|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
41-571 |
0e+00 |
|
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: 1059.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 41 IPEYFNFAKDVLDQWTNTEKTGKRLSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEW 120
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 121 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMK 200
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 201 YASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWT 280
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 281 QGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRsYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDI 360
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSS-YKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 361 YEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPDRPFGLFTHYVDNPSKTASTL 440
Cdd:cd05928 320 YEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 441 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKL 520
Cdd:cd05928 400 RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLS 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958642407 521 HDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 571
Cdd:cd05928 480 HDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
82-567 |
0e+00 |
|
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: 624.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 82 WSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 161
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 162 DtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTGPPKMIGHTHSsFGL 241
Cdd:cd05972 80 A---------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHS-YPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 242 GLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLI 321
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 322 QNDITrSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDEN 401
Cdd:cd05972 188 KQDLS-SYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 402 GTILPPGQEGDIAVQVlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEV 481
Cdd:cd05972 267 GRELPPGEEGDIAIKL---PPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 482 ESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKV 561
Cdd:cd05972 344 ESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421
|
....*.
gi 1958642407 562 KRNELR 567
Cdd:cd05972 422 RRVELR 427
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
38-571 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 608.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 38 KIEIPEYFNFAKDVLDQWTNTEKtgkrlSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKI 117
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRG-----DKVALIWEGEDGEERTLTYAELRREVNRFANALRAL-GVKKGDRVAIYLPNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 118 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD---------TLAPAVDIVAAKCENLHSKLIV---- 184
Cdd:COG0365 75 PEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVDEALEELPSLEHVIVVgrtg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 185 SQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSD 264
Cdd:COG0365 155 ADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 265 TGWAKSAWSSVFSPWTQGACVFAH-YLPRF-DSTSILQTLSKFPITVFCSAPTAYRMLIQNDIT--RSYKFNSLKHCVSA 340
Cdd:COG0365 235 IGWATGHSYIVYGPLLNGATVVLYeGRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEplKKYDLSSLRLLGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 341 GEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlp 419
Cdd:COG0365 315 GEPLNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVI---- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 420 DRPF-GLFTHYVDNPSKTASTLRGNF---YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESA 495
Cdd:COG0365 391 KGPWpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642407 496 VVSSPDPIRGEVVKAFIVLNPDYKLHDqeQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 571
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVVLKPGVEPSD--ELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
30-570 |
0e+00 |
|
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: 585.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 30 YESMKHDFKIEIPEYFNFAKDVLDQWTNTEKtgkrlSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILTeACSLQRGDR 109
Cdd:cd05970 1 YEDFHNNFSINVPENFNFAYDVVDAMAKEYP-----DKLALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 110 VMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD--DTLAPAVDIVAAKCENLHSKLIVSQH 187
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIaeDNIPEEIEKAAPECPSKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 188 SREGWGNLKEMMKYASDS----HTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSsFGLGLSVNGRFWLDLIASDVMWNTS 263
Cdd:cd05970 155 VPEGWIDFRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 264 DTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRsYKFNSLKHCVSAGEP 343
Cdd:cd05970 234 DTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSR-YDLSSLRYCTTAGEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 344 INPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPDRPF 423
Cdd:cd05970 313 LNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 424 GLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPI 503
Cdd:cd05970 393 GLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPI 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642407 504 RGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 570
Cdd:cd05970 473 RGQVVKATIVLAKGYE--PSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
26-570 |
1.26e-149 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 442.41 E-value: 1.26e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 26 NFSNYESMKHDFKI-EIPEYF--------NFAKDVLDQWTNTEKTGKrlsnPAFWWVDGNGKEvRWSFEELGSLSRKFAN 96
Cdd:PRK04319 14 NLKDYEETYATFSWeEVEKEFswletgkvNIAYEAIDRHADGGRKDK----VALRYLDASRKE-KYTYKELKELSNKFAN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 97 ILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAvdIVAAKCE 176
Cdd:PRK04319 89 VLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLER--KPADDLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 177 NLHSKLIVSQHSREGWG--NLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLI 254
Cdd:PRK04319 166 SLKHVLLVGEDVEEGPGtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM-LQHYQTGKYVLDLH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 255 ASDVMWNTSDTGWAKSAWSSVFSPWTQGA--CVFAhylPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQ--NDITRSYK 330
Cdd:PRK04319 245 EDDVYWCTADPGWVTGTSYGIFAPWLNGAtnVIDG---GRFSPERWYRILEDYKVTVWYTAPTAIRMLMGagDDLVKKYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 331 FNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPG 408
Cdd:PRK04319 322 LSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETggIMIA-NYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 409 QEGDIAVQvlPDRPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEH 488
Cdd:PRK04319 401 RMGNLAIK--KGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEH 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 489 PSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:PRK04319 478 PAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
|
..
gi 1958642407 569 KE 570
Cdd:PRK04319 556 WE 557
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-570 |
7.15e-148 |
|
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: 432.76 E-value: 7.15e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:cd05974 2 SFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 TlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLG 242
Cdd:cd05974 81 N-----------------------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 243 lSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQ 322
Cdd:cd05974 114 -HLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 323 NDITRSYKfnSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENG 402
Cdd:cd05974 193 QDLASFDV--KLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 403 TilpPGQEGDIAVQVLPDRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVE 482
Cdd:cd05974 271 A---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 483 SALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIeELPKTVSGKVK 562
Cdd:cd05974 348 SVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYE--PSPETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIR 424
|
....*...
gi 1958642407 563 RNELRRKE 570
Cdd:cd05974 425 RVELRRRE 432
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
82-570 |
3.99e-137 |
|
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: 405.73 E-value: 3.99e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 82 WSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 161
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 162 DTLAPAVDIvaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTGPPKMIGHTHSSFgL 241
Cdd:cd05969 80 EELYERTDP-------------------------------------------EDPTLLHYTSGTTGTPKGVLHVHDAM-I 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 242 GLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLI 321
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 322 QNDI--TRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFNVEI 397
Cdd:cd05969 195 KEGDelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgsIMIA-NYPCMPIKPGSMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 398 LDENGTILPPGQEGDIAVQvlPDRPfGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIG 477
Cdd:cd05969 274 VDENGNELPPGTKGILALK--PGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 478 PFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTV 557
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE--PSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
490
....*....|...
gi 1958642407 558 SGKVKRNELRRKE 570
Cdd:cd05969 429 SGKIMRRVLKAKE 441
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
76-568 |
5.23e-130 |
|
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: 387.56 E-value: 5.23e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 76 NGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKS 155
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 156 KCIITDDTLAPAVdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhnelmaIYFTSGTTGPPKMIGHT 235
Cdd:cd05971 80 SALVTDGSDDPAL--------------------------------------------------IIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 236 HSsFGLGLSVNGRFWLDLI--ASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSA 313
Cdd:cd05971 110 HR-VLLGHLPGVQFPFNLFprDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 314 PTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMeQWKKKT-GLDIYEGYGQTETVLICGNFKG-MKIKPGSMGKPSP 391
Cdd:cd05971 189 PTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELL-GWAREQfGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 392 AFNVEILDENGTILPPGQEGDIAVQvLPDrPFGLFThYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILS 471
Cdd:cd05971 268 GHRVAIVDDNGTPLPPGEVGEIAVE-LPD-PVAFLG-YWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 472 SGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIE 551
Cdd:cd05971 345 SGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVN 422
|
490
....*....|....*..
gi 1958642407 552 ELPKTVSGKVKRNELRR 568
Cdd:cd05971 423 ELPRTATGKIRRRELRA 439
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
79-574 |
1.32e-124 |
|
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: 373.76 E-value: 1.32e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:COG0318 22 GRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITddtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhnelMAIYFTSGTTGPPKMIGHTHSS 238
Cdd:COG0318 101 VT--------------------------------------------------------ALILYTSGTTGRPKGVMLTHRN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 239 FgLGLSVNGRFWLDLIASDVMWNTS----DTGWaksaWSSVFSPWTQGACVfaHYLPRFDSTSILQTLSKFPITVFCSAP 314
Cdd:COG0318 125 L-LANAAAIAAALGLTPGDVVLVALplfhVFGL----TVGLLAPLLAGATL--VLLPRFDPERVLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 315 TAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET-VLICGNFKGMK-IKPGSMGKPSPA 392
Cdd:COG0318 198 TMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETsPVVTVNPEDPGeRRPGSVGRPLPG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 393 FNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSS 472
Cdd:COG0318 278 VEVRIVDEDGRELPPGEVGEIVV-----RGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 473 GYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKKEIQEHVkkttAPYKYPRKIEFIEE 552
Cdd:COG0318 353 GENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAEL-DAEELRAFLRERL----ARYKVPRRVEFVDE 427
|
490 500
....*....|....*....|..
gi 1958642407 553 LPKTVSGKVKRNELRRKEWTTT 574
Cdd:COG0318 428 LPRTASGKIDRRALRERYAAGA 449
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
83-568 |
7.97e-111 |
|
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: 337.95 E-value: 7.97e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDd 162
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 tlapavdivAAKCENLHSKLIVsqhsregwgnlkeMMkyasdshtcvdtkhnelmaiyFTSGTTGPPKMIGHTHSSFgLG 242
Cdd:cd05973 80 ---------AANRHKLDSDPFV-------------MM---------------------FTSGTTGLPKGVPVPLRAL-AA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 243 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG-ACVFAHylPRFDSTSILQTLSKFPITVFCSAPTAYRMLI 321
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLE--GGFSVESTWRVIERLGVTNLAGSPTAYRLLM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 322 QNDITRSYKFN-SLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMK--IKPGSMGKPSPAFNVEIL 398
Cdd:cd05973 194 AAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 399 DENGTILPPGQEGDIAVQVlPDRPFGLFTHYVDNPSKTAStlrGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGP 478
Cdd:cd05973 274 DDDGDELGPGEPGRLAIDI-ANSPLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 479 FEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVS 558
Cdd:cd05973 350 FDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHE--GTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPS 427
|
490
....*....|
gi 1958642407 559 GKVKRNELRR 568
Cdd:cd05973 428 GKIQRFLLRR 437
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
59-567 |
2.97e-108 |
|
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: 332.61 E-value: 2.97e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 59 EKTGKRLSN-PAFWWvdgngKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 137
Cdd:cd05936 6 EEAARRFPDkTALIF-----MGRKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 138 TTQLTQKDILYRLQSSKSKCIITDDTLApavdivaakcenlhsKLIVSQHSREGWgnlkemmkyasdshtCVDTKHnELM 217
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVSFT---------------DLLAAGAPLGER---------------VALTPE-DVA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 218 AIYFTSGTTGPPKMIGHTHSSfglgLSVNgrfwldliASDVMWNTSDTGWAKS------------AWS-SVFSPWTQGAC 284
Cdd:cd05936 129 VLQYTSGTTGVPKGAMLTHRN----LVAN--------ALQIKAWLEDLLEGDDvvlaalplfhvfGLTvALLLPLALGAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 285 VFahYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGY 364
Cdd:cd05936 197 IV--LIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 365 GQTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAV---QVlpdrpfglFTHYVDNPSKTASTL 440
Cdd:cd05936 275 GLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVrgpQV--------MKGYWNRPEETAEAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 441 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKL 520
Cdd:cd05936 347 VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASL 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1958642407 521 hdqeqLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:cd05936 427 -----TEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
215-562 |
9.67e-106 |
|
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: 321.16 E-value: 9.67e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 215 ELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAkSAWSSVFSPWTQGACVFAHylPRFD 294
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL--PKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 295 STSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET--VLI 372
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 373 CGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGY 452
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVV-----RGPSVMKGYWNNPEATAAVDEDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 453 MDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhDQEQLKKEIQE 532
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEELRA 306
|
330 340 350
....*....|....*....|....*....|
gi 1958642407 533 HVKKTTAPYKYPRKIEFIEELPKTVSGKVK 562
Cdd:cd04433 307 HVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
43-567 |
2.55e-103 |
|
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: 321.24 E-value: 2.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 43 EYFNFAKDVLDQwtnteKTGKRLSNPAFwwVDGNGkevRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWL 122
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAF--IDDAG---SLTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 123 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSRE--GWGNLKEMMK 200
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 201 YASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWT 280
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 281 QGACVFahYLP-RFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD 359
Cdd:cd05959 230 VGATTV--LMPeRPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 360 IYEGYGQTETVLI-CGNFKGmKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS 438
Cdd:cd05959 308 ILDGIGSTEMLHIfLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYV-----RGPSSATMYWNNRDKTRD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 439 TLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDY 518
Cdd:cd05959 382 TFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1958642407 519 KlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:cd05959 462 E--DSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
79-567 |
4.50e-96 |
|
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: 300.16 E-value: 4.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDIvaakcenlhsklivsqhsregwgnlkemmkyasdshtCVdtkhnelmaIYFTSGTTGPPKMIGHTHSS 238
Cdd:cd05958 88 LCAHALTASDDI-------------------------------------CI---------LAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 239 FGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFDSTSILQTLSKFPITVFCSAPTAYR 318
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 319 MLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEIL 398
Cdd:cd05958 200 AMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 399 DENGTILPPGQEGDIAVQvlpdRPFGLftHYVDNPSKtASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGP 478
Cdd:cd05958 280 DDEGNPVPDGTIGRLAVR----GPTGC--RYLADKRQ-RTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 479 FEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVS 558
Cdd:cd05958 353 PEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVI--PGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTAT 430
|
....*....
gi 1958642407 559 GKVKRNELR 567
Cdd:cd05958 431 GKLQRFALR 439
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
81-571 |
3.60e-95 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 300.18 E-value: 3.60e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 160
Cdd:PRK06187 31 RTTYAELDERVNRLANALRAL-GVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 161 DDTLAPAVDIVAAKCENLHSKLIVSQHSREG----WGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTH 236
Cdd:PRK06187 110 DSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 237 SSFgLGLSVNGRFWLDLIASDV------MWNTSDTGWAksawssvFSPWTQGACVFahYLPRFDSTSILQTLSKFPITVF 310
Cdd:PRK06187 190 RNL-FLHSLAVCAWLKLSRDDVylvivpMFHVHAWGLP-------YLALMAGAKQV--IPRRFDPENLLDLIETERVTFF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 311 CSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNF-----KGMKIKPG 384
Cdd:PRK06187 260 FAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqlPGQWTKRR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 385 SMGKPSPAFNVEILDENGTILPP--GQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFV 462
Cdd:PRK06187 340 SAGRPLPGVEARIVDDDGDELPPdgGEVGEIIV-----RGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYIT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 463 ARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyklhdqEQLK-KEIQEHVKKTTAPY 541
Cdd:PRK06187 415 DRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG------ATLDaKELRAFLRGRLAKF 488
|
490 500 510
....*....|....*....|....*....|
gi 1958642407 542 KYPRKIEFIEELPKTVSGKVKRNELRRKEW 571
Cdd:PRK06187 489 KLPKRIAFVDELPRTSVGKILKRVLREQYA 518
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
26-567 |
2.80e-89 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 287.99 E-value: 2.80e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 26 NFSNYESMkHDFKIEIPEYF--NFAKDVLDqWTNTEKTGKRLSNPAF--WWVDG-------------------------- 75
Cdd:TIGR02188 3 NLEQYKEL-YEESIEDPDKFwaKLARELLD-WFKPFTKVLDWSFPPFykWFVGGelnvsyncvdrhlearpdkvaiiweg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 76 --NGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPGttqLTQKDILYRL 150
Cdd:TIGR02188 81 dePGEVRKITYRELHREVCRFANVLKSL-GVKKGDRVAIYMPMIPEAAIAMLACARIGaihSVVFGG---FSAEALADRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 151 QSSKSKCIITDDT---------LAPAVDIVAAKCENLHSKLIVSQH----------SREGWGNlkEMMKYASDSHTCVDT 211
Cdd:TIGR02188 157 NDAGAKLVITADEglrggkvipLKAIVDEALEKCPVSVEHVLVVRRtgnpvvpwveGRDVWWH--DLMAKASAYCEPEPM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 212 KHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHY-L 290
Cdd:TIGR02188 235 DSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEgV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 291 PRFDSTS-ILQTLSKFPITVFCSAPTAYRMLIQ--NDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD---IYEGY 364
Cdd:TIGR02188 315 PTYPDPGrFWEIIEKHKVTIFYTAPTAIRALMRlgDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKErcpIVDTW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 365 GQTET--VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILP-PGQEGDIAV-QVLPDRPFGLF---THYVDNPSKTA 437
Cdd:TIGR02188 395 WQTETggIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEgPGEGGYLVIkQPWPGMLRTIYgdhERFVDTYFSPF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 438 StlrgNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 517
Cdd:TIGR02188 475 P----GYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDG 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1958642407 518 YKLHDqeQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:TIGR02188 551 YEPDD--ELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLR 598
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
46-567 |
3.53e-86 |
|
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: 279.45 E-value: 3.53e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 46 NFAKDVLDQwtNTEKTGKRlsnPAFWWvDGN--GKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLA 123
Cdd:cd05966 53 NISYNCLDR--HLKERGDK---VAIIW-EGDepDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 124 NVACLRTG---TVLIPGttqLTQKDILYRLQSSKSKCIITDD---------TLAPAVDIVAAKCENLHsKLIVSQHS--- 188
Cdd:cd05966 126 MLACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADggyrggkviPLKEIVDEALEKCPSVE-KVLVVKRTgge 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 189 ------REGWGNlkEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNT 262
Cdd:cd05966 202 vpmtegRDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 263 SDTGWAKSAWSSVFSPWTQGA-CVFAHYLPRFDSTSIL-QTLSKFPITVFCSAPTAYRMLIQ--NDITRSYKFNSLKHCV 338
Cdd:cd05966 280 ADIGWITGHSYIVYGPLANGAtTVMFEGTPTYPDPGRYwDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHDLSSLRVLG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 339 SAGEPINPEVMEQWKKKTG---LDIYEGYGQTETVLIC-----GnfkGMKIKPGSMGKPSPAFNVEILDENGTILPPGQE 410
Cdd:cd05966 360 SVGEPINPEAWMWYYEVIGkerCPIVDTWWQTETGGIMitplpG---ATPLKPGSATRPFFGIEPAILDEEGNEVEGEVE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 411 GDIAVqvlpDRPFglfthyvdnPSkTASTLRGN--------------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRI 476
Cdd:cd05966 437 GYLVI----KRPW---------PG-MARTIYGDheryedtyfskfpgYYFTGDGARRDEDGYYWITGRVDDVINVSGHRL 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 477 GPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDqeQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKT 556
Cdd:cd05966 503 GTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRKEIGPIATPDKIQFVPGLPKT 580
|
570
....*....|.
gi 1958642407 557 VSGKVKRNELR 567
Cdd:cd05966 581 RSGKIMRRILR 591
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
83-567 |
2.56e-85 |
|
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: 272.03 E-value: 2.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 tlapavDIVAakcenlhsklivsqhsregwgnlkemmkYASdshtcvdtkhnelmaiyFTSGTTGPPKMIGHTHSSFGLG 242
Cdd:cd05919 91 ------DDIA----------------------------YLL-----------------YSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 243 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAHYLPrfDSTSILQTLSKFPITVFCSAPTAYRMLI 321
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGAsAVLNPGWP--TAERVLATLARFRPTVLYGVPTFYANLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 322 QNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDEN 401
Cdd:cd05919 198 DSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 402 GTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEV 481
Cdd:cd05919 278 GHTIPPGEEGDLLV-----RGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 482 ESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDykLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKV 561
Cdd:cd05919 353 ESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSP--AAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKL 430
|
....*.
gi 1958642407 562 KRNELR 567
Cdd:cd05919 431 QRFKLR 436
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
79-561 |
7.42e-85 |
|
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: 270.64 E-value: 7.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:cd17631 18 GRSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDdtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhneLMAIYFTSGTTGPPKMIGHTHSS 238
Cdd:cd17631 97 FDD------------------------------------------------------LALLMYTSGTTGRPKGAMLTHRN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 239 FgLGLSVNGRFWLDLIASDV------MWNTSDTGwaksawssVFSPWT--QGACVfaHYLPRFDSTSILQTLSKFPITVF 310
Cdd:cd17631 123 L-LWNAVNALAALDLGPDDVllvvapLFHIGGLG--------VFTLPTllRGGTV--VILRKFDPETVLDLIERHRVTSF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 311 CSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTETV-LICGNFKGMKI-KPGSMGK 388
Cdd:cd17631 192 FLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSpGVTFLSPEDHRrKLGSAGR 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 389 PSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDV 468
Cdd:cd17631 271 PVFFVEVRIVDPDGREVPPGEVGEIVV-----RGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 469 ILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIE 548
Cdd:cd17631 346 IISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDED-----ELIAHCRERLARYKIPKSVE 420
|
490
....*....|...
gi 1958642407 549 FIEELPKTVSGKV 561
Cdd:cd17631 421 FVDALPRNATGKI 433
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
43-567 |
4.23e-82 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 265.93 E-value: 4.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 43 EYFNFAKDVLDqwTNTEKtgKRLSNPAFwwVDGNGkevRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWL 122
Cdd:TIGR02262 1 EKYNAAEDLLD--RNVVE--GRGGKTAF--IDDIS---SLSYGELEAQVRRLAAAL-RRLGVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 123 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSkLIVSQHSREGWGNLKEMMKYA 202
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEH-RVVVGRPEAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 203 SDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG 282
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 283 ACVFAhYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYE 362
Cdd:TIGR02262 230 ATTVL-MGERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 363 GYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVlPDRPFGlfthYVDNPSKTASTLRG 442
Cdd:TIGR02262 309 GIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISG-PSSATM----YWNNRAKSRDTFQG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 443 NFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhd 522
Cdd:TIGR02262 384 EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTA-- 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1958642407 523 qeqLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:TIGR02262 462 ---LETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
46-561 |
1.67e-80 |
|
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: 264.05 E-value: 1.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 46 NFAKDVLDQwtNTEKTGKRLsnpAFWWVDGNGKEVR-WSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLAN 124
Cdd:cd17634 53 NLAANALDR--HLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMIPEAAVAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 125 VACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD---------TLAPAVDIVA-AKCENLHSKLIVSqhsREG--- 191
Cdd:cd17634 127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvPLKKNVDDALnPNVTSVEHVIVLK---RTGsdi 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 192 ------WGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDT 265
Cdd:cd17634 204 dwqegrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 266 GWAKSAWSSVFSPWTQGACVFAHY-LPRF-DSTSILQTLSKFPITVFCSAPTAYRMLIQ--NDITRSYKFNSLKHCVSAG 341
Cdd:cd17634 284 GWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAagDDAIEGTDRSSLRILGSVG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 342 EPINPEVMEQWKKKTGLD---IYEGYGQTETV-LICGNFKGM-KIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQ 416
Cdd:cd17634 364 EPINPEAYEWYWKKIGKEkcpVVDTWWQTETGgFMITPLPGAiELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVIT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 417 V-LPDRPFGLFThyvDNPSKTASTLR--GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 493
Cdd:cd17634 444 DpWPGQTRTLFG---DHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAE 520
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642407 494 SAVVSSPDPIRGEVVKAFIVLNPDykLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKV 561
Cdd:cd17634 521 AAVVGIPHAIKGQAPYAYVVLNHG--VEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
69-567 |
2.32e-78 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 259.69 E-value: 2.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 69 AFWWVDGNGKEVR-WSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPGttqLTQK 144
Cdd:PRK00174 85 AIIWEGDDPGDSRkITYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGavhSVVFGG---FSAE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 145 DILYRLQSSKSKCIITDD---------TLAPAVDIVAAKCENLHSKLIVS--------QHSREGWGNlkEMMKYASDSHT 207
Cdd:PRK00174 161 ALADRIIDAGAKLVITADegvrggkpiPLKANVDEALANCPSVEKVIVVRrtggdvdwVEGRDLWWH--ELVAGASDECE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 208 CVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFA 287
Cdd:PRK00174 239 PEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLM 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 288 HY-LPRF-DSTSILQTLSKFPITVFCSAPTAYRMLIQ--NDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD---I 360
Cdd:PRK00174 319 FEgVPNYpDPGRFWEVIDKHKVTIFYTAPTAIRALMKegDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGErcpI 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 361 YEGYGQTET--VLIC---GnfkGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpDRPFglfthyvdnPS- 434
Cdd:PRK00174 399 VDTWWQTETggIMITplpG---ATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVI----KDPW---------PGm 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 435 ------------KTA-STLRGNfYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPD 501
Cdd:PRK00174 463 mrtiygdherfvKTYfSTFKGM-YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPD 541
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642407 502 PIRGEVVKAFIVLNPDYKLHDqeQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK00174 542 DIKGQGIYAFVTLKGGEEPSD--ELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
59-567 |
3.92e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 255.60 E-value: 3.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 59 EKTGKRL-SNPAFwwVDGngkEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 137
Cdd:PRK07656 12 ARAARRFgDKEAY--VFG---DQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 138 TTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIV----SQHSREGWGNLKEMMKYASDSHTCVDTKH 213
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 214 NELMAIYFTSGTTGPPK--MIGHTHSsfglgLSvNGRFW---LDLIASD---------------VMWNTsdtgwaksaws 273
Cdd:PRK07656 166 DDVADILFTSGTTGRPKgaMLTHRQL-----LS-NAADWaeyLGLTEGDrylaanpffhvfgykAGVNA----------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 274 svfsPWTQGACVFAHylPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWK 353
Cdd:PRK07656 229 ----PLMRGATILPL--PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 354 KKTGLDIY-EGYGQTE---TVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHY 429
Cdd:PRK07656 303 SELGVDIVlTGYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLV-----RGPNVMKGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 430 VDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVV 508
Cdd:PRK07656 378 YDDPEATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVG 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642407 509 KAFIVLNPDYKLhDQEQLKKEIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK07656 458 KAYVVLKPGAEL-TEEELIAYCREHL----AKYKVPRSIEFLDELPKNATGKVLKRALR 511
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
76-561 |
5.60e-78 |
|
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: 254.44 E-value: 5.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 76 NGKEvrWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKS 155
Cdd:cd05911 7 TGKE--LTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 156 KCIITDDTLAPAVdIVAAKCENLHSKLIVSQHSREGWGNLKEMMK---YASDSH--TCVDTKHNELMAIYFTSGTTGPPK 230
Cdd:cd05911 84 KVIFTDPDGLEKV-KEAAKELGPKDKIIVLDDKPDGVLSIEDLLSptlGEEDEDlpPPLKDGKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 231 MIGHTHSSFGLGL-SVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWtQGACVfaHYLPRFDSTSILQTLSKFPITV 309
Cdd:cd05911 163 GVCLSHRNLIANLsQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATV--IIMPKFDSELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 310 FCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGK 388
Cdd:cd05911 240 LYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 389 PSPAFNVEILDENG-TILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSD 466
Cdd:cd05911 320 LLPNVEAKIVDDDGkDSLGPNEPGEICV-----RGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 467 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDqeqlkKEIQEHVKKTTAPYKYPRK 546
Cdd:cd05911 395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE-----KEVKDYVAKKVASYKQLRG 469
|
490
....*....|....*.
gi 1958642407 547 -IEFIEELPKTVSGKV 561
Cdd:cd05911 470 gVVFVDEIPKSASGKI 485
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
64-567 |
1.59e-77 |
|
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: 256.86 E-value: 1.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 64 RLSNPAFWWVDG-NGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTV--LIPG--- 137
Cdd:cd05967 64 RGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGgfa 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 138 TTQLTQkdilyRLQSSKSKCIITDDTLAPAVDIVAAKcENLHSKLIVSQH------------------SREGWGNLKEMM 199
Cdd:cd05967 143 AKELAS-----RIDDAKPKLIVTASCGIEPGKVVPYK-PLLDKALELSGHkphhvlvlnrpqvpadltKPGRDLDWSELL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 200 KYASdSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPW 279
Cdd:cd05967 217 AKAE-PVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 280 TQGAcvfahylprfdsTSIL---------------QTLSKFPITVFCSAPTAYRMLIQND----ITRSYKFNSLKHCVSA 340
Cdd:cd05967 296 LHGA------------TTVLyegkpvgtpdpgafwRVIEKYQVNALFTAPTAIRAIRKEDpdgkYIKKYDLSSLRTLFLA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 341 GEPINPEVMEQWKKKTGLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQ 416
Cdd:cd05967 364 GERLDPPTLEWAENTLGVPVIDHWWQTETgwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 417 vLPDRPFGLFTHYVDNP---SKTASTLRGnFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 493
Cdd:cd05967 444 -LPLPPGCLLTLWKNDErfkKLYLSKFPG-YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAE 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642407 494 SAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:cd05967 522 CAVVGVRDELKGQVPLGLVVLKEGVKI-TAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
75-472 |
6.20e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 249.54 E-value: 6.20e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 75 GNGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 154
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 155 SKCIITDDTL-APAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSH-TCVDTKHNELMAIYFTSGTTGPPKMI 232
Cdd:pfam00501 94 AKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPpPPPPPDPDDLAYIIYTSGTTGKPKGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 233 GHTH---SSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAHYLPRFDSTSILQTLSKFPIT 308
Cdd:pfam00501 174 MLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAtVVLPPGFPALDPAALLELIERYKVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 309 VFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET---VLICGNFKGMKIKPGS 385
Cdd:pfam00501 254 VLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtgvVTTPLPLDEDLRSLGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 386 MGKPSPAFNVEILDEN-GTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDEDGYFWFVA 463
Cdd:pfam00501 334 VGRPLPGTEVKIVDDEtGEPVPPGEPGELCV-----RGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVG 408
|
....*....
gi 1958642407 464 RSDDVILSS 472
Cdd:pfam00501 409 RKKDQIKLG 417
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
83-566 |
1.47e-75 |
|
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: 246.24 E-value: 1.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITdd 162
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 tlapavdivaakcenlHSKLivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTGPPKMIGHTHSSFgLG 242
Cdd:cd05935 80 ----------------GSEL-------------------------------DDLALIPYTSGTTGLPKGCMHTHFSA-AA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 243 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQ 322
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 323 NDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILD-EN 401
Cdd:cd05935 190 TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiET 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 402 GTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS---TLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIG 477
Cdd:cd05935 270 GRELPPNEVGEIVV-----RGPQIFKGYWNRPEETEEsfiEIKGRrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVW 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 478 PFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTV 557
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREVEFVDELPRSA 421
|
....*....
gi 1958642407 558 SGKVKRNEL 566
Cdd:cd05935 422 SGKILWRLL 430
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
55-571 |
1.64e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 247.18 E-value: 1.64e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 55 WTNTEKTGKRLSNPAFWWVDGNgkevRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVL 134
Cdd:PRK08314 13 FHNLEVSARRYPDKTAIVFYGR----AISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 135 IPGTTQLTQKDILYRLQSSKSKCIITDDTLAPAVD-----------IVAAKCENLHSK-------LIVSQHSRE-----G 191
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGSELAPKVApavgnlrlrhvIVAQYSDYLPAEpeiavpaWLRAEPPLQalapgG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 192 WGNLKEMMK--YASDSHTcvdTKHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSD----T 265
Cdd:PRK08314 169 VVAWKEALAagLAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPlfhvT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 266 GWAKSAWSSVFSpwtqGACVFahYLPRFDSTSILQTLSKFPITVFCSAPTayrMLIQ---NDITRSYKFNSLKHCVSAGE 342
Cdd:PRK08314 245 GMVHSMNAPIYA----GATVV--LMPRWDREAAARLIERYRVTHWTNIPT---MVVDflaSPGLAERDLSSLRYIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 343 PINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSpaFNVE--ILD-ENGTILPPGQEGDIAV--- 415
Cdd:PRK08314 316 AMPEAVAERLKELTGLDYVEGYGLTETMaQTHSNPPD-RPKLQCLGIPT--FGVDarVIDpETLEELPPGEVGEIVVhgp 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 416 QVlpdrpfglFTHYVDNPSKTAS---TLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSI 491
Cdd:PRK08314 393 QV--------FKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 492 AESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 571
Cdd:PRK08314 465 QEACVIATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEK 541
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
81-567 |
5.07e-74 |
|
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: 242.20 E-value: 5.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 160
Cdd:cd05934 3 RWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 161 DdtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhneLMAIYFTSGTTGPPK--MIGHTHSS 238
Cdd:cd05934 82 D------------------------------------------------------PASILYTSGTTGPPKgvVITHANLT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 239 FGLGLSVNgrfWLDLIASDVMW--------NTSDTGWAkSAWSSvfspwtQGACVFahyLPRFDSTSILQTLSKFPITVF 310
Cdd:cd05934 108 FAGYYSAR---RFGLGEDDVYLtvlplfhiNAQAVSVL-AALSV------GATLVL---LPRFSASRFWSDVRRYGATVT 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 311 CSAPTAYRMLIQNDITRSYKFNSLKHCVSAgePINPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPS 390
Cdd:cd05934 175 NYLGAMLSYLLAQPPSPDDRAHRLRAAYGA--PNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 391 PAFNVEILDENGTILPPGQEGDIAVQvlPDRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVIL 470
Cdd:cd05934 253 PGYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 471 SSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEqlkkEIQEHVKKTTAPYKYPRKIEFI 550
Cdd:cd05934 331 RRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETL-DPE----ELFAFCEGQLAYFKVPRYIRFV 405
|
490
....*....|....*..
gi 1958642407 551 EELPKTVSGKVKRNELR 567
Cdd:cd05934 406 DDLPKTPTEKVAKAQLR 422
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
81-568 |
2.59e-73 |
|
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: 240.65 E-value: 2.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIit 160
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 161 ddtLAPAVdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhnelmaIYFTSGTTGPPKMIGHTHSSfg 240
Cdd:cd05941 89 ---LDPAL--------------------------------------------------ILYTSGTTGRPKGVVLTHAN-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 241 lglsvngrfwldlIASDVMWNTSDTGWAKS--------------AWSSVFSP-WTQGACVFahyLPRFDSTSILQTLSKF 305
Cdd:cd05941 114 -------------LAANVRALVDAWRWTEDdvllhvlplhhvhgLVNALLCPlFAGASVEF---LPKFDPKEVAISRLMP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 306 PITVFCSAPTAYRMLIQ--------NDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGN-F 376
Cdd:cd05941 178 SITVFMGVPTIYTRLLQyyeahftdPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNpL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 377 KGmKIKPGSMGKPSPAFNVEILDENGT-ILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRG-NFYITGDRGYMD 454
Cdd:cd05941 258 DG-ERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQV-----RGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 455 EDGYFWFVAR-SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLKkeiqEH 533
Cdd:cd05941 332 EDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELK----EW 407
|
490 500 510
....*....|....*....|....*....|....*
gi 1958642407 534 VKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:cd05941 408 AKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
77-570 |
2.60e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 236.47 E-value: 2.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 77 GKEVrwSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 156
Cdd:PRK06710 47 GKDI--TFSVFHDKVKRFANYL-QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 157 CIITDDTLAPAVDIV--AAKCENL-----------------------HSKLIV---SQHSREGWGNLKEmmkyasDSHTC 208
Cdd:PRK06710 124 VILCLDLVFPRVTNVqsATKIEHVivtriadflpfpknllypfvqkkQSNLVVkvsESETIHLWNSVEK------EVNTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 209 VDT---KHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLdliasdvmWNTSDTGWAKSAWSSVFSPWTQGAC- 284
Cdd:PRK06710 198 VEVpcdPENDLALLQYTGGTTGFPKGVMLTHKNL-VSNTLMGVQWL--------YNCKEGEEVVLGVLPFFHVYGMTAVm 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 285 ---VFAHY----LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTG 357
Cdd:PRK06710 269 nlsIMQGYkmvlIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 358 LDIYEGYGQTETVLIC-GNFKGMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVQVlPDrpfgLFTHYVDNPSK 435
Cdd:PRK06710 349 GKLVEGYGLTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKG-PQ----IMKGYWNKPEE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 436 TASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 515
Cdd:PRK06710 424 TAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1958642407 516 pdyklHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 570
Cdd:PRK06710 504 -----EGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
46-567 |
8.38e-69 |
|
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: 233.54 E-value: 8.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 46 NFAKDVLDQWTNTEKTgkrlsNPAFWWVDGNGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANV 125
Cdd:cd05968 61 NIVEQLLDKWLADTRT-----RPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 126 ACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD---------TLAPAVDIVAAKCENLhSKLIVSQHSregwGNLK 196
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTV-EKVVVVRHL----GNDF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 197 EMMKYASDSHTCVDTKH----------NELMAIYfTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTG 266
Cdd:cd05968 210 TPAKGRDLSYDEEKETAgdgaerteseDPLMIIY-TSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 267 WAKSAWsSVFSPWTQGACVFAHY-LPRFDSTSIL-QTLSKFPITVFCSAPTAYRMLI--QNDITRSYKFNSLKHCVSAGE 342
Cdd:cd05968 289 WMMGPW-LIFGGLILGATMVLYDgAPDHPKADRLwRMVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 343 PINPEVMeQWKKKTGLD----IYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPgQEGDIAVQ- 416
Cdd:cd05968 368 PWNPEPW-NWLFETVGKgrnpIINYSGGTEISgGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLa 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 417 VLPDRPFGLF---THYVDnpskTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 493
Cdd:cd05968 446 PWPGMTRGFWrdeDRYLE----TYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642407 494 SAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:cd05968 522 SAAIGVPHPVKGEAIVCFVVLKPGVT--PTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
81-567 |
2.52e-66 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 223.98 E-value: 2.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 160
Cdd:PRK07514 28 RYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 161 DDTLAPAVDIVAAKCENLHskliVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPK--M------- 231
Cdd:PRK07514 107 DPANFAWLSKIAAAAGAPH----VETLDADGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMlshgnll 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 232 -----------------------IGHTHssfGLGLSVNGRfwldLIAsdvmwntsdtgwaksawssvfspwtqGACVFah 288
Cdd:PRK07514 183 snaltlvdywrftpddvlihalpIFHTH---GLFVATNVA----LLA--------------------------GASMI-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 289 YLPRFDSTSILQTLSKfpITVFCSAPTAY-RMLIQNDITRsykfNSLKH---CVSAGEPINPEVMEQWKKKTGLDIYEGY 364
Cdd:PRK07514 228 FLPKFDPDAVLALMPR--ATVMMGVPTFYtRLLQEPRLTR----EAAAHmrlFISGSAPLLAETHREFQERTGHAILERY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 365 GQTETVLICGN-FKGMKIkPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVQvlpdrpfG--LFTHYVDNPSKTASTL 440
Cdd:PRK07514 302 GMTETNMNTSNpYDGERR-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVK-------GpnVFKGYWRMPEKTAEEF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 441 RGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYK 519
Cdd:PRK07514 374 RADgFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAA 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1958642407 520 LhDQEQLKKEIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK07514 454 L-DEAAILAALKGRL----ARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
82-567 |
4.54e-65 |
|
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: 220.65 E-value: 4.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 82 WSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 161
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 162 D----------------TLAPAVDivAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDshtcvdtkhneLMAIYFTSGT 225
Cdd:cd05926 94 KgelgpasraasklglaILELALD--VGVLIRAPSAESLSNLLADKKNAKSEGVPLPDD-----------LALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 226 TGPPKMIGHTHssfgLGLSVNGRFwldlIASDVMWNTSDT-----------GWAKSAWSSVFSpwtQGACVFAhylPRFD 294
Cdd:cd05926 161 TGRPKGVPLTH----RNLAASATN----ITNTYKLTPDDRtlvvmplfhvhGLVASLLSTLAA---GGSVVLP---PRFS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 295 STSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYK-FNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV--L 371
Cdd:cd05926 227 ASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 372 ICGNFKGMKIKPGSMGKPspaFNVE--ILDENGTILPPGQEGDIAVQ---VlpdrpfglfTH-YVDNPSKTA-STLRGNF 444
Cdd:cd05926 307 TSNPLPPGPRKPGSVGKP---VGVEvrILDEDGEILPPGVVGEICLRgpnV---------TRgYLNNPEANAeAAFKDGW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 445 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqe 524
Cdd:cd05926 375 FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASV---- 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958642407 525 qLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:cd05926 451 -TEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
66-566 |
8.43e-64 |
|
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: 217.49 E-value: 8.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 66 SNPAFwwVDG-NGKEVrwSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQK 144
Cdd:cd05904 20 SRPAL--IDAaTGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 145 DILYRLQSSKSKCIITDDTLAPavdivaaKCENLHSKLI-VSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTS 223
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTAELAE-------KLASLALPVVlLDSAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 224 GTTGPPK--MIGH---------THSSFGLGLSVNGRFWLDLIASDVMwntsdtGWAKSAWSSVFSpwtqGACVFAhyLPR 292
Cdd:cd05904 168 GTTGRSKgvMLTHrnliamvaqFVAGEGSNSDSEDVFLCVLPMFHIY------GLSSFALGLLRL----GATVVV--MPR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 293 FDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTET-- 369
Cdd:cd05904 236 FDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGYGMTEStg 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 370 -VLICGNFKGMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYI- 446
Cdd:cd05904 316 vVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWI-----RGPSIMKGYLNNPEATAATIDKEGWLh 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 447 TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdQEQl 526
Cdd:cd05904 391 TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSL--TED- 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1958642407 527 kkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd05904 468 --EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
78-567 |
3.04e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 216.34 E-value: 3.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 78 KEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKC 157
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 158 IITDDTLAPAVDIVAAKCENLHSKLIVS---QHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGH 234
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVlggREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 235 THSSFgLGLSVNGRFWLDLIASDVMWNtsdtgwA----KSAWSSVF-SPWTQ-GACVfaHYLPRFDSTSILQTLSKFPIT 308
Cdd:PRK08316 192 THRAL-IAEYVSCIVAGDMSADDIPLH------AlplyHCAQLDVFlGPYLYvGATN--VILDAPDPELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 309 VFCSAPTAYRMLIQNDITRSYKFNSLKHCVSaGEPINP-EVMEQWKKK-TGLDIYEGYGQTE-----TVLicgNFKGMKI 381
Cdd:PRK08316 263 SFFAPPTVWISLLRHPDFDTRDLSSLRKGYY-GASIMPvEVLKELRERlPGLRFYNCYGQTEiaplaTVL---GPEEHLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 382 KPGSMGKPspAFNVE--ILDENGTILPPGQEGDIAvqvlpDRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYF 459
Cdd:PRK08316 339 RPGSAGRP--VLNVEtrVVDDDGNDVAPGEVGEIV-----HRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 460 WFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqeqLKKEIQEHVKKTTA 539
Cdd:PRK08316 412 TVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATV-----TEDELIAHCRARLA 486
|
490 500
....*....|....*....|....*...
gi 1958642407 540 PYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK08316 487 GFKVPKRVIFVDELPRNPSGKILKRELR 514
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
73-571 |
8.02e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 212.07 E-value: 8.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 73 VDGNGKEvrWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 152
Cdd:PRK08276 5 MAPSGEV--VTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 153 SKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKE----MMKYASDSHTCVDtkhneLMAiyFTSGTTGP 228
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEalaaQPDTPIADETAGA-----DML--YSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 229 PKMI------GHTHSSFGLGLSVNGRFwldliasdvMWNTSDTGWAKSA--WSSVFSPWTQGACVFAH---YLPRFDSTS 297
Cdd:PRK08276 155 PKGIkrplpgLDPDEAPGMMLALLGFG---------MYGGPDSVYLSPAplYHTAPLRFGMSALALGGtvvVMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 298 ILQTLSKFPITVFCSAPTAY-RMLIQNDITR-SYKFNSLKHCVSAGEPINPEVMEQ----WkkktGLDIYEGYGQTE--- 368
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFvRMLKLPEEVRaRYDVSSLRVAIHAAAPCPVEVKRAmidwW----GPIIHEYYASSEggg 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 369 -TVLICGNFKGmkiKPGSMGKPSPAfNVEILDENGTILPPGQEGDIAVQvLPDRPFglftHYVDNPSKTASTLRGNFYIT 447
Cdd:PRK08276 302 vTVITSEDWLA---HPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPF----EYHNDPEKTAAARNPHGWVT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 448 -GDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQL 526
Cdd:PRK08276 373 vGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGAD--AGDAL 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1958642407 527 KKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 571
Cdd:PRK08276 451 AAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYW 495
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
79-574 |
2.19e-58 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 203.84 E-value: 2.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDIVAAKCENLHSKLIV----SQHSREGWGNLKemMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGH 234
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLdapaSVSVPAGWSTAP--LPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 235 THSSFglglsvngrFW--------LDLIASDVMWNTSDTgWAKSAWSSVFSPWTQGACVfaHYLPRFDSTSILQTLSKFP 306
Cdd:PRK06155 201 PHAQF---------YWwgrnsaedLEIGADDVLYTTLPL-FHTNALNAFFQALLAGATY--VLEPRFSASGFWPAVRRHG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 307 ITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPinPEVMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKiKPGSM 386
Cdd:PRK06155 269 ATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSM 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 387 GKPSPAFNVEILDENGTILPPGQEGDIAVQVlpDRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSD 466
Cdd:PRK06155 346 GRLAPGFEARVVDEHDQELPDGEPGELLLRA--DEPFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 467 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeqlkkEIQEHVKKTTAPYKYPRK 546
Cdd:PRK06155 424 DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPV-----ALVRHCEPRLAYFAVPRY 498
|
490 500
....*....|....*....|....*...
gi 1958642407 547 IEFIEELPKTVSGKVKRNELRRKEWTTT 574
Cdd:PRK06155 499 VEFVAALPKTENGKVQKFVLREQGVTAD 526
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
82-568 |
3.81e-58 |
|
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: 199.88 E-value: 3.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 82 WSFEEL----GSLSRKFANILTeacslQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKC 157
Cdd:cd05912 2 YTFAELfeevSRLAEHLAALGV-----RKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 158 iitDDTlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhnelMAIYFTSGTTGPPKMIGHT-- 235
Cdd:cd05912 77 ---DDI-----------------------------------------------------ATIMYTSGTTGKPKGVQQTfg 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 236 -H------SSFGLGLSVNGRfWLDLIAsdvMWNTSdtgwaksAWSSVFSPWTQGACVFAHylPRFDSTSILQTLSKFPIT 308
Cdd:cd05912 101 nHwwsaigSALNLGLTEDDN-WLCALP---LFHIS-------GLSILMRSVIYGMTVYLV--DKFDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 309 VFCSAPTAYRMLIQnDITRSYKfNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTETV--LICGNFKGMKIKPGSM 386
Cdd:cd05912 168 IISVVPTMLQRLLE-ILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCsqIVTLSPEDALNKIGSA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 387 GKPSPAFNVEILDENGtilPPGQEGDIAVQ---VLPDrpfglfthYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVA 463
Cdd:cd05912 245 GKPLFPVELKIEDDGQ---PPYEVGEILLKgpnVTKG--------YLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 464 RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYklhDQEQLKKEIQEHVKKttapYKY 543
Cdd:cd05912 314 RRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKLAK----YKV 386
|
490 500
....*....|....*....|....*
gi 1958642407 544 PRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:cd05912 387 PKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
77-568 |
1.10e-57 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 200.86 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 77 GKEVRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 156
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 157 CIITDDTLAPAVDIVAAKCENLHSKLIVSqhsregwgnLKEMMKYASDShtCVDTKHNELMAIYFTSGTTGPPKMIGHTH 236
Cdd:PRK06839 103 VLFVEKTFQNMALSMQKVSYVQRVISITS---------LKEIEDRKIDN--FVEKNESASFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 237 SSFGLGlSVNGRFWLDLIASDV------MWNTSDTGWAksawssVFSPWTQGACVFahyLP-RFDSTSILQTLSKFPITV 309
Cdd:PRK06839 172 ENMFWN-ALNNTFAIDLTMHDRsivllpLFHIGGIGLF------AFPTLFAGGVII---VPrKFEPTKALSMIEKHKVTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 310 FCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTET-----VLICGNFKGmkiKPG 384
Cdd:PRK06839 242 VMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETsptvfMLSEEDARR---KVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 385 SMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVAR 464
Cdd:PRK06839 318 SIGKPVLFCDYELIDENKNKVEVGEVGELLI-----RGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 465 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqeqLKKEIQEHVKKTTAPYKYP 544
Cdd:PRK06839 393 KKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVL-----IEKDVIEHCRLFLAKYKIP 467
|
490 500
....*....|....*....|....
gi 1958642407 545 RKIEFIEELPKTVSGKVKRNELRR 568
Cdd:PRK06839 468 KEIVFLKELPKNATGKIQKAQLVN 491
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
63-568 |
8.40e-57 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 201.33 E-value: 8.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 63 KRLSNPAFWWVDGN-GKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPG- 137
Cdd:PRK10524 65 KRPEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihSVVFGGf 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 138 -TTQLTQkdilyRLQSSKSKCIITDDTLAPAVDIVAAK------CENLHSK----LIVSQhsregwgNLKEMMK------ 200
Cdd:PRK10524 144 aSHSLAA-----RIDDAKPVLIVSADAGSRGGKVVPYKplldeaIALAQHKprhvLLVDR-------GLAPMARvagrdv 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 201 -YAS------DSHT-CVDTKHNELMAIYFTSGTTGPPKMI-----GHThssFGLGLSVNGRFwlDLIASDVMWNTSDTGW 267
Cdd:PRK10524 212 dYATlraqhlGARVpVEWLESNEPSYILYTSGTTGKPKGVqrdtgGYA---VALATSMDTIF--GGKAGETFFCASDIGW 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 268 AKSAWSSVFSPWTQG-ACVFAHYLP-RFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDIT--RSYKFNSLKHCVSAGEP 343
Cdd:PRK10524 287 VVGHSYIVYAPLLAGmATIMYEGLPtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPAllRKHDLSSLRALFLAGEP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 344 INpEVMEQWKKKT-GLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFNVEILDEN-GTILPPGQEGDIAVQV 417
Cdd:PRK10524 367 LD-EPTASWISEAlGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 418 -LPdrPFGLFTHYVDNP---SKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 493
Cdd:PRK10524 446 pLP--PGCMQTVWGDDDrfvKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAE 523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642407 494 SAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQ---LKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVkrneLRR 568
Cdd:PRK10524 524 VAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKL----LRR 597
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
73-570 |
1.82e-56 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 197.11 E-value: 1.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 73 VDGNGKevrWSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 152
Cdd:PRK03640 22 EFEEKK---VTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 153 SKSKCIITDDTLApavdivaakcenlhSKLIVSQHSRegwgnLKEMMKYASDSHTCVDTKH-NELMAIYFTSGTTGPPKM 231
Cdd:PRK03640 98 AEVKCLITDDDFE--------------AKLIPGISVK-----FAELMNGPKEEAEIQEEFDlDEVATIMYTSGTTGKPKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 232 I-----GHTHSSFG----LGLSVNGRfWLdliASDVMWNTSdtgwaksAWSSVFSPWTQGACVFAHylPRFDSTSILQTL 302
Cdd:PRK03640 159 ViqtygNHWWSAVGsalnLGLTEDDC-WL---AAVPIFHIS-------GLSILMRSVIYGMRVVLV--EKFDAEKINKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 303 SKFPITVFCSAPTAYRMLIQNDITRSYKfNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTETV-LICG-NFKGMK 380
Cdd:PRK03640 226 QTGGVTIISVVSTMLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETAsQIVTlSPEDAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 381 IKPGSMGKPspAFNVEI-LDENGTILPPGQEGDIAVQ---VLPDrpfglfthYVDNPSKTASTLRGNFYITGDRGYMDED 456
Cdd:PRK03640 304 TKLGSAGKP--LFPCELkIEKDGVVVPPFEEGEIVVKgpnVTKG--------YLNREDATRETFQDGWFKTGDIGYLDEE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 457 GYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnpDYKLhDQEQLKKEIQEHVkk 536
Cdd:PRK03640 374 GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEV-TEEELRHFCEEKL-- 448
|
490 500 510
....*....|....*....|....*....|....
gi 1958642407 537 ttAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 570
Cdd:PRK03640 449 --AKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
83-566 |
9.63e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 197.19 E-value: 9.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:PRK06178 60 TYAELDELSDRFAALL-RQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 TLAPAVDIVAAKCEnLHSKLIVSQH--------------------SREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFT 222
Cdd:PRK06178 139 QLAPVVEQVRAETS-LRHVIVTSLAdvlpaeptlplpdslraprlAAAGAIDLLPALRACTAPVPLPPPALDALAALNYT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 223 SGTTGPPKMIGHTH-------SSFGlGLSVNGRfwldliASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahYLPRFDS 295
Cdd:PRK06178 218 GGTTGMPKGCEHTQrdmvytaAAAY-AVAVVGG------EDSVFLSFLPEFWIAGENFGLLFPLFSGATLV--LLARWDA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 296 TSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKH--CVSAGEPINPEVMEQWKKKTGLDIYEG-YGQTETvLI 372
Cdd:PRK06178 289 VAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQvrVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTET-HT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 373 CGNF-KGM-------KIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN 443
Cdd:PRK06178 368 CDTFtAGFqdddfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVV-----RTPSLLKGYWNKPEATAEALRDG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 444 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQ 523
Cdd:PRK06178 443 WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADL-TA 521
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958642407 524 EQLKKEIQEHVkkttAPYKYPrKIEFIEELPKTVSGKVKRNEL 566
Cdd:PRK06178 522 AALQAWCRENM----AVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
79-567 |
2.02e-54 |
|
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: 191.74 E-value: 2.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLApavdivaakcenlHSKLIVSQHSREGWgnlkemmKYASDSHtcvdtkhnELMAIYFTSGTTGPPKMIGHTHSS 238
Cdd:cd12118 106 FVDREFE-------------YEDLLAEGDPDFEW-------IPPADEW--------DPIALNYTSGTTGRPKGVVYHHRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 239 FglglsvngrfWLDLIASDVMWNTSD-------------TGWAksawssvfSPWTQGACVFAHY-LPRFDSTSILQTLSK 304
Cdd:cd12118 158 A----------YLNALANILEWEMKQhpvylwtlpmfhcNGWC--------FPWTVAAVGGTNVcLRKVDAKAIYDLIEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 305 FPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQwKKKTGLDIYEGYGQTET---VLICgnfkgmKI 381
Cdd:cd12118 220 HKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAK-MEELGFDVTHVYGLTETygpATVC------AW 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 382 KPGSMGKPSP---------------AFNVEILDENGTILPP--GQE-GDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN 443
Cdd:cd12118 293 KPEWDELPTEerarlkarqgvryvgLEEVDVLDPETMKPVPrdGKTiGEIVF-----RGNIVMKGYLKNPEATAEAFRGG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 444 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQ 523
Cdd:cd12118 368 WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1958642407 524 eqlkkEIQEHVKKTTAPYKYPRKIEFiEELPKTVSGKVKRNELR 567
Cdd:cd12118 448 -----EIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLR 485
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
50-567 |
3.93e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 192.91 E-value: 3.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 50 DVLDQwtNTEKTGKRlsnPAFWWVdgnGKEVrwSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLR 129
Cdd:PRK05605 36 DLYDN--AVARFGDR---PALDFF---GATT--TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 130 TGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAP---------------AVDIVAA------------------KCE 176
Cdd:PRK05605 105 LGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPtverlrrttpletivSVNMIAAmpllqrlalrlpipalrkARA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 177 NLHSKL-------IVSQHSREGWGNLKEMMKYASDShtcvdtkhneLMAIYFTSGTTGPPKMIGHTHSsfglGLSVN--- 246
Cdd:PRK05605 185 ALTGPApgtvpweTLVDAAIGGDGSDVSHPRPTPDD----------VALILYTSGTTGKPKGAQLTHR----NLFANaaq 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 247 GRFWLDLIASD----------------VMWNTsdtgwaksawssvFSPWTQGACVFahyLPRFDSTSILQTLSKFPITVF 310
Cdd:PRK05605 251 GKAWVPGLGDGpervlaalpmfhayglTLCLT-------------LAVSIGGELVL---LPAPDIDLILDAMKKHPPTWL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 311 CSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKP 389
Cdd:PRK05605 315 PGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 390 SPAFNVEILD-EN-GTILPPGQEGDIAV---QVlpdrpfglFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVAR 464
Cdd:PRK05605 395 FPDTEVRIVDpEDpDETMPDGEEGELLVrgpQV--------FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 465 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKkeiqEHVKKTTAPYKYP 544
Cdd:PRK05605 467 IKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAAL-DPEGLR----AYCREHLTRYKVP 541
|
570 580
....*....|....*....|...
gi 1958642407 545 RKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK05605 542 RRFYHVDELPRDQLGKVRRREVR 564
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
83-567 |
5.36e-54 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 192.16 E-value: 5.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:PRK07059 50 TYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 TLAPAVD-----------IVAAKCENLHSK-LIVSQHSRegwgNLKEMM----------------KYASDSHTCVDTKHN 214
Cdd:PRK07059 129 NFATTVQqvlaktavkhvVVASMGDLLGFKgHIVNFVVR----RVKKMVpawslpghvrfndalaEGARQTFKPVKLGPD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 215 ELMAIYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWNTSdtgWAKSAWSS---VFSPWTQGAC----VFA 287
Cdd:PRK07059 205 DVAFLQYTGGTTGVSKGATLLHRN---------------IVANVLQMEA---WLQPAFEKkprPDQLNFVCALplyhIFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 288 ---HYL--------------PRfDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVME 350
Cdd:PRK07059 267 ltvCGLlgmrtggrnilipnPR-DIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 351 QWKKKTGLDIYEGYGQTET--VLICGNFKGMKIKpGSMGKPSPAFNVEILDENGTILPPGQEGDIAV---QVLPDrpfgl 425
Cdd:PRK07059 346 RWLEMTGCPITEGYGLSETspVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIrgpQVMAG----- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 426 fthYVDNPSKTASTLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIR 504
Cdd:PRK07059 420 ---YWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHS 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642407 505 GEVVKAFIVLNpdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK07059 497 GEAVKLFVVKK------DPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
73-566 |
9.46e-54 |
|
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: 188.89 E-value: 9.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 73 VDGNGkevRWSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 152
Cdd:cd05930 7 VDGDQ---SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 153 SKSKCIITDdtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkHNELMAIYFTSGTTGPPKMI 232
Cdd:cd05930 83 SGAKLVLTD---------------------------------------------------PDDLAYVIYTSGSTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 233 GHTHSSFglglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLP---RFDSTSILQTLSKF 305
Cdd:cd05930 112 MVEHRGL-----VNLLLWmqeaYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATL--VVLPeevRKDPEALADLLAEE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 306 PITVFCSAPTAYRMLIQNDITRSykFNSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTETVLICGNF--KGMKIK 382
Cdd:cd05930 184 GITVLHLTPSLLRLLLQELELAA--LPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDATYYrvPPDDEE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 383 PGSM--GKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYM 453
Cdd:cd05930 262 DGRVpiGRPIPNTRVYVLDENLRPVPPGVPGELYI-----GGAGLARGYLNRPELTAERFVPNpfgpgerMYRTGDLVRW 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 454 DEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHdqeqlKKEIQEH 533
Cdd:cd05930 337 LPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD-----EEELRAH 411
|
490 500 510
....*....|....*....|....*....|...
gi 1958642407 534 VKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd05930 412 LAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
290-563 |
1.52e-53 |
|
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: 185.17 E-value: 1.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 290 LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHcVSAGEpiNPEVMEQWKKKTGLDIYEGYGQTET 369
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRH-VLGLD--APETIQRFEETTGATFWSLYGQTET 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 370 ---VLICGNFKgmkiKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYI 446
Cdd:cd17637 149 sglVTLSPYRE----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV-----RGPLVFQGYWNLPELTAYTFRNGWHH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 447 TGDRGYMDEDGYFWFVARS--DDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHdqe 524
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLT--- 296
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958642407 525 qlKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 563
Cdd:cd17637 297 --ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
66-572 |
5.17e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 189.04 E-value: 5.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 66 SNPAFWWVDGngkevRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIP-GTTQl 141
Cdd:PRK06188 27 DRPALVLGDT-----RLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrTALHPlGSLD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 142 tqkDILYRLQSSKSKCIITDDT--LAPAVDIvAAKCENLHSKLIVSQhSREGWGNLKEMMKYASDSHTCVDTkHNELMAI 219
Cdd:PRK06188 100 ---DHAYVLEDAGISTLIVDPApfVERALAL-LARVPSLKHVLTLGP-VPDGVDLLAAAAKFGPAPLVAAAL-PPDIAGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 220 YFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVF----------AHY 289
Cdd:PRK06188 174 AYTGGTTGKPKGVMGTHRS---------------IATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFflptllrggtVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 290 LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTE- 368
Cdd:PRK06188 239 LAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEa 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 369 ----TVLICGNFKGMKIKP-GSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN 443
Cdd:PRK06188 319 pmviTYLRKRDHDPDDPKRlTSCGRPTPGLRVALLDEDGREVAQGEVGEICV-----RGPLVMDGYWNRPEETAEAFRDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 444 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlHDQ 523
Cdd:PRK06188 394 WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAA-VDA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1958642407 524 EqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWT 572
Cdd:PRK06188 473 A----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWE 517
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
60-567 |
5.65e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 188.71 E-value: 5.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 60 KTGKRLSN-PAFWWvdgngKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGT 138
Cdd:PRK07470 15 QAARRFPDrIALVW-----GDRSWTWREIDARVDALAAALAAR-GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 139 TQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKL-IVSQHSREGWGNLkeMMKYASDSHTCVDTKHNELM 217
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVaIGGARAGLDYEAL--VARHLGARVANAAVDHDDPC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 218 AIYFTSGTTGPPKMIGHTHSSfgLGLSVNGRFwldliaSDVMWNTSDTGWaksawSSVFSPWTQGACVfaHYL------- 290
Cdd:PRK07470 167 WFFFTSGTTGRPKAAVLTHGQ--MAFVITNHL------ADLMPGTTEQDA-----SLVVAPLSHGAGI--HQLcqvarga 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 291 -------PRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEG 363
Cdd:PRK07470 232 atvllpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 364 YGQTE-----TVL-ICGNF--KGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPdrpfgLFTHYVDNPSK 435
Cdd:PRK07470 312 FGLGEvtgniTVLpPALHDaeDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPA-----VFAGYYNNPEA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 436 TASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 515
Cdd:PRK07470 387 NAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVAR 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1958642407 516 PDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK07470 467 DGAPVDEA-----ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
77-569 |
7.24e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 188.83 E-value: 7.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 77 GKEVRWSfeELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 156
Cdd:PRK07786 40 GNTTTWR--ELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 157 CIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTH 236
Cdd:PRK07786 117 VVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 237 SSfglglsVNGRFwLDLIASDVMWNTSDTGWAKS------AWSSVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPIT-V 309
Cdd:PRK07786 197 AN------LTGQA-MTCLRTNGADINSDVGFVGVplfhiaGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTgI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 310 FCsAPTAYRMLIQNDITRSYKFnSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTE----TVLICGNFKGMKIkpG 384
Cdd:PRK07786 270 FL-VPAQWQAVCAEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATfPEAQILAAFGQTEmspvTCMLLGEDAIRKL--G 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 385 SMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVAR 464
Cdd:PRK07786 346 SVGKVIPTVAARVVDENMNDVPVGEVGEIVY-----RAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 465 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLKKEIQEHVkkttAPYKYP 544
Cdd:PRK07786 421 KKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRL----ARYKHP 496
|
490 500
....*....|....*....|....*
gi 1958642407 545 RKIEFIEELPKTVSGKVKRNELRRK 569
Cdd:PRK07786 497 KALEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
83-570 |
9.34e-53 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 189.11 E-value: 9.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 TLAPAVDIVAAKCENLHSKL--IVSQHSReGWGNL--------KEMM-KY---ASDSHTCV------------DTKHNEL 216
Cdd:PRK08974 130 NFAHTLEKVVFKTPVKHVILtrMGDQLST-AKGTLvnfvvkyiKRLVpKYhlpDAISFRSAlhkgrrmqyvkpELVPEDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 217 MAIYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWntsdtgwAKSAWSSVFSPWTQGAC-------VFAHY 289
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRN---------------MLANLEQ-------AKAAYGPLLHPGKELVVtalplyhIFALT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 290 L-----------------PRfDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQW 352
Cdd:PRK08974 267 VncllfielggqnllitnPR-DIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERW 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 353 KKKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAV---QVLpdrpfglfTH 428
Cdd:PRK08974 346 VKLTGQYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVkgpQVM--------LG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 429 YVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVV 508
Cdd:PRK08974 418 YWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAV 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642407 509 KAFIVLNpdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 570
Cdd:PRK08974 498 KIFVVKK------DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
81-567 |
6.75e-52 |
|
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: 183.74 E-value: 6.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKipeWWLANV---ACLRTGTVLIPGTTQLTQKDILYRLQSSKSKC 157
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-GVGPGDVVAFQLPN---WWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 158 IITDDTlapavdivaakcenlhsklivsqhsregWGNlkemMKYASDShtcvdtkhNELMAIYFTSGTTGPPKMIGHTHS 237
Cdd:cd05903 77 FVVPER----------------------------FRQ----FDPAAMP--------DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 238 SfglgLSVNGRFWLDLIA---SDVMWNTSDTGWAKSAWSSVFSPWTQGACVfaHYLPRFDSTSILQTLSKFPITVFCSAP 314
Cdd:cd05903 117 T----LSASIRQYAERLGlgpGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKALALMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 315 TayrmlIQNDITRSYKF-----NSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICGNfkgmkIKPG----- 384
Cdd:cd05903 191 P-----FLTDLLNAVEEageplSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTS-----ITPApedrr 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 385 --SMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFV 462
Cdd:cd05903 261 lyTDGRPLPGVEIKVVDDTGATLAPGVEGELLS-----RGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRIT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 463 ARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEqlkkEIQEHV-KKTTAPY 541
Cdd:cd05903 336 GRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALL-TFD----ELVAYLdRQGVAKQ 410
|
490 500
....*....|....*....|....*.
gi 1958642407 542 KYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:cd05903 411 YWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
74-567 |
2.65e-51 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 184.12 E-value: 2.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 74 DGNGKEVRWSFEELGSLSRKFANiLTEACSLQRGDRVMVILPKIPEW---WLAnVACLrtGTVLIPGTTQLTQKDILYRL 150
Cdd:PRK08008 30 SSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFifcWFG-LAKI--GAIMVPINARLLREESAWIL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 151 QSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSqhsREGWGNLKEMMKYAS--DSHTCVDTKHNELMA-----IYFTS 223
Cdd:PRK08008 106 QNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLT---RVALPADDGVSSFTQlkAQQPATLCYAPPLSTddtaeILFTS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 224 GTTGPPKMIGHTHSsfglglsvNGRF------W-LDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFDST 296
Cdd:PRK08008 183 GTTSRPKGVVITHY--------NLRFagyysaWqCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVL--LEKYSAR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 297 SILQTLSKFPITVFCSAPtayrMLIQNDITRSYKFNSLKHCVSagepinpEVM------EQWK----KKTGLDIYEGYGQ 366
Cdd:PRK08008 253 AFWGQVCKYRATITECIP----MMIRTLMVQPPSANDRQHCLR-------EVMfylnlsDQEKdafeERFGVRLLTSYGM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 367 TETVL-ICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPDRPfgLFTHYVDNPSKTASTLRGNFY 445
Cdd:PRK08008 322 TETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKT--IFKEYYLDPKATAKVLEADGW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 446 I-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQe 524
Cdd:PRK08008 400 LhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE- 478
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958642407 525 qlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK08008 479 ----EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
83-567 |
3.87e-51 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 184.70 E-value: 3.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 TLAPAVDIVAAKCE---------------------NL---HSKLIVSQHSREGWGNLKEMMKYASdSHTC--VDTKHNEL 216
Cdd:PRK08751 132 NFGTTVQQVIADTPvkqvittglgdmlgfpkaalvNFvvkYVKKLVPEYRINGAIRFREALALGR-KHSMptLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 217 MAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRfWLD-----------LIASDVMWNTsdtgWAKSAWSSVFSPWtqGACV 285
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-WLAgtgkleegcevVITALPLYHI----FALTANGLVFMKI--GGCN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 286 FAHYLPRfDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYG 365
Cdd:PRK08751 284 HLISNPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 366 QTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAV---QVLPDrpfglfthYVDNPSKTASTLR 441
Cdd:PRK08751 363 LTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIkgpQVMKG--------YWKRPEETAKVMD 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 442 GNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdykl 520
Cdd:PRK08751 435 ADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK----- 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1958642407 521 hDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK08751 510 -DPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
79-567 |
4.88e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 181.51 E-value: 4.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 I------TDDTLAPAVDIV---------AAKCENL-HSKLIVSQHSRE-----GWGNLKEMMKYASDSHTCVDT---KHN 214
Cdd:PRK12583 122 IcadafkTSDYHAMLQELLpglaegqpgALACERLpELRGVVSLAPAPppgflAWHELQARGETVSREALAERQaslDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 215 ELMAIYFTSGTTGPPKMIGHTHSSfglgLSVNGRF---WLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahyLP 291
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHN----ILNNGYFvaeSLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLV---YP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 292 R--FDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL-DIYEGYGQTE 368
Cdd:PRK12583 275 NeaFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 369 T---VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFY 445
Cdd:PRK12583 355 TspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCT-----RGYSVMKGYWNNPEATAESIDEDGW 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 446 I-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQe 524
Cdd:PRK12583 430 MhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE- 508
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958642407 525 qlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK12583 509 ----ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
83-572 |
9.86e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 179.50 E-value: 9.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 TLAPAVDIVAAKCENLHSKLIVSQH-SREGWGNLKEMMKYASDshTCVDTKhNELMAIYFTSGTTGPPKMIGHTHSSFGL 241
Cdd:PRK13391 105 AKLDVARALLKQCPGVRHRLVLDGDgELEGFVGYAEAVAGLPA--TPIADE-SLGTDMLYSSGTTGRPKGIKRPLPEQPP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 242 GLSVNgrfWLDLIASdvMWN-TSDTGW---------AKSAWSSVfspwTQ--GACVFAhyLPRFDSTSILQTLSKFPITV 309
Cdd:PRK13391 182 DTPLP---LTAFLQR--LWGfRSDMVYlspaplyhsAPQRAVML----VIrlGGTVIV--MEHFDAEQYLALIEEYGVTH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 310 FCSAPTAY-RML-IQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLICG-NFKGMKIKPGSM 386
Cdd:PRK13391 251 TQLVPTMFsRMLkLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTAcDSEEWLAHPGTV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 387 GKPSPAfNVEILDENGTILPPGQEGDIAVQvlPDRPFglftHYVDNPSKTASTL--RGNFYITGDRGYMDEDGYFWFVAR 464
Cdd:PRK13391 331 GRAMFG-DLHILDDDGAELPPGEPGTIWFE--GGRPF----EYLNDPAKTAEARhpDGTWSTVGDIGYVDEDGYLYLTDR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 465 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyKLHDQEQLKKEIQEHVKKTTAPYKYP 544
Cdd:PRK13391 404 AAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVD--GVDPGPALAAELIAFCRQRLSRQKCP 481
|
490 500
....*....|....*....|....*...
gi 1958642407 545 RKIEFIEELPKTVSGKVKRNELRRKEWT 572
Cdd:PRK13391 482 RSIDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
80-570 |
2.30e-49 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 180.92 E-value: 2.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 80 VRWSFEELgsLSR--KFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVlIPGTTQLTQKDILYRLQSSKSKC 157
Cdd:PRK07529 57 ETWTYAEL--LADvtRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 158 IIT-----DDTLAPAVDIVAAKCENLhsKLIVSQHSREGWGNLK--------------------EMMKYASDSHTCVDTK 212
Cdd:PRK07529 133 LVTlgpfpGTDIWQKVAEVLAALPEL--RTVVEVDLARYLPGPKrlavplirrkaharildfdaELARQPGDRLFSGRPI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 213 HNELMAIYF-TSGTTGPPKMIGHTHSsfglGLSVNGrfWLdlIASDVMWNTSDTGWA-------KSAWSSVFSPWTQGA- 283
Cdd:PRK07529 211 GPDDVAAYFhTGGTTGMPKLAQHTHG----NEVANA--WL--GALLLGLGPGDTVFCglplfhvNALLVTGLAPLARGAh 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 284 CVFA--------HYLPRFdsTSILQtlsKFPITVFCSAPTAYRMLIQ-----NDITrsykfnSLKHCVSAGEPINPEVME 350
Cdd:PRK07529 283 VVLAtpqgyrgpGVIANF--WKIVE---RYRINFLSGVPTVYAALLQvpvdgHDIS------SLRYALCGAAPLPVEVFR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 351 QWKKKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFNVEI--LDENGTIL---PPGQEGDIAVQvlpdRPfG 424
Cdd:PRK07529 352 RFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVviLDDAGRYLrdcAVDEVGVLCIA----GP-N 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 425 LFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIR 504
Cdd:PRK07529 427 VFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHA 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642407 505 GEVVKAFIVLNPDYKLhDQEQLKKEIQEHVKKTTApykYPRKIEFIEELPKTVSGKVKRNELRRKE 570
Cdd:PRK07529 507 GELPVAYVQLKPGASA-TEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
46-570 |
3.42e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 179.19 E-value: 3.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 46 NFAKDV----------LDQWTNT----EKTGKRLSN-PAFWWVdgnGKEVRWSfeELGSLSRKFANILTEACSLQRGDRV 110
Cdd:PRK05677 4 NFWKDKypagiaaeinPDEYPNIqavlKQSCQRFADkPAFSNL---GKTLTYG--ELYKLSGAFAAWLQQHTDLKPGDRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 111 MVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLA-------PAVDI---VAAKCENLHS 180
Cdd:PRK05677 79 AVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAhlaekvlPKTGVkhvIVTEVADMLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 181 ---------------KLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSsfglglsv 245
Cdd:PRK05677 159 plkrllinavvkhvkKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHR-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 246 ngrfwlDLIASDVMWNTSDTGWAKSAWSSVFSP--------WTQGaCVF-----AHYL----PRfDSTSILQTLSKFPIT 308
Cdd:PRK05677 231 ------NLVANMLQCRALMGSNLNEGCEILIAPlplyhiyaFTFH-CMAmmligNHNIlisnPR-DLPAMVKELGKWKFS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 309 VFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMG 387
Cdd:PRK05677 303 GFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQ-AIQVGTIG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 388 KPSPAFNVEILDENGTILPPGQEGDIAV---QVLPDrpfglfthYVDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVA 463
Cdd:PRK05677 382 IPVPSTLCKVIDDDGNELPLGEVGELCVkgpQVMKG--------YWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 464 RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKkeiqEHVKKTTAPYKY 543
Cdd:PRK05677 454 RKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETL-TKEQVM----EHMRANLTGYKV 528
|
570 580
....*....|....*....|....*..
gi 1958642407 544 PRKIEFIEELPKTVSGKVKRNELRRKE 570
Cdd:PRK05677 529 PKAVEFRDELPTTNVGKILRRELRDEE 555
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-567 |
5.25e-49 |
|
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: 173.62 E-value: 5.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPKMIGHTHSSFglglsVNGRFwldlIASDVMWNTSDT------------GWAKSAWSSVfspwTQGA-CV 285
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNI-----VNNGY----FIGERLGLTEQDrlcipvplfhcfGSVLGVLACL----THGAtMV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 286 FAHylPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL-DIYEGY 364
Cdd:cd05917 74 FPS--PSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 365 GQTETVLICgnFKGMKIKP-----GSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS 438
Cdd:cd05917 152 GMTETSPVS--TQTRTDDSiekrvNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCI-----RGYSVMKGYWNDPEKTAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 439 TLRG-NFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 517
Cdd:cd05917 225 AIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEG 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958642407 518 YKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:cd05917 305 AELTEE-----DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
74-567 |
1.19e-48 |
|
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: 176.67 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 74 DGNGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILpkipeW--------WLAnVAClrTGTVLIPGTTQLTQKD 145
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLA-----WnthrhlelYYA-VPG--MGAVLHTINPRLFPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 146 ILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSR------EGWGNLKEMMKYASDSHTCVDTKHNELMAI 219
Cdd:cd12119 89 IAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 220 YFTSGTTGPPKMIGHTHSSFGLG-LSVNGRFWLDLIASDV------MWNTSdtgwaksAWSSVFSPWTQGACvfaHYLP- 291
Cdd:cd12119 169 CYTSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGLSESDVvlpvvpMFHVN-------AWGLPYAAAMVGAK---LVLPg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 292 -RFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQTET- 369
Cdd:cd12119 239 pYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETs 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 370 -VLICGnfkgmKIKPG--------------SMGKPSPAFNVEILDENGTILP--PGQEGDIAVQvlpdRPFgLFTHYVDN 432
Cdd:cd12119 318 pLGTVA-----RPPSEhsnlsedeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVR----GPW-VTKSYYKN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 433 PSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFI 512
Cdd:cd12119 388 DEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVV 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1958642407 513 VLNPdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:cd12119 468 VLKE-----GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
83-567 |
2.10e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 175.97 E-value: 2.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITdd 162
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 tlAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTcvDTKHNELMaiYFTSGTTGPPKMI-----GHTHS 237
Cdd:PRK13390 103 --SAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLT--EQPCGAVM--LYSSGTTGFPKGIqpdlpGRDVD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 238 SFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKS-AWSSVFSPwTQGACVFAHylpRFDSTSILQTLSKFPITVFCSAPTA 316
Cdd:PRK13390 177 APGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHA-LGGTVVLAK---RFDAQATLGHVERYRITVTQMVPTM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 317 Y-RMLIQNDITRS-YKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTE----TVLICGNFKGmkiKPGSMGKpS 390
Cdd:PRK13390 253 FvRLLKLDADVRTrYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFIDSPDWLA---HPGSVGR-S 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 391 PAFNVEILDENGTILPPGQEGDIAVQvlPDR-PFglftHYVDNPSKTASTLRGN--FYIT-GDRGYMDEDGYFWFVARSD 466
Cdd:PRK13390 329 VLGDLHICDDDGNELPAGRIGTVYFE--RDRlPF----RYLNDPEKTAAAQHPAhpFWTTvGDLGSVDEDGYLYLADRKS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 467 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDykLHDQEQLKKEIQEHVKKTTAPYKYPRK 546
Cdd:PRK13390 403 FMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEG--IRGSDELARELIDYTRSRIAHYKAPRS 480
|
490 500
....*....|....*....|.
gi 1958642407 547 IEFIEELPKTVSGKVKRNELR 567
Cdd:PRK13390 481 VEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
219-569 |
2.43e-48 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 176.49 E-value: 2.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPKmiGHTHSSFGlGLSVngrfwldliASDVMwntSDTGWAKSAWSSVFSP----WTQGACVFAHYLP--- 291
Cdd:PRK13382 201 ILLTSGTTGTPK--GARRSGPG-GIGT---------LKAIL---DRTPWRAEEPTVIVAPmfhaWGFSQLVLAASLActi 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 292 ----RFDSTSILQTLSKFPITVFCSAPTAYR--MLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYG 365
Cdd:PRK13382 266 vtrrRFDPEATLDLIDRHRATGLAVVPVMFDriMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYN 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 366 QTETVLIC-GNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVdnPSKTASTLRGnF 444
Cdd:PRK13382 346 ATEAGMIAtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFV-----RNDTQFDGYT--SGSTKDFHDG-F 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 445 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqe 524
Cdd:PRK13382 418 MASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASA---- 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958642407 525 qLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRK 569
Cdd:PRK13382 494 -TPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
81-571 |
6.69e-48 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 175.32 E-value: 6.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 160
Cdd:PRK06087 49 SYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 161 D-------------------DTLAPAVDIVAAKCEnlHSKLIVSQhsregwgnlkEMMKYASDSHTCvDTKHNELMAIYF 221
Cdd:PRK06087 128 PtlfkqtrpvdlilplqnqlPQLQQIVGVDKLAPA--TSSLSLSQ----------IIADYEPLTTAI-TTHGDELAAVLF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 222 TSGTTGPPKMIGHTHSSFGLG-LSVNGRfwLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahYLPRFDSTSILQ 300
Cdd:PRK06087 195 TSGTEGLPKGVMLTHNNILASeRAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSV--LLDIFTPDACLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 301 TLSKFPITVFCSA-PTAYRML--IQNDitrSYKFNSLKHCVSAGEPInPEVMEQWKKKTGLDIYEGYGQTETV--LICGN 375
Cdd:PRK06087 271 LLEQQRCTCMLGAtPFIYDLLnlLEKQ---PADLSALRFFLCGGTTI-PKKVARECQQRGIKLLSVYGSTESSphAVVNL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 376 FKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAvqvlpDRPFGLFTHYVDNPSKTASTL--RGNFYiTGDRGYM 453
Cdd:PRK06087 347 DDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEA-----SRGPNVFMGYLDEPELTARALdeEGWYY-SGDLCRM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 454 DEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEqlkkEIQEH 533
Cdd:PRK06087 421 DEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLE----EVVAF 496
|
490 500 510
....*....|....*....|....*....|....*....
gi 1958642407 534 V-KKTTAPYKYPRKIEFIEELPKTVSGKVKRNELrRKEW 571
Cdd:PRK06087 497 FsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL-RKDI 534
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
104-567 |
3.30e-47 |
|
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: 171.47 E-value: 3.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 104 LQRGDRVMVILPKIPE--WWLANV--ACLRTGTVLIPGTTQLTQKDILYrlqsskskcIITDdtLAPAVDIVAAKCENlH 179
Cdd:cd05922 15 GVRGERVVLILPNRFTyiELSFAVayAGGRLGLVFVPLNPTLKESVLRY---------LVAD--AGGRIVLADAGAAD-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 180 SKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRfwLDLIASDV 258
Cdd:cd05922 83 LRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANArSIAEY--LGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 259 MWNTSDTGWAkSAWSSVFSPWTQGACVFAHYLPRFDSTsILQTLSKFPITVFCSAPTAYRMLIQNDITRSyKFNSLKHCV 338
Cdd:cd05922 161 ALTVLPLSYD-YGLSVLNTHLLRGATLVLTNDGVLDDA-FWEDLREHGATGLAGVPSTYAMLTRLGFDPA-KLPSLRYLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 339 SAGEPINPEVMEQWKKK-TGLDIYEGYGQTETvlicgnFKGMKI--------KPGSMGKPSPAFNVEILDENGTILPPGQ 409
Cdd:cd05922 238 QAGGRLPQETIARLRELlPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGTPTPPGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 410 EGDIAVQvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHP 489
Cdd:cd05922 312 PGEIVHR----GPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642407 490 SIAESAVVSSPDPIrGEVVKAFIVLNPDYKLHDqeqlkkeIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:cd05922 388 LIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-------VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
59-569 |
5.54e-47 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 172.47 E-value: 5.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 59 EKTGKRLSNPAFwwVDGNGKEVrWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGT 138
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGATGRV-YTYADVELLSRRVAAGL-HKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 139 TQLTQKDILYRLQSSKSKCIITddtLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMA 218
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPKMIGHTHSsfGLGLSV---------NgrfwLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhy 289
Cdd:PLN02246 184 LPYSSGTTGLPKGVMLTHK--GLVTSVaqqvdgenpN----LYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI-- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 290 LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIY-EGYGQTE 368
Cdd:PLN02246 256 MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 369 --TVL-ICGNF--KGMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTL-R 441
Cdd:PLN02246 336 agPVLaMCLAFakEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICI-----RGPQIMKGYLNDPEATANTIdK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 442 GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLH 521
Cdd:PLN02246 411 DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEIT 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1958642407 522 DQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRK 569
Cdd:PLN02246 491 ED-----EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
291-571 |
9.29e-47 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 171.42 E-value: 9.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 291 PRFDSTSILQTLSKFPITVFCSAPTAY-RML-IQNDITRSYKFNSLKHCVSAGEPINPEV----MEQWkkktGLDIYEGY 364
Cdd:PRK12406 228 PRFDPEELLQLIERHRITHMHMVPTMFiRLLkLPEEVRAKYDVSSLRHVIHAAAPCPADVkramIEWW----GPVIYEYY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 365 GQTET--VLICGNFKGMKiKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQV--LPDrpfglFThYVDNPSKTASTL 440
Cdd:PRK12406 304 GSTESgaVTFATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIagNPD-----FT-YHNKPEKRAEID 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 441 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKL 520
Cdd:PRK12406 377 RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATL 456
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958642407 521 hDQEqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEW 571
Cdd:PRK12406 457 -DEA----DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYW 502
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
68-566 |
1.07e-46 |
|
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: 169.74 E-value: 1.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 68 PAFWWvdgngKEVRWSFEELGSLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKdil 147
Cdd:cd05945 8 PAVVE-----GGRTLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 148 yRLQSskskcIItdDTLAPAVDIVAAkcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTG 227
Cdd:cd05945 79 -RIRE-----IL--DAAKPALLIADG----------------------------------------DDNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 228 PPKMIGHTHS---SFGLGLsvNGRFwlDLIASDVMWNTSDtgwaksaWS---SVFS---PWTQGACVFAhyLPR---FDS 295
Cdd:cd05945 111 RPKGVQISHDnlvSFTNWM--LSDF--PLGPGDVFLNQAP-------FSfdlSVMDlypALASGATLVP--VPRdatADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 296 TSILQTLSKFPITVFCSAPTAYRMLIqnditRSYKFN-----SLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTET 369
Cdd:cd05945 178 KQLFRFLAEHGITVWVSTPSFAAMCL-----LSPTFTpeslpSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 370 VLICgnfKGMKIKPGSM--------GKPSPAFNVEILDENGTILPPGQEGDIAV---QVlpdrpfglFTHYVDNPSKTAS 438
Cdd:cd05945 253 TVAV---TYIEVTPEVLdgydrlpiGYAKPGAKLVILDEDGRPVPPGEKGELVIsgpSV--------SKGYLNNPEKTAA 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 439 TLRGNF----YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVL 514
Cdd:cd05945 322 AFFPDEgqraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVP 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1958642407 515 NPdyklHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd05945 402 KP----GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
213-568 |
1.19e-46 |
|
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: 167.27 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 213 HNELMAIYFTSGTTGPPKMIGHTHSSF---GLGLSVNGRFWLDliasDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAH 288
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEvynAWMLALNSLFDPD----DVLLCGLPLFHVNGSVVTLLTPLASGAhVVLAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 289 YLPRFDST---SILQTLSKFPITVFCSAPTAYRMLIQNDITRSykFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYG 365
Cdd:cd05944 77 PAGYRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNAD--ISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 366 QTE-TVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGT---ILP--PGQEGDIAVQvlpdRPfGLFTHYVDNPSKTAST 439
Cdd:cd05944 155 LTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVgrlLRDcaPDEVGEICVA----GP-GVFGGYLYTEGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 440 LRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYK 519
Cdd:cd05944 230 VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958642407 520 LhDQEQLKKEIQEHVKKTTApykYPRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:cd05944 310 V-EEEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
69-568 |
3.24e-46 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 172.39 E-value: 3.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 69 AFWWvDGN--GKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDI 146
Cdd:PLN02654 107 AIYW-EGNepGFDASLTYSELLDRVCQLANYL-KDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 147 LYRLQSSKSKCIITDDTLAPAV------DIV-AAKCENLHSKLIV---------SQHSREG--WGNLKEMM------KYA 202
Cdd:PLN02654 185 AQRIVDCKPKVVITCNAVKRGPktinlkDIVdAALDESAKNGVSVgicltyenqLAMKREDtkWQEGRDVWwqdvvpNYP 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 203 SDSHTCVDTKHNELMAIYfTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG 282
Cdd:PLN02654 265 TKCEVEWVDAEDPLFLLY-TSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNG 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 283 ACVFA-HYLPRF-DSTSILQTLSKFPITVFCSAPTAYRMLIQND---ITRsYKFNSLKHCVSAGEPINPEVMEQWKKKTG 357
Cdd:PLN02654 344 ATVLVfEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTR-HSRKSLRVLGSVGEPINPSAWRWFFNVVG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 358 ---LDIYEGYGQTETvlicGNFKGMKI------KPGSmgKPSPAFNVE--ILDENGTILPPGQEGDIAVQvlPDRPFGLF 426
Cdd:PLN02654 423 dsrCPISDTWWQTET----GGFMITPLpgawpqKPGS--ATFPFFGVQpvIVDEKGKEIEGECSGYLCVK--KSWPGAFR 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 427 THYVDNPSKTASTLR--GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIR 504
Cdd:PLN02654 495 TLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVK 574
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642407 505 GEVVKAFIVLNPDYKLhdQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:PLN02654 575 GQGIYAFVTLVEGVPY--SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
79-567 |
5.69e-46 |
|
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: 169.63 E-value: 5.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEAL-KKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDIVAAKceNLHSKLIVSQHSREGWGNLKEMMKYASdSHTCVD-----------TKHNELMAIYFTSGTTG 227
Cdd:cd17642 121 FCSKKGLQKVLNVQKK--LKIIKTIIILDSKEDYKGYQCLYTFIT-QNLPPGfneydfkppsfDRDEQVALIMNSSGSTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 228 PPKMIGHTHSSFGLGLSVngrfwldliASDVMWntsdtGWAKSAWSSVFS--PWTQG---------ACVFAH--YLPRFD 294
Cdd:cd17642 198 LPKGVQLTHKNIVARFSH---------ARDPIF-----GNQIIPDTAILTviPFHHGfgmfttlgyLICGFRvvLMYKFE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 295 STSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD-IYEGYGQTET---V 370
Cdd:cd17642 264 EELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETtsaI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 371 LICGNfkgMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYI-TG 448
Cdd:cd17642 344 LITPE---GDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCV-----KGPMIMKGYVNNPEATKALIDKDGWLhSG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 449 DRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyklHDQEQLKK 528
Cdd:cd17642 416 DIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLE-----AGKTMTEK 490
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1958642407 529 EIQEHVKKTTAPYKYPR-KIEFIEELPKTVSGKVKRNELR 567
Cdd:cd17642 491 EVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
83-570 |
5.71e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 170.11 E-value: 5.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEAcSLQRGDRVMViLPKIPEWW-LANVACLRTGTVLI-----PGTTQLtqKDILYRLqssKSK 156
Cdd:PRK07788 76 TYAELDEQSNALARGLLAL-GVRAGDGVAV-LARNHRGFvLALYAAGKVGARIIllntgFSGPQL--AEVAARE---GVK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 157 CIITDDTLAPAVDIVAAKCENLHSkLIVS----QHSREGWGNLKEMMKYASDSHTCVDTKHNELmaIYFTSGTTGPPKMI 232
Cdd:PRK07788 149 ALVYDDEFTDLLSALPPDLGRLRA-WGGNpdddEPSGSTDETLDDLIAGSSTAPLPKPPKPGGI--VILTSGTTGTPKGA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 233 GHTHSSfglGLSVNGRFwLDLI---ASDVMWNTS----DTGWAKSAWSsvfspWTQGACVFAHYlpRFDSTSILQTLSKF 305
Cdd:PRK07788 226 PRPEPS---PLAPLAGL-LSRVpfrAGETTLLPApmfhATGWAHLTLA-----MALGSTVVLRR--RFDPEATLEDIAKH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 306 PITVFCSAPTAY-RMLIQNDITRS-YKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTE----TVlicGNFKGM 379
Cdd:PRK07788 295 KATALVVVPVMLsRILDLGPEVLAkYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvafaTI---ATPEDL 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 380 KIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKtaSTLRGnFYITGDRGYMDEDGYf 459
Cdd:PRK07788 372 AEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFV-----GNGFPFEGYTDGRDK--QIIDG-LLSSGDVGYFDEDGL- 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 460 WFVA-RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHdqeqlKKEIQEHVKKTT 538
Cdd:PRK07788 443 LFVDgRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALD-----EDAIKDYVRDNL 517
|
490 500 510
....*....|....*....|....*....|..
gi 1958642407 539 APYKYPRKIEFIEELPKTVSGKVKRNELRRKE 570
Cdd:PRK07788 518 ARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
218-567 |
4.58e-45 |
|
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: 166.01 E-value: 4.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 218 AIYFTSGTTGPPKMIGHTHSsFGLGLSVNGRFWLDLIasdvmwntsdtGWakSAWSSVFSPWT------QGACVFAHYL- 290
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLP-GGPPDNDTLMAAALGF-----------GP--GADSVYLSPAPlyhaapFRWSMTALFMg 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 291 ------PRFDSTSILQTLSKFPITVFCSAPTAY-RMLIQNDITR-SYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYE 362
Cdd:cd05929 195 gtlvlmEKFDPEEFLRLIERYRVTFAQFVPTMFvRLLKLPEAVRnAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 363 GYGQTETV-LICGNFKGMKIKPGSMGKPSPAfNVEILDENGTILPPGQEGDiaVQVLPDRPFglftHYVDNPSKTA-STL 440
Cdd:cd05929 275 YYGGTEGQgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGE--VYFANGPGF----EYTNDPEKTAaARN 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 441 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAfiVLNPDYKL 520
Cdd:cd05929 348 EGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGA 425
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958642407 521 HDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:cd05929 426 DAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
74-568 |
5.34e-45 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 167.15 E-value: 5.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 74 DGNGKEVRWSFEELGSLSRKFANILTEaCSLQRGDrvmVILPKIPEWWLANV---ACLRTGTVLIPGTTQLTQKDILYRL 150
Cdd:PRK13295 48 LGTGAPRRFTYRELAALVDRVAVGLAR-LGVGRGD---VVSCQLPNWWEFTVlylACSRIGAVLNPLMPIFRERELSFML 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 151 QSSKSKCIItddtlAPAV----DIvAAKCENLHSKLIVSQH----SREGWGNLKEMM-----KYASDSHTCVDTKH---N 214
Cdd:PRK13295 124 KHAESKVLV-----VPKTfrgfDH-AAMARRLRPELPALRHvvvvGGDGADSFEALLitpawEQEPDAPAILARLRpgpD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 215 ELMAIYFTSGTTGPPKMIGHTHSS-FGLGLSVNGRfwLDLIASDVMWNTS----DTGWAKSAwssvFSPWTQGACVFahY 289
Cdd:PRK13295 198 DVTQLIYTSGTTGEPKGVMHTANTlMANIVPYAER--LGLGADDVILMASpmahQTGFMYGL----MMPVMLGATAV--L 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 290 LPRFDSTSILQTLSKFPITvFCSAPTAYRMliqnDITRSYK-----FNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGY 364
Cdd:PRK13295 270 QDIWDPARAAELIRTEGVT-FTMASTPFLT----DLTRAVKesgrpVSSLRTFLCAGAPIPGALVERARAALGAKIVSAW 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 365 GQTETVLICGnfkgmkIKPG--------SMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKT 436
Cdd:PRK13295 345 GMTENGAVTL------TKLDdpderastTDGCPLPGVEVRVVDADGAPLPAGQIGRLQV-----RGCSNFGGYLKRPQLN 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 437 ASTLRGnFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNP 516
Cdd:PRK13295 414 GTDADG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRP 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1958642407 517 DYKLhDQEQLKKEIQEHvkKTTAPYkYPRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:PRK13295 493 GQSL-DFEEMVEFLKAQ--KVAKQY-IPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
83-567 |
6.32e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 163.13 E-value: 6.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:PRK06145 29 SYAEFHQRILQAAGML-HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 TLAPAVDIVaakcenlHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTkhnELMAIYFTSGTTGPPKMIGHTHSSF--- 239
Cdd:PRK06145 108 EFDAIVALE-------TPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPT---DLVRLMYTSGTTDRPKGVMHSYGNLhwk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 240 ------GLGLSVNGRFW----------LDLIASDVMWntsdtgwaksawssvfspwtQGACVFAHYlpRFDSTSILQTLS 303
Cdd:PRK06145 178 sidhviALGLTASERLLvvgplyhvgaFDLPGIAVLW--------------------VGGTLRIHR--EFDPEAVLAAIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 304 KFPITVFCSAPTAY-RMLIQNDITRsYKFNSLKHCVSAGEPiNPE--VMEQWKKKTGLDIYEGYGQTETvliCGNFKGMK 380
Cdd:PRK06145 236 RHRLTCAWMAPVMLsRVLTVPDRDR-FDLDSLAWCIGGGEK-TPEsrIRDFTRVFTRARYIDAYGLTET---CSGDTLME 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 381 I-----KPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDE 455
Cdd:PRK06145 311 AgreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICM-----RGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 456 DGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHdqeqlKKEIQEHVK 535
Cdd:PRK06145 386 EGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT-----LEALDRHCR 460
|
490 500 510
....*....|....*....|....*....|..
gi 1958642407 536 KTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK06145 461 QRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
82-574 |
6.66e-44 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 164.38 E-value: 6.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 82 WSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 161
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 162 DTlapavdiVAAKCENLHSKLIV-SQHSREGWGNLKEMMKyASDShtCVDTKHNE------LMAIYFTSGTTGPPKMIGH 234
Cdd:PLN02330 135 DT-------NYGKVKGLGLPVIVlGEEKIEGAVNWKELLE-AADR--AGDTSDNEeilqtdLCALPFSSGTTGISKGVML 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 235 TH---------SSFGLGLSVNGRF-WLDLIASDVMWNTSDTGWAKSAwssvfspwTQGACVFahyLPRFDSTSILQTLSK 304
Cdd:PLN02330 205 THrnlvanlcsSLFSVGPEMIGQVvTLGLIPFFHIYGITGICCATLR--------NKGKVVV---MSRFELRTFLNALIT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 305 FPITVFCSAPTAYRMLIQNDITRSYKFNSLK--HCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTETVLICGNF----K 377
Cdd:PLN02330 274 QEVSFAPIVPPIILNLVKNPIVEEFDLSKLKlqAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITLTHgdpeK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 378 GMKI-KPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMD 454
Cdd:PLN02330 354 GHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCV-----RSQCVMQGYYNNKEETDRTIDEDGWLhTGDIGYID 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 455 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhdqeQLKKEIQEHV 534
Cdd:PLN02330 429 DDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAK-----ESEEDILNFV 503
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1958642407 535 KKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTTT 574
Cdd:PLN02330 504 AANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSIN 543
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
83-496 |
1.70e-43 |
|
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: 160.12 E-value: 1.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqLtqkDILY---RLQS----SKS 155
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP----L---DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 156 KCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSRegwgnlkemmkyASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHT 235
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDDA------------PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 236 HSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHY--LPRFDSTSILQTLSKFPITVFCSA 313
Cdd:TIGR01733 142 HRSLVNLLAWLARRY-GLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPedEERDDAALLAALIAEHPVTVLNLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 314 PTAYRMLIQNDITRsykFNSLKHCVSAGEPINPEVMEQWKKKTG-LDIYEGYGQTETVLICGnfkgMKIKPGSM------ 386
Cdd:TIGR01733 220 PSLLALLAAALPPA---LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWST----ATLVDPDDapresp 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 387 ---GKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTA---------STLRGNFYITGDRGYMD 454
Cdd:TIGR01733 293 vpiGRPLANTRLYVLDDDLRPVPVGVVGELYI-----GGPGVARGYLNRPELTAerfvpdpfaGGDGARLYRTGDLVRYL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958642407 455 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAV 496
Cdd:TIGR01733 368 PDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
219-568 |
7.21e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 154.38 E-value: 7.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPKmighthssfGLGLSVNGrfwldlIASDVmwntsdTGWAKsAWSsvfspWTqGACVFAHYLP------- 291
Cdd:PRK07787 133 IVYTSGTTGPPK---------GVVLSRRA------IAADL------DALAE-AWQ-----WT-ADDVLVHGLPlfhvhgl 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 292 ------------------RFDSTSILQTLSkFPITVFCSAPTAY-RmlIQNDITRSYKFNSLKHCVSAGEPINPEVMEQW 352
Cdd:PRK07787 185 vlgvlgplrignrfvhtgRPTPEAYAQALS-EGGTLYFGVPTVWsR--IAADPEAARALRGARLLVSGSAALPVPVFDRL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 353 KKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVlpdRPFGLFTHYVDN 432
Cdd:PRK07787 262 AALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETVGELQV---RGPTLFDGYLNR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 433 PSKTASTLRGN-FYITGDRGYMDEDGYFWFVAR-SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKA 510
Cdd:PRK07787 339 PDATAAAFTADgWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVA 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642407 511 FIVLNPDYKLhdqeqlkKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:PRK07787 419 YVVGADDVAA-------DELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
57-569 |
9.13e-41 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 156.03 E-value: 9.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 57 NTEKTGKRlsnPAFWWVDgNGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIP 136
Cdd:COG1022 20 RAARFPDR---VALREKE-DGIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 137 GTTQLTQKDILYRLQSSKSKCIIT-DDTLAPAVDIVAAKCENLhsKLIVSQHSREGWG-----NLKEMMKYASDSHT--- 207
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSL--RHIVVLDPRGLRDdprllSLDELLALGREVADpae 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 208 ----CVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDV------MWNTSDTGWaksawsSVFS 277
Cdd:COG1022 173 learRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRtlsflpLAHVFERTV------SYYA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 278 pWTQGACVfaHYLPRFDStsILQTLSKFPITVFCSAP------------------------------TAYRMLIQNDITR 327
Cdd:COG1022 246 -LAAGATV--AFAESPDT--LAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrklfrwalaVGRRYARARLAGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 328 S--------YKF--------------NSLKHCVSAGEPINPEV------MeqwkkktGLDIYEGYGQTET-VLICGNFKG 378
Cdd:COG1022 321 SpslllrlkHALadklvfsklrealgGRLRFAVSGGAALGPELarffraL-------GIPVLEGYGLTETsPVITVNRPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 379 mKIKPGSMGKPSPafNVEI-LDENGTIL---PpgqegdiavqvlpdrpfGLFTHYVDNPSKTASTLR--GNFYiTGDRGY 452
Cdd:COG1022 394 -DNRIGTVGPPLP--GVEVkIAEDGEILvrgP-----------------NVMKGYYKNPEATAEAFDadGWLH-TGDIGE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 453 MDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAESAVVsspdpirGE----VVkAFIVLNPDY--------- 518
Cdd:COG1022 453 LDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpfLA-ALIVPDFEAlgewaeeng 524
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642407 519 -------KLHDQEQLKKEIQEHVKKTT---APYKYPRKIEFI--------EELpkTVSGKVKRNELRRK 569
Cdd:COG1022 525 lpytsyaELAQDPEVRALIQEEVDRANaglSRAEQIKRFRLLpkeftienGEL--TPTLKLKRKVILEK 591
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
79-569 |
3.43e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 153.56 E-value: 3.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYAS-----DSHTCVDTKHNELMAIY--FTSGTTGPPKM 231
Cdd:PRK08162 120 IVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEAflasgDPDFAWTLPADEWDAIAlnYTSGTTGNPKG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 232 IGHTHSSFGLGLSVNGRFWlDLIASDV-MW-------NtsdtGWAksawssvFsPWT----QGACVFahyLPRFDSTSIL 299
Cdd:PRK08162 200 VVYHHRGAYLNALSNILAW-GMPKHPVyLWtlpmfhcN----GWC-------F-PWTvaarAGTNVC---LRKVDPKLIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 300 QTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQwKKKTGLDIYEGYGQTET---VLICGNF 376
Cdd:PRK08162 264 DLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAK-MEEIGFDLTHVYGLTETygpATVCAWQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 377 KGMKIKP--------GSMGKPSPAFN-VEILD-ENGTILPPGQE--GDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNF 444
Cdd:PRK08162 343 PEWDALPlderaqlkARQGVRYPLQEgVTVLDpDTMQPVPADGEtiGEIMF-----RGNIVMKGYLKNPKATEEAFAGGW 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 445 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhDQE 524
Cdd:PRK08162 418 FHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKD-----GAS 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1958642407 525 QLKKEIQEHVKKTTAPYKYPRKIEFiEELPKTVSGKVKRNELRRK 569
Cdd:PRK08162 493 ATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
59-567 |
3.61e-39 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 151.13 E-value: 3.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 59 EKTGKRLSN-PAFwwvdgNGKEVRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 137
Cdd:PRK12492 31 ERSCKKFADrPAF-----SNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 138 TTQLTQKDILYRLQSSKSKCIITDDTLAPAVDIVAAKCENLH---SKLIVSQHSREGW------GNLKEMMKY------- 201
Cdd:PRK12492 106 NPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYlieAKMGDLLPAAKGWlvntvvDKVKKMVPAyhlpqav 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 202 ---------ASDSHTCVDTKHNELMAIYFTSGTTGPPK--MIGH---------THSSFGLGLSVNGRFWLDliASDVMWn 261
Cdd:PRK12492 186 pfkqalrqgRGLSLKPVPVGLDDIAVLQYTGGTTGLAKgaMLTHgnlvanmlqVRACLSQLGPDGQPLMKE--GQEVMI- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 262 tsdtgwAKSAWSSVFSPWTQGACVFA---HYL----PRfDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSL 334
Cdd:PRK12492 263 ------APLPLYHIYAFTANCMCMMVsgnHNVlitnPR-DIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSAL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 335 KHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDI 413
Cdd:PRK12492 336 KLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGEL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 414 AV---QVLPDrpfglfthYVDNPSKTASTLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHP 489
Cdd:PRK12492 416 CIkgpQVMKG--------YWQQPEATAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHP 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642407 490 SIAESAVVSSPDPIRGEVVKAFIVlnPDYKLHDQEQLKKeiqeHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK12492 488 KVANCAAIGVPDERSGEAVKLFVV--ARDPGLSVEELKA----YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
208-568 |
6.10e-39 |
|
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: 149.02 E-value: 6.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 208 CVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRFwlDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVF 286
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeQITAIF--DPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 287 AHYLPrFDSTSILQTLSKFPITVFCSAPTAYRMLIQNdiTRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQ 366
Cdd:cd05909 219 FHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA--AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 367 TETV-LICGNFKGMKIKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNF 444
Cdd:cd05909 296 TECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLV-----RGPNVMLGYLNEPELTSFAFGDGW 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 445 YITGDRGYMDEDGYFWFVARsddviLSSGYRIG----PFE-VESALIEH-PSIAESAVVSSPDPIRGEVVKAFivlnpdY 518
Cdd:cd05909 371 YDTGDIGKIDGEGFLTITGR-----LSRFAKIAgemvSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL------T 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958642407 519 KLHDQEQLkkEIQEHVKKTTAPYKY-PRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:cd05909 440 TTTDTDPS--SLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
218-563 |
8.29e-39 |
|
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: 145.48 E-value: 8.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 218 AIYFTSGTTGPPKMIGHTHSSFGLGLSVngrfwldLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYL-----PR 292
Cdd:cd17635 5 AVIFTSGTTGEPKAVLLANKTFFAVPDI-------LQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLcvtggEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 293 FDSTSILQTLSKFPITVFCSAPTAYrmliqNDITRSYKfNSLKHC-------VSAGEPINPEV-MEQWKKKTglDIYEGY 364
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLL-----SKLVSELK-SANATVpslrligYGGSRAIAADVrFIEATGLT--NTAQVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 365 GQTET-VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVlPDRPFGlfthYVDNPSKTASTLRGN 443
Cdd:cd17635 150 GLSETgTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKS-PANMLG----YWNNPERTAEVLIDG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 444 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyklhDQ 523
Cdd:cd17635 225 WVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAE----LD 300
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958642407 524 EQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 563
Cdd:cd17635 301 ENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
219-563 |
1.55e-38 |
|
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: 144.57 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPK--MIGHTHSsfgLGLSVNgrfWldliaSDVMWNTSDTGWA-----------KSAWSSVFspwTQGACV 285
Cdd:cd17638 5 IMFTSGTTGRSKgvMCAHRQT---LRAAAA---W-----ADCADLTEDDRYLiinpffhtfgyKAGIVACL---LTGATV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 286 FAHYLprFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD-IYEGY 364
Cdd:cd17638 71 VPVAV--FDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 365 GQTE--TVLICGNFKGMKIKPGSMGKPSPAFNVEILDEngtilppgqeGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRG 442
Cdd:cd17638 149 GLTEagVATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLV-----RGYNVMQGYLDDPEATAEAIDA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 443 NFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLh 521
Cdd:cd17638 214 DGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTL- 292
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958642407 522 DQEQLKKEIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKR 563
Cdd:cd17638 293 TEEDVIAWCRERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
80-567 |
2.31e-38 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 148.81 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 80 VRWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCII 159
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 160 TDD------------TLAP------AVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHtcvDTKHNELMA--- 218
Cdd:PRK08315 121 AADgfkdsdyvamlyELAPelatcePGQLQSARLPELRRVIFLGDEKHPGMLNFDELLALGRAVD---DAELAARQAtld 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 ------IYFTSGTTGPPKmiGHTHSSFGLGLsvNGRF---WLDLIASD--------------VMWNTSDTgwaksawssv 275
Cdd:PRK08315 198 pddpinIQYTSGTTGFPK--GATLTHRNILN--NGYFigeAMKLTEEDrlcipvplyhcfgmVLGNLACV---------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 276 fspwTQGAC-VFAhyLPRFDSTSILQTLSKFPITVFCSAPTayrMLI--QNDITR-SYKFNSLKHCVSAGEPINPEVMEQ 351
Cdd:PRK08315 264 ----THGATmVYP--GEGFDPLATLAAVEEERCTALYGVPT---MFIaeLDHPDFaRFDLSSLRTGIMAGSPCPIEVMKR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 352 WKKKTGL-DIYEGYGQTETvlicgnfkgmkiKPGSM---------------GKPSPAFNVEILD-ENGTILPPGQEGDIA 414
Cdd:PRK08315 335 VIDKMHMsEVTIAYGMTET------------SPVSTqtrtddplekrvttvGRALPHLEVKIVDpETGETVPRGEQGELC 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 415 VqvlpdRPFGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 493
Cdd:PRK08315 403 T-----RGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642407 494 SAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK08315 478 VQVVGVPDEKYGEEVCAWIILRPGATLTEE-----DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
73-566 |
4.08e-38 |
|
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: 146.70 E-value: 4.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 73 VDGNGkevRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 152
Cdd:cd05920 35 VDGDR---RLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 153 SKSKCIITDDTLAPaVDIVAAKCENLHSklivsqhsregwgnlkemmkyasdshtcvdtkHNELMAIYFTSGTTGPPKMI 232
Cdd:cd05920 111 AEAVAYIVPDRHAG-FDHRALARELAES--------------------------------IPEVALFLLSGGTTGTPKLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 233 GHTHSSFGLGLSVngrfwldliASDVMWNTSDT----------GWAKSAWSSVFSPWTQGACVFAhylPRFDSTSILQTL 302
Cdd:cd05920 158 PRTHNDYAYNVRA---------SAEVCGLDQDTvylavlpaahNFPLACPGVLGTLLAGGRVVLA---PDPSPDAAFPLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 303 SKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLicgNFKGM--- 379
Cdd:cd05920 226 EREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL---NYTRLddp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 380 -KIKPGSMGKP-SPAFNVEILDENGTILPPGQEGDIAVQvlpdrpfGLFT--HYVDNPSKTASTLRGN-FYITGDRGYMD 454
Cdd:cd05920 303 dEVIIHTQGRPmSPDDEIRVVDEEGNPVPPGEEGELLTR-------GPYTirGYYRAPEHNARAFTPDgFYRTGDLVRRT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 455 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEhv 534
Cdd:cd05920 376 PDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPP--SAAQLRRFLRE-- 451
|
490 500 510
....*....|....*....|....*....|..
gi 1958642407 535 kKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd05920 452 -RGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
282-561 |
8.52e-38 |
|
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: 142.44 E-value: 8.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 282 GACVFahyLPRFDSTSILQTLSKFPIT-VFCSAPTAYRMLIQNDiTRSYKFNSLKHCVSAGE--PINPEVMEQWKKKTGl 358
Cdd:cd17636 67 GTNVF---VRRVDAEEVLELIEAERCThAFLLPPTIDQIVELNA-DGLYDLSSLRSSPAAPEwnDMATVDTSPWGRKPG- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 359 diyeGYGQTETV-LICGNFKGMKIKpGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTA 437
Cdd:cd17636 142 ----GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVA-----RGPTVMAGYWNRPEVNA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 438 STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 517
Cdd:cd17636 212 RRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG 291
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958642407 518 YKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKV 561
Cdd:cd17636 292 ASVTEA-----ELIEHCRARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
104-567 |
1.77e-37 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 147.49 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 104 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD----DTLAPAVDIVAAKcenlh 179
Cdd:PRK06060 52 LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSdalrDRFQPSRVAEAAE----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 180 sklIVSQHSREGWGNLKEMMKYASDSHTcvdtkhnelmaiyFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVM 259
Cdd:PRK06060 127 ---LMSEAARVAPGGYEPMGGDALAYAT-------------YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 260 WNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRfdSTSILQTLS-KFPITVFCSAPTAYRMLIqnDITRSYKFNSLKHCV 338
Cdd:PRK06060 191 LCSARMYFAYGLGNSVWFPLATGGSAVINSAPV--TPEAAAILSaRFGPSVLYGVPNFFARVI--DSCSPDSFRSLRCVV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 339 SAGEPINPEVMEQWKKK-TGLDIYEGYGQTEtvlICGNFKGMKI---KPGSMGKPSPAFNVEILDENGTILPPGQEGDIA 414
Cdd:PRK06060 267 SAGEALELGLAERLMEFfGGIPILDGIGSTE---VGQTFVSNRVdewRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLW 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 415 VqvlpdRPFGLFTHYVDNPSKTASTlrGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAES 494
Cdd:PRK06060 344 V-----RGPAIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642407 495 AVVSSPDPIRGEVVKAFIVlnPDYKLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK06060 417 AVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
73-568 |
5.67e-37 |
|
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: 144.13 E-value: 5.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 73 VDGngkEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGtvLIPGTT--QLTQKDILYRL 150
Cdd:COG1021 45 VDG---ERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFAlpAHRRAEISHFA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 151 QSSKSKCIITDDT-----LAPAVDIVAAKCENLHSKLIVsqHSREGWGNLKEMmkYASDSHTCVDTKHNELMAIYFTS-G 224
Cdd:COG1021 119 EQSEAVAYIIPDRhrgfdYRALARELQAEVPSLRHVLVV--GDAGEFTSLDAL--LAAPADLSEPRPDPDDVAFFQLSgG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 225 TTGPPKMIGHTH---------SSFGLGLSVNGRFwldLIASDVMWNtsdtgwakSAWSS--VFSPWTQGAC-VFAhylPR 292
Cdd:COG1021 195 TTGLPKLIPRTHddylysvraSAEICGLDADTVY---LAALPAAHN--------FPLSSpgVLGVLYAGGTvVLA---PD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 293 FDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYG------- 365
Cdd:COG1021 261 PSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGmaeglvn 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 366 QT------ETVLicgnfkgmkikpGSMGKP-SPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS 438
Cdd:COG1021 341 YTrlddpeEVIL------------TTQGRPiSPDDEVRIVDEDGNPVPPGEVGELLT-----RGPYTIRGYYRAPEHNAR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 439 --TLRGnFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnp 516
Cdd:COG1021 404 afTPDG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-- 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1958642407 517 dyklhDQEQLK-KEIQEHVK-KTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:COG1021 481 -----RGEPLTlAELRRFLReRGLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
83-567 |
6.93e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 143.38 E-value: 6.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEACSLQRgdRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:PRK07638 28 TYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 TLAPavDIVAAKCEnlhsklIVSqhsregWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLG 242
Cdd:PRK07638 106 YKLN--DLPDEEGR------VIE------IDEWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 243 LSVNGR-FWLD-----LIASDVMwntsdtgwaksawSSVF-----SPWTQGACVfaHYLPRFDSTSILQTLSKFPITVFC 311
Cdd:PRK07638 172 FDCNVHdFHMKredsvLIAGTLV-------------HSLFlygaiSTLYVGQTV--HLMRKFIPNQVLDKLETENISVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 312 SAPTAYRMLIQNDITRSykfNSLKhCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTE----TVLICGNFKgmkIKPGSM 386
Cdd:PRK07638 237 TVPTMLESLYKENRVIE---NKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGASElsfvTALVDEESE---RRPNSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 387 GKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdRPFgLFTHYVdNPSKTASTLRGNFYIT-GDRGYMDEDGYFWFVARS 465
Cdd:PRK07638 310 GRPFHNVQVRICNEAGEEVQKGEIGTVYVK----SPQ-FFMGYI-IGGVLARELNADGWMTvRDVGYEDEEGFIYIVGRE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 466 DDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIvlnpdyklhDQEQLKKEIQEHVKKTTAPYKYPR 545
Cdd:PRK07638 384 KNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPK 454
|
490 500
....*....|....*....|..
gi 1958642407 546 KIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK07638 455 EWHFVDEIPYTNSGKIARMEAK 476
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
209-563 |
8.10e-37 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 145.27 E-value: 8.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 209 VDTKHNelMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAksAWSSVFSPWTQGACVFAH 288
Cdd:PTZ00237 251 VESSHP--LYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWV--SFHGFLYGSLSLGNTFVM 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 289 Y-----LPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQND-----ITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL 358
Cdd:PTZ00237 327 FeggiiKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 359 DIYEGYGQTET-VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQvLPDRPFGLFTHYV-DNPSKT 436
Cdd:PTZ00237 407 KSSRGYGQTEIgITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK-LPMPPSFATTFYKnDEKFKQ 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 437 ASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNP 516
Cdd:PTZ00237 486 LFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQ 565
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958642407 517 DYKLH--DQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 563
Cdd:PTZ00237 566 DQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
104-566 |
1.46e-36 |
|
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: 142.65 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 104 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdILYRLQSSKSKCIITDDTLAPAVDIVAAKcenlhskli 183
Cdd:cd05923 50 LRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL---------INPRLKAAELAELIERGEMTAAVIAVDAQ--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 184 VSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMA--------IYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIA 255
Cdd:cd05923 112 VMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPrepeqpafVFYTSGTTGLPKGAVIPQRA---------------AE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 256 SDVMWNTSDTGWAKSAWSSVFS--PWTQGACVFA-----------HYLPR-FDSTSILQTLSKFPITVFCSAPTAYRMLI 321
Cdd:cd05923 177 SRVLFMSTQAGLRHGRHNVVLGlmPLYHVIGFFAvlvaalaldgtYVVVEeFDPADALKLIEQERVTSLFATPTHLDALA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 322 QNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVlicgNFKGMK-IKPGSMGKPspAFN-----V 395
Cdd:cd05923 257 AAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM----NSLYMRdARTGTEMRP--GFFsevriV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 396 EILDENGTILPPGQEGDIAVQVLPDRPFglfTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYR 475
Cdd:cd05923 331 RIGGSPDEALANGEEGELIVAAAADAAF---TGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGEN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 476 IGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhdqEQLKKEIQEHVKKTT--APYKYPRKIEFIEEL 553
Cdd:cd05923 408 IHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE-------GTLSADELDQFCRASelADFKRPRRYFFLDEL 480
|
490
....*....|...
gi 1958642407 554 PKTVSGKVKRNEL 566
Cdd:cd05923 481 PKNAMNKVLRRQL 493
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
81-567 |
1.47e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 142.25 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANIL-TEACSlqRGDRVMViLPKIPEWWLA-NVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLrRRGCV--DGERLAV-LARNSVWLVAlHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLApavdivAAKCENLHSKLIVSQhsregwgnlkemmkyaSDSHTCVDTKH---NELMAIYFTSGTTGPPK--MIG 233
Cdd:PRK09088 99 LGDDAVA------AGRTDVEDLAAFIAS----------------ADALEPADTPSippERVSLILFTSGTSGQPKgvMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 234 -----HTHSSFGLGLSVNGR--FWLDLiasdVMWNTsdTGWAksawSSVFSPWTQGACVFAHylPRFDSTSILQTLS--K 304
Cdd:PRK09088 157 ernlqQTAHNFGVLGRVDAHssFLCDA----PMFHI--IGLI----TSVRPVLAVGGSILVS--NGFEPKRTLGRLGdpA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 305 FPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPiNPEVMEQWKKKTGLDIYEGYGQTE--TVLicgnfkGMKI- 381
Cdd:PRK09088 225 LGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAP-HAAEDILGWLDDGIPMVDGFGMSEagTVF------GMSVd 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 382 ------KPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN-FYITGDRGYMD 454
Cdd:PRK09088 298 cdviraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLL-----RGPNLSPGYWRRPQATARAFTGDgWFRTGDIARRD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 455 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEqlkkEIQEHV 534
Cdd:PRK09088 373 ADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPL-DLE----RIRSHL 447
|
490 500 510
....*....|....*....|....*....|...
gi 1958642407 535 KKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK09088 448 STRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
82-566 |
2.27e-36 |
|
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: 141.19 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 82 WSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 161
Cdd:cd05907 6 ITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 162 DTlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhNELMAIYFTSGTTGPPKMIGHTHSSFgl 241
Cdd:cd05907 85 DP--------------------------------------------------DDLATIIYTSGTTGRPKGVMLSHRNI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 242 glsvngrfwldliasdvMWN--TSDTGWAKSA--WSSVFSP-WTQGACVFAHYLP-------RF--DSTSILQTLSKFPI 307
Cdd:cd05907 113 -----------------LSNalALAERLPATEgdRHLSFLPlAHVFERRAGLYVPllagariYFasSAETLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 308 TVFCSAPTAYRMLIQND-----------ITRSYKFNSLKHCVSAGEPINPEVMEQWKKkTGLDIYEGYGQTETV-LICGN 375
Cdd:cd05907 176 TVFLAVPRVWEKVYAAIkvkavpglkrkLFDLAVGGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSaVVTLN 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 376 FKGmKIKPGSMGKPSPAFNVEIldengtilppGQEGDIAVqvlpdRPFGLFTHYVDNPSKTA-STLRGNFYITGDRGYMD 454
Cdd:cd05907 255 PPG-DNRIGTVGKPLPGVEVRI----------ADDGEILV-----RGPNVMLGYYKNPEATAeALDADGWLHTGDLGEID 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 455 EDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAESAVVSSPDPirgeVVKAFIVLNPDY--------------- 518
Cdd:cd05907 319 EDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEAleawaeehgiaytdv 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642407 519 -KLHDQEQLKKEIQEHVK---KTTAPYKYPRKIEFIEElPKTV-------SGKVKRNEL 566
Cdd:cd05907 395 aELAANPAVRAEIEAAVEaanARLSRYEQIKKFLLLPE-PFTIengeltpTLKLKRPVI 452
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
79-567 |
6.77e-36 |
|
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: 140.56 E-value: 6.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:cd17651 18 GRRLTYAELDRRANRLAHRL-RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDIVAAkcenlhsklIVSQHSREGWGNLkemmkyASDSHTCVDTKHNELMAIYfTSGTTGPPKmighthss 238
Cdd:cd17651 97 LTHPALAGELAVELV---------AVTLLDQPGAAAG------ADAEPDPALDADDLAYVIY-TSGSTGRPK-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 239 fglGLSVNGRFWLDLIAsdvmWNT----SDTGWAKSAWSS---------VFSPWTQGACVfaHYLP---RFDSTSILQTL 302
Cdd:cd17651 153 ---GVVMPHRSLANLVA----WQArassLGPGARTLQFAGlgfdvsvqeIFSTLCAGATL--VLPPeevRTDPPALAAWL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 303 SKFPITVfCSAPTAYRMLIQNDITRSYKFN-SLKHCVSAGEP--INPEVMEQWKKKTGLDIYEGYGQTE----TVLICGN 375
Cdd:cd17651 224 DEQRISR-VFLPTVALRALAEHGRPLGVRLaALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTEthvvTALSLPG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 376 FKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTL-------RGNFYITG 448
Cdd:cd17651 303 DPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIG-----GAGLARGYLNRPELTAERFvpdpfvpGARMYRTG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 449 DRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKK 528
Cdd:cd17651 378 DLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPV-DAAELRA 456
|
490 500 510
....*....|....*....|....*....|....*....
gi 1958642407 529 EIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:cd17651 457 ALATHL----PEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
219-563 |
7.90e-36 |
|
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: 136.77 E-value: 7.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPKMIGHTHSSfglglsvngrfWldlIASDVMwntSDTGWAKSAWSSVFSPWTQG------ACVFAHYLPR 292
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERS-----------W---IESFVC---NEDLFNISGEDAILAPGPLShslflyGAISALYLGG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 293 -------FDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSykfnSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGY 364
Cdd:cd17633 68 tfigqrkFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPES----KIKSIFSSGQKLFESTKKKLKNIFpKANLIEFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 365 GQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILDENGtilppGQEGDIAVQvlpdRPFgLFTHYVDNPSKTAstlrGNF 444
Cdd:cd17633 144 GTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVK----SEM-VFSGYVRGGFSNP----DGW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 445 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyklhdqE 524
Cdd:cd17633 210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD--------K 281
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958642407 525 QLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 563
Cdd:cd17633 282 LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
212-568 |
1.08e-35 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 141.13 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 212 KHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWldliASDVMWNTSDTGWAksAWSSVFSPWtqGACVFAHYL- 290
Cdd:PLN02574 196 KQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFE----ASQYEYPGSDNVYL--AALPMFHIY--GLSLFVVGLl 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 291 ---------PRFDSTSILQTLSKFPITVFCSAPTayrmlIQNDITRSYK------FNSLKHCVSAGEPINPEVMEQWKKK 355
Cdd:PLN02574 268 slgstivvmRRFDASDMVKVIDRFKVTHFPVVPP-----ILMALTKKAKgvcgevLKSLKQVSCGAAPLSGKFIQDFVQT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 356 -TGLDIYEGYGQTETVLICG---NFKGMKiKPGSMGKPSPAFNVEILD-ENGTILPPGQEGDIAVQvlpdRPfGLFTHYV 430
Cdd:PLN02574 343 lPHVDFIQGYGMTESTAVGTrgfNTEKLS-KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ----GP-GVMKGYL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 431 DNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK 509
Cdd:PLN02574 417 NNPKATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPV 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642407 510 AFIVLNPDYKLhDQEQlkkeIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:PLN02574 497 AFVVRRQGSTL-SQEA----VINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKR 550
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
204-567 |
2.47e-35 |
|
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: 138.27 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 204 DS-HTCVDTKHNELMA-IYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFwLDLIASDVMWNTSDTGWaKSAWSSVFSPWTQ 281
Cdd:cd17649 82 DSgAGLLLTHHPRQLAyVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNF-DGAHEQLLPPLIC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 282 GACVFAHYLPRFDSTSILQTL-SKFPITVFcSAPTAY-RMLIQN-DITRSYKFNSLKHCVSAGEPINPEVMEQWKKkTGL 358
Cdd:cd17649 160 GACVVLRPDELWASADELAEMvRELGVTVL-DLPPAYlQQLAEEaDRTGDGRPPSLRLYIFGGEALSPELLRRWLK-APV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 359 DIYEGYGQTETVLICGNFK---GMKIKPGSM--GKPSPAFNVEILDENGTILPPGQEGD--IAVQvlpdrpfGLFTHYVD 431
Cdd:cd17649 238 RLFNAYGPTEATVTPLVWKceaGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGElyIGGE-------GLARGYLG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 432 NPSKTASTL--------RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPI 503
Cdd:cd17649 311 RPELTAERFvpdpfgapGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG 390
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642407 504 RGEVVkAFIVLNPDYKlhdQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:cd17649 391 GKQLV-AYVVLRAAAA---QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
77-563 |
6.13e-35 |
|
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: 137.19 E-value: 6.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 77 GKEVRWSFEELGSLSRKFANiLTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 156
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFAL-LLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 157 CIITddtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdTKHNELMAIYFTSGTTGPPKMIGHTH 236
Cdd:cd05914 82 AIFV--------------------------------------------------SDEDDVALINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 237 SSfgLGLSVNGRFWLDLI-ASDVMWNTSDTGWAKSAWSSVFSPWTQGACVfaHYLPRFdSTSILQTLSKFPITVFCSAPT 315
Cdd:cd05914 112 RN--IVSNVDGVKEVVLLgKGDKILSILPLHHIYPLTFTLLLPLLNGAHV--VFLDKI-PSAKIIALAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 316 A------YRMLIQNDITRS---YKFNS----------------------LKHCVSAGEPINPEVmEQWKKKTGLDIYEGY 364
Cdd:cd05914 187 PlviekiFKMDIIPKLTLKkfkFKLAKkinnrkirklafkkvheafggnIKEFVIGGAKINPDV-EEFLRTIGFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 365 GQTETV-LICGNFKGmKIKPGSMGKPSPAFNVEILDENgtilPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTAS--TLR 441
Cdd:cd05914 266 GMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIV-----RGPNVMKGYYKNPEATAEafDKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 442 GNFYiTGDRGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAESAVVsspdpIRGEVVKAFIVLNPDY-- 518
Cdd:cd05914 336 GWFH-TGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFld 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958642407 519 -----KLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFI-EELPKTVSGKVKR 563
Cdd:cd05914 410 vkalkQRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
83-566 |
7.93e-35 |
|
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: 137.46 E-value: 7.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:cd17655 24 TYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 TLAPAVDIvAAKCENLHSKLIVSQHSRegwgNLKemmkyasdshtcVDTKHNELMAIYFTSGTTGPPK--MIGHtHSSFG 240
Cdd:cd17655 103 HLQPPIAF-IGLIDLLDEDTIYHEESE----NLE------------PVSKSDDLAYVIYTSGSTGKPKgvMIEH-RGVVN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 241 LGLSVNGRFWLDliASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FDSTSILQTLSKFPITVFCSAPTAY 317
Cdd:cd17655 165 LVEWANKVIYQG--EHLRVALFASISFDASVTE-IFASLLSGNTL--YIVRKetvLDGQALTQYIRQNRITIIDLTPAHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 318 RMLIQNDITrsyKFNSLKHCVSAGEPINPEVMEQWKKKTGL--DIYEGYGQTETVLIC--GNFKGMKIKPGS--MGKPSP 391
Cdd:cd17655 240 KLLDAADDS---EGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVDAsiYQYEPETDQQVSvpIGKPLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 392 AFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVAR 464
Cdd:cd17655 317 NTRIYILDQYGRPQPVGVAGELYIG-----GEGVARGYLNRPELTAEKFVDDpfvpgerMYRTGDLARWLPDGNIEFLGR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 465 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdqeqlkKEIQEHVKKTTAPYKYP 544
Cdd:cd17655 392 IDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPV-------AQLREFLARELPDYMIP 464
|
490 500
....*....|....*....|..
gi 1958642407 545 RKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd17655 465 SYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
80-569 |
2.21e-34 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 137.28 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 80 VRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCII 159
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 160 TDD---TLAP-AVDIVAAKCENLHSK--LIVSQHSREGWGNLKEMM-KYASDSHTCVDTKHNEL-----------MAIYF 221
Cdd:PLN02479 123 VDQeffTLAEeALKILAEKKKSSFKPplLIVIGDPTCDPKSLQYALgKGAIEYEKFLETGDPEFawkppadewqsIALGY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 222 TSGTTGPPK-MIGHTHSSFGLGLSvNGRFWLDLIASDVMWNTSD---TGWAksawssvfSPWTQGA-CVFAHYLPRFDST 296
Cdd:PLN02479 203 TSGTTASPKgVVLHHRGAYLMALS-NALIWGMNEGAVYLWTLPMfhcNGWC--------FTWTLAAlCGTNICLRQVTAK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 297 SILQTLSKFPITVFCSAPTAYRMLIqnDITRSYKFNSLKHCV---SAGEPINPEVMEQWKKKtGLDIYEGYGQTETV--- 370
Cdd:PLN02479 274 AIYSAIANYGVTHFCAAPVVLNTIV--NAPKSETILPLPRVVhvmTAGAAPPPSVLFAMSEK-GFRVTHTYGLSETYgps 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 371 LICG----------------------NFKGMK----IKPGSMgKPSPAfnveildeNGTILppgqeGDIAVqvlpdRPFG 424
Cdd:PLN02479 351 TVCAwkpewdslppeeqarlnarqgvRYIGLEgldvVDTKTM-KPVPA--------DGKTM-----GEIVM-----RGNM 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 425 LFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIR 504
Cdd:PLN02479 412 VMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERW 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642407 505 GEVVKAFIVLNPDYKLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFiEELPKTVSGKVKRNELRRK 569
Cdd:PLN02479 492 GESPCAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
221-569 |
4.14e-34 |
|
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: 132.07 E-value: 4.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 221 FTSGTTGPPKMIGHT-----HSSFG----LGLSVNGRFWLDLIASDV-----MWNtsdtgWAKSAWSSVFSPWTQGAcvf 286
Cdd:cd17630 7 LTSGSTGTPKAVVHTaanllASAAGlhsrLGFGGGDSWLLSLPLYHVgglaiLVR-----SLLAGAELVLLERNQAL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 287 ahylprfdstsiLQTLSKFPITVFCSAPTAYRMLIQNDITRSyKFNSLKHCVSAGEPINPEVMEQWKKKtGLDIYEGYGQ 366
Cdd:cd17630 79 ------------AEDLAPPGVTHVSLVPTQLQRLLDSGQGPA-ALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 367 TETV-LICGNFKGMKiKPGSMGKPSPAFNVEIlDENGTILPPGQegdiavqvlpdrpfGLFTHYVDNPSKTASTLRGNFY 445
Cdd:cd17630 145 TETAsQVATKRPDGF-GRGGVGVLLPGRELRI-VEDGEIWVGGA--------------SLAMGYLRGQLVPEFNEDGWFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 446 iTGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhdqEQ 525
Cdd:cd17630 209 -TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRG-------PA 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958642407 526 LKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRK 569
Cdd:cd17630 281 DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
219-566 |
8.61e-34 |
|
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: 133.59 E-value: 8.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYfTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFDSTS 297
Cdd:cd17643 99 IY-TSGSTGRPKGVVVSHANV-LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWE-IWGALLHGGrLVVVPYEVARSPED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 298 ILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGL---DIYEGYGQTET-VLIc 373
Cdd:cd17643 176 FARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETtVHV- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 374 gNFKGMK---IKPGSM---GKPSPAFNVEILDENGTILPPGQEGDIAV---QVLP---DRPFGLFTHYVDNPsKTASTLR 441
Cdd:cd17643 255 -TFRPLDaadLPAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELYVsgaGVARgylGRPELTAERFVANP-FGGPGSR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 442 GnfYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyklH 521
Cdd:cd17643 333 M--YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAD-----D 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958642407 522 DQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd17643 406 GAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
83-566 |
3.99e-33 |
|
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: 132.40 E-value: 3.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:cd17646 25 TYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 TLA---PAVDIVAAKCENLHSKLIVSQHSREgwgnlkemmkYASDSHTCVdtkhnelmaIYfTSGTTGPPK--MIGHThs 237
Cdd:cd17646 104 DLAarlPAGGDVALLGDEALAAPPATPPLVP----------PRPDNLAYV---------IY-TSGSTGRPKgvMVTHA-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 238 sfglGLsVNGRFWL----DLIASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFAHYLPRFDSTSILQTLSKFPITVFCS 312
Cdd:cd17646 162 ----GI-VNRLLWMqdeyPLGPGDRVLQKTPLSFDVSVWE-LFWPLVAGARlVVARPGGHRDPAYLAALIREHGVTTCHF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 313 APTAYRMLIQNDITRSYKfnSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET---VLICGNFKGMKIKPGSMGKP 389
Cdd:cd17646 236 VPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAaidVTHWPVRGPAETPSVPIGRP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 390 SPAFNVEILDENGTILPPGQEGDI---AVQVlpdrPFGlfthYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYF 459
Cdd:cd17646 314 VPNTRLYVLDDALRPVPVGVPGELylgGVQL----ARG----YLGRPALTAERFVPDpfgpgsrMYRTGDLARWRPDGAL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 460 WFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLkkeiQEHVKKTTA 539
Cdd:cd17646 386 EFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAAL----RAHLAERLP 461
|
490 500
....*....|....*....|....*..
gi 1958642407 540 PYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd17646 462 EYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
79-566 |
5.06e-33 |
|
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: 131.94 E-value: 5.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDivaakceNLHSKLIVSQHSREGwgnlkemmkYASDSHTCVDTKHneLMAIYFTSGTTGPPKMIGHTHSS 238
Cdd:cd12117 99 LTDRSLAGRAG-------GLEVAVVIDEALDAG---------PAGNPAVPVSPDD--LAYVMYTSGSTGRPKGVAVTHRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 239 FgLGLsVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FDSTSILQTLSKFPITV-FCSAP 314
Cdd:cd12117 161 V-VRL-VKNTNYVTLGPDDRVLQTSPLAFDASTFE-IWGALLNGARL--VLAPKgtlLDPDALGALIAEEGVTVlWLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 315 TaYRMLIQNDITRsykFNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTE--TVLICGNFKGMKIKPGS--MGKP 389
Cdd:cd12117 236 L-FNQLADEDPEC---FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEntTFTTSHVVTELDEVAGSipIGRP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 390 SPAFNVEILDENGTILPPGQEGDIAVqvLPDrpfGLFTHYVDNPSKTAS-------TLRGNFYITGDRGYMDEDGYFWFV 462
Cdd:cd12117 312 IANTRVYVLDEDGRPVPPGVPGELYV--GGD---GLALGYLNRPALTAErfvadpfGPGERLYRTGDLARWLPDGRLEFL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 463 ARSDDVILSSGYRIGPFEVESALIEHPSIAESAV-VSSPDPIRGEVVkAFIVlnPDYKLHDQeqlkkEIQEHVKKTTAPY 541
Cdd:cd12117 387 GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV-AYVV--AEGALDAA-----ELRAFLRERLPAY 458
|
490 500
....*....|....*....|....*
gi 1958642407 542 KYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd12117 459 MVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
67-574 |
2.42e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 130.96 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 67 NPAFWWVDGngkevRWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIpGTTQLTQKDI 146
Cdd:PRK07867 19 DRGLYFEDS-----FTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPV-GLNPTRRGAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 147 LYR-LQSSKSKCIITDDTLAPAVDIVAAKCEnlhsklIVSQHSREgWGNlkEMMKYASDSHTCVDTKHNELMAIYFTSGT 225
Cdd:PRK07867 93 LARdIAHADCQLVLTESAHAELLDGLDPGVR------VINVDSPA-WAD--ELAAHRDAEPPFRVADPDDLFMLIFTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 226 TGPPKMIGHTHSSF-GLGLSVNGRFwlDLIASDVMWntsdtgwaksawssVFSPWTQGACVFAHYLP------------R 292
Cdd:PRK07867 164 SGDPKAVRCTHRKVaSAGVMLAQRF--GLGPDDVCY--------------VSMPLFHSNAVMAGWAValaagasialrrK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 293 FDSTSILQTLSKFPITVF--CSAPTAYRMLI-QNDITRSykfNSLKhcVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET 369
Cdd:PRK07867 228 FSASGFLPDVRRYGATYAnyVGKPLSYVLATpERPDDAD---NPLR--IVYGNEGAPGDIARFARRFGCVVVDGFGSTEG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 370 vlicgnfkGMKIK------PGSMGKPSPafNVEILD-ENGTILPPGQ-------EGDIAVQVL--PDRPfGLFTHYVDNP 433
Cdd:PRK07867 303 --------GVAITrtpdtpPGALGPLPP--GVAIVDpDTGTECPPAEdadgrllNADEAIGELvnTAGP-GGFEGYYNDP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 434 SKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIV 513
Cdd:PRK07867 372 EADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALV 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642407 514 LNPDYKLhDQEQLKKEIqeHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTTT 574
Cdd:PRK07867 452 LAPGAKF-DPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDCA 509
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
206-573 |
3.92e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 130.15 E-value: 3.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 206 HTCVDTKHNELMaiYFTSGTTGPPKMIGHTHSSFG-LGLSVNGRFwlDLIASDVMW--------NTSDTGWAKSAwssvf 276
Cdd:PRK13388 144 HREVDAMDPFML--IFTSGTTGAPKAVRCSHGRLAfAGRALTERF--GLTRDDVCYvsmplfhsNAVMAGWAPAV----- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 277 spwTQGACVFAHylPRFDSTSILQTLSKFPITVF--CSAPTAYRML-------IQNDITRSYkfnslkhcvsaGEPINPE 347
Cdd:PRK13388 215 ---ASGAAVALP--AKFSASGFLDDVRRYGATYFnyVGKPLAYILAtperpddADNPLRVAF-----------GNEASPR 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 348 VMEQWKKKTGLDIYEGYGQTETVLICGNFKGMKikPGSMGKPSPafNVEI-------------LDENGTILPPgqegDIA 414
Cdd:PRK13388 279 DIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRGAP--GVAIynpetltecavarFDAHGALLNA----DEA 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 415 VQVLPDRP-FGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 493
Cdd:PRK13388 351 IGELVNTAgAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINR 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 494 SAVVSSPDPIRGEVVKAFIVLNPDYK---------LHDQEQLkkeiqehvkkttAPYKYPRKIEFIEELPKTVSGKVKRN 564
Cdd:PRK13388 431 VAVYAVPDERVGDQVMAALVLRDGATfdpdafaafLAAQPDL------------GTKAWPRYVRIAADLPSTATNKVLKR 498
|
....*....
gi 1958642407 565 ELRRKEWTT 573
Cdd:PRK13388 499 ELIAQGWAT 507
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
77-568 |
1.27e-31 |
|
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: 127.04 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 77 GKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdilyrlqssksk 156
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP-------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 157 ciitDDTLAPAVDIVAAkCENLHSKLIVSqhsregwgnlkemmkyasdshtcvDTKHNELMAIYFTSGTTGPPKMIGHTH 236
Cdd:cd17653 77 ----LDAKLPSARIQAI-LRTSGATLLLT------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 237 SSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFAHylPRFDSTSILQTLSKFPITvfcsaPT 315
Cdd:cd17653 128 RGV-LNYVSQPPARLDVGPGSRVAQVLSIAFDACIGE-IFSTLCNGGTlVLAD--PSDPFAHVARTVDALMST-----PS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 316 AYRMLIQNDitrsykFNSLKHCVSAGEPINPEVMEQWKKktGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNV 395
Cdd:cd17653 199 ILSTLSPQD------FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTC 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 396 EILDENGTILPPGQEGDIAV---QVLPDrpfglfthYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARS 465
Cdd:cd17653 271 YILDADLQPVPEGVVGEICIsgvQVARG--------YLGNPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGRE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 466 DDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpdpIRGEVVkAFIVlnPDYKlhDQEQLKKEIQEHVkkttAPYKYPR 545
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFVT--PETV--DVDGLRSELAKHL----PSYAVPD 410
|
490 500
....*....|....*....|...
gi 1958642407 546 KIEFIEELPKTVSGKVKRNELRR 568
Cdd:cd17653 411 RIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
219-568 |
1.45e-31 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 128.76 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPKMIGHTHSSfglgLSVNGrfwLDLIA------SDVMWNTS---DTGWAKSAWSSVFSpwtqGAC-VFah 288
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHSA----LIVQS---LAKIAivgygeDDVYLHTAplcHIGGLSSALAMLMV----GAChVL-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 289 yLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQndITRSYK----FNSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEG 363
Cdd:PLN02860 244 -LPKFDAKAALQAIKQHNVTSMITVPAMMADLIS--LTRKSMtwkvFPSVRKILNGGGSLSSRLLPDAKKLfPNAKLFSA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 364 YGQTET----------VLICGNFK-----GMKIKPGS--------MGKPSPAFNVEI-LDEngtilpPGQEGDIAVqvlp 419
Cdd:PLN02860 321 YGMTEAcssltfmtlhDPTLESPKqtlqtVNQTKSSSvhqpqgvcVGKPAPHVELKIgLDE------SSRVGRILT---- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 420 dRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVS 498
Cdd:PLN02860 391 -RGPHVMLGYWGQNSETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 499 SPDPIRGEVVKAFIVLNPDYKLHDQE--------QLKKEIQEH--VKKTTAPYKYPRKIEFIEE-LPKTVSGKVKRNELR 567
Cdd:PLN02860 470 VPDSRLTEMVVACVRLRDGWIWSDNEkenakknlTLSSETLRHhcREKNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVR 549
|
.
gi 1958642407 568 R 568
Cdd:PLN02860 550 R 550
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
79-560 |
2.31e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 128.08 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:PRK07798 26 DRRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDIVAAKCENLHSKLIV----SQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYfTSGTTGPPK--MI 232
Cdd:PRK07798 105 VYEREFAPRVAEVLPRLPKLRTLVVVedgsGNDLLPGAVDYEDALAAGSPERDFGERSPDDLYLLY-TGGTTGMPKgvMW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 233 GHT---HSSFGLGLSVNGRFWLD----------------LIASDVMWNTSDtgWAksAWSSVFSpwtqGACVFAHYLPRF 293
Cdd:PRK07798 184 RQEdifRVLLGGRDFATGEPIEDeeelakraaagpgmrrFPAPPLMHGAGQ--WA--AFAALFS----GQTVVLLPDVRF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 294 DSTSILQTLSKFPITVFCSAPTAY-RMLIQN-DITRSYKFNSLKHCVSAGEPINPEVMEQW-KKKTGLDIYEGYGQTETv 370
Cdd:PRK07798 256 DADEVWRTIEREKVNVITIVGDAMaRPLLDAlEARGPYDLSSLFAIASGGALFSPSVKEALlELLPNVVLTDSIGSSET- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 371 licgNFKGMKI-KPGSMGKPSPAFN----VEILDENGTILPPGQE--GDIAvqvlpdR----PFGlfthYVDNPSKTAST 439
Cdd:PRK07798 335 ----GFGGSGTvAKGAVHTGGPRFTigprTVVLDEDGNPVEPGSGeiGWIA------RrghiPLG----YYKDPEKTAET 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 440 LR---GNFY-ITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 515
Cdd:PRK07798 401 FPtidGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLR 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1958642407 516 PDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGK 560
Cdd:PRK07798 481 EGARPDLA-----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
103-567 |
3.76e-31 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 127.83 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 103 SLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTLAP----AVDIVAAKCENL 178
Cdd:PLN03102 60 NITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPlareVLHLLSSEDSNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 179 HSKLIV------------SQHSREGWGNLKEMMKYASDSHTCVDTKHNELmAIYFTSGTTGPPK--MIGHTHSSFGLGLS 244
Cdd:PLN03102 140 NLPVIFiheidfpkrpssEELDYECLIQRGEPTPSLVARMFRIQDEHDPI-SLNYTSGTTADPKgvVISHRGAYLSTLSA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 245 VNGrfWLDLIASDVMWNTSD---TGWAKSaWSSVFSPWTQgACVFAHYLPRfdstsILQTLSKFPITVFCSAPTAYRMLI 321
Cdd:PLN03102 219 IIG--WEMGTCPVYLWTLPMfhcNGWTFT-WGTAARGGTS-VCMRHVTAPE-----IYKNIEMHNVTHMCCVPTVFNILL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 322 QNDITRSYKFNSLKHCVSAGEPiNPEVMEQWKKKTGLDIYEGYGQTET---VLICG---------NFKGMKIKPGSMGKP 389
Cdd:PLN03102 290 KGNSLDLSPRSGPVHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEAtgpVLFCEwqdewnrlpENQQMELKARQGVSI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 390 SPAFNVEILDENGTILPPgQEGDIAVQVLPdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVI 469
Cdd:PLN03102 369 LGLADVDVKNKETQESVP-RDGKTMGEIVI-KGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 470 LSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLK-----KEIQEHVKKTTAPYKYP 544
Cdd:PLN03102 447 ISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKlvtreRDLIEYCRENLPHFMCP 526
|
490 500
....*....|....*....|...
gi 1958642407 545 RKIEFIEELPKTVSGKVKRNELR 567
Cdd:PLN03102 527 RKVVFLQELPKNGNGKILKPKLR 549
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
210-561 |
9.59e-31 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 128.12 E-value: 9.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 210 DTKHNELMAIYFTSGTTGPPK--MIGHT----------------------------HSsfgLGLSVNgrFWLDLIasdvm 259
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKgvMLSHHnilsnieqisdvfnlrnddvilsslpffHS---FGLTVT--LWLPLL----- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 260 wntsdtgwaksawssvfspwtQGACVFAHYLPrFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVS 339
Cdd:PRK08633 848 ---------------------EGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 340 AGEPINPEVMEQWKKKTGLDIYEGYGQTET----------VLICGNFKGMKIKPGSMGKPSPAFNVEILD-ENGTILPPG 408
Cdd:PRK08633 906 GAEKLKPEVADAFEEKFGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPG 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 409 QEGDIAV---QVLpdrpfglfTHYVDNPSKTASTLR----GNFYITGDRGYMDEDGYFWFVARsddviLSSGYRIG---- 477
Cdd:PRK08633 986 EDGLILIggpQVM--------KGYLGDPEKTAEVIKdidgIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGgemv 1052
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 478 PF-EVESALIE--HPSIAESAVVSSPDPIRGEVvkafIVLnpdykLHDQEQLKKE-IQEHVKKTTAP--YKyPRKIEFIE 551
Cdd:PRK08633 1053 PLgAVEEELAKalGGEEVVFAVTAVPDEKKGEK----LVV-----LHTCGAEDVEeLKRAIKESGLPnlWK-PSRYFKVE 1122
|
410
....*....|
gi 1958642407 552 ELPKTVSGKV 561
Cdd:PRK08633 1123 ALPLLGSGKL 1132
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
83-567 |
7.57e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 123.70 E-value: 7.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIItdd 162
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLV--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 tLAPA---VDIVAAKCENLHSKLIVSQ--------------HSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFT-SG 224
Cdd:PRK06164 113 -VWPGfkgIDFAAILAAVPPDALPPLRaiavvddaadatpaPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTtSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 225 TTGPPKMIGHTHSSF---------GLGLSVNGRFWLDLIASDVMwntsdtgwaksAWSSVFSPWTQGACVfaHYLPRFDS 295
Cdd:PRK06164 192 TTSGPKLVLHRQATLlrharaiarAYGYDPGAVLLAALPFCGVF-----------GFSTLLGALAGGAPL--VCEPVFDA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 296 TSILQTLSKFPIT-VFCSAPTAYRMLIQNDitRSYKFNSLKHC-VSAGEPINPEVMeQWKKKTGLDIYEGYGQTE--TVL 371
Cdd:PRK06164 259 ARTARALRRHRVThTFGNDEMLRRILDTAG--ERADFPSARLFgFASFAPALGELA-ALARARGVPLTGLYGSSEvqALV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 372 ICGNFK---GMKIKPGsmGKP-SPAFNVEILD-ENGTILPPGQEGDIAVQVlpdrPfGLFTHYVDNPSKTASTLRGN-FY 445
Cdd:PRK06164 336 ALQPATdpvSVRIEGG--GRPaSPEARVRARDpQDGALLPDGESGEIEIRA----P-SLMRGYLDNPDATARALTDDgYF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 446 ITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpdPIRGE-VVKAFIVLNPDYKLhDQE 524
Cdd:PRK06164 409 RTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPTDGASP-DEA 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1958642407 525 QLKKeiqeHVKKTTAPYKYPRKIEFIEELPKTVSG---KVKRNELR 567
Cdd:PRK06164 486 GLMA----ACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
79-566 |
9.69e-30 |
|
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: 122.40 E-value: 9.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:cd12116 10 DRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLA-------PAVDIVAAKCENLHSKLIVSQHSregwGNLKEMMkyasdshtcvdtkhnelmaiyFTSGTTGPPKM 231
Cdd:cd12116 89 LTDDALPdrlpaglPVLLLALAAAAAAPAAPRTPVSP----DDLAYVI---------------------YTSGSTGRPKG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 232 IGHTHSSF-GLGLSVNGRfwLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFDSTSILQTLSKFPITV 309
Cdd:cd12116 144 VVVSHRNLvNFLHSMRER--LGLGPGDRLLAVTTYAFDISLLE-LLLPLLAGArVVIAPRETQRDPEALARLIEAHSITV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 310 FCSAPTAYRMLIQNDITRSYKFNSLkhCvsAGEPINPEVMEQWKKKTGlDIYEGYGQTETVL------ICGNFKGMKIkp 383
Cdd:cd12116 221 MQATPATWRMLLDAGWQGRAGLTAL--C--GGEALPPDLAARLLSRVG-SLWNLYGPTETTIwstaarVTAAAGPIPI-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 384 gsmGKPSPAFNVEILDENGTILPPGQEGDIAV---QVLPD---RPFGLFTHYVDNPSKTAstlRGNFYITGDRGYMDEDG 457
Cdd:cd12116 294 ---GRPLANTQVYVLDAALRPVPPGVPGELYIggdGVAQGylgRPALTAERFVPDPFAGP---GSRLYRTGDLVRRRADG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 458 YFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVLnPDYKLHDQEQLKkeiqEHVKKT 537
Cdd:cd12116 368 RLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPDAAALR----AHLRAT 441
|
490 500
....*....|....*....|....*....
gi 1958642407 538 TAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd12116 442 LPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
211-566 |
3.57e-29 |
|
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: 120.62 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 211 TKHNELMAIYFTSGTTGPPK--MIGHtHSSFGLGLSVNGRFwlDLIASDVMWNTSDTGWAKSAwSSVFSPWTQGAC-VFA 287
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKgvMIEH-QSLVNLSHGLIKEY--GITSSDRVLQFASIAFDVAA-EEIYVTLLSGATlVLR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 288 HYLPRFDSTSILQTLSKFPITVFcSAPTAYRMLIQNDITRSYK--FNSLKHCVSAGEPINPEVMEQWKKKTGLDI--YEG 363
Cdd:cd17644 179 PEEMRSSLEDFVQYIQQWQLTVL-SLPPAYWHLLVLELLLSTIdlPSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlINV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 364 YGQTETVL--ICGNFK---GMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTAS 438
Cdd:cd17644 258 YGPTEATIaaTVCRLTqltERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGV-----GLARGYLNRPELTAE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 439 TLRGN---------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK 509
Cdd:cd17644 333 KFISHpfnsseserLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLV 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642407 510 AFIVlnPDYklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd17644 413 AYIV--PHY---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
480-560 |
1.39e-28 |
|
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: 108.40 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 480 EVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYklhdqEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSG 559
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV-----ELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 1958642407 560 K 560
Cdd:pfam13193 76 K 76
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
79-574 |
2.75e-28 |
|
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: 120.73 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:COG1020 499 DQSLTYAELNARANRLAHHLR-ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLV 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDIVAAKCENLhSKLIVSQHSregwgnlkemmkyASDSHTCVDTKHneLMAIYFTSGTTGPPK--MIghTH 236
Cdd:COG1020 578 LTQSALAARLPELGVPVLAL-DALALAAEP-------------ATNPPVPVTPDD--LAYVIYTSGSTGRPKgvMV--EH 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 237 SSFG-LGLSVNGRFWLDliASDVM-WNTS---DTgwakSAWSsVFSPWTQGAC-VFAHYLPRFDSTSILQTLSKFPITVF 310
Cdd:COG1020 640 RALVnLLAWMQRRYGLG--PGDRVlQFASlsfDA----SVWE-IFGALLSGATlVLAPPEARRDPAALAELLARHRVTVL 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 311 CSAPTAYRMLIQNDITRsykFNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTETVL--ICGNFKGMKIKPGSM- 386
Cdd:COG1020 713 NLTPSLLRALLDAAPEA---LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVdsTYYEVTPPDADGGSVp 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 387 -GKPSPAFNVEILDENGTILPPGQEGDIAV---QV----LpDRPfGL----FthyVDNPSKTASTlRgnFYITGDRGYMD 454
Cdd:COG1020 790 iGRPIANTRVYVLDAHLQPVPVGVPGELYIggaGLargyL-NRP-ELtaerF---VADPFGFPGA-R--LYRTGDLARWL 861
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 455 EDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhDQEQLKKEIQEHV 534
Cdd:COG1020 862 PDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA-----GAAAAAALLRLAL 936
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1958642407 535 KKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTTT 574
Cdd:COG1020 937 ALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAA 976
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
83-563 |
3.06e-28 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 118.84 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 TLAPAVDIVAAKCENLhsKLIVSQHSREGWGNLKEMMKYASDSHTCVDT----KHNELMaIYFTSGTTGPPKMIGHTHSS 238
Cdd:PRK05852 124 DGPHDRAEPTTRWWPL--TVNVGGDSGPSGGTLSVHLDAATEPTPATSTpeglRPDDAM-IMFTGGTTGLPKMVPWTHAN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 239 fgLGLSVNGrfwldLIAS----------DVMWNTSDTGWAKSAWSSVFSpwtqGACVFAHYLPRFDSTSILQTLSKFPIT 308
Cdd:PRK05852 201 --IASSVRA-----IITGyrlsprdatvAVMPLYHGHGLIAALLATLAS----GGAVLLPARGRFSAHTFWDDIKAVGAT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 309 VFCSAPTAYRMLIQNDITRSY--KFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET--------VLICGNFKG 378
Cdd:PRK05852 270 WYTAVPTIHQILLERAATEPSgrKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAthqvtttqIEGIGQTEN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 379 MKIKPGSMGKpSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGY 458
Cdd:PRK05852 350 PVVSTGLVGR-STGAQIRIVGSDGLPLPAGAVGEVWL-----RGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 459 FWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnPDYKLHDQEQlkkEIQEHVKKTT 538
Cdd:PRK05852 424 LSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAPPTAE---ELVQFCRERL 498
|
490 500
....*....|....*....|....*
gi 1958642407 539 APYKYPRKIEFIEELPKTVSGKVKR 563
Cdd:PRK05852 499 AAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
219-566 |
3.50e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 118.18 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPKMIGHT-HSSFGLGLsvngrfWLDLIASDVMWNTSDTGWAKSAWSSV-----FSPWTQGACVFAHYlpR 292
Cdd:PRK13383 179 VLLTSGTTGKPKGVPRApQLRSAVGV------WVTILDRTRLRTGSRISVAMPMFHGLglgmlMLTIALGGTVLTHR--H 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 293 FDSTSILQTLSKFPITVFCSAPTAY-RMLIQNDITRSYK-FNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET- 369
Cdd:PRK13383 251 FDAEAALAQASLHRADAFTAVPVVLaRILELPPRVRARNpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVg 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 370 VLICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGDIAV--QVLPDRpfglfthYVDNPSKtaSTLRGnFYIT 447
Cdd:PRK13383 331 IGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVggELAGTR-------YTDGGGK--AVVDG-MTST 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 448 GDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLK 527
Cdd:PRK13383 401 GDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGV-DAAQLR 479
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958642407 528 KEIQEHVKKttapYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:PRK13383 480 DYLKDRVSR----FEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
100-566 |
6.74e-28 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 117.80 E-value: 6.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 100 EACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDIlyrlqssKSKCIITDdtlaPAVDIVAAKC---- 175
Cdd:PRK05857 59 RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAI-------ERFCQITD----PAAALVAPGSkmas 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 176 ----ENLHSKLIVSQHSREGWGNLKEMMKYASDShTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGLG---LSVNGR 248
Cdd:PRK05857 128 savpEALHSIPVIAVDIAAVTRESEHSLDAASLA-GNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 249 FWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYlprfDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRS 328
Cdd:PRK05857 207 NWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGE----NTTSLLEILTTNAVATTCLVPTLLSKLVSELKSAN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 329 YKFNSLKHCVSAG-EPINPEVmeQWKKKTGLDIYEGYGQTET-----VLICGNFKGMKIKPGSMGKPSPAFNVEILDENG 402
Cdd:PRK05857 283 ATVPSLRLVGYGGsRAIAADV--RFIEATGVRTAQVYGLSETgctalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 403 TilppgqeGDIAVQVLPDRPFGLF--------THYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGY 474
Cdd:PRK05857 361 I-------GPTAPGAGPSASFGTLwikspanmLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGV 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 475 RIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELP 554
Cdd:PRK05857 434 NIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIP 513
|
490
....*....|..
gi 1958642407 555 KTVSGKVKRNEL 566
Cdd:PRK05857 514 RTQSGKVMRASL 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
79-566 |
9.46e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 119.29 E-value: 9.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEacslqRG----DRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 154
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALIA-----RGvgpeVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSG 4648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 155 SKCIITDDTLAPAVDIVAAkcenLHSKLIVSQHSREGWGNLKEMMKYASDShtcvdtkhneLMAIYFTSGTTGPPKMIGH 234
Cdd:PRK12316 4649 AALLLTQSHLLQRLPIPDG----LASLALDRDEDWEGFPAHDPAVRLHPDN----------LAYVIYTSGSTGRPKGVAV 4714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 235 THSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAP 314
Cdd:PRK12316 4715 SHGSLVNHLHATGERY-ELTPDDRVLQFMSFSFDGSHEG-LYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPP 4792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 315 TAYRMLIQNDiTRSYKFNSLKHCVSAGEPINPEVMEQ-WKKKTGLDIYEGYGQTETVLICGNFKGMK-IKPGS----MGK 388
Cdd:PRK12316 4793 VYLQQLAEHA-ERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLLWKARDgDACGAaympIGT 4871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 389 PSPAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTL--------RGNFYITGDRGYMDEDGYFW 460
Cdd:PRK12316 4872 PLGNRSGYVLDGQLNPLPVGVAGELYLG-----GEGVARGYLERPALTAERFvpdpfgapGGRLYRTGDLARYRADGVID 4946
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 461 FVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVLNpDYKLHD----QEQLKKEIQEHVKK 536
Cdd:PRK12316 4947 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLV-GYVVPQ-DPALADadeaQAELRDELKAALRE 5024
|
490 500 510
....*....|....*....|....*....|
gi 1958642407 537 TTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:PRK12316 5025 RLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
83-517 |
3.33e-27 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 115.77 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG--TVLI-PGttqLTQKDILYRLQSSKSKCII 159
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGavPVLVdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 160 TddtlapavdIVAA---------KCENLHSKLIVSQhsREGWGN--LKEMM-KYASDSHTCVDTKHNELMAIYFTSGTTG 227
Cdd:PRK09274 119 G---------IPKAhlarrlfgwGKPSVRRLVTVGG--RLLWGGttLATLLrDGAAAPFPMADLAPDDMAAILFTSGSTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 228 PPKMIGHTHSSF---------GLGLSVNGRfwlDLIASDVMwntsdtgwaksawsSVFSPwtqgACVFAHYLPRFDST-- 296
Cdd:PRK09274 188 TPKGVVYTHGMFeaqiealreDYGIEPGEI---DLPTFPLF--------------ALFGP----ALGMTSVIPDMDPTrp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 297 ------SILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKK--KTGLDIYEGYGQTE 368
Cdd:PRK09274 247 atvdpaKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 369 TVLICgnfkgmKIkpGS------------------MGKPSPAFNVEILD---------ENGTILPPGQEGDIAVQ---VL 418
Cdd:PRK09274 327 ALPIS------SI--ESreilfatraatdngagicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAgpmVT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 419 PDrpfglfthYVDNPSKTA-----STLRGNFYITGDRGYMDEDGYFWFVAR-SDDVILSSGyRIGPFEVESALIEHPSIA 492
Cdd:PRK09274 399 RS--------YYNRPEATRlakipDGQGDVWHRMGDLGYLDAQGRLWFCGRkAHRVETAGG-TLYTIPCERIFNTHPGVK 469
|
490 500
....*....|....*....|....*.
gi 1958642407 493 ESAVVSSPDPirGEVVKAFIV-LNPD 517
Cdd:PRK09274 470 RSALVGVGVP--GAQRPVLCVeLEPG 493
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-560 |
5.39e-27 |
|
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: 112.48 E-value: 5.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPKMIGHTHSSFGLGLS-----VNGRFWLDLIASDVMWNTSDTGW--------AKSAWSSVFSPWTQGACV 285
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMggadfGTGEFTPSEDAHKAAAAAAGTVMfpapplmhGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 286 FAHylPRFDSTSILQTLSKFPITVFCSAPTAY-RMLIQN-DITRSYKFNSLKHCVSAGEPINPEVMEQW-KKKTGLDIYE 362
Cdd:cd05924 88 LPD--DRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDAlRDAGPYDLSSLFAISSGGALLSPEVKQGLlELVPNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 363 GYGQTET-VLICGNFKGMKIKPGSMGKPSPafNVEILDENGTILPPGQEGdiaVQVLPDR---PFGlfthYVDNPSKTAS 438
Cdd:cd05924 166 AFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGG---VGWIARRghiPLG----YYGDEAKTAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 439 TLR---GNFY-ITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVL 514
Cdd:cd05924 237 TFPevdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958642407 515 NPDYKLHDQeqlkkEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGK 560
Cdd:cd05924 317 REGAGVDLE-----ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
79-570 |
1.17e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.03 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILteacsLQRG---DR-VMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 154
Cdd:PRK12467 3118 DQQLSYAELNRRANRLAHRL-----IAIGvgpDVlVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSG 3192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 155 SKCIITDDTLAPAVDIVAAkcenLHSkLIVSQHSREGWgnlkemmkyaSDSHTCVDTKHNELMAIYFTSGTTGPPKMIGH 234
Cdd:PRK12467 3193 VKLLLTQAHLLEQLPAPAG----DTA-LTLDRLDLNGY----------SENNPSTRVMGENLAYVIYTSGSTGKPKGVGV 3257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 235 THSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFCSAP 314
Cdd:PRK12467 3258 RHGALANHLCWIAEAY-ELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPP 3335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 315 TAYRMLIQNDITRSYkfNSLKHCVSAGEPINPEVMEQWKKKTG-LDIYEGYGQTETVLI-----CGNFKGMKIKPGSMGK 388
Cdd:PRK12467 3336 AYLQQFAEDAGGADC--ASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTvtlwkCGGDAVCEAPYAPIGR 3413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 389 PSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTA--------STLRGNFYITGDRGYMDEDGYFW 460
Cdd:PRK12467 3414 PVAGRSIYVLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAerfvadpfSGSGGRLYRTGDLARYRADGVIE 3488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 461 FVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpDPIRGEVVKAFIVLNPdyklhDQEQLKKEIQEHVKKTTAP 540
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAD-----PQGDWRETLRDHLAASLPD 3562
|
490 500 510
....*....|....*....|....*....|
gi 1958642407 541 YKYPRKIEFIEELPKTVSGKVKRNELRRKE 570
Cdd:PRK12467 3563 YMVPAQLLVLAAMPLGPNGKVDRKALPDPD 3592
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
81-566 |
3.56e-26 |
|
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: 111.49 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIIT 160
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 161 DDtlapavdivaakcenlhsklivsqhsregwGNLKEMMkyasdshtcvdtkhnelmaiyFTSGTTGPPKMIGHTHSSFg 240
Cdd:cd17645 102 NP------------------------------DDLAYVI---------------------YTSGSTGLPKGVMIEHHNL- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 241 lglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLP---RFDSTSILQTLSKFPITV-FCS 312
Cdd:cd17645 130 ----VNLCEWhrpyFGVTPADKSLVYASFSFDASAWE-IFPHLTAGAAL--HVVPserRLDLDALNDYFNQEGITIsFLP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 313 APTAYR-MLIQNditrsykfNSLKHCVSAGEPINPevmeqwKKKTGLDIYEGYGQTETVLICGNFKGMKIKPG-SMGKPS 390
Cdd:cd17645 203 TGAAEQfMQLDN--------QSLRVLLTGGDKLKK------IERKGYKLVNNYGPTENTVVATSFEIDKPYANiPIGKPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 391 PAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVA 463
Cdd:cd17645 269 DNTRVYILDEALQLQPIGVAGELCIA-----GEGLARGYLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 464 RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnpdyklhDQEQLKKEIQEHVKKTTAPYKY 543
Cdd:cd17645 344 RLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA-------PEEIPHEELREWLKNDLPDYMI 416
|
490 500
....*....|....*....|...
gi 1958642407 544 PRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd17645 417 PTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
211-566 |
4.16e-26 |
|
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: 111.26 E-value: 4.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 211 TKHNELMAIYFTSGTTGPPKMIGHTHSSfglglSVNGRFWldliasdvmwntSDTGWAKSAWSSV--------------- 275
Cdd:cd12115 102 TDPDDLAYVIYTSGSTGRPKGVAIEHRN-----AAAFLQW------------AAAAFSAEELAGVlastsicfdlsvfel 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 276 FSPWTQGACVF----AHYL---PRFDSTSILQTLskfpitvfcsaPTAYRMLI-QNDITRSYKFNSLkhcvsAGEPINPE 347
Cdd:cd12115 165 FGPLATGGKVVladnVLALpdlPAAAEVTLINTV-----------PSAAAELLrHDALPASVRVVNL-----AGEPLPRD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 348 -VMEQWKKKTGLDIYEGYGQTE-----TVLICGnfKGMKIKPgSMGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdr 421
Cdd:cd12115 229 lVQRLYARLQVERVVNLYGPSEdttysTVAPVP--PGASGEV-SIGRPLANTQAYVLDRALQPVPLGVPGELYIG----- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 422 PFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAES 494
Cdd:cd12115 301 GAGVARGYLGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREA 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642407 495 AVVSSPDPIRGEVVKAFIVLNPDYKLhdqeqLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd12115 381 VVVAIGDAAGERRLVAYIVAEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
79-568 |
7.38e-26 |
|
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: 111.37 E-value: 7.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPavdiVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCV-DTKHNELMAIYFTSGTTGPPKMIGHTHS 237
Cdd:cd05915 101 LFDPNLLP----LVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPvRVPERAACGMAYTTGTTGLPKGVVYSHR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 238 SFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFDSTsILQTLSKFPITVFCSAPTAY 317
Cdd:cd05915 177 ALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPAS-LVELFDGEGVTFTAGVPTVW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 318 RMLI--QNDITRSYKFNSLkhcVSAGEPINPEVMEQWKKKTGLDIYEGYGQTET------VLICGNFKGMKIKPGSMGKP 389
Cdd:cd05915 256 LALAdyLESTGHRLKTLRR---LVVGGSAAPRSLIARFERMGVEVRQGYGLTETspvvvqNFVKSHLESLSEEEKLTLKA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 390 SPAFN-----VEILDENGTILPpgQEGDiAVQVLPDRPFGLFTHYV-DNPSKTASTLRGNFYITGDRGYMDEDGYFWFVA 463
Cdd:cd05915 333 KTGLPiplvrLRVADEEGRPVP--KDGK-ALGEVQLKGPWITGGYYgNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 464 RSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIvlnpdyKLHDQEQLKKEIQEHVKKTTAPYKY 543
Cdd:cd05915 410 RLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVV------VPRGEKPTPEELNEHLLKAGFAKWQ 483
|
490 500
....*....|....*....|....*.
gi 1958642407 544 -PRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:cd05915 484 lPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
79-566 |
8.85e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 113.13 E-value: 8.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:PRK12316 534 EETLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDiVAAKCENL---HSKLIVSQHSREgwgNLKemmkyasdshTCVDTKHneLMAIYFTSGTTGPPKMIGHT 235
Cdd:PRK12316 613 LSQSHLGRKLP-LAAGVQVLdldRPAAWLEGYSEE---NPG----------TELNPEN--LAYVIYTSGSTGKPKGAGNR 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 236 HSSFglglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFDSTSILQTLSKFPITVF 310
Cdd:PRK12316 677 HRAL-----SNRLCWmqqaYGLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDHRDPAKLVELINREGVDTL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 311 CSAPTAYRMLIQNDITRSykFNSLKHCVSAGEPINPEVMEQ-WKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGS--MG 387
Cdd:PRK12316 751 HFVPSMLQAFLQDEDVAS--CTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSvpIG 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 388 KPSPAFNVEILDENGTILPPGQEGDIavqVLPDRpfGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFW 460
Cdd:PRK12316 829 RPIANLACYILDANLEPVPVGVLGEL---YLAGR--GLARGYHGRPGLTAERFVPSpfvagerMYRTGDLARYRADGVIE 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 461 FVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSspdpIRGEVVKAFIVLNpdyklHDQEQLKKEIQEHVKKTTAP 540
Cdd:PRK12316 904 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLE-----SEGGDWREALKAHLAASLPE 974
|
490 500
....*....|....*....|....*.
gi 1958642407 541 YKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:PRK12316 975 YMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
79-566 |
1.05e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 112.95 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:PRK12467 535 EQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLL 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDIVAAKcenlhSKLIVSQHSREGWGnlkemmkyASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSS 238
Cdd:PRK12467 614 LTQSHLLAQLPVPAGL-----RSLCLDEPADLLCG--------YSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGA 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 239 FGLGLSVNGRfWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FDSTSILQTLSKFPITVFCSAPT 315
Cdd:PRK12467 681 LANYVCVIAE-RLQLAADDSMLMVSTFAFDLGVTE-LFGALASGATL--HLLPPdcaRDAEAFAALMADQGVTVLKIVPS 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 316 AYRMLIQNdiTRSYKFNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTETVLICGNFK----GMKIKPGSMGKPS 390
Cdd:PRK12467 757 HLQALLQA--SRVALPRPQRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPL 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 391 PAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTA--------STLRGNFYITGDRGYMDEDGYFWFV 462
Cdd:PRK12467 835 ANLGLYILDHYLNPVPVGVVGELYIG-----GAGLARGYHRRPALTAerfvpdpfGADGGRLYRTGDLARYRADGVIEYL 909
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 463 ARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVlnPDYKLHDQEQ--LKKEIQEHVKKTTAP 540
Cdd:PRK12467 910 GRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLV--PAAVADGAEHqaTRDELKAQLRQVLPD 986
|
490 500
....*....|....*....|....*.
gi 1958642407 541 YKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:PRK12467 987 YMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
81-568 |
1.12e-25 |
|
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: 110.32 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIP-GTTQLTQkdilyRLQSskskciI 159
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSL-GVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPlDPSHPLQ-----RLQE------I 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 160 TDDTLAPAVdivaakcenlhsklIVSQHSregwgnlkemmkyasdshtcvdtkhnELMAIYFTSGTTGPPKMIGHTHSSF 239
Cdd:cd05918 92 LQDTGAKVV--------------LTSSPS--------------------------DAAYVIFTSGSTGKPKGVVIEHRAL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 240 ---------GLGLSVNGRfWLDL--IASDVMWNtsdtgwaksawsSVFSPWTQGACV-----------FAHYLPRFDSTS 297
Cdd:cd05918 132 stsalahgrALGLTSESR-VLQFasYTFDVSIL------------EIFTTLAAGGCLcipseedrlndLAGFINRLRVTW 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 298 ILQTlskfpitvfcsaPTAYRMLIQNDITrsykfnSLKHCVSAGEPINPEVMEQWKKKTGLdiYEGYGQTE-TVLICGNF 376
Cdd:cd05918 199 AFLT------------PSVARLLDPEDVP------SLRTLVLGGEALTQSDVDTWADRVRL--INAYGPAEcTIAATVSP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 377 KGMKIKPGSMGKPSPAfNVEILDENGT--ILPPGQEGDIAV---QVLPDrpfglfthYVDNPSKTA-------------- 437
Cdd:cd05918 259 VVPSTDPRNIGRPLGA-TCWVVDPDNHdrLVPIGAVGELLIegpILARG--------YLNDPEKTAaafiedpawlkqeg 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 438 STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK---AFIVL 514
Cdd:cd05918 330 SGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPqlvAFVVL 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642407 515 NPDYKLHDQEQ------------LKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:cd05918 410 DGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
207-566 |
1.17e-25 |
|
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: 109.65 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 207 TCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFGlGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVf 286
Cdd:cd17652 86 ALLLTTPDNLAYVIYTSGSTGRPKGVVVTHRGLA-NLAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATL- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 287 aHYLPRFDSTS---ILQTLSKFPITVFCSAPTAYRMLIQNDITrsykfnSLKHCVSAGEPINPEVMEQWKKktGLDIYEG 363
Cdd:cd17652 163 -VLAPAEELLPgepLADLLREHRITHVTLPPAALAALPPDDLP------DLRTLVVAGEACPAELVDRWAP--GRRMINA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 364 YGQTETVL---ICGNFKGMKIKPgsMGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTA--- 437
Cdd:cd17652 234 YGPTETTVcatMAGPLPGGGVPP--IGRPVPGTRVYVLDARLRPVPPGVPGELYIA-----GAGLARGYLNRPGLTAerf 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 438 -----STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFI 512
Cdd:cd17652 307 vadpfGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYV 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958642407 513 VLNPDYKLhDQEQLKkeiqEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd17652 387 VPAPGAAP-TAAELR----AHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
76-569 |
2.70e-25 |
|
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: 109.48 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 76 NGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKS 155
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 156 KCIIT---DD--TLAPAVDivaakcENLHSkLIVSQHS----REGWGNLKEMMKYASDSHTcvdTKHNELMAIYFTSGTT 226
Cdd:cd05932 80 KALFVgklDDwkAMAPGVP------EGLIS-ISLPPPSaancQYQWDDLIAQHPPLEERPT---RFPEQLATLIYTSGTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 227 GPPKMIGHTHSSFG---------LGLSVNGRF--WLDL--IASDVMwntsdtgwaksawssVFSPWTQGACV--FAHYLP 291
Cdd:cd05932 150 GQPKGVMLTFGSFAwaaqagiehIGTEENDRMlsYLPLahVTERVF---------------VEGGSLYGGVLvaFAESLD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 292 RFdstsiLQTLSKFPITVFCSAP---TAYRMLIQNDITRSyKFNSL----------KHCVSAG-------------EPIN 345
Cdd:cd05932 215 TF-----VEDVQRARPTLFFSVPrlwTKFQQGVQDKIPQQ-KLNLLlkipvvnslvKRKVLKGlgldqcrlagcgsAPVP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 346 PEVMEqWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEIldengtilppGQEGDIAVqvlpdRPFGL 425
Cdd:cd05932 289 PALLE-WYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILV-----RSPAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 426 FTHYVDNPSKTASTLRGN-FYITGDRGYMDEDGYFWFVARSDDVILSS-GYRIGPFEVESALIEHPSIAESAVVSS--PD 501
Cdd:cd05932 353 MMGYYKDPEATAEAFTADgFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPA 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642407 502 PIRGEVVKAFIVLNPDYKlhDQEQLKKEIQEH---VKKTTAPYKYPRKIEFIEElPKTVSG-------KVKRNELRRK 569
Cdd:cd05932 433 PLALVVLSEEARLRADAF--ARAELEASLRAHlarVNSTLDSHEQLAGIVVVKD-PWSIDNgiltptlKIKRNVLEKA 507
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
81-567 |
7.62e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 108.26 E-value: 7.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILTeACSLQRGDRVMVIlpkipEW-----WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKS 155
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALA-ALGVEPGDRVGTL-----AWngyrhLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 156 KCIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNL-----KEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPK 230
Cdd:PRK07008 113 RYVLFDLTFLPLVDALAPQCPNVKGWVAMTDAAHLPAGSTpllcyETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 231 MIGHTHSS-----FGLGLSVNgrfwLDLIASDV------MWNTSdtgwaksAWSSVFS-PWTQGACVFAHylPRFDSTSI 298
Cdd:PRK07008 193 GALYSHRStvlhaYGAALPDA----MGLSARDAvlpvvpMFHVN-------AWGLPYSaPLTGAKLVLPG--PDLDGKSL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 299 LQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVLIcGNFKG 378
Cdd:PRK07008 260 YELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPL-GTLCK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 379 MKIKPGSMGKPS----------PAFNVE--ILDENGTILP-PGQE-GDIAVQ---VLpDRPFGlfthyvdnpsKTASTLR 441
Cdd:PRK07008 339 LKWKHSQLPLDEqrkllekqgrVIYGVDmkIVGDDGRELPwDGKAfGDLQVRgpwVI-DRYFR----------GDASPLV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 442 GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLH 521
Cdd:PRK07008 408 DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVT 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1958642407 522 DQEQLKkeiqeHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK07008 488 REELLA-----FYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
79-568 |
7.93e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.05 E-value: 7.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLA-PAVDIVAAKCenlhsklivsqhsregwgnLKEMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHS 237
Cdd:PRK12316 3159 LSQSHLRlPLAQGVQVLD-------------------LDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHS 3219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 238 SFGLGLSVNGRFwLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFDS-TSILQTLSKFPITVFCSAPTA 316
Cdd:PRK12316 3220 ALSNHLCWMQQA-YGLGVGDRVLQFTTFSFDVFVEE-LFWPLMSGARVVLAGPEDWRDpALLVELINSEGVDVLHAYPSM 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 317 YRMLIQNDITRSYKfnSLKHCVSAGEPINPEVMEQWKkkTGLDIYEGYGQTETVLICGNFKGMKIKPGS--MGKPSPAFN 394
Cdd:PRK12316 3298 LQAFLEEEDAHRCT--SLKRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRA 3373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 395 VEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWFVARSDD 467
Cdd:PRK12316 3374 CYILDGSLEPVPVGALGELYLG-----GEGLARGYHNRPGLTAERFVPDpfvpgerLYRTGDLARYRADGVIEYIGRVDH 3448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 468 VILSSGYRIGPFEVESALIEHPSIAESAVVSspdpIRGEVVKAFIVLNPdyklhDQEQLKKEIQEHVKKTTAPYKYPRKI 547
Cdd:PRK12316 3449 QVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPED-----EAGDLREALKAHLKASLPEYMVPAHL 3519
|
490 500
....*....|....*....|.
gi 1958642407 548 EFIEELPKTVSGKVKRNELRR 568
Cdd:PRK12316 3520 LFLERMPLTPNGKLDRKALPR 3540
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
79-567 |
1.28e-24 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 107.77 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTV------------LIPGTTQLTQKdi 146
Cdd:PRK10946 46 ERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGVApvnalfshqrseLNAYASQIEPA-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 147 lyRLQSSKSKCIITDDTLapaVDIVAAKCENLhskLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELMAIYFTSGTT 226
Cdd:PRK10946 123 --LLIADRQHALFSDDDF---LNTLVAEHSSL---RVVLLLNDDGEHSLDDAINHPAEDFTATPSPADEVAFFQLSGGST 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 227 GPPKMIGHTHSSFGL---------GLSVNGRFWLDLIASDvmwntsdtgwaKSAWSS-----VFspWTQGACVFAhylPR 292
Cdd:PRK10946 195 GTPKLIPRTHNDYYYsvrrsveicGFTPQTRYLCALPAAH-----------NYPMSSpgalgVF--LAGGTVVLA---PD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 293 FDSTSILQTLSKFPITVFCSAPTAYRMLIQ--NDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV 370
Cdd:PRK10946 259 PSATLCFPLIEKHQVNVTALVPPAVSLWLQaiAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 371 LicgNFKGMKIKP----GSMGKP-SPAFNVEILDENGTILPPGQEGDIAVQvlpdRPFgLFTHYVDNPSKTASTLRGN-F 444
Cdd:PRK10946 339 V---NYTRLDDSDerifTTQGRPmSPDDEVWVADADGNPLPQGEVGRLMTR----GPY-TFRGYYKSPQHNASAFDANgF 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 445 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKlhdQE 524
Cdd:PRK10946 411 YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLK---AV 487
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958642407 525 QLKKEIQEHvkkTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK10946 488 QLRRFLREQ---GIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
77-567 |
2.13e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 107.14 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 77 GKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSK 156
Cdd:PRK06018 35 GPIVRTTYAQIHDRALKVSQALDRD-GIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 157 CIITDDTLAPAVDIVAAKCENLHSKLIVSQHSREGWGNLKEMMKY------ASDSHTCVDTKHNELMAIYFTSGTTGPPK 230
Cdd:PRK06018 114 VVITDLTFVPILEKIADKLPSVERYVVLTDAAHMPQTTLKNAVAYeewiaeADGDFAWKTFDENTAAGMCYTSGTTGDPK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 231 MIGHTHSSFGL-GLSVNGRFWLDLIASDVMWNTSDTGWAkSAWSSVFSPWTQGACVFahyLP--RFDSTSILQTLSKFPI 307
Cdd:PRK06018 194 GVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHA-NSWGIAFSAPSMGTKLV---MPgaKLDGASVYELLDTEKV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 308 TVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPInPEVMEQWKKKTGLDIYEGYGQTETVLIcgnfkgmkikpGSMG 387
Cdd:PRK06018 270 TFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSPL-----------GTLA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 388 KPSPAFNVEILDENGTIL-----PP-GQEGDI---AVQVLP--DRPFGLFThyVDNPSKTASTLRGN--------FYITG 448
Cdd:PRK06018 338 ALKPPFSKLPGDARLDVLqkqgyPPfGVEMKItddAGKELPwdGKTFGRLK--VRGPAVAAAYYRVDgeildddgFFDTG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 449 DRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklhDQEQLKK 528
Cdd:PRK06018 416 DVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKP-----GETATRE 490
|
490 500 510
....*....|....*....|....*....|....*....
gi 1958642407 529 EIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK06018 491 EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
82-566 |
2.15e-24 |
|
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: 106.40 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 82 WSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 161
Cdd:cd17656 14 LTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 162 DTLApavdiVAAKCENLHSKLIVSQHSREGWGNLKemMKYASDshtcvdtkhnELMAIYFTSGTTGPPKMIGHTHSSFGL 241
Cdd:cd17656 93 RHLK-----SKLSFNKSTILLEDPSISQEDTSNID--YINNSD----------DLLYIIYTSGTTGKPKGVQLEHKNMVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 242 GLSVNGRFWLDLIASDVMWNTSDTgwAKSAWSSVFSPWTQGACVF-AHYLPRFDSTSILQTLSKFPITVFcSAPTAYRML 320
Cdd:cd17656 156 LLHFEREKTNINFSDKVLQFATCS--FDVCYQEIFSTLLSGGTLYiIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 321 IQNDitRSYK---FNSLKHCVSAGEP--INPEVMEQWKKKtGLDIYEGYGQTETVLIcgnfKGMKIKPGS-------MGK 388
Cdd:cd17656 233 IFSE--REFInrfPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGPSETHVV----TTYTINPEAeipelppIGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 389 PSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTASTLRGN-------FYITGDRGYMDEDGYFWF 461
Cdd:cd17656 306 PISNTWIYILDQEQQLQPQGIVGELYISGA-----SVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 462 VARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnPDYKLHDqEQLKKEIQEHVKKttapY 541
Cdd:cd17656 381 LGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNI-SQLREYLAKQLPE----Y 453
|
490 500
....*....|....*....|....*
gi 1958642407 542 KYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd17656 454 MIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
74-568 |
8.11e-24 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 105.63 E-value: 8.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 74 DGNGKEVRwSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEWW--LANVACLrtGTVLIPGTTQLTQKDILYRLQ 151
Cdd:PRK05620 32 GGAEQEQT-TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIIN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 152 SSKSKCIITDDTLAPAVDIVAAKCENLHSKLIVSQHS-REGWGNLKEMMKYAS-----DSHTCV----DTKHNELMAIYF 221
Cdd:PRK05620 109 HAEDEVIVADPRLAEQLGEILKECPCVRAVVFIGPSDaDSAAAHMPEGIKVYSyeallDGRSTVydwpELDETTAAAICY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 222 TSGTTGPPKMIGHTHSSFGLGLsvngrfwLDLIASDVMWNTSDTG-------WAKSAWSSVFSPWTQGACVFahyLPRFD 294
Cdd:PRK05620 189 STGTTGAPKGVVYSHRSLYLQS-------LSLRTTDSLAVTHGESflccvpiYHVLSWGVPLAAFMSGTPLV---FPGPD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 295 STSilQTLSKFPIT----VFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETV 370
Cdd:PRK05620 259 LSA--PTLAKIIATamprVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 371 LIcgnfkGMKIKPG-------------SMGKPSPAFNVEILDEnGTILPPG--QEGDIAVqvlpdRPFGLFTHYVDNPSK 435
Cdd:PRK05620 337 PV-----GTVARPPsgvsgearwayrvSQGRFPASLEYRIVND-GQVMESTdrNEGEIQV-----RGNWVTASYYHSPTE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 436 T----ASTLRGN-------------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVS 498
Cdd:PRK05620 406 EgggaASTFRGEdvedandrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642407 499 SPDPIRGEVVKAFIVLNPDYKLHDQ--EQLKKEIQEHVKKTTAPYKYprkiEFIEELPKTVSGKVKRNELRR 568
Cdd:PRK05620 486 YPDDKWGERPLAVTVLAPGIEPTREtaERLRDQLRDRLPNWMLPEYW----TFVDEIDKTSVGKFDKKDLRQ 553
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
73-568 |
9.33e-24 |
|
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: 105.06 E-value: 9.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 73 VDGNGKEVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPK----IPEWWlanvACLRTGTVLIPGTTQLTQKDILY 148
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPTYDEPNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 149 RLQSSK-------SKCIITDDTLAPAVDIVAAKCENLHSKLIVSQhsregwgnlkEMMKYASDSHTcVDTKHNELMAIYF 221
Cdd:cd05906 106 RLRKLRhiwqllgSPVVLTDAELVAEFAGLETLSGLPGIRVLSIE----------ELLDTAADHDL-PQSRPDDLALLML 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 222 TSGTTGPPKMIGHTHSSF---GLGLSVNGRF--------W--LDLIASDVMWNTSDtgwaksawssVFSPWTQGACVFAH 288
Cdd:cd05906 175 TSGSTGFPKAVPLTHRNIlarSAGKIQHNGLtpqdvflnWvpLDHVGGLVELHLRA----------VYLGCQQVHVPTEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 289 YLPrfDSTSILQTLSKFPITV-FcsAPT-AYRMLIQ---NDITRSYKFNSLKHCVSAGEPINPEVMEQWK---KKTGLD- 359
Cdd:cd05906 245 ILA--DPLRWLDLIDRYRVTItW--APNfAFALLNDlleEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLrllEPYGLPp 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 360 --IYEGYGQTET---VLICGNFKGMKIKPG----SMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLPdrpfgLFTHYV 430
Cdd:cd05906 321 daIRPAFGMTETcsgVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPV-----VTKGYY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 431 DNPSKTASTLR-GNFYITGDRGYMDeDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAES--AVVSSPDPIRGEV 507
Cdd:cd05906 396 NNPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDPGAETE 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642407 508 VKAfIVLNPDYKLHDQ-EQLKKEIQEHV-KKTTAPYKY----PRkiefiEELPKTVSGKVKRNELRR 568
Cdd:cd05906 475 ELA-IFFVPEYDLQDAlSETLRAIRSVVsREVGVSPAYliplPK-----EEIPKTSLGKIQRSKLKA 535
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
79-566 |
6.62e-23 |
|
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: 101.96 E-value: 6.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:cd12114 10 DGTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDIVAAkcenLHSKLIVSQHsregwgnlkemmkyASDSHTCVDTKHNELMAIYFTSGTTGPPK--MIGHTH 236
Cdd:cd12114 89 LTDGPDAQLDVAVFD----VLILDLDALA--------------APAPPPPVDVAPDDLAYVIFTSGSTGTPKgvMISHRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 237 SSFGLgLSVNGRFWLDliASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFAHYLPRFDSTSILQTLSKFPITVFCSAPT 315
Cdd:cd12114 151 ALNTI-LDINRRFAVG--PDDRVLALSSLSFDLSVYD-IFGALSAGATlVLPDEARRRDPAHWAELIERHGVTLWNSVPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 316 AYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKT-GLDIYEGYGQTETVlICGNFkgMKIKPGSM-------G 387
Cdd:cd12114 227 LLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEAS-IWSIY--HPIDEVPPdwrsipyG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 388 KPSPAFNVEILDENGTILPPGQEGDIavqvlpdrpF----GLFTHYVDNPSKTAS-----TLRGNFYITGDRGYMDEDGY 458
Cdd:cd12114 304 RPLANQRYRVLDPRGRDCPDWVPGEL---------WiggrGVALGYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 459 FWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPiRGEVVKAFIVLNPDYklhdQEQLKKEIQEHVKKTT 538
Cdd:cd12114 375 LEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDG----TPIAPDALRAFLAQTL 449
|
490 500
....*....|....*....|....*...
gi 1958642407 539 APYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd12114 450 PAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
79-532 |
1.80e-22 |
|
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: 100.51 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ItddtlapavdivaakcenlhsklivsqhsregwgnlkemmkyasdshtcVDTKHNELMAIYFTSGTTGPPKMIGHTHSS 238
Cdd:cd17640 82 V-------------------------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 239 FGLGLSvngRFW--LDLIASDVMWntsdtgwaksawsSVFSPW--TQGAC---VFA-----HYlprfdsTSI---LQTLS 303
Cdd:cd17640 113 LLHQIR---SLSdiVPPQPGDRFL-------------SILPIWhsYERSAeyfIFAcgcsqAY------TSIrtlKDDLK 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 304 KFPITVFCSAPTAYRML---IQNDITRSYKF-----------NSLKHCVSAGEPINPEVmEQWKKKTGLDIYEGYGQTET 369
Cdd:cd17640 171 RVKPHYIVSVPRLWESLysgIQKQVSKSSPIkqflflfflsgGIFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTET 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 370 --VLICGNFKGMKIkpGSMGKPSPAFNVEILDENG-TILPPGQEGDIAV---QVLpdrpfglfTHYVDNPSKTASTLRGN 443
Cdd:cd17640 250 spVVSARRLKCNVR--GSVGRPLPGTEIKIVDPEGnVVLPPGEKGIVWVrgpQVM--------KGYYKNPEATSKVLDSD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 444 -FYITGDRGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIaESAVVSSPDPIRgevVKAFIVlnPDYklh 521
Cdd:cd17640 320 gWFNTGDLGWLTCGGELVLTGRAKDTIvLSNGENVEPQPIEEALMRSPFI-EQIMVVGQDQKR---LGALIV--PNF--- 390
|
490
....*....|.
gi 1958642407 522 dqEQLKKEIQE 532
Cdd:cd17640 391 --EELEKWAKE 399
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
79-568 |
1.81e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 102.73 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 79 EVRWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCI 158
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRLRAR-GVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDIVAAkcenlhskLIVSQHSREGWgnlkemMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSS 238
Cdd:PRK12316 2105 LTQRHLLERLPLPAG--------VARLPLDRDAE------WADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGA 2170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 239 FGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFDSTSILQTLSKFPITVFcSAPTAYR 318
Cdd:PRK12316 2171 LVAHCQAAGERY-ELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTIL-DFPPVYL 2247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 319 MLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD-IYEGYGQTETVLICGNFKGMKIKPGS-----MGKPSPA 392
Cdd:PRK12316 2248 QQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRALGN 2327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 393 FNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTA--------STLRGNFYITGDRGYMDEDGYFWFVAR 464
Cdd:PRK12316 2328 RRAYILDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGR 2402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 465 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpDPIRGEVVKAFIVlnPDyklHDQEQLKKEIQEHVKKTTAPYKYP 544
Cdd:PRK12316 2403 IDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PD---DAAEDLLAELRAWLAARLPAYMVP 2476
|
490 500
....*....|....*....|....
gi 1958642407 545 RKIEFIEELPKTVSGKVKRNELRR 568
Cdd:PRK12316 2477 AHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
203-570 |
5.67e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.01 E-value: 5.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 203 SDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQG 282
Cdd:PRK12467 1707 SDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGAL-VNRLCATQEAYQLSAADVVLQFTSFAFDVSVWE-LFWPLING 1784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 283 A-CVFAHYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDiTRSYKFNSLKHCVSAGEPINPEVMEQWKKKTG-LDI 360
Cdd:PRK12467 1785 ArLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD-EQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGL 1863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 361 YEGYGQTETVL-----IC--GNFKGMKIKPgsMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNP 433
Cdd:PRK12467 1864 FNLYGPTETAVdvthwTCrrKDLEGRDSVP--IGQPIANLSTYILDASLNPVPIGVAGELYLGGV-----GLARGYLNRP 1936
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 434 SKTA--------STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSpDPIRG 505
Cdd:PRK12467 1937 ALTAerfvadpfGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANG 2015
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642407 506 EVVKAFIVLNPDYKLHD---QEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRRKE 570
Cdd:PRK12467 2016 KQLVAYVVPTDPGLVDDdeaQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPD 2083
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
219-573 |
1.06e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 97.80 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRFWLD-----LIASDVmwnTSDTGWAksawSSVFSPWTQGA--CVFAHYL 290
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIDREIeAYNEALNCEqdetpIVACPV---THSYGLI----CGVLAALTRGSkpVIITNKN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 291 PRFdstsILQTLSKFPITVFCSAPTAYRMLI---QNDITrsykFNSLkhcVSAGEPINPEVMEQWKKKTgLDIYEGYGQT 367
Cdd:PRK08308 179 PKF----ALNILRNTPQHILYAVPLMLHILGrllPGTFQ----FHAV---MTSGTPLPEAWFYKLRERT-TYMMQQYGCS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 368 ET--VLICGNFKgmkiKPGSMGKPSPAFNVEI-LDENgtilppgqegdiavqvlpdrpfglfthyvdNPSKTASTLRGNF 444
Cdd:PRK08308 247 EAgcVSICPDMK----SHLDLGNPLPHVSVSAgSDEN------------------------------APEEIVVKMGDKE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 445 YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYklhDQE 524
Cdd:PRK08308 293 IFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEI---DPV 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958642407 525 QLKKEIQEHVkkttAPYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTT 573
Cdd:PRK08308 370 QLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
219-563 |
2.98e-21 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 97.27 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPKMIGHTHSS-----------FGLGlsvNGRFWL-------DLiasDVMwntsdtgwaksawsSVFSPWT 280
Cdd:PRK04813 148 IIFTSGTTGKPKGVQISHDNlvsftnwmledFALP---EGPQFLnqapysfDL---SVM--------------DLYPTLA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 281 QGACVFAhyLPRfDSTS----ILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKK- 355
Cdd:PRK04813 208 SGGTLVA--LPK-DMTAnfkqLFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERf 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 356 TGLDIYEGYGQTE-TVLIcgnfKGMKI--------KPGSMGKPSPAFNVEILDENGTILPPGQEGDI-----AVQVlpdr 421
Cdd:PRK04813 285 PSATIYNTYGPTEaTVAV----TSIEItdemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIvisgpSVSK---- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 422 pfGlfthYVDNPSKTAS---TLRGN-FYITGDRGYMDeDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVV 497
Cdd:PRK04813 357 --G----YLNNPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV 429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642407 498 sspdPI-RGEVVK---AFIVLNPdyklHDQE---QLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKR 563
Cdd:PRK04813 430 ----PYnKDHKVQyliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
68-568 |
4.38e-21 |
|
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: 96.92 E-value: 4.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 68 PAFWWVD-GNGKEVRWSFEELGSLSRKFANILTEACslQRGDRVMVILPKIPEWWLANVACLRTGTV---LIPGTTQLTQ 143
Cdd:cd05931 10 PAYTFLDdEGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIavpLPPPTPGRHA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 144 KDILYRLQSSKSKCIITDDTLAPAV-DIVAAKCENLHSKLIVSQHSREGwgnlkemmkyASDSHTCVDTKHNELMAIYFT 222
Cdd:cd05931 88 ERLAAILADAGPRVVLTTAAALAAVrAFAASRPAAGTPRLLVVDLLPDT----------SAADWPPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 223 SGTTGPPK--MIGHthssfgLGLSVNgrfwLDLIASDVMWNTSDTGwakSAW----------SSVFSPWTQGA-CVF--- 286
Cdd:cd05931 158 SGSTGTPKgvVVTH------RNLLAN----VRQIRRAYGLDPGDVV---VSWlplyhdmgliGGLLTPLYSGGpSVLmsp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 287 AHYL--P-RFdstsiLQTLSKFPITvFCSAPT-AYRML---IQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKK---T 356
Cdd:cd05931 225 AAFLrrPlRW-----LRLISRYRAT-ISAAPNfAYDLCvrrVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAfapF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 357 GLD---IYEGYGQTE-TVLICGNFKG------------------MKIKPG-------SMGKPSPAFNVEILDENG-TILP 406
Cdd:cd05931 299 GFRpeaFRPSYGLAEaTLFVSGGPPGtgpvvlrvdrdalagravAVAADDpaarelvSCGRPLPDQEVRIVDPETgRELP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 407 PGQEGDIAVQ---VLPdrpfGlfthYVDNPSKTASTLR-------GNFYITGDRGYMDeDGYFWFVARSDDVILSSGYRI 476
Cdd:cd05931 379 DGEVGEIWVRgpsVAS----G----YWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNH 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 477 GPFEVESALIE-HPSIAES--AVVSSPDPIRGEVVKAFIVLNPDYKLhDQEQLKKEIQ-----EH-VKkttapykyPRKI 547
Cdd:cd05931 450 YPQDIEATAEEaHPALRPGcvAAFSVPDDGEERLVVVAEVERGADPA-DLAAIAAAIRaavarEHgVA--------PADV 520
|
570 580
....*....|....*....|...
gi 1958642407 548 EFIE--ELPKTVSGKVKRNELRR 568
Cdd:cd05931 521 VLVRpgSIPRTSSGKIQRRACRA 543
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
277-567 |
5.01e-21 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 96.22 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 277 SPWTQGACVFAHYlPRFDSTsilQTLSKFPITVFCS-APTAYRMLIQNDITRSYKFNSLkhcVSAGEPINPEVMEQwKKK 355
Cdd:PRK07445 181 SFLTGGKLVILPY-KRLKSG---QELPPNPSDFFLSlVPTQLQRLLQLRPQWLAQFRTI---LLGGAPAWPSLLEQ-ARQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 356 TGLDIYEGYGQTETV-LICgnfkgmKIKPG-------SMGKPSPAFNVEIldengtilPPGQEGDIAVQVlPDRPFGLFT 427
Cdd:PRK07445 253 LQLRLAPTYGMTETAsQIA------TLKPDdflagnnSSGQVLPHAQITI--------PANQTGNITIQA-QSLALGYYP 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 428 HYVDNPsktastlrgNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEV 507
Cdd:PRK07445 318 QILDSQ---------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEV 388
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 508 VKAFIVLNpdyklhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PRK07445 389 VTAIYVPK------DPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
83-566 |
1.25e-19 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 93.57 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 83 SFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDD 162
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 163 TLAPAVDIVaakcenlhSKLIVSQHSREGWGNLKEMMKYASDSHTCVdtkhnelmaIYFTSGTTGPPK--MIGHThssfg 240
Cdd:PRK10252 564 DQLPRFADV--------PDLTSLCYNAPLAPQGAAPLQLSQPHHTAY---------IIFTSGSTGRPKgvMVGQT----- 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 241 lgLSVNGRFWLD----LIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVF-----AHYlprfDSTSILQTLSKFPITV-- 309
Cdd:PRK10252 622 --AIVNRLLWMQnhypLTADDVVLQKTPCSFDVSVWE-FFWPFIAGAKLVmaepeAHR----DPLAMQQFFAEYGVTTth 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 310 --------FCSAPTayrmliQNDITRSYKfnSLKHCVSAGEPINPEVMEQWKKKTGLDIYEGYGQTETVL------ICG- 374
Cdd:PRK10252 695 fvpsmlaaFVASLT------PEGARQSCA--SLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVdvswypAFGe 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 375 ---NFKGMKIKPGSmgkpsPAFN--VEILDENGTILPPGQEGDI---AVQvlpdrpfgLFTHYVDNPSKTASTLRGN--- 443
Cdd:PRK10252 767 elaAVRGSSVPIGY-----PVWNtgLRILDARMRPVPPGVAGDLyltGIQ--------LAQGYLGRPDLTASRFIADpfa 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 444 ----FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESA----VVSSPDPIRGEVVK--AFIV 513
Cdd:PRK10252 834 pgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGGDARQlvGYLV 913
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1958642407 514 LNPDYKLhDQEQLkkeiQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:PRK10252 914 SQSGLPL-DTSAL----QAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
209-566 |
1.61e-19 |
|
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: 91.31 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 209 VDTKHNELMAIYFTSGTTGPPK--MIGHtHSSFGLGLSVNGRFWLDLIASDVMwntsdtgwaksawsSVFSPWtqgacVF 286
Cdd:cd17648 89 VITNSTDLAYAIYTSGTTGKPKgvLVEH-GSVVNLRTSLSERYFGRDNGDEAV--------------LFFSNY-----VF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 287 AHYLPRFdSTSIL--QTLSKFPITVFCSAPTAYRMLIQNDIT---------RSYKF---NSLKHCVSAGEPINPEVMEQW 352
Cdd:cd17648 149 DFFVEQM-TLALLngQKLVVPPDEMRFDPDRFYAYINREKVTylsgtpsvlQQYDLarlPHLKRVDAAGEEFTAPVFEKL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 353 KKKTGLDIYEGYGQTETVL--ICGNFKGMKIKPGSMGKPSPAFNVEILDENGTILPPGQEGD-------IAVQVLpDRPF 423
Cdd:cd17648 228 RSRFAGLIINAYGPTETTVtnHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGElylggdgVARGYL-NRPE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 424 GLFTHYVDNPSKTAS-TLRGNF---YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSS 499
Cdd:cd17648 307 LTAERFLPNPFQTEQeRARGRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAK 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642407 500 PDP-IRGEVVKAFIVlnpDYKLHDQEQL-KKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd17648 387 EDAsQAQSRIQKYLV---GYYLPEPGHVpESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
44-567 |
1.49e-18 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 89.37 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 44 YFNFAKDVLdqwtnTEKTGKRLSNPAFWWVD--GNGKEV-RWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEW 120
Cdd:PLN03052 173 VLNVAECCL-----TPKPSKTDDSIAIIWRDegSDDLPVnRMTLSELRSQVSRVANAL-DALGFEKGDAIAIDMPMNVHA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 121 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTL-----------------APAVDIVAAKCENLHSKLi 183
Cdd:PLN03052 247 VIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplysrvveakAPKAIVLPADGKSVRVKL- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 184 vsqhsREGWGNLKEMMKYAS-----DSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSfGLGLSVNGRFWLDLIASDV 258
Cdd:PLN03052 326 -----REGDMSWDDFLARANglrrpDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRKGDI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 259 M-WNTsDTGWAKSAWsSVFSPWTQGACvfahyLPRFDSTSILQTLSKF----PITVFCSAPTAYRMLIQNDITRSYKFNS 333
Cdd:PLN03052 400 VcWPT-NLGWMMGPW-LVYASLLNGAT-----LALYNGSPLGRGFAKFvqdaKVTMLGTVPSIVKTWKNTNCMAGLDWSS 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 334 LKHCVSAGEPINPE----VMEQWKKKTgldIYEGYGQTEtvlICGNF-KGMKIKPGSMGK---PSPAFNVEILDENGTIL 405
Cdd:PLN03052 473 IRCFGSTGEASSVDdylwLMSRAGYKP---IIEYCGGTE---LGGGFvTGSLLQPQAFAAfstPAMGCKLFILDDSGNPY 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 406 PPGQEGDIAVqvlpdrpfGLFTHYVDNPSKTASTLRGNFYITGD--------RGYMDE-----DGYFWFVARSDDVIlss 472
Cdd:PLN03052 547 PDDAPCTGEL--------ALFPLMFGASSTLLNADHYKVYFKGMpvfngkilRRHGDIfertsGGYYRAHGRADDTM--- 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 473 gyRIGPFEVESALIE------HPSIAESAVVSSPDPIRG--EVVKAFIVLNPDYKLHDQEQLKKEIQEHVKKTTAPYKYP 544
Cdd:PLN03052 616 --NLGGIKVSSVEIErvcnaaDESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKV 693
|
570 580
....*....|....*....|...
gi 1958642407 545 RKIEFIEELPKTVSGKVKRNELR 567
Cdd:PLN03052 694 SAVVIVPSFPRTASNKVMRRVLR 716
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
211-566 |
4.71e-18 |
|
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: 86.75 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 211 TKHNELMAIYFTSGTTGPPK--MIGH---THSSFGL-------GLSVN----GRFWLDLIASDvmwntsdtgWAKSAWS- 273
Cdd:cd17650 90 TQPEDLAYVIYTSGTTGKPKgvMVEHrnvAHAAHAWrreyeldSFPVRllqmASFSFDVFAGD---------FARSLLNg 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 274 SVFSPWTQGAcvfahylpRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEpinpEVMEQWK 353
Cdd:cd17650 161 GTLVICPDEV--------KLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSD----GCKAQDF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 354 K------KTGLDIYEGYGQTETVLICGNFK-GMKIKPGS----MGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdrP 422
Cdd:cd17650 229 KtlaarfGQGMRIINSYGVTEATIDSTYYEeGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIG-----G 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 423 FGLFTHYVDNPSKTASTLR-------GNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESA 495
Cdd:cd17650 304 AGVARGYLNRPELTAERFVenpfapgERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAV 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642407 496 VVSSPDPiRGEV-VKAFIVlnPDYKLHdqeqlKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd17650 384 VAVREDK-GGEArLCAYVV--AAATLN-----TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
82-563 |
5.07e-18 |
|
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: 87.48 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 82 WSFEELGSLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITD 161
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 162 DTlaPAVDIVAAKCENLHS--KLIVS--------QHSREGW-GNLKEMMKYASDSHTCV------DTKHNELMAIYFTSG 224
Cdd:cd17641 91 DE--EQVDKLLEIADRIPSvrYVIYCdprgmrkyDDPRLISfEDVVALGRALDRRDPGLyerevaAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 225 TTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACV-FAHylprfDSTSILQTLS 303
Cdd:cd17641 169 TTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVnFPE-----EPETMMEDLR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 304 KFPITVFCSAP------------------------------TAYRMLIQND-------------------ITRSYK---- 330
Cdd:cd17641 243 EIGPTFVLLPPrvwegiaadvrarmmdatpfkrfmfelgmkLGLRALDRGKrgrpvslwlrlaswladalLFRPLRdrlg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 331 FNSLKHCVSAGEPINPEVMeQWKKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEIlDENGTILPPGQe 410
Cdd:cd17641 323 FSRLRSAATGGAALGPDTF-RFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI-DEVGEILVRSP- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 411 gdiavqvlpdrpfGLFTHYVDNPSKTASTL-RGNFYITGDRGYMDEDGYFWFVARSDDV-ILSSGYRIGPFEVESALIEH 488
Cdd:cd17641 400 -------------GVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 489 PSIAESAVVSSPDPIrgevVKAFIVLNP---------------DYK-LHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEE 552
Cdd:cd17641 467 PYIAEAVVLGAGRPY----LTAFICIDYaivgkwaeqrgiaftTYTdLASRPEVYELIRKEVEKVNASLPEAQRIRRFLL 542
|
570 580
....*....|....*....|
gi 1958642407 553 LPK---------TVSGKVKR 563
Cdd:cd17641 543 LYKeldaddgelTRTRKVRR 562
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
38-560 |
1.74e-17 |
|
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: 85.79 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 38 KIEIPEYF-----NFAKDVLdqwtntekTGKRLSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMV 112
Cdd:cd05943 58 IMPGARWFpgarlNYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAAL-RALGVKPGDRVAG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 113 ILPKIPEwwlANVACLRT---GTVLIPGTTQLTQKDILYRLQSSKSKCIITDDT---------LAPAVDIVAAKCENLHS 180
Cdd:cd05943 129 YLPNIPE---AVVAMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAytyngkrhdVREKVAELVKGLPSLLA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 181 KLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNEL----------MAIYFTSGTTGPPKMIghTHSSFGLGLSVNGRFW 250
Cdd:cd05943 206 VVVVPYTVAAGQPDLSKIAKALTLEDFLATGAAGELefeplpfdhpLYILYSSGTTGLPKCI--VHGAGGTLLQHLKEHI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 251 L--DLIASDVM-WNTSdTGWAksAWSSVFSPWTQGA-CVFAHYLPRFDSTSILQTL-SKFPITVFCSAPTAYRMLIQNDI 325
Cdd:cd05943 284 LhcDLRPGDRLfYYTT-CGWM--MWNWLVSGLAVGAtIVLYDGSPFYPDTNALWDLaDEEGITVFGTSAKYLDALEKAGL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 326 T--RSYKFNSLKHCVSAGEPINPE----VMEQWKKktGLDIYEGYGQTEtvlICGNFKGMK----IKPGSMGKPSPAFNV 395
Cdd:cd05943 361 KpaETHDLSSLRTILSTGSPLKPEsfdyVYDHIKP--DVLLASISGGTD---IISCFVGGNpllpVYRGEIQCRGLGMAV 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 396 EILDENGTILPpGQEGD-IAVQVLPDRPfglfTHYVDNPSktASTLRGNFYIT-------GDRGYMDEDGYFWFVARSDD 467
Cdd:cd05943 436 EAFDEEGKPVW-GEKGElVCTKPFPSMP----VGFWNDPD--GSRYRAAYFAKypgvwahGDWIEITPRGGVVILGRSDG 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 468 VILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLhdQEQLKKEIQEHVKKTTAPYKYPRKI 547
Cdd:cd05943 509 TLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVEL--DDELRKRIRSTIRSALSPRHVPAKI 586
|
570
....*....|...
gi 1958642407 548 EFIEELPKTVSGK 560
Cdd:cd05943 587 IAVPDIPRTLSGK 599
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
81-501 |
2.71e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 85.31 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTV--LIpgTTQLTQKDILYRLQSSKSKCI 158
Cdd:PRK08279 62 SISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAKLGAVvaLL--NTQQRGAVLAHSLNLVDAKHL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 159 ITDDTLAPAVDIVAAKCENLHSKLIVSQ---HSREGWGNLKEMMKyASDSHTCVDTKH--NELMAIY-FTSGTTGPPKMI 232
Cdd:PRK08279 139 IVGEELVEAFEEARADLARPPRLWVAGGdtlDDPEGYEDLAAAAA-GAPTTNPASRSGvtAKDTAFYiYTSGTTGLPKAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 233 GHTH-----SSFGLGLSvngrfwLDLIASDVMWNT----SDTGwAKSAWSSVFSPwtqGACVFAHylPRFDSTSILQTLS 303
Cdd:PRK08279 218 VMSHmrwlkAMGGFGGL------LRLTPDDVLYCClplyHNTG-GTVAWSSVLAA---GATLALR--RKFSASRFWDDVR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 304 KFPITVFCsaptaY-----RMLIQNDITRSYKFNSLKHCVSAGepINPEVMEQWKKKTGLD-IYEGYGQTE--TVLIcgN 375
Cdd:PRK08279 286 RYRATAFQ-----YigelcRYLLNQPPKPTDRDHRLRLMIGNG--LRPDIWDEFQQRFGIPrILEFYAASEgnVGFI--N 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 376 FKGmkiKPGSMGKpSPAFN------VEILDENGTIL----------PPGQEGDIAVQVLPDRPfglFTHYVDnPSKT-AS 438
Cdd:PRK08279 357 VFN---FDGTVGR-VPLWLahpyaiVKYDVDTGEPVrdadgrcikvKPGEVGLLIGRITDRGP---FDGYTD-PEASeKK 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642407 439 TLRGNF------YITGDRGYMDEDGYFWFVARSDDVilssgYR-----IGPFEVESALIEHPSIAESAV--VSSPD 501
Cdd:PRK08279 429 ILRDVFkkgdawFNTGDLMRDDGFGHAQFVDRLGDT-----FRwkgenVATTEVENALSGFPGVEEAVVygVEVPG 499
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
81-568 |
5.79e-17 |
|
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: 83.63 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEW---WLAnVACLRTGTVLIpgTTQLTQKDILYRLQSSKSKC 157
Cdd:cd05939 3 HWTFRELNEYSNKVANFF-QAQGYRSGDVVALFMENRLEFvalWLG-LAKIGVETALI--NSNLRLESLLHCITVSKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 158 IITDdtlapavdivaakcenlHSKLIVSQHSREgwgnlkemmkyasdSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHS 237
Cdd:cd05939 79 LIFN-----------------LLDPLLTQSSTE--------------PPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 238 SFgLGLSVNGRFWLDLIASDVMWNTsdtgwaKSAWSSVFSPWTQGACVFahylprFDSTSILQtlSKFPITVFCSAPTAY 317
Cdd:cd05939 128 RY-YRIAAGAYYAFGMRPEDVVYDC------LPLYHSAGGIMGVGQALL------HGSTVVIR--KKFSASNFWDDCVKY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 318 RMLIQNDI--------TRSYKFNSLKHCV--SAGEPINPEVMEQWKKKTGL-DIYEGYGQTETVLICGNFKG-------- 378
Cdd:cd05939 193 NCTIVQYIgeicryllAQPPSEEEQKHNVrlAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEGNSSLVNIDNhvgacgfn 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 379 ----MKIKPGSMGKPSPAFNVEILDENGTILP--PGQEGDIAVQVLPDRPFGLFTHYVDNPSKTASTLRGNF------YI 446
Cdd:cd05939 273 srilPSVYPIRLIKVDEDTGELIRDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDVFkkgdsaFL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 447 TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKAFIVlNPDYKLhDQE 524
Cdd:cd05939 353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPG-VEGRAGMAAIV-DPERKV-DLD 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1958642407 525 QLKKEIQehvkKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:cd05939 430 RFSAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
214-566 |
3.83e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 82.52 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 214 NELMAIYFTSGTTGPPKmighthssfglGLSVNGRF----------WLDLIASDVMWNTSDTGWAKSAWSSVFSPWTqGA 283
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPK-----------GVMVEQRGmlnnqlskvpYLALSEADVIAQTASQSFDISVWQFLAAPLF-GA 3936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 284 CV------FAHylprfDSTSILQTLSKFPITVFCSAPT-AYRMLIQNDITrsykFNSLKHCVSAGEPINPEVMEQW-KKK 355
Cdd:PRK05691 3937 RVeivpnaIAH-----DPQGLLAHVQAQGITVLESVPSlIQGMLAEDRQA----LDGLRWMLPTGEAMPPELARQWlQRY 4007
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 356 TGLDIYEGYGQTETVLICGNFK-GMKIKPGS---MGKPSPAFNVEILDENGTILPPGQEGDIAVQvlpdrPFGLFTHYVD 431
Cdd:PRK05691 4008 PQIGLVNAYGPAECSDDVAFFRvDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVG 4082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 432 NPSKTASTLRGN--------FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPi 503
Cdd:PRK05691 4083 DPLRTALAFVPHpfgapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV- 4161
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642407 504 RGEVVKAFIVlnPDYKLHDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:PRK05691 4162 NGKHLVGYLV--PHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
211-497 |
4.24e-16 |
|
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: 80.97 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 211 TKHNELMAIYFTSGTTGPPKMIGHTHSSFGLGLsvngrfwlDLIASDVMWNTSDTGWAKSAWSSVFSPwtqgACVFAHYL 290
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQI--------DALRQLYGIRPGEVDLATFPLFALFGP----ALGLTSVI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 291 PRFDSTS--------ILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKK--KTGLDI 360
Cdd:cd05910 150 PDMDPTRparadpqkLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKmlSDEAEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 361 YEGYGQTETVLICG-------NFKGMKIKPGS---MGKPSPAFNVEILD---------ENGTILPPGQEGDIAV---QVL 418
Cdd:cd05910 230 LTPYGATEALPVSSigsrellATTTAATSGGAgtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVtgpTVT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 419 PDrpfglfthYVDNPSKTA----STLRGNF-YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAE 493
Cdd:cd05910 310 PT--------YVNRPVATAlakiDDNSEGFwHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRR 381
|
....
gi 1958642407 494 SAVV 497
Cdd:cd05910 382 SALV 385
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
114-567 |
1.33e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 79.47 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 114 LPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTL----------------APAVDIV-AAKCE 176
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVlrggralplyskvveaAPAKAIVlPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 177 NLHSKLivsqhsREGWGNLKEMMKYASDSHtCVDTKHNE--------LMAIYFTSGTTGPPKMIGHTHSSfGLGLSVNGR 248
Cdd:PLN03051 81 PVAVPL------REQDLSWCDFLGVAAAQG-SVGGNEYSpvyapvesVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 249 FWLDLIASDVM-WNTSdTGWAKSAWsSVFSPWTQGACVfAHYLPRFDSTSILQTLSKFPITVFCSAPTayrmliqndITR 327
Cdd:PLN03051 153 AHMDIQPGDVVcWPTN-LGWMMGPW-LLYSAFLNGATL-ALYGGAPLGRGFGKFVQDAGVTVLGLVPS---------IVK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 328 SYK-----------FNSLKHCVSAGEPINPE------VMEQWKKKT-----GLDIYEGYGQTETVLICGnfkgmkikPGS 385
Cdd:PLN03051 221 AWRhtgafamegldWSKLRVFASTGEASAVDdvlwlsSVRGYYKPVieycgGTELASGYISSTLLQPQA--------PGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 386 MGKPSPAFNVEILDENGTILPPGQE--GDIAVQVL----PDRpfgLF------THYVDNP--SKTASTLRGNfyitGDRG 451
Cdd:PLN03051 293 FSTASLGTRFVLLNDNGVPYPDDQPcvGEVALAPPmlgaSDR---LLnadhdkVYYKGMPmyGSKGMPLRRH----GDIM 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 452 YMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIE-HPSIAESAVVSSPDPIRGE----VVKAFIVLNPDYKLHDQEQL 526
Cdd:PLN03051 366 KRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEAL 445
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1958642407 527 KKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELR 567
Cdd:PLN03051 446 QKKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
213-573 |
2.25e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.21 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 213 HNELMAIYfTSGTTGPPKMIGHTHSSFGLGLSvngrfWLD----LIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFA 287
Cdd:PRK05691 1273 DNLAYVIY-TSGSTGQPKGVGNTHAALAERLQ-----WMQatyaLDDSDVLMQKAPISFDVSVWE-CFWPLITGCrLVLA 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 288 HYLPRFDSTSILQTLSKFPITVFCSAPTAYRMLIQNdiTRSYKFNSLKHCVSAGEPINPE----VMEQWKkktGLDIYEG 363
Cdd:PRK05691 1346 GPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDE--PLAAACTSLRRLFSGGEALPAElrnrVLQRLP---QVQLHNR 1420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 364 YGQTETVL-----ICGNFKGMKikpGSMGKPSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTA- 437
Cdd:PRK05691 1421 YGPTETAInvthwQCQAEDGER---SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGA-----GLARGYLGRPALTAe 1492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 438 -------STLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVsspdpIRGEVVKA 510
Cdd:PRK05691 1493 rfvpdplGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGA 1567
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642407 511 FIV--LNPDYKLHDQ-EQLKKEIQEHVKKttapYKYPRKIEFIEELPKTVSGKVKRNELRRKEWTT 573
Cdd:PRK05691 1568 QLVgyYTGEAGQEAEaERLKAALAAELPE----YMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ 1629
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
74-566 |
3.77e-15 |
|
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: 77.90 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 74 DGNGKEVRWSFEELGSLSRKFANILTEacSLQRGDRVMVI-LPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 152
Cdd:cd17654 9 DQTTSDTTVSYADLAEKISNLSNFLRK--KFQTEERAIGLrCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 153 SKSKCIITDdtlapavdivaakCENLHSKLivsqhsregwgnlkemmkYASDSHTCVDTKHNELMA-IYFTSGTTGPPKM 231
Cdd:cd17654 87 CHVSYLLQN-------------KELDNAPL------------------SFTPEHRHFNIRTDECLAyVIHTSGTTGTPKI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 232 IGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAwSSVFSPWTQGACVFAHYLPRFDSTSILQTL--SKFPITV 309
Cdd:cd17654 136 VAVPHKCI-LPNIQHFRSLFNITSEDILFLTSPLTFDPSV-VEIFLSLSSGATLLIVPTSVKVLPSKLADIlfKRHRITV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 310 FCSAPTAYRMLIQNDITRSY--KFNSLKHCVSAGEPInPE--VMEQWKKK-TGLDIYEGYGQTETVlICGNFKGMKIK-- 382
Cdd:cd17654 214 LQATPTLFRRFGSQSIKSTVlsATSSLRVLALGGEPF-PSlvILSSWRGKgNRTRIFNIYGITEVS-CWALAYKVPEEds 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 383 PGSMGKPSPAFNVEILDENGTiLPPGQ---EGDIAVQVLPDrpfglfthYVDNPsktastlRGNFYITGDRGYMdEDGYF 459
Cdd:cd17654 292 PVQLGSPLLGTVIEVRDQNGS-EGTGQvflGGLNRVCILDD--------EVTVP-------KGTMRATGDFVTV-KDGEL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 460 WFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDpirgEVVKAFIVLnpdyklhdqEQLKKEIQEHVKKTT- 538
Cdd:cd17654 355 FFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVG---------ESSSSRIHKELQLTLl 421
|
490 500
....*....|....*....|....*...
gi 1958642407 539 APYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd17654 422 SSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
219-566 |
1.80e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.13 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYfTSGTTGPPKMIGHTHSSFGLGL-SVNGRFwlDLIASDVMWNTSDTGWaKSAWSSVFSPWTQGACVFAHYLPRFDSTS 297
Cdd:PRK05691 2339 IY-TSGSTGKPKGVVVSHGEIAMHCqAVIERF--GMRADDCELHFYSINF-DAASERLLVPLLCGARVVLRAQGQWGAEE 2414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 298 ILQTLSKFPITVFCSAPTAYRMLIQNDITRsYKFNSLKHCVSAGEPINPEVMEQWKKKTGLD-IYEGYGQTETV---LIC 373
Cdd:PRK05691 2415 ICQLIREQQVSILGFTPSYGSQLAQWLAGQ-GEQLPVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTETVvmpLAC 2493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 374 GNFKGMKIKPGS--MGKPSPAFNVEILDENGTILPPGQEGDIAVQVLpdrpfGLFTHYVDNPSKTA--------STLRGN 443
Cdd:PRK05691 2494 LAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGR 2568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 444 FYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDP----IRGEVVKAFIVLNPDyk 519
Cdd:PRK05691 2569 LYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPsgkqLAGYLVSAVAGQDDE-- 2646
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958642407 520 lhDQEQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:PRK05691 2647 --AQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
218-561 |
1.85e-14 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 76.93 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 218 AIYFTSGTTGPPKMIGHTHSSFglgLS----VNGRfwLDLIASDVMWNTsdtgwaksawssvfspwtqgacvfahyLPRF 293
Cdd:PRK06814 797 VILFTSGSEGTPKGVVLSHRNL---LAnraqVAAR--IDFSPEDKVFNA---------------------------LPVF 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 294 DS---TS--ILQTLSKFPITVFCSaPTAYR------------MLIQND--------ITRSYKFNSLKHCVSAGEPINPEV 348
Cdd:PRK06814 845 HSfglTGglVLPLLSGVKVFLYPS-PLHYRiipeliydtnatILFGTDtflngyarYAHPYDFRSLRYVFAGAEKVKEET 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 349 MEQWKKKTGLDIYEGYGQTET--VLICGNfkGMKIKPGSMGKPSPAFN-----VEILDENGTILPPGqegdiavqvlPDR 421
Cdd:PRK06814 924 RQTWMEKFGIRILEGYGVTETapVIALNT--PMHNKAGTVGRLLPGIEyrlepVPGIDEGGRLFVRG----------PNV 991
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 422 PFGlfthYV--DNPSkTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSS 499
Cdd:PRK06814 992 MLG----YLraENPG-VLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSI 1066
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642407 500 PDPIRGEVvkafIVLnpdykLHDQEQLKKE-IQEHVKKTTAPYKY-PRKIEFIEELPKTVSGKV 561
Cdd:PRK06814 1067 PDARKGER----IIL-----LTTASDATRAaFLAHAKAAGASELMvPAEIITIDEIPLLGTGKI 1121
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
214-569 |
2.72e-14 |
|
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: 75.60 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 214 NELMAIYFTSGTTGPPKMIGHTHSSfglgLSVNGRfwldLIASDVMWNTSDT--GWAksawssvfsPWTQG--------A 283
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHEN----LVHNMF----AILNSTEWKTKDRilSWM---------PLTHDmgliafhlA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 284 CVFAHYLPRFDSTSI--------LQTLSKFPITVFCSAPTAYRMLI---QNDITRSYKFNSLKHCVSAGEPINPEVMEQW 352
Cdd:cd05908 169 PLIAGMNQYLMPTRLfirrpilwLKKASEHKATIVSSPNFGYKYFLktlKPEKANDWDLSSIRMILNGAEPIDYELCHEF 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 353 KK---KTGLD---IYEGYGQTE-TVLICGNFKGMKIKPG---------------------------SMGKPSPAFNVEIL 398
Cdd:cd05908 249 LDhmsKYGLKrnaILPVYGLAEaSVGASLPKAQSPFKTItlgrrhvthgepepevdkkdsecltfvEVGKPIDETDIRIC 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 399 DENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGN-FYITGDRGYMdEDGYFWFVARSDDVILSSGYRIG 477
Cdd:cd05908 329 DEDNKILPDGYIGHIQI-----RGKNVTPGYYNNPEATAKVFTDDgWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVY 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 478 PFEVESALIEHPSIAESAVVS---SPDPIRGEVVKAFIVLNPdyKLHDQEQLKKEIQEHVKKTTApyKYPRKIEFIEELP 554
Cdd:cd05908 403 PHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRK--SEDDFYPLGKKIKKHLNKRGG--WQINEVLPIRRIP 478
|
410
....*....|....*
gi 1958642407 555 KTVSGKVKRNELRRK 569
Cdd:cd05908 479 KTTSGKVKRYELAQR 493
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
81-556 |
3.51e-14 |
|
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: 75.41 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILTEACSLQRGDRVMVILPKIPEW---WLAnVACLRTGTVLIPgtTQLTQKDILYRLQSSKSKC 157
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLG-LAKLGCPVAFLN--TNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 158 IITDDTLAPAVDIV--AAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHNELM---AIY-FTSGTTGPPK- 230
Cdd:cd05938 82 LVVAPELQEAVEEVlpALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIkspALYiYTSGTTGLPKa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 231 -MIGHTHSSFGLG-LSVNGrfwldLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAhylPRFDSTSILQTLSKFPI 307
Cdd:cd05938 162 aRISHLRVLQCSGfLSLCG-----VTADDVIYITLPLYHSSGFLLGIGGCIELGAtCVLK---PKFSASQFWDDCRKHNV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 308 TVF----------CSAPtayrmliQNDITRSYKFNslkhcVSAGEPINPEVMEQWKKKTG-LDIYEGYGQTETVLICGNF 376
Cdd:cd05938 234 TVIqyigellrylCNQP-------QSPNDRDHKVR-----LAIGNGLRADVWREFLRRFGpIRIREFYGSTEGNIGFFNY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 377 KGmkiKPGSMGKPS-------P----AFNVE----ILDENGTILP--PGQEGDIAVQVLPDRPfglFTHYVDNPSKTAST 439
Cdd:cd05938 302 TG---KIGAVGRVSylykllfPfeliKFDVEkeepVRDAQGFCIPvaKGEPGLLVAKITQQSP---FLGYAGDKEQTEKK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 440 L------RGNFYI-TGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKA 510
Cdd:cd05938 376 LlrdvfkKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPG-HEGRIGMA 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1958642407 511 FIVLNPDYKLhDQEQLkkeiQEHVKKTTAPYKYPRKIEFIEELPKT 556
Cdd:cd05938 455 AVKLKPGHEF-DGKKL----YQHVREYLPAYARPRFLRIQDSLEIT 495
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
445-568 |
7.00e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 73.16 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 445 YITGDRGYMDeDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyklHDQE 524
Cdd:PRK07824 236 FRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDG----GPAP 310
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1958642407 525 QLkKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:PRK07824 311 TL-EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
81-568 |
9.17e-14 |
|
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: 73.54 E-value: 9.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 81 RWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLtqkdilyRLQSskskciit 160
Cdd:cd05940 3 ALTYAELDAMANRYARWL-KSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNL-------RGES-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 161 ddtLAPAVDIVAAKcenlhsklivsqhsregwgnlkemmkyasdsHTCVDTkhneLMAIYfTSGTTGPPKMIGHTHSSFG 240
Cdd:cd05940 67 ---LAHCLNVSSAK-------------------------------HLVVDA----ALYIY-TSGTTGLPKAAIISHRRAW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 241 LGLSVNGrFWLDLIASDVMWNTsdtgwaksawssvfspwtqgacvfahyLPRFDSTSILQTLS-------------KFPI 307
Cdd:cd05940 108 RGGAFFA-GSGGALPSDVLYTC---------------------------LPLYHSTALIVGWSaclasgatlvirkKFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 308 TVFCSAPTAYR-MLIQ--NDITRsYKFNS------LKHCVSA--GEPINPEVMEQWKKKTGL-DIYEGYGQTETVLICGN 375
Cdd:cd05940 160 SNFWDDIRKYQaTIFQyiGELCR-YLLNQppkpteRKHKVRMifGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFIN 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 376 FKGmkiKPGSMG-------KPSPAFNVEILDENGTIL----------PPGQEGDIAVQVLPDRPFglfTHYVDNPSKTAS 438
Cdd:cd05940 239 FFG---KPGAIGrnpsllrKVAPLALVKYDLESGEPIrdaegrcikvPRGEPGLLISRINPLEPF---DGYTDPAATEKK 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 439 TLRGNF------YITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKA 510
Cdd:cd05940 313 ILRDVFkkgdawFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMA 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642407 511 FIVLNPDYKLhDQEQLKKeiqeHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNELRR 568
Cdd:cd05940 392 AIVLQPNEEF-DLSALAA----HLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
46-563 |
3.07e-13 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 72.52 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 46 NFAKDVLdqwtntekTGKRLSNPAFWWVDGNGKEVRWSFEELGSLSRKFANILtEACSLQRGDRVMVILPKIPEwwlANV 125
Cdd:PRK03584 87 NYAENLL--------RHRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAAL-RALGVGPGDRVAAYLPNIPE---TVV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 126 ACLRT---GTVLIPGTTQLTQKDILYRLQSSKSKCIITDD------TLAPAVDIVAAKCENLHS--KLIVSQHSREG--- 191
Cdd:PRK03584 155 AMLATaslGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggKAFDRRAKVAELRAALPSleHVVVVPYLGPAaaa 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 192 --------WGNLkeMMKYASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHssfG---------LGLSvngrfwLDLI 254
Cdd:PRK03584 235 aalpgallWEDF--LAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGH---GgillehlkeLGLH------CDLG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 255 ASD-VMWNTSdTGWAksAWSSVFSPWTQGACVfahYL----PRFDSTSIL-QTLSKFPITVFCSAPTAYRMLIQNDIT-- 326
Cdd:PRK03584 304 PGDrFFWYTT-CGWM--MWNWLVSGLLVGATL---VLydgsPFYPDPNVLwDLAAEEGVTVFGTSAKYLDACEKAGLVpg 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 327 RSYKFNSLKHCVSAGEPINPE----VMEQWKKktglDIY--EGYGQTEtvlICGNFKG----MKIKPGSMGKPSPAFNVE 396
Cdd:PRK03584 378 ETHDLSALRTIGSTGSPLPPEgfdwVYEHVKA----DVWlaSISGGTD---ICSCFVGgnplLPVYRGEIQCRGLGMAVE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 397 ILDENGTilpP--GQEGDIAV-QVLPDRPFGlFTHYVDNpsktaSTLRGNFYIT-------GDRGYMDEDGYFWFVARSD 466
Cdd:PRK03584 451 AWDEDGR---PvvGEVGELVCtKPFPSMPLG-FWNDPDG-----SRYRDAYFDTfpgvwrhGDWIEITEHGGVVIYGRSD 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 467 DVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKLHDQeqLKKEIQEHVKKTTAPYKYPRK 546
Cdd:PRK03584 522 ATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDA--LRARIRTTIRTNLSPRHVPDK 599
|
570 580
....*....|....*....|..
gi 1958642407 547 IEFIEELPKTVSGK-----VKR 563
Cdd:PRK03584 600 IIAVPDIPRTLSGKkvelpVKK 621
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
118-568 |
1.18e-12 |
|
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: 70.32 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 118 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDTlapaVDIVAakcenlhsklivsqhsregwgnLKE 197
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDAG----VKVYS----------------------LEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 198 MMK-YASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVmwntsdtgwaksawSSVF 276
Cdd:cd05927 97 FEKlGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGN---------------IVSNV--------------AGVF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 277 SPWTQGACVFAH-----YLP-----------------------RFDSTSILQTLSKFPITVFCSAPTAY-RML--IQNDI 325
Cdd:cd05927 148 KILEILNKINPTdvyisYLPlahifervvealflyhgakigfySGDIRLLLDDIKALKPTVFPGVPRVLnRIYdkIFNKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 326 TRS-------------YKFNSLKH---------------------------CVSAGEPINPEVMEQWKKKTGLDIYEGYG 365
Cdd:cd05927 228 QAKgplkrklfnfalnYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 366 QTETV-LICGNFKGMKIkPGSMGKPSPAFNVEILD--E-NGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLR 441
Cdd:cd05927 308 QTECTaGATLTLPGDTS-VGHVGGPLPCAEVKLVDvpEmNYDAKDPNPRGEVCI-----RGPNVFSGYYKDPEKTAEALD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 442 GN-FYITGDRGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAESAVvsspdpiRGEVVKAF----IVLN 515
Cdd:cd05927 382 EDgWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFV-------YGDSLKSFlvaiVVPD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 516 PDY-------KLHDQ---------EQLKKEIQEHVKKTTA-----PYKYPRKI-----EFIEE---LpkTVSGKVKRNEL 566
Cdd:cd05927 455 PDVlkewaasKGGGTgsfeelcknPEVKKAILEDLVRLGKenglkGFEQVKAIhlepePFSVEnglL--TPTFKLKRPQL 532
|
..
gi 1958642407 567 RR 568
Cdd:cd05927 533 KK 534
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
202-563 |
1.12e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 67.33 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 202 ASDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHssfglglsvnGRFWLDL----------IASDVMwntsdtgwakSA 271
Cdd:PRK07768 140 AADPIDPVETGEDDLALMQLTSGSTGSPKAVQITH----------GNLYANAeamfvaaefdVETDVM----------VS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 272 WSSVF----------SPWTQGACVF----AHYLPrfDSTSILQTLSKFPITVFCSAPTAY----RMLIQNDITRSYKFNS 333
Cdd:PRK07768 200 WLPLFhdmgmvgfltVPMYFGAELVkvtpMDFLR--DPLLWAELISKYRGTMTAAPNFAYallaRRLRRQAKPGAFDLSS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 334 LKHCVSAGEPINPEVMEQW---KKKTGLD---IYEGYGQTETVLI-----CGNfkGMKI------------------KPG 384
Cdd:PRK07768 278 LRFALNGAEPIDPADVEDLldaGARFGLRpeaILPAYGMAEATLAvsfspCGA--GLVVdevdadllaalrravpatKGN 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 385 -----SMGKPSPAFNVEILDENGTILPPGQEGDIAVQ---VLPdrpfglftHYVDNPSKTASTLRGNFYITGDRGYMDED 456
Cdd:PRK07768 356 trrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRgesVTP--------GYLTMDGFIPAQDADGWLDTGDLGYLTEE 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 457 GYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPiRGEVVKAFIVLNPDYKLHDQE---QLKKEIQEH 533
Cdd:PRK07768 428 GEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD-AGHSREGFAVAVESNAFEDPAevrRIRHQVAHE 506
|
410 420 430
....*....|....*....|....*....|..
gi 1958642407 534 VKKTTApyKYPRKIEFIE--ELPKTVSGKVKR 563
Cdd:PRK07768 507 VVAEVG--VRPRNVVVLGpgSIPKTPSGKLRR 536
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
219-560 |
5.69e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 62.03 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFA-----HY--LP 291
Cdd:PRK08043 370 ILFTSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypsplHYriVP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 292 R----------FDSTSILQTLSKFpitvfcsaptayrmliqndiTRSYKFNSLKHCVSAGEPINPEVMEQWKKKTGLDIY 361
Cdd:PRK08043 449 ElvydrnctvlFGTSTFLGNYARF--------------------ANPYDFARLRYVVAGAEKLQESTKQLWQDKFGLRIL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 362 EGYGQTETVLICGNFKGMKIKPGSMGKPSPAFNVEILD----ENGTIL----PPGQEGDIAVQvlpdRPFGLFTHYVDNP 433
Cdd:PRK08043 509 EGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSvpgiEQGGRLqlkgPNIMNGYLRVE----KPGVLEVPTAENA 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 434 sktASTLRGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVES-ALIEHPSiAESAVVSSPDPIRGEvvkAFI 512
Cdd:PRK08043 585 ---RGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPD-KQHATAIKSDASKGE---ALV 657
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958642407 513 VLNPDYKLHdQEQLKKEIQEHVKKTTApykYPRKIEFIEELPKTVSGK 560
Cdd:PRK08043 658 LFTTDSELT-REKLQQYAREHGVPELA---VPRDIRYLKQLPLLGSGK 701
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
118-497 |
2.57e-09 |
|
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: 60.06 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 118 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKSKCIITDDtlAPAVDIVAAKCENL-HSKLIVsQHSRE------ 190
Cdd:cd05933 44 PEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN--QKQLQKILQIQDKLpHLKAII-QYKEPlkekep 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 191 ---GWGNLKEMMKYASDS--HTCVDT-KHNELMAIYFTSGTTGPPK--MIGHTHSSF-GLGLSVNGRF------------ 249
Cdd:cd05933 121 nlySWDEFMELGRSIPDEqlDAIISSqKPNQCCTLIYTSGTTGMPKgvMLSHDNITWtAKAASQHMDLrpatvgqesvvs 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 250 WLDL--IASDVMwntsdtgwaksawsSVFSPWTQGACVfahYLPRFDST--SILQTLSKFPITVFCSAP----------- 314
Cdd:cd05933 201 YLPLshIAAQIL--------------DIWLPIKVGGQV---YFAQPDALkgTLVKTLREVRPTAFMGVPrvwekiqekmk 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 315 ------TAYRMLI---------------QNDITRSYKFN---------------SLKHCV---SAGEPINPEVMEQWkkk 355
Cdd:cd05933 264 avgaksGTLKRKIaswakgvgletnlklMGGESPSPLFYrlakklvfkkvrkalGLDRCQkffTGAAPISRETLEFF--- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 356 TGLDI--YEGYGQTE-----TVLICGNFKgmkikPGSMGKPSPAFNVEILDEN----GTILPPGQEgdiavqvlpdrpfg 424
Cdd:cd05933 341 LSLNIpiMELYGMSEtsgphTISNPQAYR-----LLSCGKALPGCKTKIHNPDadgiGEICFWGRH-------------- 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642407 425 LFTHYVDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDD-VILSSGYRIGPFEVESALIEHPSIAESAVV 497
Cdd:cd05933 402 VFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAVKKELPIISNAML 476
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
387-567 |
2.89e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.63 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 387 GKPSPAFNVEILDENGTILPPGQEGDIAVqvlpdRPFGLFTHYVDNPSKTASTLRGNFYITGDRGYMdEDGYFWFVARSD 466
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICV-----RGPSLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 467 DVILSSGYRIGPFEVESALIEHPSI--AESAVVSSPDPiRGEVVKAFI---VLNPDyklhDQEQLKKEIQEHVKKTTApy 541
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVqcrISDEE----RRGQLIHALAALVRSEFG-- 534
|
170 180
....*....|....*....|....*...
gi 1958642407 542 kYPRKIEFI--EELPKTVSGKVKRNELR 567
Cdd:PRK09192 535 -VEAAVELVppHSLPRTSSGKLSRAKAK 561
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
335-571 |
1.17e-08 |
|
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: 57.44 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 335 KHCVSA--GEPINPEVMEQWKKKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGKPSP---------AFNVEILDENG 402
Cdd:cd05937 201 DHKVRVawGNGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLirrwkfenqVVLVKMDPETD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 403 TIL-----------PPGQEGDIAVQVLPDrPFGLFTHYVDNPSKTASTL------RGN-FYITGDRGYMDEDGYFWFVAR 464
Cdd:cd05937 281 DPIrdpktgfcvraPVGEPGEMLGRVPFK-NREAFQGYLHNEDATESKLvrdvfrKGDiYFRTGDLLRQDADGRWYFLDR 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 465 SDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDP-IRGEVVKAFIVLNPDYKLHDQEQlKKEIQEHVKKTTAPYKY 543
Cdd:cd05937 360 LGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEESSAVPTEFT-KSLLASLARKNLPSYAV 438
|
250 260
....*....|....*....|....*...
gi 1958642407 544 PRKIEFIEELPKTVSGKVKRNELRRKEW 571
Cdd:cd05937 439 PLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
219-488 |
3.39e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 56.36 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 219 IYFTSGTTGPPKMIGHTHSSfglgLSVNGRFWLDLIA---SDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPrFDS 295
Cdd:PRK06334 188 ILFTSGTEKLPKGVPLTHAN----LLANQRACLKFFSpkeDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNP-LYP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 296 TSILQTLSKFPITVFCSAPTAYRMLIQNDITRSYKFNSLKHCVSAGEPINPEVMEQWKKK-TGLDIYEGYGQTE-TVLIC 373
Cdd:PRK06334 263 KKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTfPHIQLRQGYGTTEcSPVIT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 374 GNFKGMKIKPGSMGKPSPAFNVEILDENGTI-LPPGQEGDIAVqvlpdRPFGLFTHYVDN-PSKTASTLRG-NFYITGDR 450
Cdd:PRK06334 343 INTVNSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLT-----RGTSLFSGYLGEdFGQGFVELGGeTWYVTGDL 417
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958642407 451 GYMDEDGYFWFVARsddviLSSGYRIGPFEV-----ESALIEH 488
Cdd:PRK06334 418 GYVDRHGELFLKGR-----LSRFVKIGAEMVslealESILMEG 455
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
222-569 |
4.68e-08 |
|
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: 55.71 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 222 TSGTTGPPKMIGHTHSSFglglsvngRFWLDLIA----------SDVMWNTsdTGwaksawssvFSPWTQGACvfAHY-L 290
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDL--------DVWAELVArcldaagvtpGDRVQNA--YG---------YGLFTGGLG--FHYgA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 291 PRFDSTSI----------LQTLSKFPITVFCSAPT--------AYRMLIqnDITRSykfnSLKHCVSAGEPINPEVMEQW 352
Cdd:cd05913 145 ERLGALVIpagggnterqLQLIKDFGPTVLCCTPSyalylaeeAEEEGI--DPREL----SLKVGIFGAEPWTEEMRKRI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 353 KKKTGLDIYEGYGQTE-----TVLICGNFKGMKIKpgsmgkpSPAFNVEILD-ENGTILPPGQEGDIavqvlpdrpfgLF 426
Cdd:cd05913 219 ERRLGIKAYDIYGLTEiigpgVAFECEEKDGLHIW-------EDHFIPEIIDpETGEPVPPGEVGEL-----------VF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 427 THYvdnpSKTASTLRgnFYITGD------------RGYMDEDGyfwFVARSDDVILSSGYRIGPFEVESALIEHPSIAES 494
Cdd:cd05913 281 TTL----TKEAMPLI--RYRTRDitrllpgpcpcgRTHRRIDR---ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPH 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 495 A--VVSSPDP-----IRGEVVKAFIVLNPDyklhdqEQLKKEIQEHVKKTTA--PykyprKIEFIE--ELPKTvSGKVKR 563
Cdd:cd05913 352 YqlILTRQEHldeltIKVEVRPEADDDEKL------EALKQRLERHIKSVLGvtV-----EVELVEpgSLPRS-EGKAKR 419
|
....*.
gi 1958642407 564 NELRRK 569
Cdd:cd05913 420 VIDKRK 425
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
222-563 |
7.17e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 51.69 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 222 TSGTTGPPKMIGHTHSSFGLglsvngrfWLDLIA----------SDVMWNTsdTGwaksawssvFSPWTQGacVFAHY-L 290
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDR--------WAELFArslraagvrpGDRVQNA--FG---------YGLFTGG--LGLHYgA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 291 PRF----------DSTSILQTLSKFPITVFCSAPT--------AYRMLIqnDITRSykfnSLKHCVSAGEPInPEVMEQW 352
Cdd:COG1541 150 ERLgatvipagggNTERQLRLMQDFGPTVLVGTPSyllylaevAEEEGI--DPRDL----SLKKGIFGGEPW-SEEMRKE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 353 -KKKTGLDIYEGYGQTET-VLI---CGNFKGMKIKPGSmgkpspaFNVEILD-ENGTILPPGQEGDIavqvlpdrpfgLF 426
Cdd:COG1541 223 iEERWGIKAYDIYGLTEVgPGVayeCEAQDGLHIWEDH-------FLVEIIDpETGEPVPEGEEGEL-----------VV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 427 THYvdnpSKTASTL-RgnfYITGDRGYMDED---------------GyfwfvaRSDDVILSSGYRIGPFEVESALIEHPS 490
Cdd:COG1541 285 TTL----TKEAMPLiR---YRTGDLTRLLPEpcpcgrthprigrilG------RADDMLIIRGVNVFPSQIEEVLLRIPE 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642407 491 IAESAVVSSPDPIRGEVVKAFIVLNPDYklhDQEQLKKEIQEHVKKTTapyKYPRKIEFIE--ELPKTVsGKVKR 563
Cdd:COG1541 352 VGPEYQIVVDREGGLDELTVRVELAPGA---SLEALAEAIAAALKAVL---GLRAEVELVEpgSLPRSE-GKAKR 419
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
104-510 |
8.33e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 52.02 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 104 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdiLY-RLQSSKSKCIITDDTLApAVDIVAAKCENLHS-- 180
Cdd:PLN02736 100 IPKGACVGLYFINRPEWLIVDHACSAYSYVSVP----------LYdTLGPDAVKFIVNHAEVA-AIFCVPQTLNTLLScl 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 181 ------KLIV----------SQHSREGwgnlKEMMKYA-------SDSHTCVDTKHNELMAIYFTSGTTGPPKMIGHTHs 237
Cdd:PLN02736 169 seipsvRLIVvvggadeplpSLPSGTG----VEIVTYSkllaqgrSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTH- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 238 sfglglsvngrfwLDLIAS------DVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRF---DSTSILQTLSKFPIT 308
Cdd:PLN02736 244 -------------GNLIANvagsslSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFyqgDNLKLMDDLAALRPT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 309 VFCSAPTAYRMlIQNDITRSYK-------------FNSLKHC------------------------------VSAGEPIN 345
Cdd:PLN02736 311 IFCSVPRLYNR-IYDGITNAVKesgglkerlfnaaYNAKKQAlengknpspmwdrlvfnkikaklggrvrfmSSGASPLS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 346 PEVMEQWKKKTGLDIYEGYGQTET-VLICGNFKGMKIKpGSMGKPSPAFNVEILDengtiLP---------PGQEGDIAV 415
Cdd:PLN02736 390 PDVMEFLRICFGGRVLEGYGMTETsCVISGMDEGDNLS-GHVGSPNPACEVKLVD-----VPemnytsedqPYPRGEICV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 416 qvlpdRPFGLFTHYVDNPSKTASTLRGNFYI-TGDRGYMDEDGYFWFVARSDDVI-LSSGYRIGPFEVESALIEHPSIAE 493
Cdd:PLN02736 464 -----RGPIIFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQ 538
|
490 500
....*....|....*....|....*...
gi 1958642407 494 SAV-----------VSSPDPirgEVVKA 510
Cdd:PLN02736 539 CFVygdslnsslvaVVVVDP---EVLKA 563
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
210-566 |
6.02e-06 |
|
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: 49.14 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 210 DTKHNELMAIYFTSGTTGPPKMIGHTHSSF-----GLGLSVNGRFW--------------LDLIASDV--MWNT------ 262
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLvagiaGLGDRVPELLGpddrylaylplahiFELAAENVclYRGGtigygs 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 263 ----SDTGWAKSAWS-SVFSPwTQGACVfahylPR-FDST-----SILQTLSKFPITVFCSAPTAYRMLIQNDITRSY-- 329
Cdd:cd17639 164 prtlTDKSKRGCKGDlTEFKP-TLMVGV-----PAiWDTIrkgvlAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLld 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 330 --KFNS--------LKHCVSAGEPINPEVMEqWKKKTGLDIYEGYGQTETvliCGNfkGMKIKPGSM-----GKPSPAFN 394
Cdd:cd17639 238 elVFKKvraalggrLRYMLSGGAPLSADTQE-FLNIVLCPVIQGYGLTET---CAG--GTVQDPGDLetgrvGPPLPCCE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 395 VEILD--ENG--TILPPGQeGDIAVQvlpdRPFgLFTHYVDNPSKTASTLRGN--FYiTGDRGYMDEDGYFWFVARSDD- 467
Cdd:cd17639 312 IKLVDweEGGysTDKPPPR-GEILIR----GPN-VFKGYYKNPEKTKEAFDGDgwFH-TGDIGEFHPDGTLKIIDRKKDl 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 468 VILSSGYRIGPFEVESALIEHPSIAESAVVSspDPIRGEVVkAFIVLN------------------PDYkLHDQEQLK-- 527
Cdd:cd17639 385 VKLQNGEYIALEKLESIYRSNPLVNNICVYA--DPDKSYPV-AIVVPNekhltklaekhgvinsewEEL-CEDKKLQKav 460
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958642407 528 -KEIQEHVKKTT-APYKYPRKIEFIEEL--PK----TVSGKVKRNEL 566
Cdd:cd17639 461 lKSLAETARAAGlEKFEIPQGVVLLDEEwtPEnglvTAAQKLKRKEI 507
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
441-566 |
7.44e-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: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 441 RGNFYITGDRGYMDEDGYFWFVARSDDVILSSGYRIGPFEVESALIEHPSIAES------------AVVS--SPDPIRGE 506
Cdd:cd17647 370 RDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKPD 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642407 507 VVKAFIVLNPDYKLHDQ--------EQLKKEIQEHVKKTTAPYKYPRKIEFIEELPKTVSGKVKRNEL 566
Cdd:cd17647 450 DESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
441-568 |
3.42e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 46.68 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 441 RGNFYITGDRGYMDEDGYFwFVARSDDVILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGevVKAFIVLNPDYKL 520
Cdd:PRK05851 394 PDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEFRG 470
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958642407 521 HDQEQLKKEIQEHVKKTTApyKYPRKIEFIE--ELPKTVSGKVKRNELRR 568
Cdd:PRK05851 471 PDEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
338-551 |
3.74e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 46.73 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 338 VSAGEPINPEVMEQWKKKTGLDIYEGYGQTETvliCGnfkgmkikPGSMGKPspafnveilDEN---GTILPPGQEGDIA 414
Cdd:PLN02430 389 ISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET---LG--------PTTLGFP---------DEMcmlGTVGAPAVYNELR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 415 VQVLPD---RPFG-------------LFTHYVDNPSKTASTLRGNFYITGDRGYMDEDGYFWFVARSDDVI-LSSGYRIG 477
Cdd:PLN02430 449 LEEVPEmgyDPLGepprgeicvrgkcLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVA 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 478 PFEVESALIEHPSIAESAVVSspDPIRGEVVkAFIVLNPD---------------YKLHDQEQLKKEIQEHVKKTTAPYK 542
Cdd:PLN02430 529 LEYLENVYGQNPIVEDIWVYG--DSFKSMLV-AVVVPNEEntnkwakdngftgsfEELCSLPELKEHILSELKSTAEKNK 605
|
....*....
gi 1958642407 543 YpRKIEFIE 551
Cdd:PLN02430 606 L-RGFEYIK 613
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
362-471 |
3.34e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 40.47 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 362 EGYGQTETVLICGNFKGMKIkpGSMGKPSP--------AFNVE----ILDENGTIlppgQEGDIA-VQVLPDRPFGLFTh 428
Cdd:PRK07868 749 EFFATTDGQAVLANVSGAKI--GSKGRPLPgagrvelaAYDPEhdliLEDDRGFV----RRAEVNeVGVLLARARGPID- 821
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958642407 429 yvdnpsKTASTLRGNFyITGDR----GYM---DEDGYFWFVARSDDVILS 471
Cdd:PRK07868 822 ------PTASVKRGVF-APADTwistEYLfrrDDDGDYWLVDRRGSVIRT 864
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
158-254 |
3.39e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 40.34 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642407 158 IITDDTLAPAVDIvaakcenlHSKLIVSqhsregWGNLKEMMKYASDSHTC-VDTKHNELMAIYFTSGTTGPPKMIGHTH 236
Cdd:PTZ00216 221 IIYLDSLPASVDT--------EGCRLVA------WTDVVAKGHSAGSHHPLnIPENNDDLALIMYTSGTTGDPKGVMHTH 286
|
90
....*....|....*....
gi 1958642407 237 SSFGLG-LSVNGRFwLDLI 254
Cdd:PTZ00216 287 GSLTAGiLALEDRL-NDLI 304
|
|
| |
