRWRaRGPGARLINLYGPTETTVW 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 373 VSFSPLSVP----QWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDG-------- 440
Cdd:TIGR01733 277 STATLVDPDdaprESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPfaggdgar 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 522138377 441 WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVA 492
Cdd:TIGR01733 357 LYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAV 408
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
214-558 |
3.44e-56 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 191.78 E-value: 3.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 DIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPfldEGKEVIITALPLYHI--FALVVNCLLflrhGCRNVLITN 291
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGF---GGGDSWLLSLPLYHVggLAILVRSLL----AGAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 292 PRDMAAfcVELKRSGFTAITGVNTLFNGLLHAPGFAElDFSRFKLAVGGGTAVQQAVAEKWQKvTGVGLTEGYGLTECSP 371
Cdd:cd17630 74 RNQALA--EDLAPPGVTHVSLVPTQLQRLLDSGQGPA-ALKSLRAVLLGGAPIPPELLERAAD-RGIPLYTTYGMTETAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 372 VVSFSPLSVPQwNGTIGVPLPSTLVSLRDeeenevppgqPGELCVKGPQVMQGYWQKPEEsaKVFTKDGWLKTGDVAVFE 451
Cdd:cd17630 150 QVATKRPDGFG-RGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 452 PNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPkVFVVKKDPALTEAELRAYCHENLTG 531
Cdd:cd17630 217 ADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRP-VAVIVGRGPADPAELRAWLKDKLAR 295
|
330 340
....*....|....*....|....*..
gi 522138377 532 YKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd17630 296 FKLPKRIYPVPELPRTGGGKVDRRALR 322
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
56-557 |
4.22e-56 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 196.19 E-value: 4.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAEL-DRLTQDFASYLQnvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVI 134
Cdd:cd05923 29 LTYSELrARIEAVAARLHA--RGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 135 venfcttlqQVIANtpiqhvittqigdlapfPKRAIVNFVVKRVKKMVpawsLPGTtgfRAALAKGRAQPYArvQLGPDD 214
Cdd:cd05923 107 ---------AVDAQ-----------------VMDAIFQSGVRVLALSD----LVGL---GEPESAGPLIEDP--PREPEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 215 IAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGK-EVIITALPLYHI---FALVVNCLLFlrhGCRNVLIT 290
Cdd:cd05923 152 PAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAG--LRHGRhNVVLGLMPLYHVigfFAVLVAALAL---DGTYVVVE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 291 NprDMAAFCVEL-KRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTEC 369
Cdd:cd05923 227 E--FDPADALKLiEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 370 SPVVsFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVK--GPQVMQGYWQKPEESAKVFtKDGWLKTGDV 447
Cdd:cd05923 305 MNSL-YMRDARTGTEMRPGFFSEVRIVRIGGSPDEALANGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 448 AVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPALTEAELRAYCHE 527
Cdd:cd05923 383 GYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRA 462
|
490 500 510
....*....|....*....|....*....|.
gi 522138377 528 N-LTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd05923 463 SeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
34-551 |
6.09e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 196.64 E-value: 6.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 34 AMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNP 113
Cdd:PRK07798 7 DLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIA-QGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 114 LYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTP-IQHVIttQIGDLAPFPkraivnfvvkrvkkmvpawSLPGTTG 192
Cdd:PRK07798 86 RYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPkLRTLV--VVEDGSGND-------------------LLPGAVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 193 FRAALAKGRAQPyARVQLGPDDIAFLqYTGGTTGLSKGAVLTH---------------GNVTANVQQVSAWIgpfLDEGK 257
Cdd:PRK07798 145 YEDALAAGSPER-DFGERSPDDLYLL-YTGGTTGMPKGVMWRQedifrvllggrdfatGEPIEDEEELAKRA---AAGPG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 258 EVIITALPLYHIFAL--VVNCLLFlrhGCRNVLITNPR-DMAAFCVELKRSGFTAITGVNTLFNG-LLHA---PGfaELD 330
Cdd:PRK07798 220 MRRFPAPPLMHGAGQwaAFAALFS---GQTVVLLPDVRfDADEVWRTIEREKVNVITIVGDAMARpLLDAleaRG--PYD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 331 FSRFKLAVGGGTAVQQAVAEKWQK-VTGVGLTEGYGLTEC----SPVVSFSPLSVPQWNGTIGvplPSTLVSlrDEEENE 405
Cdd:PRK07798 295 LSSLFAIASGGALFSPSVKEALLElLPNVVLTDSIGSSETgfggSGTVAKGAVHTGGPRFTIG---PRTVVL--DEDGNP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 406 VPPG--QPGELCVKGPqVMQGYWQKPEESAKVF-TKDG--WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEG 480
Cdd:PRK07798 370 VEPGsgEIGWIARRGH-IPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEE 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522138377 481 VVAQHPGVLEVACIGVPDEKSG-EVPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGK 551
Cdd:PRK07798 449 ALKAHPDVADALVVGVPDERWGqEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
54-500 |
1.27e-55 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 194.11 E-value: 1.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLQnVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIV 133
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 134 iVENfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqpyarvqlGPD 213
Cdd:cd17640 83 -VEN-------------------------------------------------------------------------DSD 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 DIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPflDEGKEViITALPLYHIFALVVNCLLFLRhGCrNVLITNPR 293
Cdd:cd17640 89 DLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPP--QPGDRF-LSILPIWHSYERSAEYFIFAC-GC-SQAYTSIR 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 294 DMAAfcvELKRSGFTAITGVNTLFNGL-------LHAPGFAE-------LDFSRFKLAVGGGTAVQQAVaEKWQKVTGVG 359
Cdd:cd17640 164 TLKD---DLKRVKPHYIVSVPRLWESLysgiqkqVSKSSPIKqflflffLSGGIFKFGISGGGALPPHV-DTFFEAIGIE 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 360 LTEGYGLTECSPVVSFSPLSVPQwNGTIGVPLPSTLVSLRDEEENEV-PPGQPGELCVKGPQVMQGYWQKPEESAKVFTK 438
Cdd:cd17640 240 VLNGYGLTETSPVVSARRLKCNV-RGSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDS 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522138377 439 DGWLKTGDVAVFEPNGYLRIVDRKKDMILVS-GFNVYPNEIEGVVAQHPGVLEVACIGvPDEK 500
Cdd:cd17640 319 DGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG-QDQK 380
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
45-557 |
2.44e-55 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 192.91 E-value: 2.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQL 124
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRA-EGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 125 RDSGAKAIVivenfcttlqqviantpiqhvitTQigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqp 204
Cdd:cd17643 81 ADSGPSLLL-----------------------TD---------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 205 yarvqlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEgkevIITalpLYHIFAL---VVNCLLFLR 281
Cdd:cd17643 92 -------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDD----VWT---LFHSYAFdfsVWEIWGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 282 HGCRNVLITN--PRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVG 359
Cdd:cd17643 158 HGGRLVVVPYevARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 360 ---LTEGYGLTECSPVVSFSPLS----VPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEES 432
Cdd:cd17643 238 rpqLVNMYGITETTVHVTFRPLDaadlPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 433 AKVFTKDGW-------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVP 505
Cdd:cd17643 318 AERFVANPFggpgsrmYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRL 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 522138377 506 KVFVVKKD-PALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd17643 398 VAYVVADDgAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
37-558 |
9.95e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 193.62 E-value: 9.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 37 EQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYT 116
Cdd:PRK08162 25 ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALAR-RGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 117 PRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIgDLAPFPKRAIVnfvvkrvkkmvpawslpGTTGFRAA 196
Cdd:PRK08162 104 AASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDV-DDPEYPGGRFI-----------------GALDYEAF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 197 LAKGraQPYARVQLgPDD----IAfLQYTGGTTGLSKGAVLTH-GNVTANVQQVSAWigpflDEGKE-VIITALPLYH-- 268
Cdd:PRK08162 166 LASG--DPDFAWTL-PADewdaIA-LNYTSGTTGNPKGVVYHHrGAYLNALSNILAW-----GMPKHpVYLWTLPMFHcn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 269 ---------IFALVVNCLlflrhgcRNVlitnprDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVG 339
Cdd:PRK08162 237 gwcfpwtvaARAGTNVCL-------RKV------DPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 340 GGTAVQQAVAEKWQKVtGVGLTEGYGLTEcspvvSFSPLSV----PQW-----------NGTIGVPLP--STLVSLRDEE 402
Cdd:PRK08162 304 AGAAPPAAVIAKMEEI-GFDLTHVYGLTE-----TYGPATVcawqPEWdalplderaqlKARQGVRYPlqEGVTVLDPDT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 403 ENEVP-PGQP-GELCVKGPQVMQGYWQKPEESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEG 480
Cdd:PRK08162 378 MQPVPaDGETiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVED 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522138377 481 VVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA-LTEAELRAYCHENLTGYKMPKYITFlPELPKSNVGKVLRKELR 558
Cdd:PRK08162 457 VLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGAsATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLR 534
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
57-560 |
9.18e-54 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 190.75 E-value: 9.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 57 SFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVE 136
Cdd:cd05928 43 SFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 137 NFCTTLQQVIANTPiqhvittqigDLapfpkraivnfvvkRVKKMVPAWSLPGTTGFRAaLAKGRAQPYARVQLGPDDIA 216
Cdd:cd05928 123 ELAPEVDSVASECP----------SL--------------KTKLLVSEKSRDGWLNFKE-LLNEASTEHHCVETGSQEPM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 217 FLQYTGGTTGLSKGAVLTHGnvtanvqqvSAWIGPFLDEGKEVIITA--------------LPLYHIFALVVN-CLLFLR 281
Cdd:cd05928 178 AIYFTSGTTGSPKMAEHSHS---------SLGLGLKVNGRYWLDLTAsdimwntsdtgwikSAWSSLFEPWIQgACVFVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 282 HgcrnvlitNPR-DMAAFCVELKRSGFTAITGVNTLFNGLLHApGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGL 360
Cdd:cd05928 249 H--------LPRfDPLVILKTLSSYPITTFCGAPTVYRMLVQQ-DLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 361 TEGYGLTEcSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVK-GPQ----VMQGYWQKPEESAKV 435
Cdd:cd05928 320 YEGYGQTE-TGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAAT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 436 FTKDGWLkTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV----- 510
Cdd:cd05928 399 IRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqf 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 522138377 511 -KKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELRGK 560
Cdd:cd05928 478 lSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
33-557 |
1.36e-52 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 186.71 E-value: 1.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 33 VAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQnVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVN 112
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLR-ARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 113 PLYTPRELEHQLRDSGAKaivivenfcttlqqviantpiqhVITTQIGDLAPFPKraivnfvvkrvkkmvpawSLPGTTG 192
Cdd:cd17646 80 PGYPADRLAYMLADAGPA-----------------------VVLTTADLAARLPA------------------GGDVALL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 193 FRAALAKGRAQPYARVqLGPDDIAFLQYTGGTTGLSKGAVLTHGNVtanVQQVSAWIGPFLDEGKEVIITALPL------ 266
Cdd:cd17646 119 GDEALAAPPATPPLVP-PRPDNLAYVIYTSGSTGRPKGVMVTHAGI---VNRLLWMQDEYPLGPGDRVLQKTPLsfdvsv 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 267 YHIF-ALVVN-CLLFLRHGCRnvlitnpRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRfkLAVGGGTAV 344
Cdd:cd17646 195 WELFwPLVAGaRLVVARPGGH-------RDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSCASLR--RVFCSGEAL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 345 QQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLSVPQWNGT--IGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVM 422
Cdd:cd17646 266 PPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSvpIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 423 QGYWQKPEESAKVFTKDGW------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGV 496
Cdd:cd17646 346 RGYLGRPALTAERFVPDPFgpgsrmYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVAR 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522138377 497 PDEKSGEVPKVFVVKKD--PALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd17646 426 AAPAGAARLVGYVVPAAgaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
44-557 |
1.61e-52 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 185.96 E-value: 1.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 44 GDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYtPRE-LEH 122
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRA-RGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY-PADrLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 123 QLRDSGAKAIVivenfcttlqqviantpiqhvitTQIGDLAPFPKRAivnfvvkrvkkMVPAwslpgttgfRAALAKGRA 202
Cdd:cd12116 79 ILEDAEPALVL-----------------------TDDALPDRLPAGL-----------PVLL---------LALAAAAAA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 203 QPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIITALPLYHIFALVVncLLFLRH 282
Cdd:cd12116 116 PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLG--LGPGDRLLAVTTYAFDISLLEL--LLPLLA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 283 GCRNVL-----ITNPRDMAAFcveLKRSGFTAITGVNTLFNGLLHApGFAELDFSRfklAVGGGTAVQQAVAEKWQKVTG 357
Cdd:cd12116 192 GARVVIapretQRDPEALARL---IEAHSITVMQATPATWRMLLDA-GWQGRAGLT---ALCGGEALPPDLAARLLSRVG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 358 VgLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFT 437
Cdd:cd12116 265 S-LWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 438 KDG-------WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV 510
Cdd:cd12116 344 PDPfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVL 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 522138377 511 KKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd12116 424 KAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
31-558 |
2.88e-52 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 192.76 E-value: 2.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 31 SLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVN 110
Cdd:COG1020 477 TLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRA-LGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 111 VNPLYtPRE-LEHQLRDSGAKAIVivenfcttlqqviantpiqhvitTQIGDLAPFPKRAivnfvvkrvkkmVPAWSLPg 189
Cdd:COG1020 556 LDPAY-PAErLAYMLEDAGARLVL-----------------------TQSALAARLPELG------------VPVLALD- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 190 ttgfRAALAKGRAQPyARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGkEVIITALPL--- 266
Cdd:COG1020 599 ----ALALAAEPATN-PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYG--LGPG-DRVLQFASLsfd 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 267 ---YHIFAlvvnCLLflrHGCRNVLITN--PRDMAAFCVELKRSGFTAITGVNTLFNGLLHApgfAELDFSRFKLAVGGG 341
Cdd:COG1020 671 asvWEIFG----ALL---SGATLVLAPPeaRRDPAALAELLARHRVTVLNLTPSLLRALLDA---APEALPSLRLVLVGG 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 342 TAVQQAVAEKWQKVT-GVGLTEGYGLTECSPVVSFSPLSVPQWNG---TIGVPLPSTLVSLRDEEENEVPPGQPGELCVK 417
Cdd:COG1020 741 EALPPELVRRWRARLpGARLVNLYGPTETTVDSTYYEVTPPDADGgsvPIGRPIANTRVYVLDAHLQPVPVGVPGELYIG 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 418 GPQVMQGYWQKPEESAKVFTKDGWL-------KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLE 490
Cdd:COG1020 821 GAGLARGYLNRPELTAERFVADPFGfpgarlyRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVRE 900
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522138377 491 VACIGVPDEKSGE-VPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:COG1020 901 AVVVAREDAPGDKrLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALP 969
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
45-558 |
1.37e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 184.95 E-value: 1.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNVlGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQL 124
Cdd:PRK06164 25 DAVALIDEDRPLSRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHIL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 125 RDSGAKAIVIVENFcttlqqvianTPIQHV-ITTQIGDLAPFPKRAIvnFVVKRVKKMVPAwSLPGTTGFRAALAKGRAQ 203
Cdd:PRK06164 104 GRGRARWLVVWPGF----------KGIDFAaILAAVPPDALPPLRAI--AVVDDAADATPA-PAPGARVQLFALPDPAPP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 204 PYARVQLGPDDIAFLQYT-GGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGkEVIITALPLYHIFALvvNCLLFLRH 282
Cdd:PRK06164 171 AAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYG--YDPG-AVLLAALPFCGVFGF--STLLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 283 GCRNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGfAELDFSRFKLAvgGGTAVQQAVAE--KWQKVTGVGL 360
Cdd:PRK06164 246 GGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAG-ERADFPSARLF--GFASFAPALGElaALARARGVPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 361 TEGYGLTECSPVVSFSPLSVP---QWNGTiGVPL-PSTLVSLRDEEENEV-PPGQPGELCVKGPQVMQGYWQKPEESAKV 435
Cdd:PRK06164 323 TGLYGSSEVQALVALQPATDPvsvRIEGG-GRPAsPEARVRARDPQDGALlPDGESGEIEIRAPSLMRGYLDNPDATARA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 436 FTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVpDEKSGEVPKVFVVKKDPA 515
Cdd:PRK06164 402 LTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGA 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 522138377 516 -LTEAELRAYCHENLTGYKMPKYITFLPELP---KSNVGKVLRKELR 558
Cdd:PRK06164 481 sPDEAGLMAACREALAGFKVPARVQVVEAFPvteSANGAKIQKHRLR 527
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
193-544 |
1.78e-51 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 184.73 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 193 FRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEGKE-VIITALPLYHIFA 271
Cdd:cd05927 94 LEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTdVYISYLPLAHIFE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 272 LVVNCLlFLRHGCR--------------------NVLITNPR------DMAAFCVE----LKRSGFTAI--TGVNTLFNG 319
Cdd:cd05927 174 RVVEAL-FLYHGAKigfysgdirlllddikalkpTVFPGVPRvlnriyDKIFNKVQakgpLKRKLFNFAlnYKLAELRSG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 320 LLHAPGFAE-LDFSRFKLAVGG-------GTA-VQQAVAEKWQKVTGVGLTEGYGLTECSPVVSfspLSVPQ-WN-GTIG 388
Cdd:cd05927 253 VVRASPFWDkLVFNKIKQALGGnvrlmltGSApLSPEVLEFLRVALGCPVLEGYGQTECTAGAT---LTLPGdTSvGHVG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 389 VPLPSTLVSLRDEEENE----VPPGQpGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKD 464
Cdd:cd05927 330 GPLPCAEVKLVDVPEMNydakDPNPR-GEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKN 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 465 MI-LVSGFNVYPNEIEGVVAQHPGVLEV-----------ACIGVPD---------EKSGEVPKVFVVKKDPALTEA---E 520
Cdd:cd05927 409 IFkLSQGEYVAPEKIENIYARSPFVAQIfvygdslksflVAIVVPDpdvlkewaaSKGGGTGSFEELCKNPEVKKAileD 488
|
410 420
....*....|....*....|....*
gi 522138377 521 LRAYCHEN-LTGYKMPKYITFLPEL 544
Cdd:cd05927 489 LVRLGKENgLKGFEQVKAIHLEPEP 513
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
187-558 |
2.51e-51 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 182.96 E-value: 2.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 187 LPGTTGFRAALAKGRAQPYARVQLGPDdiafLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEGKEVIITALPL 266
Cdd:cd05929 103 LDGLEDYEAAEGGSPETPIEDEAAGWK----MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPGADSVYLSPAPL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 267 YHIFALVVnCLLFLRHGCRNVLitnprdMAAFCVE-----LKRSGFTAITGVNTLFNGLLHAPG--FAELDFSRFKLAVG 339
Cdd:cd05929 179 YHAAPFRW-SMTALFMGGTLVL------MEKFDPEeflrlIERYRVTFAQFVPTMFVRLLKLPEavRNAYDLSSLKRVIH 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 340 GGTAVQQAVAEKWQKVTGVGLTEGYGLTECspvVSFSPLSVPQW---NGTIGVPLPSTlVSLRDEEENEVPPGQPGELCV 416
Cdd:cd05929 252 AAAPCPPWVKEQWIDWGGPIIWEYYGGTEG---QGLTIINGEEWlthPGSVGRAVLGK-VHILDEDGNEVPPGEIGEVYF 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 417 KGPQVMQgYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGV 496
Cdd:cd05929 328 ANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGV 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522138377 497 PDEKSGEVPKVFV-----VKKDPALtEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05929 407 PDEELGQRVHAVVqpapgADAGTAL-AEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
56-560 |
9.86e-51 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 180.39 E-value: 9.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVnvnPLYT---PRELEHQLRDSGAKAi 132
Cdd:cd05969 1 YTFAQLKVLSARFANVLKS-LGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC---PLFSafgPEAIRDRLENSEAKV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 vivenfcttlqqviantpiqhVITTQigdlapfpkraivnfvvkrvkkmvpawslpgttgfraALAKGRAqpyarvqlgP 212
Cdd:cd05969 76 ---------------------LITTE-------------------------------------ELYERTD---------P 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTHGNVTANVQqVSAWIgpfLDEGKEVII--TALP------LYHIFALVVNcllflrhGC 284
Cdd:cd05969 89 EDPTLLHYTSGTTGTPKGVLHVHDAMIFYYF-TGKYV---LDLHPDDIYwcTADPgwvtgtVYGIWAPWLN-------GV 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 285 RNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGF--AELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTE 362
Cdd:cd05969 158 TNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDElaRKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 363 GYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKG--PQVMQGYWQKPEESAKVFtKDG 440
Cdd:cd05969 238 TWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 441 WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-KKDPALTEA 519
Cdd:cd05969 317 WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlKEGFEPSDE 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 522138377 520 ---ELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELRGK 560
Cdd:cd05969 397 lkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
22-555 |
3.51e-50 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 181.24 E-value: 3.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 22 RTIDTGAVPSLVAMFEQSCARFGDQIAYECMGQ--TLSFAELDRLTQDFASYLQNVlGLQRGDRVALMMPNLLQYPVSLF 99
Cdd:PRK05852 8 APMASDFGPRIADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 100 GVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVenfcttlqqviantpiqhviTTQIGDLAPFPKRAIVNFVVKRVK 179
Cdd:PRK05852 87 AASRADLVVVPLDPALPIAEQRVRSQAAGARVVLID--------------------ADGPHDRAEPTTRWWPLTVNVGGD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 180 KMVPAWSLPGTTGFRAALAKGRAQPYArvqLGPDDiAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAW--IGPfldegK 257
Cdd:PRK05852 147 SGPSGGTLSVHLDAATEPTPATSTPEG---LRPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGyrLSP-----R 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 258 EVIITALPLYHIFALVVNCLLFLRHGCRNVLITNPRDMA-AFCVELKRSGFTAITGVNTLFNGLLHAP-------GFAEL 329
Cdd:PRK05852 218 DATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAhTFWDDIKAVGATWYTAVPTIHQILLERAatepsgrKPAAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 330 DFSRFKLAvgggtAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLsvpQWNG-------TIGVPLPSTLVSLR--D 400
Cdd:PRK05852 298 RFIRSCSA-----PLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQI---EGIGqtenpvvSTGLVGRSTGAQIRivG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 401 EEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTkDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEG 480
Cdd:PRK05852 370 SDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEG 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522138377 481 VVAQHPGVLEVACIGVPDEKSGE-VPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRK 555
Cdd:PRK05852 449 VLASHPNVMEAAVFGVPDQLYGEaVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
55-560 |
1.12e-49 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 179.57 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 55 TLSFAELDRLTQDFASYLQNVLGLQRgDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVI 134
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEP-RVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIY 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 135 VENFCTTLQQVIANTPIqhviTTQIGDLAPFPKRAIVNFVVKrvkkmvpawslpgttgfraalAKGRAQPYARVQLGpdD 214
Cdd:PRK13382 147 DEEFSATVDRALADCPQ----ATRIVAWTDEDHDLTVEVLIA---------------------AHAGQRPEPTGRKG--R 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 215 IAFLqyTGGTTGLSKGAVlthgnvtanvQQVSAWIGPF---LD----EGKEVIITALPLYH-------IFALVVNCLLFL 280
Cdd:PRK13382 200 VILL--TSGTTGTPKGAR----------RSGPGGIGTLkaiLDrtpwRAEEPTVIVAPMFHawgfsqlVLAASLACTIVT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 281 RHGCRnvlitnPRDMAAFcVELKRSgfTAITGVNTLFNGLLHAP--GFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGV 358
Cdd:PRK13382 268 RRRFD------PEATLDL-IDRHRA--TGLAVVPVMFDRIMDLPaeVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 359 GLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYwqkPEESAKVFtK 438
Cdd:PRK13382 339 VIYNNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY---TSGSTKDF-H 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 439 DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-KKDPALT 517
Cdd:PRK13382 415 DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVlKPGASAT 494
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 522138377 518 EAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELRGK 560
Cdd:PRK13382 495 PETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
101-552 |
3.84e-49 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 183.20 E-value: 3.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 101 VLRAGLVVVNVNplYTprelehqlrdSGAKAivivenfcttLQQVIANTPIQHVITTQ--------IGDLAPFPKRAIVN 172
Cdd:PRK08633 685 LLLAGKVPVNLN--YT----------ASEAA----------LKSAIEQAQIKTVITSRkfleklknKGFDLELPENVKVI 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 173 FVVKRVKKMvpawslpGTTGFRAALAKGRAQPYARVQL------GPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVS 246
Cdd:PRK08633 743 YLEDLKAKI-------SKVDKLTALLAARLLPARLLKRlygptfKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQIS 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 247 AWIGPFLDEgkeVIITALPLYHIFALVVNCLLFLRHGCRNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGF 326
Cdd:PRK08633 816 DVFNLRNDD---VILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 327 AELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVS------FSPLSVPQW---NGTIGVPLPSTLVS 397
Cdd:PRK08633 893 HPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASvnlpdvLAADFKRQTgskEGSVGMPLPGVAVR 972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 398 LRDEEE-NEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFT---KDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNV 473
Cdd:PRK08633 973 IVDPETfEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKdidGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMV 1052
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 474 YPNEIEGVVAQ--HPGVLEVACIGVPDEKSGEvpKVFVVKKDPALTEAELRAYCHE-NLTGYKMPKYITFLPELPKSNVG 550
Cdd:PRK08633 1053 PLGAVEEELAKalGGEEVVFAVTAVPDEKKGE--KLVVLHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSG 1130
|
..
gi 522138377 551 KV 552
Cdd:PRK08633 1131 KL 1132
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
45-557 |
9.42e-48 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 172.43 E-value: 9.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQL 124
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALAS-LGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 125 RDSGAKAIVIVenfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqp 204
Cdd:cd05945 85 DAAKPALLIAD--------------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 205 yarvqlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVqqvsAWIGPFLDEGKEVIITALPLYHiFALVVNCLlFLRHGC 284
Cdd:cd05945 96 -------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFT----NWMLSDFPLGPGDVFLNQAPFS-FDLSVMDL-YPALAS 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 285 RNVLITNPRDMAAFCVEL----KRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVT-GVG 359
Cdd:cd05945 163 GATLVPVPRDATADPKQLfrflAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDAR 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 360 LTEGYGLTECSPVVSFSPLSVPQWNG----TIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKV 435
Cdd:cd05945 243 IYNTYGPTEATVAVTYIEVTPEVLDGydrlPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAA 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 436 FTKD---GWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKK 512
Cdd:cd05945 323 FFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPK 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 522138377 513 --DPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd05945 403 pgAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
44-558 |
7.94e-47 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 172.39 E-value: 7.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 44 GDQIAYECMG----QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVvnvNPLYT--- 116
Cdd:PRK04319 58 KDKVALRYLDasrkEKYTYKELKELSNKFANVLKE-LGVEKGDRVFIFMPRIPELYFALLGALKNGAIV---GPLFEafm 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 117 PRELEHQLRDSGAKAIVivenfcTT---LQQVIAN-TP-IQHVIttqigdlapfpkraIVNFVVKrvkkmvpawSLPGTT 191
Cdd:PRK04319 134 EEAVRDRLEDSEAKVLI------TTpalLERKPADdLPsLKHVL--------------LVGEDVE---------EGPGTL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 192 GFRAALAKGRAQpYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTAnvQQVSA-WIgpfLD--EGKEVIITALP--- 265
Cdd:PRK04319 185 DFNALMEQASDE-FDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQ--HYQTGkYV---LDlhEDDVYWCTADPgwv 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 266 ---LYHIFALvvncllfLRHGCRNVLitnprDMAAFCVE-----LKRSG----FTAITGVNTLFN-GLLHAPGFaelDFS 332
Cdd:PRK04319 259 tgtSYGIFAP-------WLNGATNVI-----DGGRFSPErwyriLEDYKvtvwYTAPTAIRMLMGaGDDLVKKY---DLS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 333 --RFKLAVG----------GGTAVQQAVAEK-WQKVTGVGLTEGYGLTECSPvvsfsplsvpqwnGTIGVPLPSTLVSLR 399
Cdd:PRK04319 324 slRHILSVGeplnpevvrwGMKVFGLPIHDNwWMTETGGIMIANYPAMDIKP-------------GSMGKPLPGIEAAIV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 400 DEEENEVPPGQPGELCVKG--PQVMQGYWQKPEESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNE 477
Cdd:PRK04319 391 DDQGNELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 478 IEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-KKDPALTEA---ELRAYCHENLTGYKMPKYITFLPELPKSNVGKVL 553
Cdd:PRK04319 470 VESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVAlRPGYEPSEElkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIM 549
|
....*
gi 522138377 554 RKELR 558
Cdd:PRK04319 550 RRVLK 554
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
36-558 |
8.07e-47 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 169.41 E-value: 8.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 36 FEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLY 115
Cdd:cd17653 3 FERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQ-LGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 116 TPRELEHQLRDSGAKAIVivenfCTTlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfra 195
Cdd:cd17653 82 PSARIQAILRTSGATLLL-----TTD------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 196 alakgraqpyarvqlGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAwigpfldegkeviitalplyhifalvvn 275
Cdd:cd17653 103 ---------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPA---------------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 276 cLLFLRHGCRNVLITNPrdmaafcvelkrsGFTAITGV--NTLFNG--LL---HAPGFAEL------------------- 329
Cdd:cd17653 140 -RLDVGPGSRVAQVLSI-------------AFDACIGEifSTLCNGgtLVladPSDPFAHVartvdalmstpsilstlsp 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 330 -DFSRFKLAVGGGTAVQQAVAEKWQKvtGVGLTEGYGLTECSPVVSFSPLSvPQWNGTIGVPLPSTLVSLRDEEENEVPP 408
Cdd:cd17653 206 qDFPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELL-PGQPVTIGKPIPNSTCYILDADLQPVPE 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 409 GQPGELCVKGPQVMQGYWQKPEESAKVFTKDGW------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVV 482
Cdd:cd17653 283 GVVGEICISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVV 362
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522138377 483 AQHPGVLEVACIGVpdekSGEVPKVFVVKKDpaLTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd17653 363 LQSQPEVTQAAAIV----VNGRLVAFVTPET--VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
56-558 |
1.30e-46 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 169.24 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVnvnPLYT---PRELEHQLRDSGAKAI 132
Cdd:cd05973 1 LTFGELRALSARFANALQE-LGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTafgPKAIEHRLRTSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIvenfcttlqqviantpiqhvittqigDLAPfpkraivnfvvkrvkkmvpawslpgttgfRAALAkgraqpyarvqlgp 212
Cdd:cd05973 77 VT--------------------------DAAN-----------------------------RHKLD-------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGavlthgnVTANVQQVSAWiGPFLDEGKEVI------ITALP--LYHIFALVVNCLLFlrhGC 284
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKG-------VPVPLRALAAF-GAYLRDAVDLRpedsfwNAADPgwAYGLYYAITGPLAL---GH 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 285 RNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFS-RFKLAVGGGTAVQQAVAEKWQKVTGVGLTEG 363
Cdd:cd05973 157 PTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDH 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 364 YGLTECS-PVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCV---KGPQV-MQGYWQKPEESAKvftk 438
Cdd:cd05973 237 YGQTELGmVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAID---- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 439 DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-----KKD 513
Cdd:cd05973 313 GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrgghEGT 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 522138377 514 PALtEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05973 393 PAL-ADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
220-546 |
1.96e-46 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 165.55 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 220 YTGGTTGLSKGAVLTHGNVTAnvQQVSAWIGPFLDEGKeVIITALPLYHIFALVVNCLLFLRHGcRNVLI--TNPRDMAA 297
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLA--QALVLAVLQAIDEGT-VFLNSGPLFHIGTLMFTLATFHAGG-TNVFVrrVDAEEVLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 298 FCV-ELKRSGFT------AITGVNtlfngllhAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGvglteGYGLTECS 370
Cdd:cd17636 83 LIEaERCTHAFLlpptidQIVELN--------ADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPG-----GYGQTEVM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 371 PVVSFSPLSVPQwNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVfTKDGWLKTGDVAVF 450
Cdd:cd17636 150 GLATFAALGGGA-IGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARR-TRGGWHHTNDLGRR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 451 EPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA-LTEAELRAYCHENL 529
Cdd:cd17636 228 EPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGAsVTEAELIEHCRARI 307
|
330
....*....|....*..
gi 522138377 530 TGYKMPKYITFLPELPK 546
Cdd:cd17636 308 ASYKKPKSVEFADALPR 324
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
54-558 |
5.69e-46 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 169.39 E-value: 5.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDsgakaiv 133
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQ-LGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRK------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 134 iVENFCTTLQQviantPiqHVITTQigDLAPfpkraivnfvvkRVKKMVPAWSLPGTTGFRAALAKGRAQPYARVQLGPD 213
Cdd:cd05906 110 -LRHIWQLLGS-----P--VVLTDA--ELVA------------EFAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRPD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 DIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSaWIGPFLDegKEVIITALPLYHIFALVVNCLLFLRHGCRNV------ 287
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKI-QHNGLTP--QDVFLNWVPLDHVGGLVELHLRAVYLGCQQVhvptee 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 288 LITNPrdmaafcvelkrsgftaitgvnTLFNGLLH--------APGFA--------------ELDFSRFKLAVGGGTAVQ 345
Cdd:cd05906 245 ILADP----------------------LRWLDLIDryrvtitwAPNFAfallndlleeiedgTWDLSSLRYLVNAGEAVV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 346 QAVAEKWQKVTG-VGLTE-----GYGLTE-CSPVVSFSPLSVPQWNGT-----IGVPLPSTLVSLRDEEENEVPPGQPGE 413
Cdd:cd05906 303 AKTIRRLLRLLEpYGLPPdairpAFGMTEtCSGVIYSRSFPTYDHSQAlefvsLGRPIPGVSMRIVDDEGQLLPEGEVGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 414 LCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAvFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLE--V 491
Cdd:cd05906 383 LQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfT 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522138377 492 ACIGVPDEKSG-EVPKVFVVkkdPALTEAELRAYCHENLTGYKM------PKYITFLP--ELPKSNVGKVLRKELR 558
Cdd:cd05906 462 AAFAVRDPGAEtEELAIFFV---PEYDLQDALSETLRAIRSVVSrevgvsPAYLIPLPkeEIPKTSLGKIQRSKLK 534
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
35-557 |
1.13e-45 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 166.72 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 35 MFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQnVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPL 114
Cdd:cd12115 4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLR-AAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 115 YTPRELEHQLRDSGAKaivivenfcttlqqviantpiqHVITTqigdlapfpkraivnfvvkrvkkmvpawslpgttgfr 194
Cdd:cd12115 83 YPPERLRFILEDAQAR----------------------LVLTD------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 195 aalakgraqpyarvqlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPflDEGKEVIITA-----LPLYHI 269
Cdd:cd12115 104 -----------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSA--EELAGVLASTsicfdLSVFEL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 270 FALvvncllfLRHGCRNVLITN---PRDMAAfcvelkRSGFTAITGVNTLFNGLLHAPGFAEldfSRFKLAVGGGTAVQQ 346
Cdd:cd12115 165 FGP-------LATGGKVVLADNvlaLPDLPA------AAEVTLINTVPSAAAELLRHDALPA---SVRVVNLAGEPLPRD 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 347 AVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLSvPQWNG--TIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQG 424
Cdd:cd12115 229 LVQRLYARLQVERVVNLYGPSEDTTYSTVAPVP-PGASGevSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 425 YWQKPEESAKVFTKDGWL------KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEvACIGVPD 498
Cdd:cd12115 308 YLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVRE-AVVVAIG 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522138377 499 EKSGEVPKV-FVVKKDP-ALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd12115 387 DAAGERRLVaYIVAEPGaAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
45-558 |
1.62e-45 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 168.24 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNVlGLQRGDRVALMMPNLLQYPVSLFGVLRAGlvVVNVNPLYTPRELE--- 121
Cdd:PRK10946 38 DAIAVICGERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSElna 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 122 --HQLrdsgAKAIVIVEN---------FCTTLQQVIANtpIQHVITtqIGDlapfpkraivnfvvkrvkkmvpawslPGT 190
Cdd:PRK10946 115 yaSQI----EPALLIADRqhalfsdddFLNTLVAEHSS--LRVVLL--LND--------------------------DGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 191 TGFRAALAKGrAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQvSAWIGPFLDEGKevIITALPLYHIF 270
Cdd:PRK10946 161 HSLDDAINHP-AEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRR-SVEICGFTPQTR--YLCALPAAHNY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 271 ALVVNCLL--FLRHGCRnVLITNPRDMAAF-CVELKRSGFTAIT--GVnTLFNGLLHAPGF-AELdfSRFKLAVGGGTAV 344
Cdd:PRK10946 237 PMSSPGALgvFLAGGTV-VLAPDPSATLCFpLIEKHQVNVTALVppAV-SLWLQAIAEGGSrAQL--ASLKLLQVGGARL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 345 QQAVAEKWQKVTGVGLTEGYGLTEcsPVVSFSPLSVPQWN--GTIGVPL-PSTLVSLRDEEENEVPPGQPGELCVKGPQV 421
Cdd:PRK10946 313 SETLARRIPAELGCQLQQVFGMAE--GLVNYTRLDDSDERifTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 422 MQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKS 501
Cdd:PRK10946 391 FRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELM 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 522138377 502 GEVPKVFVVKKDPaLTEAELRAYCHE-NLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK10946 471 GEKSCAFLVVKEP-LKAVQLRRFLREqGIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
212-557 |
3.23e-45 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 166.62 E-value: 3.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 PDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEgKEVIITALPLYHIFALVVNCLLFLRhGCRnVLITN 291
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP-DDRYLAYLPLAHIFELAAENVCLYR-GGT-IGYGS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 292 PRDM--AAF------CVELKRSGFTAITGV-------------------NTLFNG--------LLHAPG---FAELDFSR 333
Cdd:cd17639 164 PRTLtdKSKrgckgdLTEFKPTLMVGVPAIwdtirkgvlaklnpmgglkRTLFWTayqsklkaLKEGPGtplLDELVFKK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 334 FKLAVGG-------GTAVQQAVAEKWQKVTGVGLTEGYGLTE---CSPVvsfspLSVPQWN-GTIGVPLPSTLVSLRDEE 402
Cdd:cd17639 244 VRAALGGrlrymlsGGAPLSADTQEFLNIVLCPVIQGYGLTEtcaGGTV-----QDPGDLEtGRVGPPLPCCEIKLVDWE 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 403 E----NEVPPGQpGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMI-LVSGFNVYPNE 477
Cdd:cd17639 319 EggysTDKPPPR-GEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 478 IEGVVAQHPGVLEVACIGVPDEKSgevPKVFVVKKDPALT---------EAELRAYCHE------------------NLT 530
Cdd:cd17639 398 LESIYRSNPLVNNICVYADPDKSY---PVAIVVPNEKHLTklaekhgviNSEWEELCEDkklqkavlkslaetaraaGLE 474
|
410 420 430
....*....|....*....|....*....|...
gi 522138377 531 GYKMPKYITFLPEL--PKSNV----GKVLRKEL 557
Cdd:cd17639 475 KFEIPQGVVLLDEEwtPENGLvtaaQKLKRKEI 507
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
36-558 |
5.15e-45 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 165.98 E-value: 5.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 36 FEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLY 115
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRA-RGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 116 TPRELEHQLRDSGAKAIVivenfcttlqqviantpiqhvitTQIGDLAPFPKRAIVnfvvkrvkkmVPAWSLPGTTgfra 195
Cdd:cd17651 80 PAERLAFMLADAGPVLVL-----------------------THPALAGELAVELVA----------VTLLDQPGAA---- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 196 alAKGRAQPyaRVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQ------------QVSAWIGPFLDEGKEVIITA 263
Cdd:cd17651 123 --AGADAEP--DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAwqarasslgpgaRTLQFAGLGFDVSVQEIFST 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 264 LplyhifaLVVNCLLFLRHGCRnvliTNPRDMAAFCVElkrsgftaiTGVNTLF--NGLLHA------PGFAELDFSRFk 335
Cdd:cd17651 199 L-------CAGATLVLPPEEVR----TDPPALAAWLDE---------QRISRVFlpTVALRAlaehgrPLGVRLAALRY- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 336 LAVGGGTAV-QQAVAEKWQKVTGVGLTEGYGLTECSPVvsfSPLSVPQWNG------TIGVPLPSTLVSLRDEEENEVPP 408
Cdd:cd17651 258 LLTGGEQLVlTEDLREFCAGLPGLRLHNHYGPTETHVV---TALSLPGDPAawpappPIGRPIDNTRVYVLDAALRPVPP 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 409 GQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWL------KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVV 482
Cdd:cd17651 335 GVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAAL 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522138377 483 AQHPGVLEVACIGVPDEKSGEVPKVFVV-KKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd17651 415 ARHPGVREAVVLAREDRPGEKRLVAYVVgDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
62-558 |
5.85e-44 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 164.81 E-value: 5.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 62 DRLTQDFASYLQnvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTT 141
Cdd:PLN03102 47 DRCCRLAASLIS--LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 142 LQQVIantpiqHVITTQigDLAPFPKRAIVNfvvkrvKKMVPAWSLPGTTGFRAALAKGRAQP--YAR---VQLGPDDIA 216
Cdd:PLN03102 125 AREVL------HLLSSE--DSNLNLPVIFIH------EIDFPKRPSSEELDYECLIQRGEPTPslVARmfrIQDEHDPIS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 217 fLQYTGGTTGLSKGAVLTH-GNVTANVQQVSAW-IGPFldegkEVIITALPLYHIFALVVNCLLFLRHGCrNVLItnpRD 294
Cdd:PLN03102 191 -LNYTSGTTADPKGVVISHrGAYLSTLSAIIGWeMGTC-----PVYLWTLPMFHCNGWTFTWGTAARGGT-SVCM---RH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 295 MAAFCV--ELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVtGVGLTEGYGLTECSPV 372
Cdd:PLN03102 261 VTAPEIykNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL-GFQVMHAYGLTEATGP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 373 VSFSPLSvPQWN-----------GTIGVP-LPSTLVSLRDEEENEVPP--GQP-GELCVKGPQVMQGYWQKPEESAKVFt 437
Cdd:PLN03102 340 VLFCEWQ-DEWNrlpenqqmelkARQGVSiLGLADVDVKNKETQESVPrdGKTmGEIVIKGSSIMKGYLKNPKATSEAF- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 438 KDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKK----- 512
Cdd:PLN03102 418 KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEkgett 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 522138377 513 -----DPALT-EAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PLN03102 498 kedrvDKLVTrERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
35-558 |
6.66e-44 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 162.71 E-value: 6.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 35 MFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPL 114
Cdd:cd05918 4 LIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRS-LGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 115 YtPRE-LEHQLRDSGAKaIVIVENfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgf 193
Cdd:cd05918 83 H-PLQrLQEILQDTGAK-VVLTSS-------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 194 raalakgraqpyarvqlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIITA-----LPLYH 268
Cdd:cd05918 105 ------------------PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG--LTSESRVLQFAsytfdVSILE 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 269 IF-ALVVNCLLFL--RHGCRNvlitnprDMAAFCVELKrsgftaitgVNTLFnglLhAPGFAEL----DFSRFKLAVGGG 341
Cdd:cd05918 165 IFtTLAAGGCLCIpsEEDRLN-------DLAGFINRLR---------VTWAF---L-TPSVARLldpeDVPSLRTLVLGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 342 TAVQQAVAEKWQKvtGVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPST--LVSLRDEEEnEVPPGQPGELCVKGP 419
Cdd:cd05918 225 EALTQSDVDTWAD--RVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATcwVVDPDNHDR-LVPIGAVGELLIEGP 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 420 QVMQGYWQKPEESAKVFTKD-GWL------------KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHP 486
Cdd:cd05918 302 ILARGYLNDPEKTAAAFIEDpAWLkqegsgrgrrlyRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSL 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 487 GVLEVACIGVPDEKSGEVPK---VFVVKKDPALTE------------------AELRAYCHENLTGYKMPKYITFLPELP 545
Cdd:cd05918 382 PGAKEVVVEVVKPKDGSSSPqlvAFVVLDGSSSGSgdgdslflepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLP 461
|
570
....*....|...
gi 522138377 546 KSNVGKVLRKELR 558
Cdd:cd05918 462 LTASGKIDRRALR 474
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
35-557 |
2.30e-43 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 161.34 E-value: 2.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 35 MFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQnVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPL 114
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLR-EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 115 YTPRELEHQLRDSGAKAIVIVENfcttLQQVIANtpIQHVITTQIGDLAPFPKRAivnfvVKRVKKmvpawslpgttgfr 194
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSH----LQPPIAF--IGLIDLLDEDTIYHEESEN-----LEPVSK-------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 195 aalakgraqpyarvqlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVqqVSAWIGPFLDEGKEVIITA-----LPLYHI 269
Cdd:cd17655 136 -----------------SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLV--EWANKVIYQGEHLRVALFAsisfdASVTEI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 270 FAlvvnCLLflrhgCRNVLITNPR----DMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFklaVGGGTAVQ 345
Cdd:cd17655 197 FA----SLL-----SGNTLYIVRKetvlDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHL---IVGGEALS 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 346 QAVAEKWQKV--TGVGLTEGYGLTECSpVVSFSPLSVPQWNGT----IGVPLPSTLVSLRDEEENEVPPGQPGELCVKGP 419
Cdd:cd17655 265 TELAKKIIELfgTNPTITNAYGPTETT-VDASIYQYEPETDQQvsvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 420 QVMQGYWQKPEESAKVFTKDGWL------KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVAC 493
Cdd:cd17655 344 GVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVV 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522138377 494 IGVPDEKSGEVPKVFVVkKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd17655 424 IARKDEQGQNYLCAYIV-SEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
34-557 |
2.65e-43 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 166.49 E-value: 2.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 34 AMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNVlGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNP 113
Cdd:PRK12467 516 QLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 114 LYtPRE-LEHQLRDSGAKaivivenFCTTLQQVIANTPIQHVITTQIGDLApfpkraivnfvvkrvkkmvpawslpgttg 192
Cdd:PRK12467 595 EY-PQDrLAYMLDDSGVR-------LLLTQSHLLAQLPVPAGLRSLCLDEP----------------------------- 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 193 frAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEgkEVIITALPLYHIFAL 272
Cdd:PRK12467 638 --ADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADD--SMLMVSTFAFDLGVT 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 273 VvnclLF--LRHGcRNVLITNP---RDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELdfSRFKLAVGGGTAVQQA 347
Cdd:PRK12467 714 E----LFgaLASG-ATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQRALVCGGEALQVD 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 348 VAEKW-QKVTGVGLTEGYGLTECSPVVSFSPLS---VPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQ 423
Cdd:PRK12467 787 LLARVrALGPGARLINHYGPTETTVGVSTYELSdeeRDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLAR 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 424 GYWQKPEESAKVFTKDGW-------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGV 496
Cdd:PRK12467 867 GYHRRPALTAERFVPDPFgadggrlYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ 946
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522138377 497 PDEKSGE-----VPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK12467 947 PGDAGLQlvaylVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
6-553 |
9.61e-43 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 161.21 E-value: 9.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 6 AAGEFVWFQEYPPSVPRTIDTGAVPSlVAMFEQS----CARF--------GDQIA--YE----CMGQTLSFAELDRLTQD 67
Cdd:cd17634 18 EAGKILDWITPYQKVKNTSFAPGAPS-IKWFEDAtlnlAANAldrhlrenGDRTAiiYEgddtSQSRTISYRELHREVCR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 68 FASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVia 147
Cdd:cd17634 97 FAGTLLD-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSV-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 148 ntPIQHVITTQIGDLAPFPKRAIVnfvVKRVKKMVpAWSLPGTTGFRAALAKGRAQpYARVQLGPDDIAFLQYTGGTTGL 227
Cdd:cd17634 174 --PLKKNVDDALNPNVTSVEHVIV---LKRTGSDI-DWQEGRDLWWRDLIAKASPE-HQPEAMNAEDPLFILYTSGTTGK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 228 SKGAVLTHGNVTANVQQVSAW---IGP------FLDEGkevIITALPlYHIFA-LVVNCLLFLRHGcrnvlITNPRDMAA 297
Cdd:cd17634 247 PKGVLHTTGGYLVYAATTMKYvfdYGPgdiywcTADVG---WVTGHS-YLLYGpLACGATTLLYEG-----VPNWPTPAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 298 FCVELKRSGFTAITGVNTLFNGLLHA--PGFAELDFSRFKLAVGGGTAVQ-QAVAEKWQKVTGVG--LTEGYGLTECS-P 371
Cdd:cd17634 318 MWQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILGSVGEPINpEAYEWYWKKIGKEKcpVVDTWWQTETGgF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 372 VVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGP---QVMQGYWQKPEESAKVF-TKDGWLKTGDV 447
Cdd:cd17634 398 MITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpgQTRTLFGDHERFEQTYFsTFKGMYFSGDG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 448 AVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKK----DPALTEAELRA 523
Cdd:cd17634 478 ARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNhgvePSPELYAELRN 557
|
570 580 590
....*....|....*....|....*....|
gi 522138377 524 YCHENLTGYKMPKYITFLPELPKSNVGKVL 553
Cdd:cd17634 558 WVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
53-558 |
2.94e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 158.63 E-value: 2.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNVlGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:PRK13390 22 GEQVSYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIvenfCTTLQQVIAntpiqhvittQIGdlAPFPKRaiVNFvvkrvkkmvpAWSLPGTTGFRAALAkGRAQPYARVQLGp 212
Cdd:PRK13390 101 VA----SAALDGLAA----------KVG--ADLPLR--LSF----------GGEIDGFGSFEAALA-GAGPRLTEQPCG- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 ddiAFLQYTGGTTGLSKGAV--LTHGNVTANVQQVSAWIGPFLD-EGKEVIITALPLYHIFALVVNCLLFLRHGcrNVLI 289
Cdd:PRK13390 151 ---AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDiSESDIYYSSAPIYHAAPLRWCSMVHALGG--TVVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 290 TNPRDMAAFCVELKRSGFTAITGVNTLFNGLL--HAPGFAELDFSRFKLAVGGGTA----VQQAVAEkWqkvTGVGLTEG 363
Cdd:PRK13390 226 AKRFDAQATLGHVERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLRAVIHAAAPcpvdVKHAMID-W---LGPIVYEY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 364 YGLTEcspVVSFSPLSVPQW---NGTIGVPLPSTLvSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVF--TK 438
Cdd:PRK13390 302 YSSTE---AHGMTFIDSPDWlahPGSVGRSVLGDL-HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQhpAH 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 439 DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKV---FVVKKDPA 515
Cdd:PRK13390 378 PFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAviqLVEGIRGS 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 522138377 516 LTEA-ELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK13390 458 DELArELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
220-554 |
3.10e-42 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 154.10 E-value: 3.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 220 YTGGTTGLSKGAVLTHgnvtanvqqvSAWIGPF-------LDEGKEVIITALPLYHIFALVvNCLLFLRHGcRNVLITNP 292
Cdd:cd17633 7 FTSGTTGLPKAYYRSE----------RSWIESFvcnedlfNISGEDAILAPGPLSHSLFLY-GAISALYLG-GTFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 293 RDMAAFCVELKRSGFTAITGVNTLFNGLLHApgfaELDFSRFKLAVGGGTAVQQAVAEKWQKVT-GVGLTEGYGLTEcsp 371
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQALART----LEPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 372 vVSFSPLSVPQWN---GTIGVPLPSTLVSLRDEEENEVppgqpGELCVKGPQVMQGYWqkpeeSAKVFTKDGWLKTGDVA 448
Cdd:cd17633 148 -LSFITYNFNQESrppNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSEMVFSGYV-----RGGFSNPDGWMSVGDIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 449 VFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPkVFVVKKDpALTEAELRAYCHEN 528
Cdd:cd17633 217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSGD-KLTYKQLKRFLKQK 294
|
330 340
....*....|....*....|....*.
gi 522138377 529 LTGYKMPKYITFLPELPKSNVGKVLR 554
Cdd:cd17633 295 LSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
25-490 |
8.57e-42 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 159.49 E-value: 8.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 25 DTGAVPSLVAMFEQSCARFGDqiaYECMG------------QTLSFAEL-DRLTQDFASYLQnvLGLQRGDRVALMMPNL 91
Cdd:PLN02736 39 DHPEIGTLHDNFVYAVETFRD---YKYLGtrirvdgtvgeyKWMTYGEAgTARTAIGSGLVQ--HGIPKGACVGLYFINR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 92 LQYPVSLFGVLRAGLVVVnvnPLYtprelehqlrDS-GAKAIVIVENFCTTlqQVIANTPiqHVITTQIGDLAPFPK-RA 169
Cdd:PLN02736 114 PEWLIVDHACSAYSYVSV---PLY----------DTlGPDAVKFIVNHAEV--AAIFCVP--QTLNTLLSCLSEIPSvRL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 170 IVnfVVKRVKKMVPawSLPGTTG-----FRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANV-- 242
Cdd:PLN02736 177 IV--VVGGADEPLP--SLPSGTGveivtYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVag 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 243 QQVSAWIGPfldegKEVIITALPLYHIFALVvNCLLFLRHGCR-------NVLITNprDMAA-----FC----------- 299
Cdd:PLN02736 253 SSLSTKFYP-----SDVHISYLPLAHIYERV-NQIVMLHYGVAvgfyqgdNLKLMD--DLAAlrptiFCsvprlynriyd 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 300 ---VELKRSGFTAITGVNTLFNGLLHA--------PGFAELDFSRFKLAVGG--------GTAVQQAVAEKWQKVTGVGL 360
Cdd:PLN02736 325 gitNAVKESGGLKERLFNAAYNAKKQAlengknpsPMWDRLVFNKIKAKLGGrvrfmssgASPLSPDVMEFLRICFGGRV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 361 TEGYGLTECSPVVSFSPLSvPQWNGTIGVPLPSTLVSLRD-EEENEVPPGQP---GELCVKGPQVMQGYWQKPEESAKVF 436
Cdd:PLN02736 405 LEGYGMTETSCVISGMDEG-DNLSGHVGSPNPACEVKLVDvPEMNYTSEDQPyprGEICVRGPIIFKGYYKDEVQTREVI 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 522138377 437 TKDGWLKTGDVAVFEPNGYLRIVDRKKDMI-LVSGFNVYPNEIEGVVAQHPGVLE 490
Cdd:PLN02736 484 DEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQ 538
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
212-559 |
8.89e-41 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 155.34 E-value: 8.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 PDDIAFLQYTGGTTGLSKGAVLTHgnvTANVQQVSAWIGPFLDEGKEVIITALPLYHIFALVvNCLLFLRHGCRNVLItn 291
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISH---SALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLS-SALAMLMVGACHVLL-- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 292 PRDMAAFCVE-LKRSGFTAITGVNTLFNGLLHAPGFAELDFSR---FKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLT 367
Cdd:PLN02860 245 PKFDAKAALQaIKQHNVTSMITVPAMMADLISLTRKSMTWKVFpsvRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 368 E-CS--------------------PVVSFSPLSVPQWNGT-IGVPLPSTLVSLRDEEENEVppgqpGELCVKGPQVMQGY 425
Cdd:PLN02860 325 EaCSsltfmtlhdptlespkqtlqTVNQTKSSSVHQPQGVcVGKPAPHVELKIGLDESSRV-----GRILTRGPHVMLGY 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 426 WQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVP 505
Cdd:PLN02860 400 WGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMV 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522138377 506 KVFV---------------VKKDPALTEAELRAYCHE-NLTGYKMPK-YITFLPELPKSNVGKVLRKELRG 559
Cdd:PLN02860 480 VACVrlrdgwiwsdnekenAKKNLTLSSETLRHHCREkNLSRFKIPKlFVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
76-558 |
9.12e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 154.86 E-value: 9.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 76 LGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTP-IQHv 154
Cdd:PRK07008 59 LGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLTFLPLVDALAPQCPnVKG- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 155 ittqigdlapfpkraivnFVVKRVKKMVPAWSLPGTTgfRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLT 234
Cdd:PRK07008 138 ------------------WVAMTDAAHLPAGSTPLLC--YETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 235 H--------GNVTANVQQVSAwigpfldegKEVIITALPLYHIFA--LVVNCLLFlrhGCRNVLITNPRDMAAF--CVEL 302
Cdd:PRK07008 198 HrstvlhayGAALPDAMGLSA---------RDAVLPVVPMFHVNAwgLPYSAPLT---GAKLVLPGPDLDGKSLyeLIEA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 303 KRSGFTAitGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSPLSVPQ 382
Cdd:PRK07008 266 ERVTFSA--GVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKLKWKH 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 383 wngtIGVPLPSTL------------VSLR--DEEENEVP-PGQP-GELCVKGPQVMQGYWqKPEESAKVftkDGWLKTGD 446
Cdd:PRK07008 344 ----SQLPLDEQRkllekqgrviygVDMKivGDDGRELPwDGKAfGDLQVRGPWVIDRYF-RGDASPLV---DGWFPTGD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 447 VAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPA-LTEAELRAYC 525
Cdd:PRK07008 416 VATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAeVTREELLAFY 495
|
490 500 510
....*....|....*....|....*....|...
gi 522138377 526 HENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK07008 496 EGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
14-558 |
6.19e-40 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 153.01 E-value: 6.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 14 QEYPPSVPRTIDTGAV---PSLVAMFEQSCArfgdqiayecmgQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPN 90
Cdd:PRK05620 6 QDVPLSLTRILEYGSTvhgDTTVTTWGGAEQ------------EQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 91 LLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTP-IQHVITtqIGDlAPFPKRA 169
Cdd:PRK05620 74 CAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKECPcVRAVVF--IGP-SDADSAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 170 IVnfvvkrVKKMVPAWSLpgttgfrAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAwI 249
Cdd:PRK05620 151 AH------MPEGIKVYSY-------EALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRT-T 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 250 GPFLDEGKEVIITALPLYHIFALVVNCLLFLRhGCRNVL----ITNPRDMAAFCVELKRSGFtaitGVNTLFNGLL---- 321
Cdd:PRK05620 217 DSLAVTHGESFLCCVPIYHVLSWGVPLAAFMS-GTPLVFpgpdLSAPTLAKIIATAMPRVAH----GVPTLWIQLMvhyl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 322 -HAPgfaeldfSRFKLA--VGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPV--VSFSPLSVP---QWN-----GTIG 388
Cdd:PRK05620 292 kNPP-------ERMSLQeiYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVgtVARPPSGVSgeaRWAyrvsqGRFP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 389 VPLPSTLVSlrDEEENEVPPGQPGELCVKGPQVMQGYWQKP----------------EESAKVFTKDGWLKTGDVAVFEP 452
Cdd:PRK05620 365 ASLEYRIVN--DGQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 453 NGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKD---PALTEAE-LRAYCHEN 528
Cdd:PRK05620 443 DGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPgiePTRETAErLRDQLRDR 522
|
570 580 590
....*....|....*....|....*....|
gi 522138377 529 LTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK05620 523 LPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
45-558 |
3.66e-39 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 148.67 E-value: 3.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQL 124
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRA-LGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 125 RDSGAkaivivenfcttlqqviantpiqHVITTQigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqp 204
Cdd:cd17649 81 EDSGA-----------------------GLLLTH---------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 205 yarvqlGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfldegkeviITA----LPLYHI-FALVVNCLLF 279
Cdd:cd17649 92 ------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYG----------LTPgdreLQFASFnFDGAHEQLLP 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 280 -LRHGCRNVLITNPR-DMAAFCVELKRSGFTAITGVNT--LFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKv 355
Cdd:cd17649 156 pLICGACVVLRPDELwASADELAEMVRELGVTVLDLPPayLQQLAEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLK- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 356 TGVGLTEGYGLTE---------CSPVVSFSPLSVPqwngtIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYW 426
Cdd:cd17649 235 APVRLFNAYGPTEatvtplvwkCEAGAARAGASMP-----IGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 427 QKPEESAKVFTKDG-------WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDE 499
Cdd:cd17649 310 GRPELTAERFVPDPfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522138377 500 KSGEVPKVFVVKKDPALTE--AELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd17649 390 GGKQLVAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
45-557 |
5.73e-39 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 148.96 E-value: 5.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQL 124
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKA-AGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 125 RDSGAKAIVivenfcttlqqviantpiqhvitTQIGDLAPFPKRAIVNFVVKrvkkmvpawslpgttgfrAALAKGRAQP 204
Cdd:cd12114 81 ADAGARLVL-----------------------TDGPDAQLDVAVFDVLILDL------------------DALAAPAPPP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 205 YARVQlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAwigPFLDEGKEVI--ITAL----PLYHIFALvvncll 278
Cdd:cd12114 120 PVDVA--PDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR---RFAVGPDDRVlaLSSLsfdlSVYDIFGA------ 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 279 fLRHGCRNVLIT--NPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQK-- 354
Cdd:cd12114 189 -LSAGATLVLPDeaRRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRAla 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 355 ----VTGVGltegyGLTECS------PV--VSFSPLSVPqwngtIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVM 422
Cdd:cd12114 268 pdarLISLG-----GATEASiwsiyhPIdeVPPDWRSIP-----YGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 423 QGYWQKPEESAKVFTKDG----WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPD 498
Cdd:cd12114 338 LGYLGDPELTAARFVTHPdgerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGD 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 499 EKSGEVPKVFVVK-KDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd12114 418 PGGKRLAAFVVPDnDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
56-558 |
6.92e-39 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 150.16 E-value: 6.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVnvnPLYTP-----RE-----LEHQLR 125
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLA-LGLKPGDRVALIAETDGDFVEAFFACQYAGLVPV---PLPLPmgfggREsyiaqLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 126 DSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAPfpkraivnfvvkrvkkmVPAWSLPGTTgfraalakgraqpy 205
Cdd:PRK09192 126 SAQPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKALP-----------------EADVALPRPT-------------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 206 arvqlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAwIGPFLDEGKEVIiTALPLYHIFALVvNCLL------- 278
Cdd:PRK09192 175 ------PDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISH-DGLKVRPGDRCV-SWLPFYHDMGLV-GFLLtpvatql 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 279 ---------FLRhgcRNV----LITNPRDMAA----FCVEL--KRSGFTAItgvntlfngllhapgfAELDFSRFKLAVG 339
Cdd:PRK09192 246 svdylptrdFAR---RPLqwldLISRNRGTISysppFGYELcaRRVNSKDL----------------AELDLSCWRVAGI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 340 GG----TAVQQAVAEKWqkvTGVGLTE-----GYGLTECSPVVSFSPL-------------------SVPQWNGT----- 386
Cdd:PRK09192 307 GAdmirPDVLHQFAEAF---APAGFDDkafmpSYGLAEATLAVSFSPLgsgivveevdrdrleyqgkAVAPGAETrrvrt 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 387 ---IGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKpEESAKVFTKDGWLKTGDVAvFEPNGYLRIVDRKK 463
Cdd:PRK09192 384 fvnCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRD-EESQDVLAADGWLDTGDLG-YLLDGYLYITGRAK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 464 DMILVSGFNVYPNEIEGVVAQHPGVL--EVACIGVPDEkSGEVPKVFVVKKdpaLTEAELRAYCHENLTGY-----KMPK 536
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQE-NGEKIVLLVQCR---ISDEERRGQLIHALAALvrsefGVEA 537
|
570 580
....*....|....*....|....
gi 522138377 537 YITFLP--ELPKSNVGKVLRKELR 558
Cdd:PRK09192 538 AVELVPphSLPRTSSGKLSRAKAK 561
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
36-544 |
1.07e-38 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 150.02 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 36 FEQSCARFGDQIA--YEcmGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNP 113
Cdd:PRK08279 43 FEEAAARHPDRPAllFE--DQSISYAELNARANRYAHWAAA-RGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 114 LYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAPFPkRAIVNFvvkrvkkmvpawslpgttgf 193
Cdd:PRK08279 120 QQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDP-EGYEDL-------------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 194 rAALAKGRAQ--PYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTAnvqqVSAWIGPFLD-EGKEVIITALPLYHIF 270
Cdd:PRK08279 179 -AAAAAGAPTtnPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLK----AMGGFGGLLRlTPDDVLYCCLPLYHNT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 271 ALVVnCLlflrhGCrnVLitnprdMAAFCVELKR----SGF---------TAITGVNTLFNGLLHAPGfAELDFS-RFKL 336
Cdd:PRK08279 254 GGTV-AW-----SS--VL------AAGATLALRRkfsaSRFwddvrryraTAFQYIGELCRYLLNQPP-KPTDRDhRLRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 337 AVGGGTavQQAVAEKWQKVTGVG-LTEGYGLTECSpvVSFSPL-SVPqwnGTIG-VPL----PSTLVS--------LRDE 401
Cdd:PRK08279 319 MIGNGL--RPDIWDEFQQRFGIPrILEFYAASEGN--VGFINVfNFD---GTVGrVPLwlahPYAIVKydvdtgepVRDA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 402 EEN--EVPPGQPGELC--VKGPQVMQGYwQKPEESAK-----VFTK-DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGF 471
Cdd:PRK08279 392 DGRciKVKPGEVGLLIgrITDRGPFDGY-TDPEASEKkilrdVFKKgDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 472 NVYPNEIEGVVAQHPGVLEVACIGVpdeksgEVPKV--------FVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPE 543
Cdd:PRK08279 471 NVATTEVENALSGFPGVEEAVVYGV------EVPGTdgragmaaIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPE 544
|
.
gi 522138377 544 L 544
Cdd:PRK08279 545 L 545
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
35-557 |
1.21e-38 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 147.32 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 35 MFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNVlGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPL 114
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGK-GVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 115 YTPRELEHQLRDSGAKaivivenfcttlqqviantpiqhVITTQigdlapfpkraivnfvvkrvkkmvpawslpgttgfr 194
Cdd:cd17645 82 YPGERIAYMLADSSAK-----------------------ILLTN------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 195 aalakgraqpyarvqlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTanvqQVSAWIGPFLDEGKEVIITALPLYHIFALVV 274
Cdd:cd17645 103 -----------------PDDLAYVIYTSGSTGLPKGVMIEHHNLV----NLCEWHRPYFGVTPADKSLVYASFSFDASAW 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 275 NCLLFLRHGCRNVLITNPR--DMAAFCVELKRSGFTaitgVNTLFNGLlhAPGFAELDFSRFKLAVGGGTAVQQAVAEKW 352
Cdd:cd17645 162 EIFPHLTAGAALHVVPSERrlDLDALNDYFNQEGIT----ISFLPTGA--AEQFMQLDNQSLRVLLTGGDKLKKIERKGY 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 353 QkvtgvgLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEES 432
Cdd:cd17645 236 K------LVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 433 AKVFTKDGWL------KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPK 506
Cdd:cd17645 310 AEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLV 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 522138377 507 VFVVKKDPALTEaELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd17645 390 AYVTAPEEIPHE-ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
45-557 |
1.76e-38 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 146.84 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQL 124
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRG-LGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 125 RDSGAKAIVIVenfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqp 204
Cdd:cd17650 81 EDSGAKLLLTQ--------------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 205 yarvqlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTanvQQVSAWigpfldeGKEVIITALPLYHI----FALVVNCLLFL 280
Cdd:cd17650 92 -------PEDLAYVIYTSGTTGKPKGVMVEHRNVA---HAAHAW-------RREYELDSFPVRLLqmasFSFDVFAGDFA 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 281 RHGCR-NVLITNPR----DMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGtavqQAVAEKWQKV 355
Cdd:cd17650 155 RSLLNgGTLVICPDevklDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGS----DGCKAQDFKT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 356 ------TGVGLTEGYGLTECSPVVSFSPLS---------VPqwngtIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQ 420
Cdd:cd17650 231 laarfgQGMRIINSYGVTEATIDSTYYEEGrdplgdsanVP-----IGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 421 VMQGYWQKPEESAKVFTKDGW------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEvACI 494
Cdd:cd17650 306 VARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVV 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522138377 495 GVPDEKSGEVPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd17650 385 AVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
31-557 |
3.37e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 151.08 E-value: 3.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 31 SLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVN 110
Cdd:PRK12467 1575 LVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIA-LGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 111 VNPLYTPRELEHQLRDSGAKAIVIVENFCttlQQVIANTPIQHVITTQIGDlapfpkraivnfvvkrvkkmvpaWslpgt 190
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSGIELLLTQSHLQ---ARLPLPDGLRSLVLDQEDD-----------------------W----- 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 191 tgfraalAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEgkeviitALPLYHIF 270
Cdd:PRK12467 1703 -------LEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAAD-------VVLQFTSF 1768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 271 ALVVNCLLF---LRHGCRnVLITNP---RDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSrFKLAVGGGTAV 344
Cdd:PRK12467 1769 AFDVSVWELfwpLINGAR-LVIAPPgahRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS-LRRVVCGGEAL 1846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 345 QQAVAEKW-QKVTGVGLTEGYGLTECSPVVSFSPLSVPQWNGT----IGVPLPSTLVSLRDEEENEVPPGQPGELCVKGP 419
Cdd:PRK12467 1847 EVEALRPWlERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRdsvpIGQPIANLSTYILDASLNPVPIGVAGELYLGGV 1926
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 420 QVMQGYWQKPEESAKVF------TKDGWL-KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVA 492
Cdd:PRK12467 1927 GLARGYLNRPALTAERFvadpfgTVGSRLyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAV 2006
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522138377 493 CIGVpDEKSGEVPKVFVVKKDPALTE---------AELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK12467 2007 VIAQ-DGANGKQLVAYVVPTDPGLVDddeaqvalrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
30-557 |
4.29e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 150.88 E-value: 4.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 30 PSLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVV 109
Cdd:PRK12316 4551 RCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIA-RGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYV 4629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 110 NVNPLYtPRE-LEHQLRDSGAkAIVIVENFctTLQQVIANTPIQHVITTQIGDLAPFPKRAivnfvvkrvkkmvPAwslp 188
Cdd:PRK12316 4630 PLDPEY-PRErLAYMMEDSGA-ALLLTQSH--LLQRLPIPDGLASLALDRDEDWEGFPAHD-------------PA---- 4688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 189 gttgfraalakgraqpyarVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVqqvsAWIGPFLDEGKEVIITALPLYH 268
Cdd:PRK12316 4689 -------------------VRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHL----HATGERYELTPDDRVLQFMSFS 4745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 269 IFALVVNCLLFLRHGCRnVLITNPR--DMAAFCVELKRSGFTAITGVNTLFNGLL-HAPGFAELdfSRFKLAVGGGTAVQ 345
Cdd:PRK12316 4746 FDGSHEGLYHPLINGAS-VVIRDDSlwDPERLYAEIHEHRVTVLVFPPVYLQQLAeHAERDGEP--PSLRVYCFGGEAVA 4822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 346 QA-VAEKWQKVTGVGLTEGYGLTECSPVVSF---------SPLSVPqwngtIGVPLPSTLVSLRDEEENEVPPGQPGELC 415
Cdd:PRK12316 4823 QAsYDLAWRALKPVYLFNGYGPTETTVTVLLwkardgdacGAAYMP-----IGTPLGNRSGYVLDGQLNPLPVGVAGELY 4897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 416 VKGPQVMQGYWQKPEESAKVFTKDGW-------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGV 488
Cdd:PRK12316 4898 LGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4977
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522138377 489 LEVACIGVPDeKSGEVPKVFVVKKDPALTEA---------ELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK12316 4978 REAVVIAQEG-AVGKQLVGYVVPQDPALADAdeaqaelrdELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
44-558 |
6.00e-38 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 147.85 E-value: 6.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 44 GDQIA------YECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTP 117
Cdd:cd05967 65 GDQIAliydspVTGTERTYTYAELLDEVSRLAGVLRK-LGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 118 RELEHQLRDSGAKAIV----------IVEnFCTTLQQVI--ANTPIQHVITTQIGDLAPFPKRaivnfvvkrvkkmvpaw 185
Cdd:cd05967 144 KELASRIDDAKPKLIVtascgiepgkVVP-YKPLLDKALelSGHKPHHVLVLNRPQVPADLTK----------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 186 slPGTT-GFRAALAKgrAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGN----VTANVQQVSAwIGPfldegKEVI 260
Cdd:cd05967 206 --PGRDlDWSELLAK--AEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGhavaLNWSMRNIYG-IKP-----GDVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 261 ITALPLyhifALVVN----CLLFLRHGCRNVLI----TNPRDMAAF---CVELK-RSGFTAITGVNTLFNGLLHAPGFAE 328
Cdd:cd05967 276 WAASDV----GWVVGhsyiVYGPLLHGATTVLYegkpVGTPDPGAFwrvIEKYQvNALFTAPTAIRAIRKEDPDGKYIKK 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 329 LDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTE-----CSPVVSFSPLSVPQwnGTIGVPLPSTLVSLRDEEE 403
Cdd:cd05967 352 YDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTEtgwpiTANPVGLEPLPIKA--GSPGKPVPGYQVQVLDEDG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 404 NEVPPGQPGELCVKGP---QVMQGYWQKPEE-SAKVFTKD-GWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEI 478
Cdd:cd05967 430 EPVGPNELGNIVIKLPlppGCLLTLWKNDERfKKLYLSKFpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEM 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 479 EGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-----KKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVL 553
Cdd:cd05967 510 EESVLSHPAVAECAVVGVRDELKGQVPLGLVVlkegvKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKIL 589
|
....*
gi 522138377 554 RKELR 558
Cdd:cd05967 590 RRTLR 594
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
30-557 |
9.09e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 149.72 E-value: 9.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 30 PSLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVV 109
Cdd:PRK12316 2003 PGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRA-RGVGPEVRVAIAAERSFELVVALLAVLKAGGAYV 2081
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 110 NVNPLYtPRE-LEHQLRDSGAkaivivenfcttlqqviantpiqHVITTQIGDLAPFPkraivnfvvkrvkkmvPAWSLP 188
Cdd:PRK12316 2082 PLDPNY-PAErLAYMLEDSGA-----------------------ALLLTQRHLLERLP----------------LPAGVA 2121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 189 GTTGFRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQqvsaWIGPFLDEGKEVIITALPLYH 268
Cdd:PRK12316 2122 RLPLDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQ----AAGERYELSPADCELQFMSFS 2197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 269 IFALVVNCLLFLRHGCRNVL----ITNPRDMAAfcvELKRSGFTAITGVNTLFNGLLHApgfAELDFSRFKLAVG--GGT 342
Cdd:PRK12316 2198 FDGAHEQWFHPLLNGARVLIrddeLWDPEQLYD---EMERHGVTILDFPPVYLQQLAEH---AERDGRPPAVRVYcfGGE 2271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 343 AVQQAVAEK-WQKVTGVGLTEGYGLTE---------CSPVVSFSPLSVPqwngtIGVPLPSTLVSLRDEEENEVPPGQPG 412
Cdd:PRK12316 2272 AVPAASLRLaWEALRPVYLFNGYGPTEavvtpllwkCRPQDPCGAAYVP-----IGRALGNRRAYILDADLNLLAPGMAG 2346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 413 ELCVKGPQVMQGYWQKPEESAKVFTKDGW-------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQH 485
Cdd:PRK12316 2347 ELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAH 2426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522138377 486 PGVLEVACIGVpDEKSGEVPKVFVVKKDPA-LTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK12316 2427 PAVREAVVVAQ-DGASGKQLVAYVVPDDAAeDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
54-501 |
1.28e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 146.63 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLqNVLGlQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVnvnPLYTPRELEHQLRDSGakaiv 133
Cdd:PRK05850 34 ETLTWSQLYRRTLNVAEEL-RRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAV---PLSVPQGGAHDERVSA----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 134 ivenfcttlqqVIANTPIQHVITTQigdlapfpkrAIVNFVVKRVKKMvPAWSLPGTTGFRAALAKGRAQPYARVQLGPD 213
Cdd:PRK05850 104 -----------VLRDTSPSVVLTTS----------AVVDDVTEYVAPQ-PGQSAPPVIEVDLLDLDSPRGSDARPRDLPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 dIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAwiGPFLDEGKEV-----IITALPLYHIFALVVNCLLFLRHGCRNVL 288
Cdd:PRK05850 162 -TAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMS--DYFGDTGGVPppdttVVSWLPFYHDMGLVLGVCAPILGGCPAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 289 iTNPrdmAAFcveLKR------------SGFTAitgvntlfngllhAPGFAeldfsrFKLAVG------------GGTAV 344
Cdd:PRK05850 239 -TSP---VAF---LQRparwmqllasnpHAFSA-------------APNFA------FELAVRktsdddmagldlGGVLG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 345 QQAVAEKWQKVT---------GVGLTE-----GYGLTEC------------SPVVSFSP--LSVPQ------WNGT---- 386
Cdd:PRK05850 293 IISGSERVHPATlkrfadrfaPFNLREtairpSYGLAEAtvyvatrepgqpPESVRFDYekLSAGHakrcetGGGTplvs 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 387 IGVPlPSTLVSLRDEEEN-EVPPGQPGELCVKGPQVMQGYWQKPEESAKVF----------TKDG-WLKTGDVAvFEPNG 454
Cdd:PRK05850 373 YGSP-RSPTVRIVDPDTCiECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLG-FISEG 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 522138377 455 YLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVlEVACIGVPDEKS 501
Cdd:PRK05850 451 ELFIVGRIKDLLIVDGRNHYPDDIEATIQEITGG-RVAAISVPDDGT 496
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
68-560 |
1.31e-37 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 146.53 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 68 FASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVI- 146
Cdd:PLN02479 58 LASALAK-RSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALk 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 147 -----ANTPIQHVITTQIGDLAPFPKraivnfvvkrvkkmvpawslpgttGFRAALAKGRAQPYARVQLG--------PD 213
Cdd:PLN02479 137 ilaekKKSSFKPPLLIVIGDPTCDPK------------------------SLQYALGKGAIEYEKFLETGdpefawkpPA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 D----IAfLQYTGGTTGLSKGAVLTHGNvtANVQQVSAWIGPFLDEGKeVIITALPLYH------IFALVVNCL--LFLR 281
Cdd:PLN02479 193 DewqsIA-LGYTSGTTASPKGVVLHHRG--AYLMALSNALIWGMNEGA-VYLWTLPMFHcngwcfTWTLAALCGtnICLR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 282 HgcrnvlITNPRDMAAfcveLKRSGFTAITGVNTLFNGLLHAPGfAE--LDFSRFKLAVGGGTA----VQQAVAEKWQKV 355
Cdd:PLN02479 269 Q------VTAKAIYSA----IANYGVTHFCAAPVVLNTIVNAPK-SEtiLPLPRVVHVMTAGAApppsVLFAMSEKGFRV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 356 TGV-GLTEGYG-LTECS--------PVVSFSPLSVPQWNGTIG------------VPLPSTLVSLrdeeenevppgqpGE 413
Cdd:PLN02479 338 THTyGLSETYGpSTVCAwkpewdslPPEEQARLNARQGVRYIGlegldvvdtktmKPVPADGKTM-------------GE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 414 LCVKGPQVMQGYWQKPEESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVAC 493
Cdd:PLN02479 405 IVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522138377 494 IGVPDEKSGEVPKVFVVKK------DPALTEAELRAYCHENLTGYKMPKYITFLPeLPKSNVGKVLRKELRGK 560
Cdd:PLN02479 484 VARPDERWGESPCAFVTLKpgvdksDEAALAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAK 555
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
54-558 |
2.76e-37 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 146.10 E-value: 2.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIV 133
Cdd:cd05968 90 RTLTYGELLYEVKRLANGLRA-LGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 134 IVENFC---------TTLQQVIANTP-IQHVIttqigdlapfpkraivnfVVKRVKKMVPawslPGTTGFRAALAKGRAQ 203
Cdd:cd05968 169 TADGFTrrgrevnlkEEADKACAQCPtVEKVV------------------VVRHLGNDFT----PAKGRDLSYDEEKETA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 204 PYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWigPF-LDEGKEVI-ITAL-----PLYHIFALVVNC 276
Cdd:cd05968 227 GDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYF--QFdLKPGDLLTwFTDLgwmmgPWLIFGGLILGA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 277 LLFLRHGCRNvlITNPRDMAAFcVELKRSGFTAITGvnTLFNGLLHAPGFAELDFSRFKLAVGGGTAvqqavaEKWQKVT 356
Cdd:cd05968 305 TMVLYDGAPD--HPKADRLWRM-VEDHEITHLGLSP--TLIRALKPRGDAPVNAHDLSSLRVLGSTG------EPWNPEP 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 357 GVGLTEGYGLTECsPVVSFS----------------PLSVPQWNGtigvPLPSTLVSLRDEEENEVPPgQPGELCVKGPQ 420
Cdd:cd05968 374 WNWLFETVGKGRN-PIINYSggteisggilgnvlikPIKPSSFNG----PVPGMKADVLDESGKPARP-EVGELVLLAPW 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 421 V--MQGYWQKPEESAKVFTK--DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGV 496
Cdd:cd05968 448 PgmTRGFWRDEDRYLETYWSrfDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGV 527
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522138377 497 PDEKSGEVPKVFVVKKD-----PALTEaELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05968 528 PHPVKGEAIVCFVVLKPgvtptEALAE-ELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
54-531 |
3.53e-37 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 144.15 E-value: 3.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIV 133
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRA-LGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 134 ivenfcttLQQVIANTPIQHVITTQIGDLApfpkraivnfvvkrvkkMVPAWSLPGTTGFRAALAKGraQPY-ARVQLGP 212
Cdd:cd05932 84 --------VGKLDDWKAMAPGVPEGLISIS-----------------LPPPSAANCQYQWDDLIAQH--PPLeERPTRFP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPfldEGKEVIITALPLYHIFALVVNCLLFLRHGcrnVLITNP 292
Cdd:cd05932 137 EQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGT---EENDRMLSYLPLAHVTERVFVEGGSLYGG---VLVAFA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 293 RDMAAFCVELKRSGFTAITGVN---TLFN-GLLHAPGFAELD---------------------FSRFKLAVGGGTAVQQA 347
Cdd:cd05932 211 ESLDTFVEDVQRARPTLFFSVPrlwTKFQqGVQDKIPQQKLNlllkipvvnslvkrkvlkglgLDQCRLAGCGSAPVPPA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 348 VAEkWQKVTGVGLTEGYGLTECSpvvSFSPLSVP--QWNGTIGVPLPStlVSLRDEEEnevppgqpGELCVKGPQVMQGY 425
Cdd:cd05932 291 LLE-WYRSLGLNILEAYGMTENF---AYSHLNYPgrDKIGTVGNAGPG--VEVRISED--------GEILVRSPALMMGY 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 426 WQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVS-GFNVYPNEIEGVVAQHPGVlEVACI---GVPDEKS 501
Cdd:cd05932 357 YKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRV-EMVCVigsGLPAPLA 435
|
490 500 510
....*....|....*....|....*....|
gi 522138377 502 GEVPKVFVVKKDPALTEAELRAYCHENLTG 531
Cdd:cd05932 436 LVVLSEEARLRADAFARAELEASLRAHLAR 465
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
45-557 |
1.42e-36 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 141.24 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQL 124
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAA-RGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 125 RDSGAKAIVivenfcttlqqviantpiqhvitTQigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqp 204
Cdd:cd17652 81 ADARPALLL-----------------------TT---------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 205 yarvqlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIITALPLYHIFALVVncLLFLRHGC 284
Cdd:cd17652 92 -------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFD--VGPGSRVLQFASPSFDASVWEL--LMALLAGA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 285 RNVLITNPR-----DMAAFcveLKRSGFTAIT----GVNTLFNGLLhaPGFAELdfsrfklaVGGGTAVQQAVAEKWqkV 355
Cdd:cd17652 161 TLVLAPAEEllpgePLADL---LREHRITHVTlppaALAALPPDDL--PDLRTL--------VVAGEACPAELVDRW--A 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 356 TGVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKV 435
Cdd:cd17652 226 PGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAER 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 436 FTKDGW-------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEvACIGVPDEKSGEVPKV- 507
Cdd:cd17652 306 FVADPFgapgsrmYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE-AVVVVRDDRPGDKRLVa 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 522138377 508 -FVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd17652 385 yVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
31-558 |
1.89e-36 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 145.70 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 31 SLVAMFEQSCARFGDQIAYECMGQT------LSFAELDRLTQDFASYLQNVLGLqrGDRVALMMPNLLQYPVSLFGVLRA 104
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 105 GLVVVnvnPLYTPREL--EHQLR------DSGAKAIVIVENFCTTLQQVIANTpiqhvittqiGDLAPfpkraivnfvvk 176
Cdd:PRK05691 88 GVIAV---PAYPPESArrHHQERllsiiaDAEPRLLLTVADLRDSLLQMEELA----------AANAP------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 177 rvkkmvpawSLPGTTGFRAALAKGRAQPyarvQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEG 256
Cdd:PRK05691 143 ---------ELLCVDTLDPALAEAWQEP----ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFG--IDLN 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 257 -KEVIITALPLYHIFALVVNCLLFLRHGCRNVLITnprdmAAFCVELKRSGFTAITGVNTLFNGllhAPGFA-------- 327
Cdd:PRK05691 208 pDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMS-----PAYFLERPLRWLEAISEYGGTISG---GPDFAyrlcserv 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 328 ------ELDFSRFKLAVGGGTAVQQAVAEKW-QKVTGVGLTE-----GYGLTECSPVVSFSP------------------ 377
Cdd:PRK05691 280 sesaleRLDLSRWRVAYSGSEPIRQDSLERFaEKFAACGFDPdsffaSYGLAEATLFVSGGRrgqgipaleldaealarn 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 378 LSVPQWNGTI---GVPLPSTLVSLRDEEENEV-PPGQPGELCVKGPQVMQGYWQKPEESAKVFTK-DG--WLKTGDVAvF 450
Cdd:PRK05691 360 RAEPGTGSVLmscGRSQPGHAVLIVDPQSLEVlGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLG-F 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 451 EPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVL---EVAC----------IGVPDEKSGEV-----PKVFVVKK 512
Cdd:PRK05691 439 LRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVrkgRVAAfavnhqgeegIGIAAEISRSVqkilpPQALIKSI 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 522138377 513 DPALTEAelrayCHEnltgykMPKYITFL-P-ELPKSNVGKVLRKELR 558
Cdd:PRK05691 519 RQAVAEA-----CQE------APSVVLLLnPgALPKTSSGKLQRSACR 555
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
54-523 |
3.71e-35 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 139.26 E-value: 3.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLqNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKA-I 132
Cdd:PRK09274 40 DELSFAELDARSDAIAHGL-NAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAfI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIvenfcttlqqviantPIQHVITTqigdLAPFPKRAI-VNFVVKRvkkmvpAWSLPGTTgFRAALAKGRAQPYARVQLG 211
Cdd:PRK09274 119 GI---------------PKAHLARR----LFGWGKPSVrRLVTVGG------RLLWGGTT-LATLLRDGAAAPFPMADLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 PDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQV-SAW-IGPflDEgkeviiTALPLYHIFALVVNCLlflrhGCRNVL- 288
Cdd:PRK09274 173 PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALrEDYgIEP--GE------IDLPTFPLFALFGPAL-----GMTSVIp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 289 -------IT-NPRDMaafcvelkrsgFTAIT--GVNTLF------NGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKW 352
Cdd:PRK09274 240 dmdptrpATvDPAKL-----------FAAIEryGVTNLFgspallERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 353 QKV--TGVGLTEGYGLTECSPVVSFSPLSV--PQWNGT-------IGVPLPSTLVSLRD---------EEENEVPPGQPG 412
Cdd:PRK09274 309 RAMlpPDAEILTPYGATEALPISSIESREIlfATRAATdngagicVGRPVDGVEVRIIAisdapipewDDALRLATGEIG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 413 ELCVKGPQVMQGYWQKPEES--AKVFTKDG--WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGV 488
Cdd:PRK09274 389 EIVVAGPMVTRSYYNRPEATrlAKIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGV 468
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 522138377 489 LEVACIGVPdeKSGEVPKVFVVKKDPALT------EAELRA 523
Cdd:PRK09274 469 KRSALVGVG--VPGAQRPVLCVELEPGVAcsksalYQELRA 507
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
81-552 |
4.31e-35 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 141.26 E-value: 4.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 81 GDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNplYTprelehqlrdSGAKAIViveNFCTTLQqviantpIQHVITTqig 160
Cdd:PRK06814 682 GENVGVMLPNANGAAVTFFALQSAGRVPAMIN--FS----------AGIANIL---SACKAAQ-------VKTVLTS--- 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 161 dlapfpkRAivnFVVK-RVKKMVPAWS----------LPGTTGF----RAALAKGRAQPYaRVQLGPDDIAFLQYTGGTT 225
Cdd:PRK06814 737 -------RA---FIEKaRLGPLIEALEfgiriiyledVRAQIGLadkiKGLLAGRFPLVY-FCNRDPDDPAVILFTSGSE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 226 GLSKGAVLTHGNVTANVQQVSAWIgPFldEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLITNPRDMAAFCVELKRS 305
Cdd:PRK06814 806 GTPKGVVLSHRNLLANRAQVAARI-DF--SPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSPLHYRIIPELIYDT 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 306 GFTAITGVNTLFNGllHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSfspLSVPQWN- 384
Cdd:PRK06814 883 NATILFGTDTFLNG--YARYAHPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIA---LNTPMHNk 957
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 385 -GTIGVPLPstLVSLRDEEENEVPPGqpGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKK 463
Cdd:PRK06814 958 aGTVGRLLP--GIEYRLEPVPGIDEG--GRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAK 1033
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 464 DMILVSGFNVYPNEIEGVVAQ-HPGVLEVAcIGVPDEKSGEvpKVFVVKKDPALTEAELRAYCHEN-LTGYKMPKYITFL 541
Cdd:PRK06814 1034 RFAKIAGEMISLAAVEELAAElWPDALHAA-VSIPDARKGE--RIILLTTASDATRAAFLAHAKAAgASELMVPAEIITI 1110
|
490
....*....|.
gi 522138377 542 PELPKSNVGKV 552
Cdd:PRK06814 1111 DEIPLLGTGKI 1121
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-557 |
9.42e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 140.86 E-value: 9.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 35 MFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPL 114
Cdd:PRK12316 516 LFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPE 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 115 YTPRELEHQLRDSGAKAIvivenfcttLQQviantpiqhvitTQIGDLAPFPkRAIVNFVVKRVKKMVPAWSlpgttgfr 194
Cdd:PRK12316 595 YPAERLAYMLEDSGVQLL---------LSQ------------SHLGRKLPLA-AGVQVLDLDRPAAWLEGYS-------- 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 195 aalakgRAQPyaRVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIITAlplyhIFALVV 274
Cdd:PRK12316 645 ------EENP--GTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYG--LGVGDTVLQKT-----PFSFDV 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 275 NCLLF---LRHGCRNVLIT--NPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRfKLAVGG----GTAVQ 345
Cdd:PRK12316 710 SVWEFfwpLMSGARLVVAApgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLR-RIVCSGealpADAQE 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 346 QAVAEKWQKvtgvGLTEGYGLTE------CSPVVSFSPLSVPqwngtIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGP 419
Cdd:PRK12316 789 QVFAKLPQA----GLYNLYGPTEaaidvtHWTCVEEGGDSVP-----IGRPIANLACYILDANLEPVPVGVLGELYLAGR 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 420 QVMQGYWQKPEESAKVFTKDGWL------KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVAC 493
Cdd:PRK12316 860 GLARGYHGRPGLTAERFVPSPFVagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 939
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522138377 494 IGVpdekSGEVPKVFVVKKDPALTEAE-LRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK12316 940 LAV----DGKQLVGYVVLESEGGDWREaLKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
53-558 |
1.17e-34 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 135.94 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKS-LGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIvenfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqpyarvqlgp 212
Cdd:cd05940 80 VV------------------------------------------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 dDIAFLQYTGGTTGLSKGAVLTHG---NVTANVQqvsawiGPFLDEGKEVIITALPLYHIFALVVNCLLFLRHGCrNVLI 289
Cdd:cd05940 82 -DAALYIYTSGTTGLPKAAIISHRrawRGGAFFA------GSGGALPSDVLYTCLPLYHSTALIVGWSACLASGA-TLVI 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 290 TNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPgfAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVG-LTEGYGLTE 368
Cdd:cd05940 154 RKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQP--PKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPrIAEFYAATE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 369 CspVVSFspLSVPQWNGTIGV-PLPSTLVS--------------LRDEEE--NEVPPGQPGELC--VKGPQVMQGYWQKP 429
Cdd:cd05940 232 G--NSGF--INFFGKPGAIGRnPSLLRKVAplalvkydlesgepIRDAEGrcIKVPRGEPGLLIsrINPLEPFDGYTDPA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 430 EESAK----VFTK-DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVP----DEK 500
Cdd:cd05940 308 ATEKKilrdVFKKgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgtDGR 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 522138377 501 SGEVpkVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05940 388 AGMA--AIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
302-558 |
1.28e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 136.45 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 302 LKRSGFTAITGVNTLFNGLLHAPGFAEldfSRFKLAVGG---GTAVQQAVAEKWQKVTgvgLTEGYGLTECSPVVSFSPL 378
Cdd:PRK07638 227 LETENISVMYTVPTMLESLYKENRVIE---NKMKIISSGakwEAEAKEKIKNIFPYAK---LYEFYGASELSFVTALVDE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 379 SVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVfTKDGWLKTGDVAVFEPNGYLRI 458
Cdd:PRK07638 301 ESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAREL-NADGWMTVRDVGYEDEEGFIYI 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 459 VDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPkVFVVKKDPalTEAELRAYCHENLTGYKMPKYI 538
Cdd:PRK07638 380 VGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKP-VAIIKGSA--TKQQLKSFCLQRLSSFKIPKEW 456
|
250 260
....*....|....*....|
gi 522138377 539 TFLPELPKSNVGKVLRKELR 558
Cdd:PRK07638 457 HFVDEIPYTNSGKIARMEAK 476
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
31-479 |
5.91e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 136.40 E-value: 5.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 31 SLVAMFEQSCARFGDQIAYECM---------GQTLSFAELDRLTQDFASYLQNVLglQRGDRVALMMPNLLQYPVSLFGV 101
Cdd:PRK07769 22 NLVRHVERWAKVRGDKLAYRFLdfsterdgvARDLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 102 LRAGLVVVnvnPLYTPRELEHQLRdsgakaivivenfcttLQQVIANTPIQHVITTQigDLAPFPKRAIVNFVVKRVKKM 181
Cdd:PRK07769 100 LYAGRIAV---PLFDPAEPGHVGR----------------LHAVLDDCTPSAILTTT--DSAEGVRKFFRARPAKERPRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 182 VPAWSLPGTTGfraalakgraQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIi 261
Cdd:PRK07769 159 IAVDAVPDEVG----------ATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALE--GQEGDRGV- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 262 TALPLYHIFALVVncLLFLRHGCRNVLITNPrdmAAFCV-------ELKRSGftaiTGVNTLFNGllhAPGFA------- 327
Cdd:PRK07769 226 SWLPFFHDMGLIT--VLLPALLGHYITFMSP---AAFVRrpgrwirELARKP----GGTGGTFSA---APNFAfehaaar 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 328 --------ELDFSRFKLAVGGGTAVQQAVAEKWQKVTG-VGLTE-----GYGLTECSPVVSFSPL--------------- 378
Cdd:PRK07769 294 glpkdgepPLDLSNVKGLLNGSEPVSPASMRKFNEAFApYGLPPtaikpSYGMAEATLFVSTTPMdeeptviyvdrdeln 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 379 -------------SVPQWN-GTIGVPLPSTLVSlrDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVF-------- 436
Cdd:PRK07769 374 agrfvevpadapnAVAQVSaGKVGVSEWAVIVD--PETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrl 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 522138377 437 -------TKDG--WLKTGDVAVFEpNGYLRIVDRKKDMILVSGFNVYPNEIE 479
Cdd:PRK07769 452 seshaegAPDDalWVRTGDYGVYF-DGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
31-557 |
7.39e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 137.99 E-value: 7.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 31 SLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLqnvlgLQRG---DR-VALMMPNLLQYPVSLFGVLRAGL 106
Cdd:PRK12467 3096 LVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRL-----IAIGvgpDVlVGVAVERSVEMIVALLAVLKAGG 3170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 107 VVVNVNPLYtPRE-LEHQLRDSGAKAIVivenfctTLQQVIANTPIQ---HVITTQIGDLAPFPKRaivnfvvkrvkkmv 182
Cdd:PRK12467 3171 AYVPLDPEY-PRErLAYMIEDSGVKLLL-------TQAHLLEQLPAPagdTALTLDRLDLNGYSEN-------------- 3228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 183 pawslpgttgfraalakgraQPYARVQlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIit 262
Cdd:PRK12467 3229 --------------------NPSTRVM--GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYE--LDANDRVL-- 3282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 263 alpLYHIFAL---VVNCLLFLRHGCRNVLITNP-RDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELdfSRFKLAV 338
Cdd:PRK12467 3283 ---LFMSFSFdgaQERFLWTLICGGCLVVRDNDlWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADC--ASLDIYV 3357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 339 GGGTAVQ-QAVAEKWQKVTGVGLTEGYGLTECSPVVSF---------SPLSVPqwngtIGVPLPSTLVSLRDEEENEVPP 408
Cdd:PRK12467 3358 FGGEAVPpAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLwkcggdavcEAPYAP-----IGRPVAGRSIYVLDGQLNPVPV 3432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 409 GQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWL-------KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGV 481
Cdd:PRK12467 3433 GVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgsggrlyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEAR 3512
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522138377 482 VAQHPGVLEVACIGVpDEKSGEVPKVFVVKKDP-ALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK12467 3513 LLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPqGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
66-560 |
1.21e-33 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 135.93 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 66 QDFASYLQNVL---GLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTL 142
Cdd:PRK06060 37 HDGAARLGEVLrnrGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 143 QqviantpiqhviTTQIGDLAPFPKRAivnfvvkrvkkmvpawslpgttgfraalakGRAQPYARVQLGPDDIAFLQYTG 222
Cdd:PRK06060 117 Q------------PSRVAEAAELMSEA------------------------------ARVAPGGYEPMGGDALAYATYTS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 223 GTTGLSKGAVLTHGNVTANVQQV---SAWIGPfldegKEVIITALPLYHIFALVVNCLLFLRHGCRNVLitNPRDMAAFC 299
Cdd:PRK06060 155 GTTGPPKAAIHRHADPLTFVDAMcrkALRLTP-----EDTGLCSARMYFAYGLGNSVWFPLATGGSAVI--NSAPVTPEA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 300 VELKRSGF--TAITGVNTLFNGLLHApgFAELDFSRFKLAVGGGTAVQQAVAEKWQKV-TGVGLTEGYGLTECSPvvSFS 376
Cdd:PRK06060 228 AAILSARFgpSVLYGVPNFFARVIDS--CSPDSFRSLRCVVSAGEALELGLAERLMEFfGGIPILDGIGSTEVGQ--TFV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 377 PLSVPQWN-GTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEesaKVFTKDGWLKTGDVAVFEPNGY 455
Cdd:PRK06060 304 SNRVDEWRlGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPVANEGWLDTRDRVCIDSDGW 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 456 LRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPALTEAELRAYCHE----NLTG 531
Cdd:PRK06060 381 VTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRgllnRLSA 460
|
490 500
....*....|....*....|....*....
gi 522138377 532 YKMPKYITFLPELPKSNVGKVLRKELRGK 560
Cdd:PRK06060 461 FKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
77-558 |
4.47e-33 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 132.95 E-value: 4.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 77 GLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQviantpiqhvit 156
Cdd:PRK06018 60 GIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLTFVPILEK------------ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 157 tqIGDLAPFPKRaivnFVVKRVKKMVPAWSLPGTTGFRAALAKGRAQpYARVQLGPDDIAFLQYTGGTTGLSKGAVLTH- 235
Cdd:PRK06018 128 --IADKLPSVER----YVVLTDAAHMPQTTLKNAVAYEEWIAEADGD-FAWKTFDENTAAGMCYTSGTTGDPKGVLYSHr 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 236 GNVtanVQQVSAWIGPFLDEG-KEVIITALPLYHIFA--LVVNCLLFlrhGCRNVLITNPRDMAAFCVELKRSGFTAITG 312
Cdd:PRK06018 201 SNV---LHALMANNGDALGTSaADTMLPVVPLFHANSwgIAFSAPSM---GTKLVMPGAKLDGASVYELLDTEKVTFTAG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 313 VNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVtGVGLTEGYGLTECSPVVSFSPLSVP----------Q 382
Cdd:PRK06018 275 VPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMTEMSPLGTLAALKPPfsklpgdarlD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 383 WNGTIGVPLPSTLVSLRDEEENEVP-PGQ-PGELCVKGPQVMQGYWQkpeESAKVFTKDGWLKTGDVAVFEPNGYLRIVD 460
Cdd:PRK06018 354 VLQKQGYPPFGVEMKITDDAGKELPwDGKtFGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRITD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 461 RKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKK-DPALTEAELRAYCHENLTGYKMPKYIT 539
Cdd:PRK06018 431 RSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKpGETATREEILKYMDGKIAKWWMPDDVA 510
|
490
....*....|....*....
gi 522138377 540 FLPELPKSNVGKVLRKELR 558
Cdd:PRK06018 511 FVDAIPHTATGKILKTALR 529
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
214-554 |
6.19e-33 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 128.92 E-value: 6.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 DIAFLQYTGGTTGLSKGAVLTHGN-VTANVQQVSAWIGPFLDEgkeVIITALPLYHIFALVvNCLLFLRHGCRNVLITNP 292
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNWVVGD---VTYLPLPATHIGGLW-WILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 293 RDMAAFCVELKRSGFTAITGVNTLFNGL--LHAPGFAELDFSRFkLAVGGGTAVQQAVAE-KWQKVTGVglTEGYGLTEC 369
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLvsELKSANATVPSLRL-IGYGGSRAIAADVRFiEATGLTNT--AQVYGLSET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 370 SpVVSFSPLSVPQWN-GTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTkDGWLKTGDVA 448
Cdd:cd17635 155 G-TALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 449 VFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDpALTEAELRAYCHE- 527
Cdd:cd17635 233 ERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA-ELDENAIRALKHTi 311
|
330 340
....*....|....*....|....*....
gi 522138377 528 --NLTGYKMPKYITFLPELPKSNVGKVLR 554
Cdd:cd17635 312 rrELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
212-558 |
7.00e-33 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 131.84 E-value: 7.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 PDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQV---SAWigpfldEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVL 288
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAIlnsTEW------KTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 289 ITNprdmAAFCVE----LKRSGFTAITGVNT------LFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGV 358
Cdd:cd05908 179 MPT----RLFIRRpilwLKKASEHKATIVSSpnfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 359 -GLTEG-----YGLTECSPVVSFSPLSVPQWNGTI---------------------------GVPLPSTLVSLRDEEENE 405
Cdd:cd05908 255 yGLKRNailpvYGLAEASVGASLPKAQSPFKTITLgrrhvthgepepevdkkdsecltfvevGKPIDETDIRICDEDNKI 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 406 VPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAvFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQH 485
Cdd:cd05908 335 LPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEEL 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 486 PGVL--EVACIGVPDEKS-GEVPKVFVVKKDpalTEAELRAYC-----HENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd05908 414 EGVElgRVVACGVNNSNTrNEEIFCFIEHRK---SEDDFYPLGkkikkHLNKRGGWQINEVLPIRRIPKTTSGKVKRYEL 490
|
.
gi 522138377 558 R 558
Cdd:cd05908 491 A 491
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
102-557 |
9.56e-32 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 128.97 E-value: 9.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 102 LRAGLVVVNVNPLYTprELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDLAPF----------PKRAIV 171
Cdd:PRK05857 42 LRYRELVAEVGGLAA--DLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAaierfcqitdPAAALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 172 N-------FVVKRVKKMVPAWSLPGTTGFRAALAKG-RAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQ 243
Cdd:PRK05857 120 ApgskmasSAVPEALHSIPVIAVDIAAVTRESEHSLdAASLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVPD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 244 QVSA----WIgPFLDegKEVIITALPLYHIFAL--VVNCLLflrHGcrNVLITNPRDMAAFCVELKRSGFTAITGVNTLF 317
Cdd:PRK05857 200 ILQKeglnWV-TWVV--GETTYSPLPATHIGGLwwILTCLM---HG--GLCVTGGENTTSLLEILTTNAVATTCLVPTLL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 318 NGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAeKWQKVTGVGLTEGYGLTE------CSPVVSFSPLSVPQwnGTIGVPL 391
Cdd:PRK05857 272 SKLVSELKSANATVPSLRLVGYGGSRAIAADV-RFIEATGVRTAQVYGLSEtgctalCLPTDDGSIVKIEA--GAVGRPY 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 392 PSTLVSLRDEE--ENEVPPGQP----GELCVKGPQVMQGYWQKPEESAKVFTkDGWLKTGDVAVFEPNGYLRIVDRKKDM 465
Cdd:PRK05857 349 PGVDVYLAATDgiGPTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERREDGFFYIKGRSSEM 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 466 ILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKdPALTEAELRAYCHENLTGYK-------MPKYI 538
Cdd:PRK05857 428 IICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVAS-AELDESAARALKHTIAARFRresepmaRPSTI 506
|
490
....*....|....*....
gi 522138377 539 TFLPELPKSNVGKVLRKEL 557
Cdd:PRK05857 507 VIVTDIPRTQSGKVMRASL 525
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
56-559 |
9.63e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 128.58 E-value: 9.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAELDRLTQDFASYLqNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIV 135
Cdd:PRK13383 61 LSYRELQRATESLARRL-TRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVAD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 136 ENFcttLQQVIANTPIQHVITtqigdlapfpkraivnfvvkrvkkmvpawslPGTTGFRAALAKGRAQPYARVQLgpddi 215
Cdd:PRK13383 140 NEF---AERIAGADDAVAVID-------------------------------PATAGAEESGGRPAVAAPGRIVL----- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 216 aflqYTGGTTGLSKGavlthgnvTANVQQVSAWIG---PFLDEGK----EVIITALPLYHIFALVVNCLLFLRHGcrNVL 288
Cdd:PRK13383 181 ----LTSGTTGKPKG--------VPRAPQLRSAVGvwvTILDRTRlrtgSRISVAMPMFHGLGLGMLMLTIALGG--TVL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 289 ITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPG--FAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGL 366
Cdd:PRK13383 247 THRHFDAEAALAQASLHRADAFTAVPVVLARILELPPrvRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 367 TECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYwqkpEESAKVFTKDGWLKTGD 446
Cdd:PRK13383 327 TEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY----TDGGGKAVVDGMTSTGD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 447 VAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-KKDPALTEAELRAYC 525
Cdd:PRK13383 403 MGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVlHPGSGVDAAQLRDYL 482
|
490 500 510
....*....|....*....|....*....|....
gi 522138377 526 HENLTGYKMPKYITFLPELPKSNVGKVLRKELRG 559
Cdd:PRK13383 483 KDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
35-557 |
1.10e-31 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 127.94 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 35 MFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPL 114
Cdd:cd17644 5 LFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQS-LGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 115 YTPRELEHQLRDSGAKaivivenfcttlqqviantpiqhVITTQigdlapfpkraivnfvvkrvkkmvpawslpgttgfr 194
Cdd:cd17644 84 YPQERLTYILEDAQIS-----------------------VLLTQ------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 195 aalakgraqpyarvqlgPDDIAFLQYTGGTTGLSKGAVLTHG---NVTANVQQV-----SAWIGPFLDEGKEVIITALpl 266
Cdd:cd17644 105 -----------------PENLAYVIYTSGSTGKPKGVMIEHQslvNLSHGLIKEygitsSDRVLQFASIAFDVAAEEI-- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 267 yhIFALVVNCLLFLRhgcRNVLITNPRDMAAFCVELKRSGFTAITG-----VNTLFNGLLHAPgfaeldfSRFKLAVGGG 341
Cdd:cd17644 166 --YVTLLSGATLVLR---PEEMRSSLEDFVQYIQQWQLTVLSLPPAywhllVLELLLSTIDLP-------SSLRLVIVGG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 342 TAVQQAVAEKWQKVTG--VGLTEGYGLTECSPVVSFSPLSVPQWNG----TIGVPLPSTLVSLRDEEENEVPPGQPGELC 415
Cdd:cd17644 234 EAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvPIGRPIANTQVYILDENLQPVPVGVPGELH 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 416 VKGPQVMQGYWQKPEESAKVFTKDGWL--------KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPG 487
Cdd:cd17644 314 IGGVGLARGYLNRPELTAEKFISHPFNsseserlyKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHND 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522138377 488 VLEVACIGVPDEKSGEVPKVFVV-KKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd17644 394 VKTAVVIVREDQPGNKRLVAYIVpHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
52-558 |
3.01e-31 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 128.06 E-value: 3.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 52 MGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKA 131
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKS-LGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 132 IVivenfcTTLQQVIANTPIQHvitTQIGDLA----PFPKRAIVnfvVKRVKKMVPaWSlPGTTGFRAALAKGRAQPYAR 207
Cdd:cd05966 160 VI------TADGGYRGGKVIPL---KEIVDEAlekcPSVEKVLV---VKRTGGEVP-MT-EGRDLWWHDLMAKQSPECEP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 208 VQLGPDDIAFLQYTGGTTGLSKGAV-----------LTHGNV-----------TANVqqvsAWI--------GPFLDEGK 257
Cdd:cd05966 226 EWMDSEDPLFILYTSGSTGKPKGVVhttggyllyaaTTFKYVfdyhpddiywcTADI----GWItghsyivyGPLANGAT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 258 EVIITALPLY---HIFALVVNcllflRHGCrNVLITNPrdmaafcvelkrsgfTAITgvntlfngLLHAPGFAELD-FSR 333
Cdd:cd05966 302 TVMFEGTPTYpdpGRYWDIVE-----KHKV-TIFYTAP---------------TAIR--------ALMKFGDEWVKkHDL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 334 FKLAVGGgtAVQQAVA-EKWQ---KVTGVGltegygltECsPVVS-----------FSPL--SVPQWNGTIGVPLPSTLV 396
Cdd:cd05966 353 SSLRVLG--SVGEPINpEAWMwyyEVIGKE--------RC-PIVDtwwqtetggimITPLpgATPLKPGSATRPFFGIEP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 397 SLRDEEENEVPPGQPGELCVKG--PQVMQGYWQKPEESAKVFTKD--GWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFN 472
Cdd:cd05966 422 AILDEEGNEVEGEVEGYLVIKRpwPGMARTIYGDHERYEDTYFSKfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHR 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 473 VYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKD----PALTEAELRAYCHENLTGYKMPKYITFLPELPKSN 548
Cdd:cd05966 502 LGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDgeepSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTR 581
|
570
....*....|
gi 522138377 549 VGKVLRKELR 558
Cdd:cd05966 582 SGKIMRRILR 591
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
54-450 |
3.15e-31 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 128.07 E-value: 3.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYT-----PRELEHQLR--- 125
Cdd:PRK08180 68 RRLTYAEALERVRAIAQALLD-RGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSlvsqdFGKLRHVLEllt 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 126 ------DSG---AKAIVIVENFCTTlqqVIANTPIQhvittqigdlapfPKRAIVNFVvkrvkkmvpawSLPGTTGFRAA 196
Cdd:PRK08180 147 pglvfaDDGaafARALAAVVPADVE---VVAVRGAV-------------PGRAATPFA-----------ALLATPPTAAV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 197 LAKgraqpYARVqlGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQV-SAWigPFLDEGKEVIITALPLYHIFALVVN 275
Cdd:PRK08180 200 DAA-----HAAV--GPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLaQTF--PFLAEEPPVLVDWLPWNHTFGGNHN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 276 CLLFLRHG------------------CRNVlitnpRDMAAfcvelkrsgfTAITGVNTLFNGLLHA----PGFAELDFSR 333
Cdd:PRK08180 271 LGIVLYNGgtlyiddgkptpggfdetLRNL-----REISP----------TVYFNVPKGWEMLVPAlerdAALRRRFFSR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 334 FKLAVGGGTAVQQAVAEKWQKVTG------VGLTEGYGLTECSPVVSFS--PLSVPqwnGTIGVPLPSTLVSLrdeeene 405
Cdd:PRK08180 336 LKLLFYAGAALSQDVWDRLDRVAEatcgerIRMMTGLGMTETAPSATFTtgPLSRA---GNIGLPAPGCEVKL------- 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 522138377 406 VPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVF 450
Cdd:PRK08180 406 VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRF 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-557 |
9.38e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 128.54 E-value: 9.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 35 MFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPL 114
Cdd:PRK12316 3062 LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIE-RGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPE 3140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 115 YTPRELEHQLRDSGAKaivivenfcttlqqviantpiqhVITTQigdlapfpkraivnfvvkrvkkmvPAWSLPGTTGFR 194
Cdd:PRK12316 3141 YPEERLAYMLEDSGAQ-----------------------LLLSQ------------------------SHLRLPLAQGVQ 3173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 195 AALAKGRAQPYAR----VQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQqvsaWIGPFLDEGKEVIITALPLYHIF 270
Cdd:PRK12316 3174 VLDLDRGDENYAEanpaIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLC----WMQQAYGLGVGDRVLQFTTFSFD 3249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 271 ALVVNCLLFLRHGCRNVL--ITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAelDFSRFKLAVGGGTAVQQAV 348
Cdd:PRK12316 3250 VFVEELFWPLMSGARVVLagPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAH--RCTSLKRIVCGGEALPADL 3327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 349 AEKWqkVTGVGLTEGYGLTECSPVVSFSPLSVPQWNGT-IGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQ 427
Cdd:PRK12316 3328 QQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAVpIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHN 3405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 428 KPEESAKVFTKDGW------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVpdekS 501
Cdd:PRK12316 3406 RPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV----D 3481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 522138377 502 GEVPKVFVVKKDP--ALTEAeLRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK12316 3482 GRQLVAYVVPEDEagDLREA-LKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
56-558 |
1.06e-30 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 124.60 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAELDRLTQDFASYLQNVlGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLrDSGAKAIVIV 135
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSI-GVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRV-DRGGAVYAAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 136 EnfcttlQQVIANTPIqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqpyarvqlgpddi 215
Cdd:cd05974 79 D------ENTHADDPM---------------------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 216 aFLQYTGGTTglSKGAVLTHGNVTANVQQVSA--WIGpfLDEGKEVIITALPLYHIFALvvNCLLF-LRHGCRNVLITNP 292
Cdd:cd05974 89 -LLYFTSGTT--SKPKLVEHTHRSYPVGHLSTmyWIG--LKPGDVHWNISSPGWAKHAW--SCFFApWNAGATVFLFNYA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 293 R-DMAAFCVELKRSGFTAITGVNTLFNGLLHApgfaelDFSRFKLA----VGGGTAVQQAVAEKWQKVTGVGLTEGYGLT 367
Cdd:cd05974 162 RfDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ------DLASFDVKlrevVGAGEPLNPEVIEQVRRAWGLTIRDGYGQT 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 368 ECSPVVSFSPlSVPQWNGTIGVPLPSTLVSLRDEEENevpPGQPGELCV-----KGPQVMQGYWQKPEESAKVFtKDGWL 442
Cdd:cd05974 236 ETTALVGNSP-GQPVKAGSMGRPLPGYRVALLDPDGA---PATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 443 KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-----KKDPAlT 517
Cdd:cd05974 311 RTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragyEPSPE-T 389
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 522138377 518 EAELRAYCHENLTGYKMPKYITFLpELPKSNVGKVLRKELR 558
Cdd:cd05974 390 ALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELR 429
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
30-463 |
2.75e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 125.86 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 30 PSLVAMFEQSCARFGDQ--IAY---ECMG----------------------QTLSFAELDRLTQDFASYLQNvLGLQRGD 82
Cdd:PTZ00216 69 PNFLQRLERICKERGDRraLAYrpvERVEkevvkdadgkertmevthfnetRYITYAELWERIVNFGRGLAE-LGLTKGS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 83 RVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIQHVITTQIGDL 162
Cdd:PTZ00216 148 NVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLLRLMKSGGMPNTTIIYLDSL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 163 APfpkraivnfVVKRVKKMVPAWSlpgttgfrAALAKGRAQPYARVQLGP---DDIAFLQYTGGTTGLSKGAVLTHGNVT 239
Cdd:PTZ00216 228 PA---------SVDTEGCRLVAWT--------DVVAKGHSAGSHHPLNIPennDDLALIMYTSGTTGDPKGVMHTHGSLT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 240 ANV----QQVSAWIGPFldEGKEVIITALPLYHIFAL-VVNCLLFlrhgcRNVLIT--NPR-----------DMAAF--- 298
Cdd:PTZ00216 291 AGIlaleDRLNDLIGPP--EEDETYCSYLPLAHIMEFgVTNIFLA-----RGALIGfgSPRtltdtfarphgDLTEFrpv 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 299 --------------CVE--------LKRSGFtaitgvNTLFNGLLHA-------PGFAELDFSRFKLAVGG-------GT 342
Cdd:PTZ00216 364 fligvprifdtikkAVEaklppvgsLKRRVF------DHAYQSRLRAlkegkdtPYWNEKVFSAPRAVLGGrvramlsGG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 343 AVQQAVAEKWQKVTGVGLTEGYGLTE---CSPVVSFSPLSVpqwnGTIGVPLPSTLVSLRDEEE---NEVPpgQP-GELC 415
Cdd:PTZ00216 438 GPLSAATQEFVNVVFGMVIQGWGLTEtvcCGGIQRTGDLEP----NAVGQLLKGVEMKLLDTEEykhTDTP--EPrGEIL 511
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 522138377 416 VKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKK 463
Cdd:PTZ00216 512 LRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
79-551 |
7.92e-30 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 124.44 E-value: 7.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 79 QRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNplYTprelehqlrdSGAKAivivenfcttLQQVIANTPIQHVITT- 157
Cdd:PRK08043 253 VEGERIGLMLPNATISAAVIFGASLRRRIPAMMN--YT----------AGVKG----------LTSAITAAEIKTIFTSr 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 158 ---QIGDLAPFPKRAI-VNFV--------VKRVKKMVPAWSLpgttgfraaLAKGRAQpyarVQLGPDDIAFLQYTGGTT 225
Cdd:PRK08043 311 qflDKGKLWHLPEQLTqVRWVyledlkddVTTADKLWIFAHL---------LMPRLAQ----VKQQPEDAALILFTSGSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 226 GLSKGAVLTHGNVTANVQQVSAwIGPFLDEGKevIITALPLYHIFALVVNCLLFLRHGCRNVLITNPRDMAAFCVELKRS 305
Cdd:PRK08043 378 GHPKGVVHSHKSLLANVEQIKT-IADFTPNDR--FMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDR 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 306 GFTAITGVNTLfngLLHAPGFAE-LDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSfspLSVPQW- 383
Cdd:PRK08043 455 NCTVLFGTSTF---LGNYARFANpYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVS---INVPMAa 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 384 -NGTIGVPLP---STLVSLrdeeenevpPG--QPGELCVKGPQVMQGYW--QKP-------EESAKVFTKDGWLKTGDVA 448
Cdd:PRK08043 529 kPGTVGRILPgmdARLLSV---------PGieQGGRLQLKGPNIMNGYLrvEKPgvlevptAENARGEMERGWYDTGDIV 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 449 VFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVkkDPALTEAELRAYCHEN 528
Cdd:PRK08043 600 RFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT--DSELTREKLQQYAREH 677
|
490 500
....*....|....*....|....
gi 522138377 529 -LTGYKMPKYITFLPELPKSNVGK 551
Cdd:PRK08043 678 gVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
25-557 |
1.65e-29 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 124.00 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 25 DTG-AVPS--LVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGV 101
Cdd:PRK10252 450 ATAvEIPEttLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRE-RGVKPGDSVAVALPRSVFLTLALHAI 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 102 LRAGLVVVNVNPLYTPRELEHQLRDSGAKAivivenfcttlqqviantpiqhVITTQiGDLAPFPkraivnfvvkrvkkm 181
Cdd:PRK10252 529 VEAGAAWLPLDTGYPDDRLKMMLEDARPSL----------------------LITTA-DQLPRFA--------------- 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 182 vpawSLPGTT--GFRAALAKGRAQPYARVQlgPDDIAFLQYTGGTTGLSKGAVLTHgnvTANVQQ--------------- 244
Cdd:PRK10252 571 ----DVPDLTslCYNAPLAPQGAAPLQLSQ--PHHTAYIIFTSGSTGRPKGVMVGQ---TAIVNRllwmqnhypltaddv 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 245 ----------VSAW--IGPFLDEGKEVIitALPLYH--IFALVVnclLFLRHGcrnvlITN----PRDMAAFCVELkrsg 306
Cdd:PRK10252 642 vlqktpcsfdVSVWefFWPFIAGAKLVM--AEPEAHrdPLAMQQ---FFAEYG-----VTTthfvPSMLAAFVASL---- 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 307 ftaitgvntlfngllhAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSPVVSFSP--------- 377
Cdd:PRK10252 708 ----------------TPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPafgeelaav 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 378 --LSVPqwngtIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWL------KTGDVAV 449
Cdd:PRK10252 772 rgSSVP-----IGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVAR 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 450 FEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEV---ACIGVPDEKSGEVPKVFV----VKKDPALTEAELR 522
Cdd:PRK10252 847 WLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthACVINQAAATGGDARQLVgylvSQSGLPLDTSALQ 926
|
570 580 590
....*....|....*....|....*....|....*
gi 522138377 523 AYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK10252 927 AQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
31-557 |
1.85e-29 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 124.51 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 31 SLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQnVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVN 110
Cdd:PRK05691 3721 SYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALR-AAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLP 3799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 111 VNPLYTPRELEHQLRDSGAKAIVivenfCTTLQQVIANTPiqhvittqigdLAPFPkraivnfVVKRVKKMVpaWSlpgt 190
Cdd:PRK05691 3800 LDPGLPAQRLQRIIELSRTPVLV-----CSAACREQARAL-----------LDELG-------CANRPRLLV--WE---- 3850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 191 tgfrAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANvqQVSAWIGPFLDEGKEVIITALPLYHIF 270
Cdd:PRK05691 3851 ----EVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNN--QLSKVPYLALSEADVIAQTASQSFDIS 3924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 271 alVVNCLLFLRHGCRNVLITN--PRDMAAFCVELKRSGFTAITGVNTLFNGLLhAPGFAELDFSRFKLAVGggTAVQQAV 348
Cdd:PRK05691 3925 --VWQFLAAPLFGARVEIVPNaiAHDPQGLLAHVQAQGITVLESVPSLIQGML-AEDRQALDGLRWMLPTG--EAMPPEL 3999
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 349 AEKW-QKVTGVGLTEGYGLTECSPVVSFSPLSVPQWNGT---IGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQG 424
Cdd:PRK05691 4000 ARQWlQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRG 4079
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 425 YWQKPEESAKVFTKDGW-------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVAcIGVP 497
Cdd:PRK05691 4080 YVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQ 4158
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522138377 498 DEKSGEVPKVFVVKKDPALTEAELRAYCHENLTG----YKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK05691 4159 EGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAelpdYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
55-450 |
2.86e-29 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 121.77 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 55 TLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEH----QLRDSGAK 130
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLD-LGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLaklkHLFELLKP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 131 AIVIVENfCTTLQQVIANTPIQHviTTQIGDLAPFPKRAIVNFVvkrvkkmvpawSLPGTTGfRAALAKgraqpyARVQL 210
Cdd:cd05921 104 GLVFAQD-AAPFARALAAIFPLG--TPLVVSRNAVAGRGAISFA-----------ELAATPP-TAAVDA------AFAAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 211 GPDDIAFLQYTGGTTGLSKGAVLTHGNVTANvQQVSAWIGPFLDEGKEVIITALPLYHIFALVVNCLLFLRHGcRNVLIT 290
Cdd:cd05921 163 GPDTVAKFLFTSGSTGLPKAVINTQRMLCAN-QAMLEQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNG-GTLYID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 291 NPRDMAAFCVELKRS--------GFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKV----TG- 357
Cdd:cd05921 241 DGKPMPGGFEETLRNlreisptvYFNVPAGWEMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALavatVGe 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 358 -VGLTEGYGLTECSPVVSFS--PLSVPqwnGTIGVPLPSTLVSLrdeeeneVPPGQPGELCVKGPQVMQGYWQKPEESAK 434
Cdd:cd05921 321 rIPMMAGLGATETAPTATFThwPTERS---GLIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQPELTAQ 390
|
410
....*....|....*.
gi 522138377 435 VFTKDGWLKTGDVAVF 450
Cdd:cd05921 391 AFDEEGFYCLGDAAKL 406
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
212-551 |
7.41e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 117.87 E-value: 7.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 PDDIaFLQYTGGTTGLSKGAVLTHG----------NVTANVQQVSAWIGPFLDEGKE-VIITALPLYHIFALVVNCLLFL 280
Cdd:cd05924 3 ADDL-YILYTGGTTGMPKGVMWRQEdifrmlmggaDFGTGEFTPSEDAHKAAAAAAGtVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 281 rhGCRNVLITNPR-DMAAFCVELKRSGFTAITGVNTLFNgllhAPGFAEL------DFSRFKLAVGGGTAVQQAVAEKWQ 353
Cdd:cd05924 82 --GGQTVVLPDDRfDPEEVWRTIEKHKVTSMTIVGDAMA----RPLIDALrdagpyDLSSLFAISSGGALLSPEVKQGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 354 K-VTGVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSlrDEEENEVPPGQPGE--LCVKGpQVMQGYWQKPE 430
Cdd:cd05924 156 ElVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVVL--DDDGRVVPPGSGGVgwIARRG-HIPLGYYGDEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 431 ESAKVF-TKDG--WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSG-EVpk 506
Cdd:cd05924 233 KTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGqEV-- 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 522138377 507 VFVVKKDPA--LTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGK 551
Cdd:cd05924 311 VAVVQLREGagVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
54-557 |
1.39e-28 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 119.12 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIV 133
Cdd:cd17656 12 QKLTYRELNERSNQLARFLRE-KGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 134 IvenfCTTLQQVIANTPIQHVIttqIGDLAPFPKRAIVNFVVKRvkkmvpawslpgttgfraalakgraqpyarvqlgpD 213
Cdd:cd17656 91 T----QRHLKSKLSFNKSTILL---EDPSISQEDTSNIDYINNS-----------------------------------D 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 DIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIITALP----LYH-IFALVVN--CLLFLRHGCR- 285
Cdd:cd17656 129 DLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTN--INFSDKVLQFATCsfdvCYQeIFSTLLSggTLYIIREETKr 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 286 ------NVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHApgfaeldfsrfkLAVGGGTAVQQAVAEKWQKvTGVG 359
Cdd:cd17656 207 dveqlfDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHI------------ITAGEQLVITNEFKEMLHE-HNVH 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 360 LTEGYGLTECSPVVSFSPLSVPQWN--GTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFT 437
Cdd:cd17656 274 LHNHYGPSETHVVTTYTINPEAEIPelPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 438 KDGW------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVK 511
Cdd:cd17656 354 PDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 522138377 512 KDpALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd17656 434 EQ-ELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
202-488 |
2.19e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 118.95 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 202 AQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIITALPLYHIFALVVNCLLFLR 281
Cdd:PRK07768 141 ADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAE--FDVETDVMVSWLPLFHDMGMVGFLTVPMY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 282 HGCRNVLITnPRDMAAFCV---EL---KRSGFTAitgvntlfngllhAPGFA---------------ELDFSRFKLAVGG 340
Cdd:PRK07768 219 FGAELVKVT-PMDFLRDPLlwaELiskYRGTMTA-------------APNFAyallarrlrrqakpgAFDLSSLRFALNG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 341 GTAVQQAVAEKWQKVTG-VGLTEG-----YGLTECSPVVSFSPL-------------------SVPQWNG------TIGV 389
Cdd:PRK07768 285 AEPIDPADVEDLLDAGArFGLRPEailpaYGMAEATLAVSFSPCgaglvvdevdadllaalrrAVPATKGntrrlaTLGP 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 390 PLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWqkpEESAKVFTKD--GWLKTGDVAVFEPNGYLRIVDRKKDMIL 467
Cdd:PRK07768 365 PLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL---TMDGFIPAQDadGWLDTGDLGYLTEEGEVVVCGRVKDVII 441
|
330 340
....*....|....*....|.
gi 522138377 468 VSGFNVYPNEIEGVVAQHPGV 488
Cdd:PRK07768 442 MAGRNIYPTDIERAAARVEGV 462
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
26-557 |
2.67e-28 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 120.66 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 26 TGAVPSLVAMFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAG 105
Cdd:PRK05691 1127 APAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAG 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 106 LVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQVIANTPIqhviTTQIGDLAPFPKRAivnfvvkrvkkmvpaw 185
Cdd:PRK05691 1206 GAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAI----ALDSLHLDSWPSQA---------------- 1265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 186 slPGttgfraalakgraqpyarVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGkEVIITALP 265
Cdd:PRK05691 1266 --PG------------------LHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYA--LDDS-DVLMQKAP 1322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 266 LYhiFALVV-NCLLFLRHGCRNVLIT-----NPRDMAAFcveLKRSGFTAITGVNTLFNGLLHAPGFAELdfSRFKLAVG 339
Cdd:PRK05691 1323 IS--FDVSVwECFWPLITGCRLVLAGpgehrDPQRIAEL---VQQYGVTTLHFVPPLLQLFIDEPLAAAC--TSLRRLFS 1395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 340 GGTAVQQAVAEK-WQKVTGVGLTEGYGLTEcspvvsfSPLSVPQWN--------GTIGVPLPSTLVSLRDEEENEVPPGQ 410
Cdd:PRK05691 1396 GGEALPAELRNRvLQRLPQVQLHNRYGPTE-------TAINVTHWQcqaedgerSPIGRPLGNVLCRVLDAELNLLPPGV 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 411 PGELCVKGPQVMQGYWQKPEESAKVFTKDGW-------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVA 483
Cdd:PRK05691 1469 AGELCIGGAGLARGYLGRPALTAERFVPDPLgedgarlYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLL 1548
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522138377 484 QHPGVLEVACIGVPDEKSGEVPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK05691 1549 AQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
35-557 |
1.01e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 119.12 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 35 MFEQSCARFGDQIAYECMGQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPL 114
Cdd:PRK05691 2193 LFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRE-RGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPE 2271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 115 YTPRELEHQLRDSGakaivivenfcttlqqviantpiqhvITTQIGDLAPFPKRAIVNFVVKRvkkmvpaWSLPGTTgfr 194
Cdd:PRK05691 2272 YPLERLHYMIEDSG--------------------------IGLLLSDRALFEALGELPAGVAR-------WCLEDDA--- 2315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 195 AALAKGRAQPYARVQLgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEGKeviitaLPLYHI-FALV 273
Cdd:PRK05691 2316 AALAAYSDAPLPFLSL-PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCE------LHFYSInFDAA 2388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 274 VNCLLF-LRHGCRNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVqqaVAEKW 352
Cdd:PRK05691 2389 SERLLVpLLCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEAL---TGEHL 2465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 353 QKVTGV----GLTEGYGLTE--CSPVVSFSPLSVPQwnGTIGVPLPStLVSLR-----DEEENEVPPGQPGELCVKGPQV 421
Cdd:PRK05691 2466 QRIRQAfapqLFFNAYGPTEtvVMPLACLAPEQLEE--GAASVPIGR-VVGARvayilDADLALVPQGATGELYVGGAGL 2542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 422 MQGYWQKPEESAKVFTKD------GWL-KTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACI 494
Cdd:PRK05691 2543 AQGYHDRPGLTAERFVADpfaadgGRLyRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVL 2622
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 495 GVpDEKSGEVPKVFVVKKDPALTEAE-------LRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK05691 2623 AL-DTPSGKQLAGYLVSAVAGQDDEAqaalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
213-558 |
4.42e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 112.45 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfldeGKEVIITALPLYHIFALVVncllFLRH---GCRNVLI 289
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-----GPGQWLLALPAHHIAGLQV----LVRSviaGSEPVEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 290 T-----NPRDMAAFCVELK--RSgFTAITGVNtLFNGLLHAPGFAELdfSRFKLAVGGGTAVQQAVAEKwQKVTGVGLTE 362
Cdd:PRK07824 106 DvsagfDPTALPRAVAELGggRR-YTSLVPMQ-LAKALDDPAATAAL--AELDAVLVGGGPAPAPVLDA-AAAAGINVVR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 363 GYGLTECSpvvsfsplsvpqwNGTI--GVPLPSTLVSLRDeeenevppgqpGELCVKGPQVMQGYWQKPEESAkvFTKDG 440
Cdd:PRK07824 181 TYGMSETS-------------GGCVydGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVDPDP--FAEPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 441 WLKTGDVAVFEpNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGE-VPKVFVVKKDPALTEA 519
Cdd:PRK07824 235 WFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQrVVAAVVGDGGPAPTLE 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 522138377 520 ELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK07824 314 ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
54-495 |
5.14e-27 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 115.21 E-value: 5.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLlqyPVSLFGVLRAGLVVVNVNPLYT---PRELEHQLRDSGAK 130
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLA-LGVGRGDVVAILGDNR---PEWVWAELAAQAIGALSLGIYQdsmAEEVAYLLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 131 AIVivenfCTTLQQViantpiQHVITtqIGDLAPFpkraiVNFVVKRVKKMVPAWSLPGTTGFRAALAKGRAQPYARVQL 210
Cdd:cd17641 86 VVI-----AEDEEQV------DKLLE--IADRIPS-----VRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRDPGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 211 G--------PDDIAFLQYTGGTTGLSKGAVLTHGNV---TANVQQVS--------------AWIGPFldegkeVIITALP 265
Cdd:cd17641 148 YerevaagkGEDVAVLCTTSGTTGKPKLAMLSHGNFlghCAAYLAADplgpgdeyvsvlplPWIGEQ------MYSVGQA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 266 LYHIFAlvVNC-------LLFLRHGCRNVLITNPR---DMAAF-------CVELKRSGFTAITGV-----NTLFNG---- 319
Cdd:cd17641 222 LVCGFI--VNFpeepetmMEDLREIGPTFVLLPPRvweGIAADvrarmmdATPFKRFMFELGMKLglralDRGKRGrpvs 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 320 --LLHAPGFAE----------LDFSRFKLAVGGGTAVQQAVAEKWQKVtGVGLTEGYGLTEcspvvsFSPLSVPQWNG-- 385
Cdd:cd17641 300 lwLRLASWLADallfrplrdrLGFSRLRSAATGGAALGPDTFRFFHAI-GVPLKQLYGQTE------LAGAYTVHRDGdv 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 386 ---TIGVPLPSTLVSLrDEEenevppgqpGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRK 462
Cdd:cd17641 373 dpdTVGVPFPGTEVRI-DEV---------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRA 442
|
490 500 510
....*....|....*....|....*....|....
gi 522138377 463 KD-MILVSGFNVYPNEIEGVVAQHPGVLEVACIG 495
Cdd:cd17641 443 KDvGTTSDGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
176-491 |
1.72e-26 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 114.14 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 176 KRVKKMVPAWSLPGTTGFRAA------------LAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQ 243
Cdd:PLN02430 171 KRLKAIVSFTSVTEEESDKASqigvktyswidfLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 244 QVSAWIGPFLDE--GKEVIITALPLYHIFALVVNCLLFLR-------HGCRNVLitnpRDMaafCVELKRSGFTAITGV- 313
Cdd:PLN02430 251 GVDLFMEQFEDKmtHDDVYLSFLPLAHILDRMIEEYFFRKgasvgyyHGDLNAL----RDD---LMELKPTLLAGVPRVf 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 314 ----------------------NTLFN--------GLLH--APGFAE-LDF--------SRFKLAVGGGTAVQQAVaEKW 352
Cdd:PLN02430 324 erihegiqkalqelnprrrlifNALYKyklawmnrGYSHkkASPMADfLAFrkvkaklgGRLRLLISGGAPLSTEI-EEF 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 353 QKVTGVG-LTEGYGLTE-CSPVVSFSPLSVPQWnGTIGVPlpSTLVSLRDEEENEV---PPGQP--GELCVKGPQVMQGY 425
Cdd:PLN02430 403 LRVTSCAfVVQGYGLTEtLGPTTLGFPDEMCML-GTVGAP--AVYNELRLEEVPEMgydPLGEPprGEICVRGKCLFSGY 479
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522138377 426 WQKPEESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVS-GFNVYPNEIEGVVAQHPGVLEV 491
Cdd:PLN02430 480 YKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEYLENVYGQNPIVEDI 545
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
45-552 |
2.40e-26 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 112.11 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQL 124
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 125 RDSGAKAivivenfcttlqqviantpiqhVITTqigdlapfpkraivnfvvkrvkkmvpawslpgttgfraalakgraqp 204
Cdd:cd17648 82 EDTGARV----------------------VITN----------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 205 yarvqlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpFLDEGKEVIITaLPLYHIFALVVNCLLFLRHGc 284
Cdd:cd17648 93 -------STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYF-GRDNGDEAVLF-FSNYVFDFFVEQMTLALLNG- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 285 rNVLITNPRDMA----AFCVELKRSGFTAITGVNTLFNgllhapgfaELDFSR---FKLAVGGGTAVQQAVAEKWQKVTG 357
Cdd:cd17648 163 -QKLVVPPDEMRfdpdRFYAYINREKVTYLSGTPSVLQ---------QYDLARlphLKRVDAAGEEFTAPVFEKLRSRFA 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 358 VGLTEGYGLTECS--PVVSFSPlSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKV 435
Cdd:cd17648 233 GLIINAYGPTETTvtNHKRFFP-GDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAER 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 436 FTKDGW--------------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKS 501
Cdd:cd17648 312 FLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQ 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 522138377 502 GEVPKV-----FVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKV 552
Cdd:cd17648 392 AQSRIQkylvgYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
53-558 |
3.40e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 112.47 E-value: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLytpRELEHQLRDsgakai 132
Cdd:PRK07867 26 DSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPT---RRGAALARD------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 vivenfcttlqqvIANTPIQHVITtqigDLAPFPKRAIVNFVVKRVKKMVPAWSlpgttgfrAALAKGRAQPYARVQLGP 212
Cdd:PRK07867 97 -------------IAHADCQLVLT----ESAHAELLDGLDPGVRVINVDSPAWA--------DELAAHRDAEPPFRVADP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEgkeVIITALPLYHIFALVVNCLLFLRHGCRNVLitnP 292
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDD---VCYVSMPLFHSNAVMAGWAVALAAGASIAL---R 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 293 RDMAA--FCVELKRSGFTAITGVNTLFNGLLHAPgfAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECS 370
Cdd:PRK07867 226 RKFSAsgFLPDVRRYGATYANYVGKPLSYVLATP--ERPDDADNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTEGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 371 PVVSFSPLSVPqwnGTIGvPLPSTLVSLRDEEENEVPPGQP------------GELC-VKGPQVMQGYWQKPEESAKVFt 437
Cdd:PRK07867 304 VAITRTPDTPP---GALG-PLPPGVAIVDPDTGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERM- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 438 KDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSG-EVPKVFVVKKDPAL 516
Cdd:PRK07867 379 RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGdQVMAALVLAPGAKF 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 522138377 517 TEAELRAYCHE--NLtGYKM-PKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK07867 459 DPDAFAEFLAAqpDL-GPKQwPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
31-520 |
6.75e-26 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 112.14 E-value: 6.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 31 SLVAMFEQSCARFGDQIAYECM-------GQT--LSFAELDRLTQDFASYLQNVLglQRGDRVALMMPNLLQYPVSLFGV 101
Cdd:PRK12476 35 TLISLIERNIANVGDTVAYRYLdhshsaaGCAveLTWTQLGVRLRAVGARLQQVA--GPGDRVAILAPQGIDYVAGFFAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 102 LRAGLVVVnvnPLYTPRELEHQLRdsgakaivivenfcttLQQVIANTPIQHVITTQIGdlapfpKRAIVNFVVKRVK-- 179
Cdd:PRK12476 113 IKAGTIAV---PLFAPELPGHAER----------------LDTALRDAEPTVVLTTTAA------AEAVEGFLRNLPRlr 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 180 --KMVPAWSLPGTTGfraalakgraQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpFLDEGK 257
Cdd:PRK12476 168 rpRVIAIDAIPDSAG----------ESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSID-LLDRNT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 258 EVIiTALPLYHIFALVVncLLF-LRHGCRNVLItnprDMAAFcveLKRSG--FTAITGVNTLFNGLLHAPGFA------- 327
Cdd:PRK12476 237 HGV-SWLPLYHDMGLSM--IGFpAVYGGHSTLM----SPTAF---VRRPQrwIKALSEGSRTGRVVTAAPNFAyewaaqr 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 328 -------ELDFSRFKLAVGGgTAVQQAVAEKWQKVTG-VGLTE-----GYGLTECS------------------------ 370
Cdd:PRK12476 307 glpaegdDIDLSNVVLIIGS-EPVSIDAVTTFNKAFApYGLPRtafkpSYGIAEATlfvatiapdaepsvvyldreqlga 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 371 ----PVVSFSPLSVPQWN-GTIGVPLPSTLVSlrDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVF--------- 436
Cdd:PRK12476 386 gravRVAADAPNAVAHVScGQVARSQWAVIVD--PDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrla 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 437 -------TKDG--WLKTGDVAVFEpNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQ-HPGVLE--VACIGVPDEKSGEV 504
Cdd:PRK12476 464 egshadgAADDgtWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMVRRgyVTAFTVPAEDNERL 542
|
570
....*....|....*.
gi 522138377 505 pkVFVVKKDPALTEAE 520
Cdd:PRK12476 543 --VIVAERAAGTSRAD 556
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
53-538 |
1.00e-25 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 110.84 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIVENFCTTLQQViantpiqhvittqigdLAPFPKRAIVNFVvkrvkkMVPAWSLPGTTGFRAALAKGRAQP---YARVQ 209
Cdd:cd05938 83 VVAPELQEAVEEV----------------LPALRADGVSVWY------LSHTSNTEGVISLLDKVDAASDEPvpaSLRAH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 210 LGPDDIAFLQYTGGTTGLSKGAVLTHGNVTA--NVQQVSawiGPFLDegkEVIITALPLYHIFALVVNCllflrHGCRNV 287
Cdd:cd05938 141 VTIKSPALYIYTSGTTGLPKAARISHLRVLQcsGFLSLC---GVTAD---DVIYITLPLYHSSGFLLGI-----GGCIEL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 288 LIT---NPRDMAA-FCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGtaVQQAVAEKWQKVTG-VGLTE 362
Cdd:cd05938 210 GATcvlKPKFSASqFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNG--LRADVWREFLRRFGpIRIRE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 363 GYGLTECSpvVSFSplsvpQWNGTIGVP----------LPSTLVS--------LRDEEEN--EVPPGQPGELCVKGPQV- 421
Cdd:cd05938 288 FYGSTEGN--IGFF-----NYTGKIGAVgrvsylykllFPFELIKfdvekeepVRDAQGFciPVAKGEPGLLVAKITQQs 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 422 -MQGYWQKPEESAK-----VFTK-DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACI 494
Cdd:cd05938 361 pFLGYAGDKEQTEKkllrdVFKKgDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVY 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 522138377 495 GVPDE-KSGEVPKVFVVKKDPALTEAElRAYCH--ENLTGYKMPKYI 538
Cdd:cd05938 441 GVTVPgHEGRIGMAAVKLKPGHEFDGK-KLYQHvrEYLPAYARPRFL 486
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
218-557 |
1.44e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 108.97 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 218 LQYTGGTTGLSKgavlTHGNVTANVQ-QVSAWIGPFLDEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLIT--NPRD 294
Cdd:PRK08308 106 LQYSSGTTGEPK----LIRRSWTEIDrEIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITnkNPKF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 295 MAAfcvELKRSGFTAITGVNTLfnglLHAPG-FAELDFsRFKLAVGGGTAVQQAVAEKWQKVTGVgLTEGYGLTE--Csp 371
Cdd:PRK08308 182 ALN---ILRNTPQHILYAVPLM----LHILGrLLPGTF-QFHAVMTSGTPLPEAWFYKLRERTTY-MMQQYGCSEagC-- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 372 vVSFSP-LSVPqwnGTIGVPLPSTLVSLRDEEEnevppgQPGELCVKgpqvmqgywqkpeesakvfTKDGWLKTGDVAVF 450
Cdd:PRK08308 251 -VSICPdMKSH---LDLGNPLPHVSVSAGSDEN------APEEIVVK-------------------MGDKEIFTKDLGYK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 451 EPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVkKDPALTEAELRAYCHENLT 530
Cdd:PRK08308 302 SERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI-SHEEIDPVQLREWCIQHLA 380
|
330 340
....*....|....*....|....*..
gi 522138377 531 GYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:PRK08308 381 PYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
68-558 |
1.49e-25 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 110.21 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 68 FASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIVENFCTTLQQV-- 145
Cdd:cd05915 37 LMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIrg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 146 ----IANTPIQHVITTQIGDLAPfpkraivnfvvkrvkkmvpawslPGTTGFRAALAKGRAQPYArvqlgpddiafLQYT 221
Cdd:cd05915 116 elktVQHFVVMDEKAPEGYLAYE-----------------------EALGEEADPVRVPERAACG-----------MAYT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 222 GGTTGLSKGAVLTHGNVTANVQQVSAwIGPFLDEGKEVIITALPLYHI-----------FALVVNCLlflrhgcRNVlit 290
Cdd:cd05915 162 TGTTGLPKGVVYSHRALVLHSLAASL-VDGTALSEKDVVLPVVPMFHVnawclpyaatlVGAKQVLP-------GPR--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 291 nPRDMAAFCVELKRSgFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQaVAEKWQKVTGVGLTEGYGlteCS 370
Cdd:cd05915 231 -LDPASLVELFDGEG-VTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPR-SLIARFERMGVEVRQGYG---LT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 371 PVVSFSP--LSVPQW-----------NGTIGVPLPSTLVSLRDEEENEVPpgQPGE----LCVKGPQVMQGYWQKPEESA 433
Cdd:cd05915 305 ETSPVVVqnFVKSHLeslseeekltlKAKTGLPIPLVRLRVADEEGRPVP--KDGKalgeVQLKGPWITGGYYGNEEATR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 434 KVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKD 513
Cdd:cd05915 383 SALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRG 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 522138377 514 PALTEAELRAYCHENLTGYKM-PKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05915 463 EKPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
53-558 |
7.66e-25 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 107.90 E-value: 7.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 53 GQTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAI 132
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQA-QGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIveNFCTTLQQVIANTPiqhvittqigdlapfPKRAIVNFvvkrvkkmvpawslpgttgfraalakgraqpyarvqlgp 212
Cdd:cd05939 80 IF--NLLDPLLTQSSTEP---------------PSQDDVNF--------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTHgnvtANVQQVSAWIGPFLDEGKE-VIITALPLYHIFALVV---NCLLflrHGCrNVL 288
Cdd:cd05939 104 RDKLFYIYTSGTTGLPKAAVIVH----SRYYRIAAGAYYAFGMRPEdVVYDCLPLYHSAGGIMgvgQALL---HGS-TVV 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 289 ITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAvqqavAEKWQKVTG------VGltE 362
Cdd:cd05939 176 IRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLR-----PQIWEQFVRrfgipqIG--E 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 363 GYGLTEC-SPVVSFsplsvpqwNGTIG----VP-LPSTLVSLR----DEEENE---------VP--PGQPGELC---VKG 418
Cdd:cd05939 249 FYGATEGnSSLVNI--------DNHVGacgfNSrILPSVYPIRlikvDEDTGElirdsdglcIPcqPGEPGLLVgkiIQN 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 419 PQVMQ--GYWQKPEESAK----VFTK-DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEV 491
Cdd:cd05939 321 DPLRRfdGYVNEGATNKKiardVFKKgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDV 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522138377 492 ACIGVpdeksgEVPKV--------FVVKK---DPALTEAELRaychENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05939 401 VVYGV------EVPGVegragmaaIVDPErkvDLDRFSAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
56-450 |
9.52e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 108.59 E-value: 9.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEH----QLRDSGAKA 131
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLD-LGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHaklkHLFDLVKPR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 132 IVIVEnfcttlqqviantpiqhvittqigDLAPFPK-RAIVNFVVKRVKKMVPAWSLPGTTGFRAALAK--GRAQPYARV 208
Cdd:PRK12582 160 VVFAQ------------------------SGAPFARaLAALDLLDVTVVHVTGPGEGIASIAFADLAATppTAAVAAAIA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 209 QLGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEGKEVIITALPLYHIFALVVNCLLFLRHGcRNVL 288
Cdd:PRK12582 216 AITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGG-GTLY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 289 ITNPRDMAAFCVE----LKRSGFTAITGVNTLFNGLLHA----PGFAELDFSRFKLAVGGGTAVQQAVAEKWQKV----T 356
Cdd:PRK12582 295 IDDGKPLPGMFEEtirnLREISPTVYGNVPAGYAMLAEAmekdDALRRSFFKNLRLMAYGGATLSDDLYERMQALavrtT 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 357 G--VGLTEGYGLTECSPVvsfsPLSVpQWN----GTIGVPLPSTLVSLrdeeeneVPPGQPGELCVKGPQVMQGYWQKPE 430
Cdd:PRK12582 375 GhrIPFYTGYGATETAPT----TTGT-HWDtervGLIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPE 442
|
410 420
....*....|....*....|
gi 522138377 431 ESAKVFTKDGWLKTGDVAVF 450
Cdd:PRK12582 443 LTAAAFDEEGFYRLGDAARF 462
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
31-466 |
2.19e-24 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 107.51 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 31 SLVAMFEQSCARFGDQ--------IAYEC-------------MGQT--LSFAELDRLTQDFASYLQNvLGLQRGDRVALM 87
Cdd:PLN02387 59 TLAALFEQSCKKYSDKrllgtrklISREFetssdgrkfeklhLGEYewITYGQVFERVCNFASGLVA-LGHNKEERVAIF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 88 MPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVivenfCTT--LQQVIAntpIQHVITTqigdlapf 165
Cdd:PLN02387 138 ADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVI-----CDSkqLKKLID---ISSQLET-------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 166 pkraivnfvVKRVKKM-----VPAWSLPGTTG-----FRAALAKGRAQPYARVQLGPDDIAFLQYTGGTTGLSKGAVLTH 235
Cdd:PLN02387 202 ---------VKRVIYMddegvDSDSSLSGSSNwtvssFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTH 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 236 GNVTANVQQVSAWIgPFLdEGKEVIITALPLYHIFALVVNCLLF--------------------LRHGCR-NVLITNPRD 294
Cdd:PLN02387 273 GNIVATVAGVMTVV-PKL-GKNDVYLAYLPLAHILELAAESVMAavgaaigygspltltdtsnkIKKGTKgDASALKPTL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 295 MAAFCVELKRSGFTAITGVN-------TLFN------------GLLHAPGFAE-----LDFSRFKLAVGG-------GTA 343
Cdd:PLN02387 351 MTAVPAILDRVRDGVRKKVDakgglakKLFDiaykrrlaaiegSWFGAWGLEKllwdaLVFKKIRAVLGGrirfmlsGGA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 344 VQQAVAEKWQKVT-GVGLTEGYGLTECSPVVSFSplsvpQWN----GTIGVPLPSTLVSLRDEEENEV----PPGQPGEL 414
Cdd:PLN02387 431 PLSGDTQRFINIClGAPIGQGYGLTETCAGATFS-----EWDdtsvGRVGPPLPCCYVKLVSWEEGGYlisdKPMPRGEI 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 522138377 415 CVKGPQVMQGYWQKPEESAKVFTKDG----WLKTGDVAVFEPNGYLRIVDRKKDMI 466
Cdd:PLN02387 506 VIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIV 561
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
332-558 |
5.70e-24 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 104.69 E-value: 5.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 332 SRFKLA-VGGGTA----VQQAvaekwqKVTGVGLTEGYGLTE-CSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRdeeene 405
Cdd:PRK07445 230 AQFRTIlLGGAPAwpslLEQA------RQLQLRLAPTYGMTEtASQIATLKPDDFLAGNNSSGQVLPHAQITIP------ 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 406 vpPGQPGELCVKGPQVMQGYWQKPEESAKVFTkdgwlkTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQH 485
Cdd:PRK07445 298 --ANQTGNITIQAQSLALGYYPQILDSQGIFE------TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522138377 486 PGVLEVACIGVPDEKSGEVPKVFVVKKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK07445 370 GLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
81-500 |
1.87e-23 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 104.13 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 81 GDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVivenfctTLQQVIantpiQHVITTQiG 160
Cdd:PRK06334 67 DQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVL-------TSKQLM-----QHLAQTH-G 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 161 DLAPFPKRAIVnfvVKRVKKMVPAW---------SLPGTTGFRAALAKGRaqpyarvqlGPDDIAFLQYTGGTTGLSKGA 231
Cdd:PRK06334 134 EDAEYPFSLIY---MEEVRKELSFWekcrigiymSIPFEWLMRWFGVSDK---------DPEDVAVILFTSGTEKLPKGV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 232 VLTHGNVTANVQQVSAWIGPFLDEgkeVIITALPLYHIFALVVNCLLFLRHGCRNVLITNPRDMAAFCVELKRSGFTAIT 311
Cdd:PRK06334 202 PLTHANLLANQRACLKFFSPKEDD---VMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 312 GVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKV-TGVGLTEGYGLTECSPVVSFSPLSVPQWNGTIGVP 390
Cdd:PRK06334 279 STPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTfPHIQLRQGYGTTECSPVITINTVNSPKHESCVGMP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 391 LPSTLVSLRDEEEN-EVPPGQPGELCVKGPQVMQGYW-QKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILV 468
Cdd:PRK06334 359 IRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKI 438
|
410 420 430
....*....|....*....|....*....|....*....
gi 522138377 469 SGFNVYPNEIEGVVAQHPGVLE-------VACiGVPDEK 500
Cdd:PRK06334 439 GAEMVSLEALESILMEGFGQNAadhagplVVC-GLPGEK 476
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
212-484 |
2.22e-23 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 104.33 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 PDDIAFLQYTGGTTGLSKGAVLTHGNV---TANVQQVSAWIGPFLDEgKEVIITALPLYHIFALVVN-CllFLRHGCR-- 285
Cdd:PLN02614 222 KSDICTIMYTSGTTGDPKGVMISNESIvtlIAGVIRLLKSANAALTV-KDVYLSYLPLAHIFDRVIEeC--FIQHGAAig 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 286 ------NVLItnpRDMAafcvELKRSGFTAITGV-NTLFNGLLH---------------------------------APG 325
Cdd:PLN02614 299 fwrgdvKLLI---EDLG----ELKPTIFCAVPRVlDRVYSGLQKklsdggflkkfvfdsafsykfgnmkkgqshveaSPL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 326 FAELDFSRFKLAVGG-------GTAVQQAVAEKWQKVTGV-GLTEGYGLTE-CSPVVSFSPLSVPQWnGTIGVPLPST-- 394
Cdd:PLN02614 372 CDKLVFNKVKQGLGGnvriilsGAAPLASHVESFLRVVACcHVLQGYGLTEsCAGTFVSLPDELDML-GTVGPPVPNVdi 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 395 -LVSLRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVFTkDGWLKTGDVAVFEPNGYLRIVDRKKDMI-LVSGFN 472
Cdd:PLN02614 451 rLESVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEY 529
|
330
....*....|..
gi 522138377 473 VYPNEIEGVVAQ 484
Cdd:PLN02614 530 VAVENIENIYGE 541
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
198-558 |
2.39e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 103.57 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 198 AKGRAQPYARVqlGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGkEVIITALPLYHIFALVVNCL 277
Cdd:PRK13388 137 AAGALTPHREV--DAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFG--LTRD-DVCYVSMPLFHSNAVMAGWA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 278 LFLRHGCRNVLitnPRDMAA--FCVELKRSGFTAITGVNTLFNGLLHAPGFAelDFSRFKLAVGGGTAVQQAVAEKWQKV 355
Cdd:PRK13388 212 PAVASGAAVAL---PAKFSAsgFLDDVRRYGATYFNYVGKPLAYILATPERP--DDADNPLRVAFGNEASPRDIAEFSRR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 356 TGVGLTEGYGLTECSPVVSFSPLSVPqwnGTIGVPLPStlVSLRDEEE-NEVPPGQ-------------PGELCVK-GPQ 420
Cdd:PRK13388 287 FGCQVEDGYGSSEGAVIVVREPGTPP---GSIGRGAPG--VAIYNPETlTECAVARfdahgallnadeaIGELVNTaGAG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 421 VMQGYWQKPEESAKVFtKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEK 500
Cdd:PRK13388 362 FFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDER 440
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522138377 501 SGEVPKVFVVKKDPA-LTEAELRAYCH--ENLtGYKM-PKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK13388 441 VGDQVMAALVLRDGAtFDPDAFAAFLAaqPDL-GTKAwPRYVRIAADLPSTATNKVLKRELI 501
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
477-551 |
2.49e-21 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 87.99 E-value: 2.49e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522138377 477 EIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVV-KKDPALTEAELRAYCHENLTGYKMPKYITFLPELPKSNVGK 551
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
54-482 |
2.96e-21 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 97.43 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFA-SYLQnvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKaI 132
Cdd:cd05933 7 HTLTYKEYYEACRQAAkAFLK--LGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEAN-I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 133 VIVENfCTTLQQVIantpiqhvittQIGDLAPFPKrAIVNFvvkrvkKMVPAWSLPGTTGFRAALAKGRAQPYARVQ--- 209
Cdd:cd05933 84 LVVEN-QKQLQKIL-----------QIQDKLPHLK-AIIQY------KEPLKEKEPNLYSWDEFMELGRSIPDEQLDaii 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 210 --LGPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIG-PFLDEGKEVIITALPLYHIFALVVNCLLFLRHG--- 283
Cdd:cd05933 145 ssQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDlRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGgqv 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 284 -------CRNVLITNPRDM----------------------AAFCVELKRSGFTAITGVN-----TLFNGLLHAPGF--- 326
Cdd:cd05933 225 yfaqpdaLKGTLVKTLREVrptafmgvprvwekiqekmkavGAKSGTLKRKIASWAKGVGletnlKLMGGESPSPLFyrl 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 327 -AELDFSRFKLAVG---------GGTAVQQAVAEKWQKVTgVGLTEGYGLTECSPVVSfspLSVPQWNG--TIGVPLPST 394
Cdd:cd05933 305 aKKLVFKKVRKALGldrcqkfftGAAPISRETLEFFLSLN-IPIMELYGMSETSGPHT---ISNPQAYRllSCGKALPGC 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 395 LVSLRDEEENevppGQpGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVS-GFNV 473
Cdd:cd05933 381 KTKIHNPDAD----GI-GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAgGENV 455
|
....*....
gi 522138377 474 YPNEIEGVV 482
Cdd:cd05933 456 PPVPIEDAV 464
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
212-558 |
4.12e-21 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 96.35 E-value: 4.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 PDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIiTALPLYHIFALV---VNCLlflrHGCRNVL 288
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLN--LKNGDRTY-TCMPLYHGTAAFlgaCNCL----MSGGTLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 289 ITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPgfAELDFSRFKLAVGGGTAVQQAVAEKWQKVTGVG-LTEGYGLT 367
Cdd:cd05937 159 LSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTP--PSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPeIGEFYAAT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 368 EcsPVVSFSPLSVPQWN-GTIG--------------VPL---PSTLVSLRDEEEN---EVPPGQPGELCVKGP----QVM 422
Cdd:cd05937 237 E--GVFALTNHNVGDFGaGAIGhhglirrwkfenqvVLVkmdPETDDPIRDPKTGfcvRAPVGEPGEMLGRVPfknrEAF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 423 QGYWQKPEESAK-----VFTK-DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGV 496
Cdd:cd05937 315 QGYLHNEDATESklvrdVFRKgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGV 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522138377 497 PDEK-SGEVPKVFVVKKDPALTEAE-----LRAYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:cd05937 395 KVPGhDGRAGCAAITLEESSAVPTEftkslLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
195-558 |
1.72e-20 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 94.83 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 195 AALAKGRAQPYARVQLGpdDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEGKEVIITALPLYHIFALVv 274
Cdd:PRK05851 136 TAAHTNRSASLTPPDSG--GPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG--LDAATDVGCSWLPLYHDMGLA- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 275 ncllFLRHGCRNVLITNPRDMAAFCVelkrSGFTAITGVNTLFNGLLHAPGFA------------ELDFSRFKLAVGGGT 342
Cdd:PRK05851 211 ----FLLTAALAGAPLWLAPTTAFSA----SPFRWLSWLSDSRATLTAAPNFAynligkyarrvsDVDLGALRVALNGGE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 343 AVQQAVAEKWQKVTG-VGLTEG-----YGLTECSPVVSFSPL--------------SVPQWNGTIGVPLPSTLVSLR-DE 401
Cdd:PRK05851 283 PVDCDGFERFATAMApFGFDAGaaapsYGLAESTCAVTVPVPgiglrvdevttddgSGARRHAVLGNPIPGMEVRISpGD 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 402 EENEVPPGQPGELCVKGPQVMQGYW-QKPEESakvftkDGWLKTGDVAVFEPNGyLRIVDRKKDMILVSGFNVYPNEIEG 480
Cdd:PRK05851 363 GAAGVAGREIGEIEIRGASMMSGYLgQAPIDP------DDWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIER 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 481 VVAQHPGVLEVACIGVPDEKSGEVPKVFV----VKKDPALTEAEL----RAYChenltGYkMPKYITFLP--ELPKSNVG 550
Cdd:PRK05851 436 VAAQVRGVREGAVVAVGTGEGSARPGLVIaaefRGPDEAGARSEVvqrvASEC-----GV-VPSDVVFVApgSLPRTSSG 509
|
....*...
gi 522138377 551 KVLRKELR 558
Cdd:PRK05851 510 KLRRLAVK 517
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
213-503 |
3.11e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 94.52 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 213 DDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAwigpFLDEGKEVIITA------LPLYHIFALVVNCLLFLRHGCRN 286
Cdd:PLN02861 220 TDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDH----LLKVTDRVATEEdsyfsyLPLAHVYDQVIETYCISKGASIG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 287 VLITNPRDMAAFCVELKRSGFTAI--------TGVN-----------TLFN------------GLLH---APGFAELDFS 332
Cdd:PLN02861 296 FWQGDIRYLMEDVQALKPTIFCGVprvydriyTGIMqkissggmlrkKLFDfaynyklgnlrkGLKQeeaSPRLDRLVFD 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 333 RFKLAVGG-------GTAVQQAVAEKWQKVTGVG-LTEGYGLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEE- 403
Cdd:PLN02861 376 KIKEGLGGrvrlllsGAAPLPRHVEEFLRVTSCSvLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIEARLESVPEm 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 404 -----NEVPPGqpgELCVKGPQVMQGYWQKPEESAKVFTkDGWLKTGDVAVFEPNGYLRIVDRKKDMILVS-GFNVYPNE 477
Cdd:PLN02861 456 gydalSDVPRG---EICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVEN 531
|
330 340 350
....*....|....*....|....*....|....*..
gi 522138377 478 IEGVVAQHPGVLEVACIG-----------VPDEKSGE 503
Cdd:PLN02861 532 LENTYSRCPLIASIWVYGnsfesflvavvVPDRQALE 568
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
54-558 |
3.40e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 94.44 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLV--VVNVNplYTPRELEHQLRDSGAKA 131
Cdd:PRK00174 97 RKITYRELHREVCRFANALKS-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsVVFGG--FSAEALADRIIDAGAKL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 132 IVivenfcTTLQQV---------------IANTP-IQHVIttqigdlapfpkraivnfVVKRVKKMVPaWSlPGttgfR- 194
Cdd:PRK00174 174 VI------TADEGVrggkpiplkanvdeaLANCPsVEKVI------------------VVRRTGGDVD-WV-EG----Rd 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 195 ------AALAKGRAQPyarVQLGPDDIAFLQYTGGTTGLSKG-----------AVLTHGNV-----------TANVqqvs 246
Cdd:PRK00174 224 lwwhelVAGASDECEP---EPMDAEDPLFILYTSGSTGKPKGvlhttggylvyAAMTMKYVfdykdgdvywcTADV---- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 247 AWI--------GPFLDEGKEVIITALPLY---HIFALVVNcllflRHGCrNVLITNPrdmaafcvelkrsgfTAITgvnt 315
Cdd:PRK00174 297 GWVtghsyivyGPLANGATTLMFEGVPNYpdpGRFWEVID-----KHKV-TIFYTAP---------------TAIR---- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 316 lfngLLHAPG---FAELDFSRFKLAvggGTavqqaVAE-------KW-QKVTGVGltegygltECsPVVS---------- 374
Cdd:PRK00174 352 ----ALMKEGdehPKKYDLSSLRLL---GS-----VGEpinpeawEWyYKVVGGE--------RC-PIVDtwwqtetggi 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 375 -FSPL--SVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGELCVKG--PQVMQGYWQKPEESAKVF--TKDGWLKTGDV 447
Cdd:PRK00174 411 mITPLpgATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDpwPGMMRTIYGDHERFVKTYfsTFKGMYFTGDG 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 448 AVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPALTEA----ELRA 523
Cdd:PRK00174 491 ARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDelrkELRN 570
|
570 580 590
....*....|....*....|....*....|....*
gi 522138377 524 YCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PRK00174 571 WVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
55-536 |
3.53e-20 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 94.06 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 55 TLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVnvnPLYT---PRELEHQLRDSGAKA 131
Cdd:cd17632 67 TITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSV---PLQAgasAAQLAPILAETEPRL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 132 I-VIVENFCTTLQQVI-ANTPIQHVI---TTQIGDlapfpKRAIVNfvvkRVKKMVPAWSLPGTTGFRAALAKGRAQPYA 206
Cdd:cd17632 144 LaVSAEHLDLAVEAVLeGGTPPRLVVfdhRPEVDA-----HRAALE----SARERLAAVGIPVTTLTLIAVRGRDLPPAP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 207 RVQLGPDD--IAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPflDEGKEVIITALPLYHIFAlvvncllflrhgc 284
Cdd:cd17632 215 LFRPEPDDdpLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDI--RPPASITLNFMPMSHIAG------------- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 285 RNVLITNprdmaafcveLKRSG---FTAITGVNTLFNGLLHA--------PGFAELDFSRF------KLAVGG--GTAVQ 345
Cdd:cd17632 280 RISLYGT----------LARGGtayFAAASDMSTLFDDLALVrptelflvPRVCDMLFQRYqaeldrRSVAGAdaETLAE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 346 QAVAEKWQKVTG--------------------------VGLTEGYGLTECSPVVSfsplsvpqwNGTIGVPlPSTLVSLR 399
Cdd:cd17632 350 RVKAELRERVLGgrllaavcgsaplsaemkafmeslldLDLHDGYGSTEAGAVIL---------DGVIVRP-PVLDYKLV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 400 DeeeneVP---------PGQPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDV-AVFEPNgYLRIVDRKKDMI-LV 468
Cdd:cd17632 420 D-----VPelgyfrtdrPHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVmAELGPD-RLVYVDRRNNVLkLS 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 469 SGFNVYPNEIEGVVAQHPGVLEVACIGvpdekSGE---VPKVFVVKKDP--ALTEAELRAYCHE---------NLTGYKM 534
Cdd:cd17632 494 QGEFVTVARLEAVFAASPLVRQIFVYG-----NSErayLLAVVVPTQDAlaGEDTARLRAALAEslqriareaGLQSYEI 568
|
..
gi 522138377 535 PK 536
Cdd:cd17632 569 PR 570
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
45-557 |
3.84e-20 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 93.81 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 45 DQIAYECMGQTLSFAELDRLTQDFASYLQnvlGLQRGDRVALMM-----PNLLqypVSLFGVLRAGLVVVNVNpLYTPRE 119
Cdd:PRK04813 17 DFPAYDYLGEKLTYGQLKEDSDALAAFID---SLKLPDKSPIIVfghmsPEML---ATFLGAVKAGHAYIPVD-VSSPAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 120 LEHQLRDSGAKAIVI-VENFCTTLqqvianTPIQHVITTQIGDLAPFPKRAIVNFVVKrvkkmvpawslpgttgfraala 198
Cdd:PRK04813 90 RIEMIIEVAKPSLIIaTEELPLEI------LGIPVITLDELKDIFATGNPYDFDHAVK---------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 199 kgraqpyarvqlgPDDIAFLQYTGGTTGLSKGAVLTHgnvtANVQQVSAWIGPFLDEGKEVIITALPLYHiFALVV---- 274
Cdd:PRK04813 142 -------------GDDNYYIIFTSGTTGKPKGVQISH----DNLVSFTNWMLEDFALPEGPQFLNQAPYS-FDLSVmdly 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 275 NCLLflRHGCRNVL----ITNPRDMAAfcvELKRSGFTaiTGVNTlfngllhaPGFAEL-----DFS--------RFKLA 337
Cdd:PRK04813 204 PTLA--SGGTLVALpkdmTANFKQLFE---TLPQLPIN--VWVST--------PSFADMclldpSFNeehlpnltHFLFC 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 338 vggGTAVQQAVAEKwqkvtgvgLTE---------GYGLTECSPVVS-----------FSPLsvPqwngtIGVPLPSTLVS 397
Cdd:PRK04813 269 ---GEELPHKTAKK--------LLErfpsatiynTYGPTEATVAVTsieitdemldqYKRL--P-----IGYAKPDSPLL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 398 LRDEEENEVPPGQPGELCVKGPQVMQGYWQKPEESAKVF-TKDGW--LKTGDVAVFEpNGYLRIVDRKKDMILVSGFNVY 474
Cdd:PRK04813 331 IIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIE 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 475 PNEIEGVVAQHPGVLEvaCIGVPDEKSGEV--------PKVFVVKKDPALTEAeLRAYCHENLTGYKMPKYITFLPELPK 546
Cdd:PRK04813 410 LEEIEQNLRQSSYVES--AVVVPYNKDHKVqyliayvvPKEEDFEREFELTKA-IKKELKERLMEYMIPRKFIYRDSLPL 486
|
570
....*....|.
gi 522138377 547 SNVGKVLRKEL 557
Cdd:PRK04813 487 TPNGKIDRKAL 497
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
54-557 |
9.18e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 92.14 E-value: 9.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLqNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIV 133
Cdd:cd05910 1 SRLSFRELDERSDRIAQGL-TAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 134 IVenfcttlqqviantpiqhvittqigdlapfpkraivnfvvkrvkkmvpawslpgttgFRAalakgraqpyarvqlgpD 213
Cdd:cd05910 80 GI---------------------------------------------------------PKA-----------------D 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 214 DIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPfldEGKEVIITALPLYHIF------ALVVNCLLFLRHGCrnv 287
Cdd:cd05910 86 EPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI---RPGEVDLATFPLFALFgpalglTSVIPDMDPTRPAR--- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 288 liTNPRDMAAFcveLKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKLAVGGGTAVQQAVAEKWQKVT--GVGLTEGYG 365
Cdd:cd05910 160 --ADPQKLVGA---IRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 366 LTECSPVVSFSPLSV--------PQWNGT-IGVPLPSTLVSL---RDE------EENEVPPGQPGELCVKGPQVMQGYWQ 427
Cdd:cd05910 235 ATEALPVSSIGSRELlatttaatSGGAGTcVGRPIPGVRVRIieiDDEpiaewdDTLELPRGEIGEITVTGPTVTPTYVN 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 428 KPEESA--KVFTKDG--WLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVpdEKSGE 503
Cdd:cd05910 315 RPVATAlaKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV--GKPGC 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522138377 504 VPKVFVVKKDP------ALTEAELRAYCHENLTGYKMPKYI--TFLPELPKSNvGKVLRKEL 557
Cdd:cd05910 393 QLPVLCVEPLPgtitprARLEQELRALAKDYPHTQRIGRFLihPSFPVDIRHN-AKIFREKL 453
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
330-554 |
1.67e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 92.11 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 330 DFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTE--CSPVVSFSPLSVPqwNGTIGVPLPSTLVSLRDEEENEVP 407
Cdd:PTZ00237 378 DLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEigITYLYCYGHINIP--YNATGVPSIFIKPSILSEDGKELN 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 408 PGQPGELCVK---GPQVMQGYWQKPEESAKVFTK-DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVA 483
Cdd:PTZ00237 456 VNEIGEVAFKlpmPPSFATTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSIL 535
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522138377 484 QHPGVLEVACIGVPDEKSGEVPKVFVVKKDPALTEA--------ELRAYCHENLTGYKMPKYITFLPELPKSNVGKVLR 554
Cdd:PTZ00237 536 KHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnklknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
54-558 |
4.04e-19 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 91.16 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIV 133
Cdd:PRK10524 83 RTYTFRQLHDEVNRMAAMLRS-LGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 134 IVE---------NFCTTLQQVI--ANTPIQHVITTQIGdLAPFPKRA--IVNFVVKRVKKM---VP-AWslpgttgfraa 196
Cdd:PRK10524 162 SADagsrggkvvPYKPLLDEAIalAQHKPRHVLLVDRG-LAPMARVAgrDVDYATLRAQHLgarVPvEW----------- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 197 lakgraqpyarvqLGPDDIAFLQYTGGTTGLSKGavlthgnvtanVQQvsawigpflDEGKEVIITALPLYHIFALVVNC 276
Cdd:PRK10524 230 -------------LESNEPSYILYTSGTTGKPKG-----------VQR---------DTGGYAVALATSMDTIFGGKAGE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 277 LLF------------------LRHGCRNV----LITNPrDMAAF--CVELKRSG--FTAITGVNTLFNgllHAPGF-AEL 329
Cdd:PRK10524 277 TFFcasdigwvvghsyivyapLLAGMATImyegLPTRP-DAGIWwrIVEKYKVNrmFSAPTAIRVLKK---QDPALlRKH 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 330 DFSRFKLAVGGGTAVQQAVAEKWQKVTGVGLTEGYGLTECS-PVVSFSP--LSVPQWNGTIGVPLPSTLVSLRDEEENE- 405
Cdd:PRK10524 353 DLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGwPILAIARgvEDRPTRLGSPGVPMYGYNVKLLNEVTGEp 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 406 VPPGQPGELCVKGP---QVMQGYWQKPEEsakvFTKDGW-------LKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYP 475
Cdd:PRK10524 433 CGPNEKGVLVIEGPlppGCMQTVWGDDDR----FVKTYWslfgrqvYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGT 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 476 NEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPALT---------EAELRAYCHENLTGYKMPKYITFLPELPK 546
Cdd:PRK10524 509 REIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLadrearlalEKEIMALVDSQLGAVARPARVWFVSALPK 588
|
570
....*....|..
gi 522138377 547 SNVGKVLRKELR 558
Cdd:PRK10524 589 TRSGKLLRRAIQ 600
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
55-558 |
2.02e-17 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 85.48 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 55 TLSFAELDRLTQDFASYLQNVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVI 134
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 135 VEnfcttlqqviANTPiQHVITTqigdLAPFPKRAIVNFVVkrVKKMVPAWSLPgttgFRAALAKGRAQPYARVQlgPDD 214
Cdd:cd05905 94 VE----------ACLK-GLPKKL----LKSKTAAEIAKKKG--WPKILDFVKIP----KSKRSKLKKWGPHPPTR--DGD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 215 IAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGpfLDEgKEVIITALPLYHIFALVVNCLLFLRHGCRNVLI----- 289
Cdd:cd05905 151 TAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACE--LYE-SRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIppelm 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 290 -TNPrdmAAFCVELKR-SGFTAITGVNTLFNGLLHAPGFAE------LDFSRFK-LAVGGGTAVQQAVAEKWQKVTGvgl 360
Cdd:cd05905 228 kTNP---LLWLQTLSQyKVRDAYVKLRTLHWCLKDLSSTLAslknrdVNLSSLRmCMVPCENRPRISSCDSFLKLFQ--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 361 TEGYGLTECSPVVSFSPLSVPQWNGTIGvPLPST-LVSLRDEEENEVPP------------------------------- 408
Cdd:cd05905 302 TLGLSPRAVSTEFGTRVNPFICWQGTSG-PEPSRvYLDMRALRHGVVRLderdkpnslplqdsgkvlpgaqvaivnpetk 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 409 -----GQPGELCVKGPQVMQGYWQKPEE------------SAKVFTKDGWLKTGD------VAVFEPNGY----LRIVDR 461
Cdd:cd05905 381 glckdGEIGEIWVNSPANASGYFLLDGEtndtfkvfpstrLSTGITNNSYARTGLlgflrpTKCTDLNVEehdlLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 462 KKDMILVSGFNVYPNEIEG-VVAQHPGVLEVA-------------CIGVPDEKSGE-VPKVFVVkkdpALTEAELRAYCh 526
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEAtVMRVHPYRGRCAvfsitglvvvvaeQPPGSEEEALDlVPLVLNA----ILEEHQVIVDC- 535
|
570 580 590
....*....|....*....|....*....|....
gi 522138377 527 enltgykmpkyITFLP--ELPKSNVGKVLRKELR 558
Cdd:cd05905 536 -----------VALVPpgSLPKNPLGEKQRMEIR 558
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
42-558 |
2.44e-17 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 84.54 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 42 RFGDQIAYECMGQTLSFAELDRLTQDFASYLQnVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPlYTPRELE 121
Cdd:PRK09029 15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFA-QQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNP-QLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 122 HQLrdsgakaivivenfCTTLQqviantpIQHVITTQiGDLAPFPKRAIVnfvvkrvkkmvpawslpgttgfraaLAKGR 201
Cdd:PRK09029 93 EEL--------------LPSLT-------LDFALVLE-GENTFSALTSLH-------------------------LQLVE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 202 AQPYARVQlgPDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIgPFldegkeviiTA-------LPLYHI--FAL 272
Cdd:PRK09029 126 GAHAVAWQ--PQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLM-PF---------TAqdswllsLPLFHVsgQGI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 273 VVNcllFLRHGCRNVLitnpRDMAAFCVELkrSGFTAITGVNTLFNGLLHAPGFAeLDFSRFKLavgGGTAVQQAVAEKW 352
Cdd:PRK09029 194 VWR---WLYAGATLVV----RDKQPLEQAL--AGCTHASLVPTQLWRLLDNRSEP-LSLKAVLL---GGAAIPVELTEQA 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 353 QKvTGVGLTEGYGLTECSpvvsfSPLSVPQWNGTIGV--PLPSTLVSLRDeeenevppgqpGELCVKGPQVMQGYWQkpe 430
Cdd:PRK09029 261 EQ-QGIRCWCGYGLTEMA-----STVCAKRADGLAGVgsPLPGREVKLVD-----------GEIWLRGASLALGYWR--- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 431 eSAKVFT---KDGWLKTGDVAVFEpNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPkV 507
Cdd:PRK09029 321 -QGQLVPlvnDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRP-V 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 522138377 508 FVVKKDPALTEAELRAYCHENLTGYKMP-KYITFLPELPKSNVgKVLRKELR 558
Cdd:PRK09029 398 AVVESDSEAAVVNLAEWLQDKLARFQQPvAYYLLPPELKNGGI-KISRQALK 448
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
212-469 |
1.28e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 83.23 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 212 PDDIAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWiGPFLDEGKEVIITALPLYHIFALVVNCLLFLRHGCRNVLitn 291
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKH-SIFKKYNPKTHLSYLPISHIYERVIAYLSFMLGGTINIW--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 292 PRDMAAFCVELKRSGFTAITGVNTLFNgLLHAPGFAELD------------------------FSRF------------- 334
Cdd:PTZ00342 379 SKDINYFSKDIYNSKGNILAGVPKVFN-RIYTNIMTEINnlpplkrflvkkilslrksnnnggFSKFlegithisskikd 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 335 ----KLAV--GGGTAVQQAVAEKWQKVTGVGLTEGYGLTECSpvvsfSPLSVPQWNGT----IGVPL-PSTLVSLRDEEE 403
Cdd:PTZ00342 458 kvnpNLEVilNGGGKLSPKIAEELSVLLNVNYYQGYGLTETT-----GPIFVQHADDNntesIGGPIsPNTKYKVRTWET 532
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522138377 404 ---NEVPPgqPGELCVKGPQVMQGYWQKPEESAKVFTKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVS 469
Cdd:PTZ00342 533 ykaTDTLP--KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLS 599
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
4-558 |
3.81e-11 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 65.69 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 4 STAAGEFVWFQEYPPS--VPRTIDTGAVPSLVAMFEQSCARF-------------GDQIAYECMGQ------TLSFAEL- 61
Cdd:PLN02654 48 SDIASQFYWKQKWEGDevCSENLDVRKGPISIEWFKGGKTNIcyncldrnveagnGDKIAIYWEGNepgfdaSLTYSELl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 62 DRLTQdFASYLQNVlGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIvenfCTT 141
Cdd:PLN02654 128 DRVCQ-LANYLKDV-GVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVIT----CNA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 142 LQQviantpiqhvittqigDLAPFPKRAIVNFVVKRVKKMVPAWSLPGTTGFRAALAK-------GRAQPYARV------ 208
Cdd:PLN02654 202 VKR----------------GPKTINLKDIVDAALDESAKNGVSVGICLTYENQLAMKRedtkwqeGRDVWWQDVvpnypt 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 209 -----QLGPDDIAFLQYTGGTTGLSKGAVLTHGNV---------------TANVQQVSA---WI--------GPFLDEGK 257
Cdd:PLN02654 266 kceveWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYmvytattfkyafdykPTDVYWCTAdcgWItghsyvtyGPMLNGAT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 258 EVIITALPLY----HIFALVVNCLLFLRHGCRNVLITNPRDMAAFCVELKRSGFTAITGVNTLFNGLLHAPGFAELDFSR 333
Cdd:PLN02654 346 VLVFEGAPNYpdsgRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSR 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 334 FKLAvgggtavqqavAEKWQKVTGvglteGYGLTecsPVvsfsPLSVPQWNGTIGVPLPSTLVSLRDEEENEVPPGQPGE 413
Cdd:PLN02654 426 CPIS-----------DTWWQTETG-----GFMIT---PL----PGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGY 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 414 LCVKG--PQVMQGYWQKPEESAKVFTK--DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVL 489
Cdd:PLN02654 483 LCVKKswPGAFRTLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCA 562
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522138377 490 EVACIGVPDEKSGEVPKVFVVKKDPALTEAELRA----YCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PLN02654 563 EAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKslilTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
56-553 |
1.03e-09 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 61.05 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAELDRLTQDFASYLQnVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIV 135
Cdd:TIGR01217 115 VTWAELRRQVASLAAALR-ALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 136 ENFCTTLQQVIANTPIQHVItTQIGDLAPFpkrAIVNFVVKRVKKmvpAWSLPGTTGFRAALAKGRAQPYARVQLGPDDI 215
Cdd:TIGR01217 194 DGYRYNGKEHDRRDKVAEVR-KELPTLRAV---VHIPYLGPRETE---APKIDGALDLEDFTAAAQAAELVFEQLPFDHP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 216 AFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAWIGPFLDEGKEVIITALPL----YHIFALVVNCLLFLRHGCRNVLITN 291
Cdd:TIGR01217 267 LWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWmmwnWLVSGLATGATLVLYDGSPGFPATN 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 292 PR-DMAAfcvelkRSGFTaITGVNTLFNGLLHAPGFA---ELDFSRFKLAVGGGTAVQ----QAVAEKWQKVTGVGLTEG 363
Cdd:TIGR01217 347 VLwDIAE------RTGAT-LFGTSAKYVMACRKAGVHparTHDLSALQCVASTGSPLPpdgfRWVYDEIKADVWLASISG 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 364 yGLTECSPVVSFSPlSVPQWNGTIGVPLPSTLVSLRDEEENEVpPGQPGELCVKGPQVMQG--YWQKPEES---AKVFTK 438
Cdd:TIGR01217 420 -GTDICSCFAGANP-TLPVHIGEIQAPGLGTAVQSWDPEGKPV-TGEVGELVCTNPMPSMPirFWNDPDGSkyrDAYFDT 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 439 -DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFV-----VKK 512
Cdd:TIGR01217 497 yPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDGGYRVVLFVhlapgATL 576
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 522138377 513 DPALTEaELRAYCHENLTGYKMPKYITFLPELPKSNVGKVL 553
Cdd:TIGR01217 577 DDALLD-RIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRV 616
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
215-557 |
6.95e-09 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 58.25 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 215 IAFLQYTGGTTGLSKGAVLTHGNVTANVQQVSAwigpFLDEGKEVIITALPLYHIFALVVNCLLFLRHGCrnVLITNPRD 294
Cdd:cd17654 120 LAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRS----LFNITSEDILFLTSPLTFDPSVVEIFLSLSSGA--TLLIVPTS 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 295 MAAFCVEL-----KRSGFTAITGVNTLFNGLLHAPGFAELdFSRFK----LAVGGGTAVQQAVAEKW-QKVTGVGLTEGY 364
Cdd:cd17654 194 VKVLPSKLadilfKRHRITVLQATPTLFRRFGSQSIKSTV-LSATSslrvLALGGEPFPSLVILSSWrGKGNRTRIFNIY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 365 GLTECSPVVSFSPLSVPQWNGTIGVPLPSTLVSLRDEEENEvppgQPGELCVKGPQ---VMQGYWQKPEESakvftkdgW 441
Cdd:cd17654 273 GITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSE----GTGQVFLGGLNrvcILDDEVTVPKGT--------M 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 442 LKTGDVaVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSgevpKVFVV-KKDPALTEAE 520
Cdd:cd17654 341 RATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRL----IAFIVgESSSSRIHKE 415
|
330 340 350
....*....|....*....|....*....|....*..
gi 522138377 521 LRAychENLTGYKMPKYITFLPELPKSNVGKVLRKEL 557
Cdd:cd17654 416 LQL---TLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
56-560 |
1.00e-08 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 58.05 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 56 LSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIV 135
Cdd:cd05943 99 VTWAELRRRVARLAAALRA-LGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 136 E---------NFCTTLQQVIANTP-IQHVIttqigdlapfpkraIVNFVVKRVKKMVPawSLPGTTGFRAALAKGRAQPY 205
Cdd:cd05943 178 DaytyngkrhDVREKVAELVKGLPsLLAVV--------------VVPYTVAAGQPDLS--KIAKALTLEDFLATGAAGEL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 206 ARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGnvtanvqqvsawiGPFLDEGKEVII---------------TALPLYH-- 268
Cdd:cd05943 242 EFEPLPFDHPLYILYSSGTTGLPKCIVHGAG-------------GTLLQHLKEHILhcdlrpgdrlfyyttCGWMMWNwl 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 269 IFALVVNCLLFLRHGC-----RNVLItnprDMAAfcvelkRSGFTaITGVNTLFNGLLHAPGF---AELDFSRFK--LAV 338
Cdd:cd05943 309 VSGLAVGATIVLYDGSpfypdTNALW----DLAD------EEGIT-VFGTSAKYLDALEKAGLkpaETHDLSSLRtiLST 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 339 GGGTAVQQA--VAEKWQKvtGVGLTEGYGLTE-CSPVVSFSPLsVPQWNGTIGVPLPSTLVSLRDEEENEVPpGQPGEL- 414
Cdd:cd05943 378 GSPLKPESFdyVYDHIKP--DVLLASISGGTDiISCFVGGNPL-LPVYRGEIQCRGLGMAVEAFDEEGKPVW-GEKGELv 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 415 CVKG-PQVMQGYWQKPEES---AKVFTK-DGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQHPGVL 489
Cdd:cd05943 454 CTKPfPSMPVGFWNDPDGSryrAAYFAKyPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVE 533
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522138377 490 EVACIGVPDEKSGEVPKVFVV-KKDPALTEA---ELRAYCHENLTGYKMPKYITFLPELPKSNVGKVL----RKELRGK 560
Cdd:cd05943 534 DSLVVGQEWKDGDERVILFVKlREGVELDDElrkRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVevavKKIIAGR 612
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
74-558 |
6.40e-07 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 52.39 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 74 NVLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIVIvenfcttlQQVIANTPIQH 153
Cdd:PLN03052 226 DALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFT--------QDVIVRGGKSI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 154 VITTQIGDLApfPKRAIV------NFVVK-RVKKMVpaWS--LPGTTGFRaalakgRAQPYARVQLGPDDIAFLQYTGGT 224
Cdd:PLN03052 298 PLYSRVVEAK--APKAIVlpadgkSVRVKlREGDMS--WDdfLARANGLR------RPDEYKAVEQPVEAFTNILFSSGT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 225 TGLSKGAVLTH---------GNVTANVQQ--VSAW-------IGPFLdegkeviitalplyhIFALVVN-CLLFLRHGcr 285
Cdd:PLN03052 368 TGEPKAIPWTQltplraaadAWAHLDIRKgdIVCWptnlgwmMGPWL---------------VYASLLNgATLALYNG-- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 286 nvlitNP--RDMAAFcveLKRSGFTAITGVNTLFNGLLHAPGFAELDFSRFKL--AVGGGTAVQQAV---AEKWQKvtgv 358
Cdd:PLN03052 431 -----SPlgRGFAKF---VQDAKVTMLGTVPSIVKTWKNTNCMAGLDWSSIRCfgSTGEASSVDDYLwlmSRAGYK---- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 359 GLTEGYGLTEC-SPVVSFSPLSvPQWNGTIGVPLPSTLVSLRDEEENEVPPGQP--GElCVKGPQVMQG----------- 424
Cdd:PLN03052 499 PIIEYCGGTELgGGFVTGSLLQ-PQAFAAFSTPAMGCKLFILDDSGNPYPDDAPctGE-LALFPLMFGAsstllnadhyk 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 425 -YWQ-KPEESAKVFTKDGwlktgdvAVFE--PNGYLRIVDRKKDMILVSGFNVYPNEIEGVV-AQHPGVLEVACIGVPDE 499
Cdd:PLN03052 577 vYFKgMPVFNGKILRRHG-------DIFErtSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPP 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522138377 500 KSG-EVPKVFVVKKDP---ALTEAELR----AYCHENLTGYKMPKYITFLPELPKSNVGKVLRKELR 558
Cdd:PLN03052 650 GGGpEQLVIAAVLKDPpgsNPDLNELKkifnSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLR 716
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
329-519 |
2.03e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.15 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 329 LDFSRFKLAVG------GGTAVQQAVAEKWqkvtGVGLTEGYGLTECSPVVSFSPlsvPQWNGTIgVPLPSTLVSLRDEE 402
Cdd:COG1541 198 IDPRDLSLKKGifggepWSEEMRKEIEERW----GIKAYDIYGLTEVGPGVAYEC---EAQDGLH-IWEDHFLVEIIDPE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 403 ENE-VPPGQPGELcvkgpqvmqgywqkpeesakVFT---KDGW----LKTGDVAVFEP------NGYLRIV---DRKKDM 465
Cdd:COG1541 270 TGEpVPEGEEGEL--------------------VVTtltKEAMplirYRTGDLTRLLPepcpcgRTHPRIGrilGRADDM 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 522138377 466 ILVSGFNVYPNEIEGVVAQHPGVLEVACIGVPDEKSGEVPKVFVVKKDPALTEA 519
Cdd:COG1541 330 LIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLEA 383
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
406-557 |
7.49e-06 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 48.67 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 406 VPPGQPGELCVKGPQVMQGYWQKPeesakvftKDGWLKTGDVAVFEPNGYLRIVDRKKDMILVSGFNVYPNEIEGVVAQH 485
Cdd:cd17647 346 VEPDHWNYLDKDNNEPWRQFWLGP--------RDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQH 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 486 PGVLE---------------VACI--------------GVPDEKSGEVPKVFVVKKDPALTEaELRAYCHENLTGYKMPK 536
Cdd:cd17647 418 PLVREnitlvrrdkdeeptlVSYIvprfdkpddesfaqEDVPKEVSTDPIVKGLIGYRKLIK-DIREFLKKRLASYAIPS 496
|
170 180
....*....|....*....|.
gi 522138377 537 YITFLPELPKSNVGKVLRKEL 557
Cdd:cd17647 497 LIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
54-238 |
1.83e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 44.40 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 54 QTLSFAELDRLTQDFASYLQNvLGLQRGDRVALMMPNLLQYPVSLFGVLRAGLVVVNVNPLYTPRELEHQLRDSGAKAIV 133
Cdd:PRK03584 113 RELSWAELRRQVAALAAALRA-LGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLI 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 134 IVENF---------CTTLQQVIANTP-IQHVIttqigdlapfpkraivnfVVKRVKKMVPAWSLPGTTGFRAALAKGRAQ 203
Cdd:PRK03584 192 AVDGYryggkafdrRAKVAELRAALPsLEHVV------------------VVPYLGPAAAAAALPGALLWEDFLAPAEAA 253
|
170 180 190
....*....|....*....|....*....|....*
gi 522138377 204 PYARVQLGPDDIAFLQYTGGTTGLSKGAVLTHGNV 238
Cdd:PRK03584 254 ELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGI 288
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
400-488 |
1.74e-03 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 41.07 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 400 DEEENE-VPPGQPGELcvkgpqvmqgywqkpeesakVFT---KDGWL----KTGDVA--VFEPNGY-------LRIVDRK 462
Cdd:cd05913 263 DPETGEpVPPGEVGEL--------------------VFTtltKEAMPliryRTRDITrlLPGPCPCgrthrriDRITGRS 322
|
90 100
....*....|....*....|....*.
gi 522138377 463 KDMILVSGFNVYPNEIEGVVAQHPGV 488
Cdd:cd05913 323 DDMLIIRGVNVFPSQIEDVLLKIPGL 348
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
409-552 |
3.45e-03 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 40.43 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 409 GQPGELCVKGPQVMQGYWQKPEESAKVF---------------------TKDGWL-------KTGDVAVFEPNGYLRIVD 460
Cdd:TIGR03443 619 GEVGEIYVRAGGLAEGYLGLPELNAEKFvnnwfvdpshwidldkennkpEREFWLgprdrlyRTGDLGRYLPDGNVECCG 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522138377 461 RKKDMILVSGFNVYPNEIEGVVAQHPGVLE---------------VACIgVPDEKSGEV--------------PKVFVVK 511
Cdd:TIGR03443 699 RADDQVKIRGFRIELGEIDTHLSQHPLVREnvtlvrrdkdeeptlVSYI-VPQDKSDELeefksevddeessdPVVKGLI 777
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 522138377 512 KDPALTEaELRAYCHENLTGYKMPKYITFLPELPKSNVGKV 552
Cdd:TIGR03443 778 KYRKLIK-DIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKV 817
|
|
| |
