|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
75-609 |
0e+00 |
|
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: 966.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 75 YEGDVYTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPK 154
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 155 AMVVGEDLLGSLEEILPSLPKH-IRVWGM-KDSVPEGIVSLKEKLSLASDEPVPPSHHVTSSLKSTCLYIFTSGTTGLPK 232
Cdd:cd05938 81 VLVVAPELQEAVEEVLPALRADgVSVWYLsHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 233 AAVISQFQVLKGSFGLWAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVTVFQYIG 312
Cdd:cd05938 161 AARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 313 ELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGNIKMCEFYGATEGNICFMNHTGKIGSVGRVNFFYNLLFS 392
Cdd:cd05938 241 ELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 393 FELIKYDFQKDEPLRNEQGWCYCVRKGEPGLLVSRVNKKNPFFGYTGSYKQTKSKLLFDVFKKGDVYFNTGDLMFQDHEN 472
Cdd:cd05938 321 FELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSPFLGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 473 FLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYEGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAY 552
Cdd:cd05938 401 FLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAY 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 149064320 553 ACPRFLRIQDKMETTGTFKLKKLQLVEEGFNPLKIADPLYFMDNLKKSYVPLTQEIY 609
Cdd:cd05938 481 ARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
58-612 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 720.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 58 DKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNS 137
Cdd:PRK08279 41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARG-VGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 138 NLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLPKHIRVW---GMKDSVPEGIVSLKEKLSLASDEPvpPSHHVTSS 214
Cdd:PRK08279 120 QQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWvagGDTLDDPEGYEDLAAAAAGAPTTN--PASRSGVT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 215 LKSTCLYIFTSGTTGLPKAAVISQFQVLK--GSFG-LWAFgcTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKF 291
Cdd:PRK08279 198 AKDTAFYIYTSGTTGLPKAAVMSHMRWLKamGGFGgLLRL--TPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 292 SASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGNIKMCEFYGATEGNICFM 371
Cdd:PRK08279 276 SASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 372 NHTGKIGSVGRVNFFynLLFSFELIKYDFQKDEPLRNEQGWCYCVRKGEPGLLVSRVNKKNPFFGYTgSYKQTKSKLLFD 451
Cdd:PRK08279 356 NVFNFDGTVGRVPLW--LAHPYAIVKYDVDTGEPVRDADGRCIKVKPGEVGLLIGRITDRGPFDGYT-DPEASEKKILRD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 452 VFKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYEGKAGMTSIILK 531
Cdd:PRK08279 433 VFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAIVLA 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 532 PNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVEEGFNPLKIADPLYFMDNLKKSYVPLTQEIYNQ 611
Cdd:PRK08279 513 DGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPLTAELYAE 592
|
.
gi 149064320 612 V 612
Cdd:PRK08279 593 I 593
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
77-584 |
0e+00 |
|
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: 607.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 77 GDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAM 156
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLG-LKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 157 VVgedllgsleeilpslpkhirvwgmkdsvpegivslkeklslasdepvppshhvtsslkSTCLYIFTSGTTGLPKAAVI 236
Cdd:cd05940 80 VV----------------------------------------------------------DAALYIYTSGTTGLPKAAII 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 237 SQFQVLKGSFGLWAFGCTAD-DIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVTVFQYIGELC 315
Cdd:cd05940 102 SHRRAWRGGAFFAGSGGALPsDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELC 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 316 RYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGNIKMCEFYGATEGNICFMNHTGKIGSVGRVNFFYNLLFSFEL 395
Cdd:cd05940 182 RYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLAL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 396 IKYDFQKDEPLRNEQGWCYCVRKGEPGLLVSRVNKKNPFFGYTGSYKQTKsKLLFDVFKKGDVYFNTGDLMFQDHENFLY 475
Cdd:cd05940 262 VKYDLESGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFDGYTDPAATEK-KILRDVFKKGDAWFNTGDLMRLDGEGFWY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 476 FWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYEGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACP 555
Cdd:cd05940 341 FVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARP 420
|
490 500
....*....|....*....|....*....
gi 149064320 556 RFLRIQDKMETTGTFKLKKLQLVEEGFNP 584
Cdd:cd05940 421 LFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
80-584 |
0e+00 |
|
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: 522.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVG 159
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQG-YRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 160 --EDLLGSLEEILPSLPkhirvwgmkdsvpegIVSLKEKLslasdepvppshhvtsslkstcLYIFTSGTTGLPKAAVIS 237
Cdd:cd05939 83 llDPLLTQSSTEPPSQD---------------DVNFRDKL----------------------FYIYTSGTTGLPKAAVIV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 238 QFQVLK-GSFGLWAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVTVFQYIGELCR 316
Cdd:cd05939 126 HSRYYRiAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 317 YLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGNIKMCEFYGATEGNICFMNHTGKIGSVGRVNFFYNLLFSFELI 396
Cdd:cd05939 206 YLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRLI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 397 KYDFQKDEPLRNEQGWCYCVRKGEPGLLVSRVNKKNP---FFGYTgSYKQTKSKLLFDVFKKGDVYFNTGDLMFQDHENF 473
Cdd:cd05939 286 KVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPlrrFDGYV-NEGATNKKIARDVFKKGDSAFLSGDVLVMDELGY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 474 LYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYEGKAGMTSIIlKPNKSLDLEKMYDQVVTSLPAYA 553
Cdd:cd05939 365 LYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIV-DPERKVDLDRFSAVLAKSLPPYA 443
|
490 500 510
....*....|....*....|....*....|.
gi 149064320 554 CPRFLRIQDKMETTGTFKLKKLQLVEEGFNP 584
Cdd:cd05939 444 RPQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
75-584 |
1.34e-143 |
|
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: 424.92 E-value: 1.34e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 75 YEGDVYTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPK 154
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 155 AMVVGEDllgsleeilpslpkhirvwgmkdsvpegivslkeklslasdepvppshhvtsslkSTCLYIFTSGTTGLPKAA 234
Cdd:cd05937 81 FVIVDPD-------------------------------------------------------DPAILIYTSGTTGLPKAA 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 235 VISQFQVLKGS--FGLWaFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVTVFQYIG 312
Cdd:cd05937 106 AISWRRTLVTSnlLSHD-LNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 313 ELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGNIKMCEFYGATEGNICFMNH-TGK--IGSVGRVNFFYNL 389
Cdd:cd05937 185 ELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnVGDfgAGAIGHHGLIRRW 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 390 LFSFE--LIKYDFQKDEPLR-NEQGWCYCVRKGEPGLLVSRVNKKN--PFFGYTGSYKQTKSKLLFDVFKKGDVYFNTGD 464
Cdd:cd05937 265 KFENQvvLVKMDPETDDPIRdPKTGFCVRAPVGEPGEMLGRVPFKNreAFQGYLHNEDATESKLVRDVFRKGDIYFRTGD 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 465 LMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYEGKAGMTSIILKPNKSLDLEK---M 541
Cdd:cd05937 345 LLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSAVPTEFtksL 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 149064320 542 YDQVVTS-LPAYACPRFLRIQDKMETTGTFKLKKLQLVEEGFNP 584
Cdd:cd05937 425 LASLARKnLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVDP 468
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
77-577 |
4.85e-90 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 285.34 E-value: 4.85e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 77 GDVYTYEDVDKRSNRVAHALLNHSDlKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAM 156
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGI-RPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 157 VVgedllgsleeilpslpkhirvwgmkdsvpegivslkeklslasdepvppshhvtsslkSTCLYIFTSGTTGLPKAAVI 236
Cdd:cd05934 80 VV----------------------------------------------------------DPASILYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 237 SQFQVL-KGSFGLWAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVTVFQYIGELC 315
Cdd:cd05934 102 THANLTfAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAML 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 316 RYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGnIKMCEFYGATEGNICFMN---HTGKIGSVGRVNFFYNLLfs 392
Cdd:cd05934 182 SYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG-VRLLEGYGMTETIVGVIGprdEPRRPGSIGRPAPGYEVR-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 393 felikydfqkdepLRNEQGwcYCVRKGEPGLLVSRVNKKNPFFgyTGSYKQTKSKLlfDVFKKGdvYFNTGDLMFQDHEN 472
Cdd:cd05934 259 -------------IVDDDG--QELPAGEPGELVIRGLRGWGFF--KGYYNMPEATA--EAMRNG--WFHTGDLGYRDADG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 473 FLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgYEGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAY 552
Cdd:cd05934 318 FFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDE-VGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYF 396
|
490 500
....*....|....*....|....*
gi 149064320 553 ACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd05934 397 KVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
56-580 |
1.48e-89 |
|
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: 284.78 E-value: 1.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 56 VLDKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHsDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRAL-GVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 136 NSNLRFESLLHCIRTSEPKAMVvgedllgsleeilpslpkhirvwgmkdsvpegivslkeklslasdepvppshhvtssl 215
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALV---------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 216 ksTCLYIFTSGTTGLPKAAVISQFQVLKGSFGL-WAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSAS 294
Cdd:COG0318 102 --TALILYTSGTTGRPKGVMLTHRNLLANAAAIaAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 295 QFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAV--GNGMSSDVWRQFLDRFGnIKMCEFYGATEGN-ICFM 371
Cdd:COG0318 180 RVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFG-VRIVEGYGLTETSpVVTV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 372 N----HTGKIGSVGRVnffynlLFSFELIkydfqkdepLRNEQGwcYCVRKGEPGLLVSRVNkkNPFFGYTGSYKQTKsk 447
Cdd:COG0318 259 NpedpGERRPGSVGRP------LPGVEVR---------IVDEDG--RELPPGEVGEIVVRGP--NVMKGYWNDPEATA-- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 448 llfDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTS 527
Cdd:COG0318 318 ---EAFRDG--WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW-GERVVAF 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 149064320 528 IILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVEE 580
Cdd:COG0318 392 VVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
64-584 |
1.52e-81 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 266.62 E-value: 1.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFES 143
Cdd:PRK06155 31 AERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 144 LLHCIRTSEPKAMVVGEDLLGSLEEILPSLPKHIRVWgMKDSVPEGIVSLKEKLS--LASDEPVPPshhVTSSLKSTCLY 221
Cdd:PRK06155 110 LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVW-LLDAPASVSVPAGWSTAplPPLDAPAPA---AAVQPGDTAAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 222 IFTSGTTGLPKAAVISQFQvlkgsFGLW------AFGCTADDIVYITLPLYHSSgALLGIGGCVELGATCVLKKKFSASQ 295
Cdd:PRK06155 186 LYTSGTTGPSKGVCCPHAQ-----FYWWgrnsaeDLEIGADDVLYTTLPLFHTN-ALNAFFQALLAGATYVLEPRFSASG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 296 FWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGnIKMCEFYGATEGN-ICFMNH- 373
Cdd:PRK06155 260 FWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFG-VDLLDGYGSTETNfVIAVTHg 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 374 TGKIGSVGRvnffynLLFSFELIKYDfQKDEPLRNeqgwcycvrkGEPGLLVSRVNKKNPFF-GYTGSYKQTkskllfdV 452
Cdd:PRK06155 339 SQRPGSMGR------LAPGFEARVVD-EHDQELPD----------GEPGELLLRADEPFAFAtGYFGMPEKT-------V 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 453 FKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYEGKAgMTSIILKP 532
Cdd:PRK06155 395 EAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEV-MAAVVLRD 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 149064320 533 NKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVEEGFNP 584
Cdd:PRK06155 474 GTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTA 525
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
60-487 |
3.04e-63 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 214.48 E-value: 3.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 60 FLSHARRQPKK-AFIIYEGDVYTYEDVDKRSNRVAHALLNHsDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSN 138
Cdd:pfam00501 1 LERQAARTPDKtALEVGEGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 139 LRFESLLHCIRTSEPKAMVVGEDLLgsLEEILPSLPKHIRVWGMKDSVPEGIVSLKEKLSLASDEPVPPSHHVTSSLKST 218
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALK--LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 219 CLYIFTSGTTGLPKAAVISQFQVL-----KGSFGLWAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSA 293
Cdd:pfam00501 158 AYIIYTSGTTGKPKGVMLTHRNLVanvlsIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 294 ---SQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVR--LAVGNGMSSDVWRQFLDRFGNiKMCEFYGATEGNI 368
Cdd:pfam00501 238 ldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRlvLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 369 CFMN------HTGKIGSVGRVNFFYnllfsfELIKYDFQKDEPlrneqgwcycVRKGEPGLLVSRvnKKNPFFGYTGSYK 442
Cdd:pfam00501 317 VVTTplpldeDLRSLGSVGRPLPGT------EVKIVDDETGEP----------VPPGEPGELCVR--GPGVMKGYLNDPE 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 149064320 443 QTKskllfDVFKKGDvYFNTGDLMFQDHENFLYFWDRIGDTFRWK 487
Cdd:pfam00501 379 LTA-----EAFDEDG-WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
73-592 |
2.50e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 209.92 E-value: 2.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 73 IIYEGDVYTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVhVWFGLAKL-GCVVAFLNSNLRFESLLHCIRTS 151
Cdd:PRK07867 22 LYFEDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFS-LLLGAAALsGIVPVGLNPTRRGAALARDIAHA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 152 EPKAMVVGEDLLGSLEEILPSLPkHIRVwgmkDSVPegivsLKEKLSLASDEPVPPShhvTSSLKSTCLYIFTSGTTGLP 231
Cdd:PRK07867 101 DCQLVLTESAHAELLDGLDPGVR-VINV----DSPA-----WADELAAHRDAEPPFR---VADPDDLFMLIFTSGTSGDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 232 KAAVISQFQV------LKGSFGLwafgcTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNV 305
Cdd:PRK07867 168 KAVRCTHRKVasagvmLAQRFGL-----GPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 306 TVFQYIGELCRYLCKQPQREGEKDHRVRLAVGN-GMSSDVWRqFLDRFGnIKMCEFYGATEGNICFMNHTG-KIGSVGRV 383
Cdd:PRK07867 243 TYANYVGKPLSYVLATPERPDDADNPLRIVYGNeGAPGDIAR-FARRFG-CVVVDGFGSTEGGVAITRTPDtPPGALGPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 384 nffynllfsFELIK-YDFQKDEPL-RNEQGWCYCVRKGEP-GLLVSrVNKKNPFFGYTGSYKQTKSKLlfdvfkKGDVYF 460
Cdd:PRK07867 321 ---------PPGVAiVDPDTGTECpPAEDADGRLLNADEAiGELVN-TAGPGGFEGYYNDPEADAERM------RGGVYW 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 461 nTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSIILKPNKSLDLEK 540
Cdd:PRK07867 385 -SGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVV-GDQVMAALVLAPGAKFDPDA 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 149064320 541 MYDQVVTS--LPAYACPRFLRIQDKMETTGTFKLKKLQLVEEGFNplkIADPLY 592
Cdd:PRK07867 463 FAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVD---CADPVW 513
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
64-577 |
3.91e-58 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 203.76 E-value: 3.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKKAFIIYE---GDV--YTYEDVDKRSNRVAHALLNhSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSN 138
Cdd:PRK08008 17 ADVYGHKTALIFEssgGVVrrYSYLELNEEINRTANLFYS-LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 139 LRFESLLHCIRTSEPKAMVVGEDLLGSLEEIL---PSLPKHIRVWGMKDSVPEGIVSLKEklsLASDEPVPPSHHVTSSL 215
Cdd:PRK08008 96 LLREESAWILQNSQASLLVTSAQFYPMYRQIQqedATPLRHICLTRVALPADDGVSSFTQ---LKAQQPATLCYAPPLST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 216 KSTCLYIFTSGTTGLPKAAVISQFQVL-KGSFGLWAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSAS 294
Cdd:PRK08008 173 DDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSAR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 295 QFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVR-----LAVGNGMSSDvwrqFLDRFGnIKMCEFYGATEGNIc 369
Cdd:PRK08008 253 AFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEKDA----FEERFG-VRLLTSYGMTETIV- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 370 fmnhtGKIG----------SVGRVNFFYnllfsfELIKYDFQKDEPLRNEQGWcYCVrKGEPGllvsrvnkKNPFFGYTG 439
Cdd:PRK08008 327 -----GIIGdrpgdkrrwpSIGRPGFCY------EAEIRDDHNRPLPAGEIGE-ICI-KGVPG--------KTIFKEYYL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 440 SYKQTKSKLlfdvfkKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgY 519
Cdd:PRK08008 386 DPKATAKVL------EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDS-I 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 149064320 520 EGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:PRK08008 459 RDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
218-573 |
1.64e-56 |
|
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: 194.04 E-value: 1.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 218 TCLYIFTSGTTGLPKAAVISQFQVL-KGSFGLWAFGCTADDIVYITLPLYHSSGaLLGIGGCVELGATCVLKKKFSASQF 296
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLaAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 297 WNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNG--MSSDVWRQFLDRFGnIKMCEFYGATEGNICFM--- 371
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPG-IKLVNGYGLTETGGTVAtgp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 372 --NHTGKIGSVGRVNFFynllFSFELIKYDFQKDEPlrneqgwcycvrkGEPGLLVsrVNKKNPFFGYTGSYKQTKskll 449
Cdd:cd04433 160 pdDDARKPGSVGRPVPG----VEVRIVDPDGGELPP-------------GEIGELV--VRGPSVMKGYWNNPEATA---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 450 fdvFKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSII 529
Cdd:cd04433 217 ---AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEW-GERVVAVVV 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 149064320 530 LKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLK 573
Cdd:cd04433 293 LRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
63-574 |
1.78e-55 |
|
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: 194.37 E-value: 1.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 63 HARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLnHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFE 142
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALR-ALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 143 SLLHCIRTSEPKAMVvgEDLlgsleeilpslpkhirvwgmkdsvpegivslkeklslasdepvppshhvtsslkstCLYI 222
Cdd:cd17631 83 EVAYILADSGAKVLF--DDL--------------------------------------------------------ALLM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 223 FTSGTTGLPKAAVISQFQVLKGSFG-LWAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCR 301
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRNLLWNAVNaLAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 302 KYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNG--MSSDVWRQFLDRfgNIKMCEFYGATE--GNICFM---NHT 374
Cdd:cd17631 185 RHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapMPERLLRALQAR--GVKFVQGYGMTEtsPGVTFLspeDHR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 375 GKIGSVGRVNFFynllfsfelIKYDFQKDEplRNEqgwcycVRKGEPGLLVSRvnKKNPFFGYTGSYKQTKSkllfdVFK 454
Cdd:cd17631 263 RKLGSAGRPVFF---------VEVRIVDPD--GRE------VPPGEVGEIVVR--GPHVMAGYWNRPEATAA-----AFR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 455 KGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSIILKPNK 534
Cdd:cd17631 319 DG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKW-GEAVVAVVVPRPGA 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 149064320 535 SLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKK 574
Cdd:cd17631 396 ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
73-581 |
1.45e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 191.78 E-value: 1.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 73 IIYEGDVYTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVhVWFGLAKL-GCVVAFLNSNLRFESLLHCIRTS 151
Cdd:PRK13388 20 VRYGDRTWTWREVLAEAAARAAALIALADPDRPLHVGVLLGNTPEML-FWLAAAALgGYVLVGLNTTRRGAALAADIRRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 152 EPKAMVV---GEDLLGSLEeiLPSLPKhIRVwgmkdSVPEgivsLKEKLSLASD-EPVPPshhVTSslKSTCLYIFTSGT 227
Cdd:PRK13388 99 DCQLLVTdaeHRPLLDGLD--LPGVRV-LDV-----DTPA----YAELVAAAGAlTPHRE---VDA--MDPFMLIFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 228 TGLPKAAVISQFQVLKGSFGLWA-FGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVT 306
Cdd:PRK13388 162 TGAPKAVRCSHGRLAFAGRALTErFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGAT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 307 VFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGnIKMCEFYGATEGNICFMNHTGK-IGSVGRvnf 385
Cdd:PRK13388 242 YFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFG-CQVEDGYGSSEGAVIVVREPGTpPGSIGR--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 386 fynllfSFE-LIKYDFQKDEPlrneqgwCYCVRKGEPGLLVSR-------VNKKNPFFgYTGSYKQTKSKLlfDVFKKGD 457
Cdd:PRK13388 318 ------GAPgVAIYNPETLTE-------CAVARFDAHGALLNAdeaigelVNTAGAGF-FEGYYNNPEATA--ERMRHGM 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 458 VYfnTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgYEGKAGMTSIILKPNKSLD 537
Cdd:PRK13388 382 YW--SGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE-RVGDQVMAALVLRDGATFD 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 149064320 538 LEKMYDQVVTS--LPAYACPRFLRIQDKMETTGTFKLKKLQLVEEG 581
Cdd:PRK13388 459 PDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELIAQG 504
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
76-552 |
3.53e-49 |
|
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: 178.56 E-value: 3.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 76 EGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKA 155
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 156 MVVGEDLLGSLEEILPSLPKHIRVWGMKDSVPE--GIVSLKEKLSLASDEPVPPSHHVTSslKSTCLYIFTSGTTGLPKA 233
Cdd:cd05911 86 IFTDPDGLEKVKEAAKELGPKDKIIVLDDKPDGvlSIEDLLSPTLGEEDEDLPPPLKDGK--DDTAAILYSSGTTGLPKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 234 AVIS------QFQVLKGSFGLWAfgcTADDIVYITLPLYHSSGALLGIGGCVeLGATCVLKKKFSASQFWNDCRKYNVTV 307
Cdd:cd05911 164 VCLShrnliaNLSQVQTFLYGND---GSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIMPKFDSELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 308 FQYIGELCRYLCKQPQREGEKDHRVR-LAVGngmSSDVWRQFLD----RFGNIKMCEFYGATE-GNICFMN--HTGKIGS 379
Cdd:cd05911 240 LYLVPPIAAALAKSPLLDKYDLSSLRvILSG---GAPLSKELQEllakRFPNATIKQGYGMTEtGGILTVNpdGDDKPGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 380 VGRvnffynLLFSFElIKYdfqKDEPLRNEQGwcycvrKGEPGLLvsRVNKKNPFFGYTGSYKQTKSklLFDvfKKGdvY 459
Cdd:cd05911 317 VGR------LLPNVE-AKI---VDDDGKDSLG------PNEPGEI--CVRGPQVMKGYYNNPEATKE--TFD--EDG--W 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 460 FNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgYEGKAGMTSIILKPNKSLDLE 539
Cdd:cd05911 373 LHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDE-VSGELPRAYVVRKPGEKLTEK 451
|
490
....*....|...
gi 149064320 540 KMYDQVVTSLPAY 552
Cdd:cd05911 452 EVKDYVAKKVASY 464
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
53-578 |
1.27e-47 |
|
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: 173.52 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 53 LVTVLDKflSHARRQPKKAFIIYeGDVYTYEDVDKRSNRVAHALLNhSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVV 132
Cdd:cd05936 1 LADLLEE--AARRFPDKTALIFM-GRKLTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGALKAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 133 AFLNSNLRFESLLHCIRTSEPKAMVVgedllgsleeilpslpkhirvwgmkdsvpegIVSLKEKLSLASDEPVPPshhvT 212
Cdd:cd05936 77 VPLNPLYTPRELEHILNDSGAKALIV-------------------------------AVSFTDLLAAGAPLGERV----A 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 213 SSLKSTCLYIFTSGTTGLPKAAVISQFQVLKGSFGLWA---FGCTADDIVYITLPLYHSSGalLGIGG--CVELGATCVL 287
Cdd:cd05936 122 LTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAwleDLLEGDDVVLAALPLFHVFG--LTVALllPLALGATIVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 288 KKKFSASQFWNDCRKYNVTVFQ-----YIGelcryLCKQPQREGEKDHRVRLAVGNGMS--SDVWRQFLDRFGNiKMCEF 360
Cdd:cd05936 200 IPRFRPIGVLKEIRKHRVTIFPgvptmYIA-----LLNAPEFKKRDFSSLRLCISGGAPlpVEVAERFEELTGV-PIVEG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 361 YGATEGN--ICFmNHTG---KIGSVGRVnffynlLFSFELIKYDFQKDEplrneqgwcycVRKGEPGLLVsrVNKKNPFF 435
Cdd:cd05936 274 YGLTETSpvVAV-NPLDgprKPGSIGIP------LPGTEVKIVDDDGEE-----------LPPGEVGELW--VRGPQVMK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 436 GYTGSYKQTKskllfDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVP 515
Cdd:cd05936 334 GYWNRPEETA-----EAFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVP 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149064320 516 VPgYEGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLV 578
Cdd:cd05936 407 DP-YSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
55-577 |
2.38e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 168.44 E-value: 2.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 55 TVLDKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNhSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 135 LNSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLP--KHIRVWGMKDSVPEGI--VSLKEKLSLASDEpvPPSHH 210
Cdd:PRK06187 86 INIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPtvRTVIVEGDGPAAPLAPevGEYEELLAAASDT--FDFPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 211 VTSSlkSTCLYIFTSGTTGLPKAAVISQFQVLKGSFGLWA-FGCTADDIVYITLPLYHSSGALLGIGGcVELGATCVLKK 289
Cdd:PRK06187 164 IDEN--DAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAwLKLSRDDVYLVIVPMFHVHAWGLPYLA-LMAGAKQVIPR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 290 KFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAV--GNGMSSDVWRQFLDRFGnIKMCEFYGATE-- 365
Cdd:PRK06187 241 RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFG-IDLVQGYGMTEts 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 366 GNICF-------MNHTGKIGSVGRVNFFYNLlfsfELIKYDfqkdeplRNEQGWcycvRKGEPGLLVSR---VNKknpff 435
Cdd:PRK06187 320 PVVSVlppedqlPGQWTKRRSAGRPLPGVEA----RIVDDD-------GDELPP----DGGEVGEIIVRgpwLMQ----- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 436 GYTGSYKQTKSKllfdvFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVP 515
Cdd:PRK06187 380 GYWNRPEATAET-----IDGG--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVP 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149064320 516 VP--GYEGKAgmtSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:PRK06187 453 DEkwGERPVA---VVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
56-556 |
5.24e-44 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 165.67 E-value: 5.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 56 VLDKflsHARRQPKKAFIIYEGD-----VYTYEDVDKRSNRVAHALLNHsDLKRGDVVALLMSNEPDFVHVWFGLAKLGC 130
Cdd:COG0365 14 CLDR---HAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRAL-GVKKGDRVAIYLPNIPEAVIAMLACARIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 131 VVAFLNSNLRFESLLHCIRTSEPKAMVVGE---------DLLGSLEEILPSLP--KHIRVWG--MKDSVPEGIVSLKEKL 197
Cdd:COG0365 90 VHSPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVDEALEELPslEHVIVVGrtGADVPMEGDLDWDELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 198 SLASD----EPVPPSHhvtsslksTCLYIFTSGTTGLPKAAVISQ----FQVLKgsFGLWAFGCTADDIVYITLPLY--- 266
Cdd:COG0365 170 AAASAefepEPTDADD--------PLFILYTSGTTGKPKGVVHTHggylVHAAT--TAKYVLDLKPGDVFWCTADIGwat 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 267 -HSS---GALLgiggcveLGATCVL---KKKF-SASQFWNDCRKYNVTVFqyigelC------RYLCKQPQREGEKDHRV 332
Cdd:COG0365 240 gHSYivyGPLL-------NGATVVLyegRPDFpDPGRLWELIEKYGVTVF------FtaptaiRALMKAGDEPLKKYDLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 333 RL----AVGNGMSSDVWRQFLDRFGnIKMCEFYGATEGNICFMNHTG----KIGSVGRVnffynlLFSFELIkydfqkde 404
Cdd:COG0365 307 SLrllgSAGEPLNPEVWEWWYEAVG-VPIVDGWGQTETGGIFISNLPglpvKPGSMGKP------VPGYDVA-------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 405 pLRNEQGwcYCVRKGEPGLLVsrVNKKNP--FFGYTGSYKQTKSKlLFDVFKkgDVYFnTGDLMFQDHENFLYFWDRIGD 482
Cdd:COG0365 372 -VVDEDG--NPVPPGEEGELV--IKGPWPgmFRGYWNDPERYRET-YFGRFP--GWYR-TGDGARRDEDGYFWILGRSDD 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 483 TFRWKGENVATTEVANVLGRLDFIQEANVYGVP-------VPGYegkagmtsIILKPNKSLD--LEK-MYDQVVTSLPAY 552
Cdd:COG0365 443 VINVSGHRIGTAEIESALVSHPAVAEAAVVGVPdeirgqvVKAF--------VVLKPGVEPSdeLAKeLQAHVREELGPY 514
|
....
gi 149064320 553 ACPR 556
Cdd:COG0365 515 AYPR 518
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
69-579 |
1.20e-43 |
|
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: 163.25 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 69 KKAFIIYEGD-VYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHC 147
Cdd:cd05926 3 APALVVPGSTpALTYADLAELVDDLARQLAALG-IKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 148 IRTSEPKAMVVGEDLLGSLEEILPSLPKHIRVWGMKDSVPEGIVSlKEKLSLASDEPVPPSHHVTSSLKSTCLYIFTSGT 227
Cdd:cd05926 82 LADLGSKLVLTPKGELGPASRAASKLGLAILELALDVGVLIRAPS-AESLSNLLADKKNAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 228 TGLPKAAVISQFQVL------KGSFGLwafgcTADDIVYITLPLYHSSG------ALLGIGGCVelgatcVLKKKFSASQ 295
Cdd:cd05926 161 TGRPKGVPLTHRNLAasatniTNTYKL-----TPDDRTLVVMPLFHVHGlvasllSTLAAGGSV------VLPPRFSAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 296 FWNDCRKYNVTVFQYIGELCRYLCKQPQREGEK-DHRVRLA--VGNGMSSDVWRQFLDRFGnIKMCEFYGATEG-NICFM 371
Cdd:cd05926 230 FWPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIrsCSASLPPAVLEALEATFG-APVLEAYGMTEAaHQMTS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 372 N----HTGKIGSVGRVnffynllFSFELIKYDfQKDEPLRNEQgwcycvrKGEpgllVSrVNKKNPFFGYTGSYKQTKsk 447
Cdd:cd05926 309 NplppGPRKPGSVGKP-------VGVEVRILD-EDGEILPPGV-------VGE----IC-LRGPNVTRGYLNNPEANA-- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 448 llfDVFKKGDvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTS 527
Cdd:cd05926 367 ---EAAFKDG-WFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKY-GEEVAAA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 149064320 528 IILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVE 579
Cdd:cd05926 442 VVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
64-613 |
3.11e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 166.82 E-value: 3.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNhSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLnsnlrfes 143
Cdd:PRK07868 457 ARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIA-VGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLM-------- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 144 llhcirtsEPKAMVVGEDLLGSLEEIL--PS-------LPKHIRVWGMKDS----VPEG--IVSLkEKLSLASDEpVPPS 208
Cdd:PRK07868 528 --------PPDTDLAAAVRLGGVTEIItdPTnleaarqLPGRVLVLGGGESrdldLPDDadVIDM-EKIDPDAVE-LPGW 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 209 HHVTSSLKSTCLYIFTSGTTG--LPKaavisqfQVLKGSFGLWAFGC--TAD----DIVYITLPLYHSSGALLGIGGCVE 280
Cdd:PRK07868 598 YRPNPGLARDLAFIAFSTAGGelVAK-------QITNYRWALSAFGTasAAAldrrDTVYCLTPLHHESGLLVSLGGAVV 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 281 LGATCVLKKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGNIKMCEF 360
Cdd:PRK07868 671 GGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEF 750
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 361 YGATEGNICFMNHTG-KIGSVGR-------VnffynllfsfELIKYDFQKDEPLRNEQGWCYCVRKGEPGLLVSRVNkkn 432
Cdd:PRK07868 751 FATTDGQAVLANVSGaKIGSKGRplpgagrV----------ELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLARAR--- 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 433 pffgytGSYKQTKSkLLFDVFKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVY 512
Cdd:PRK07868 818 ------GPIDPTAS-VKRGVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTY 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 513 GVPVPGYEgkAGMTSIILKPNKSLDLEKMYDqVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVEEGFnPLKIADPLY 592
Cdd:PRK07868 891 GVEVGGRQ--LAVAAVTLRPGAAITAADLTE-ALASLPVGLGPDIVHVVPEIPLSATYRPTVSALRAAGI-PKPGRQAWY 966
|
570 580
....*....|....*....|.
gi 149064320 593 FmDNLKKSYVPLTQEIYNQVM 613
Cdd:PRK07868 967 F-DPETNRYRRLTPAVRAELT 986
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
55-580 |
3.72e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 156.60 E-value: 3.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 55 TVLDKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 135 LNSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLP--KHIRVWGMKDSVPEGIVSLKEKLSLASDEPVPPSHHVT 212
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPalEHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAPEVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 213 SSlkSTCLYIFTSGTTGLPKAAVISQFQVLKgSFGLWA--FGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKK 290
Cdd:PRK07656 165 PD--DVADILFTSGTTGRPKGAMLTHRQLLS-NAADWAeyLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 291 FSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDV--WRQFLDRFGNIKMCEFYGATE--G 366
Cdd:PRK07656 242 FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPValLERFESELGVDIVLTGYGLSEasG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 367 NICFMNHTGKI----GSVGRvnffynllfSFELIKydfqkdepLR--NEQGwcYCVRKGEPGLLVSRvnkknpffGYT-- 438
Cdd:PRK07656 322 VTTFNRLDDDRktvaGTIGT---------AIAGVE--------NKivNELG--EEVPVGEVGELLVR--------GPNvm 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 439 -GSYKQ---TKSKLlfdvfkKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGV 514
Cdd:PRK07656 375 kGYYDDpeaTAAAI------DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149064320 515 PVPGYeGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVEE 580
Cdd:PRK07656 449 PDERL-GEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
64-577 |
1.45e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 143.53 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFES 143
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLG-LKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 144 LLHCIRTSEPKAMVVGEDLLGSLEEILPSLPKHIRVWGMKDSVPEGIVSLKEKLSLASDEPVP-PSHHVTSSLKSTCLYi 222
Cdd:PRK08316 100 LAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAePDVELADDDLAQILY- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 223 fTSGTTGLPKAAVISQFQVLKGSFG-LWAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCR 301
Cdd:PRK08316 179 -TSGTESLPKGAMLTHRALIAEYVScIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 302 KYNVTVF-----QYIGelcryLCKQPQREgekdhRVRLAV-------GNGMSSDVWRQFLDRFGNIKMCEFYGATE-GNI 368
Cdd:PRK08316 258 AERITSFfapptVWIS-----LLRHPDFD-----TRDLSSlrkgyygASIMPVEVLKELRERLPGLRFYNCYGQTEiAPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 369 CFM----NHTGKIGSVGRVNFFynllfsFEL-IKYDFQKDeplrneqgwcycVRKGEPGLLVSRvnkkNP--FFGYTGSY 441
Cdd:PRK08316 328 ATVlgpeEHLRRPGSAGRPVLN------VETrVVDDDGND------------VAPGEVGEIVHR----SPqlMLGYWDDP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 442 KQTKskllfDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgYEG 521
Cdd:PRK08316 386 EKTA-----EAFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDP-KWI 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 149064320 522 KAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:PRK08316 458 EAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
64-579 |
1.73e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 140.00 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFES 143
Cdd:PRK06839 12 AYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 144 LLHCIRTSEPKAMVVGEDLLGSLEEILPSLPKHIRVWgmkdsvpegIVSLKEKLSLASDEPVPPSHhvtsslKSTCLYIF 223
Cdd:PRK06839 92 LIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVIS---------ITSLKEIEDRKIDNFVEKNE------SASFIICY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 224 TSGTTGLPKAAVISQFQVLKGSF-GLWAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRK 302
Cdd:PRK06839 157 TSGTTGKPKGAVLTQENMFWNALnNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 303 YNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSS--DVWRQFLDR---FGnikmcEFYGATEGN-ICFM----N 372
Cdd:PRK06839 237 HKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCpeELMREFIDRgflFG-----QGFGMTETSpTVFMlseeD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 373 HTGKIGSVGRVNFFYNllfsFELIKYDFQKDEPlrneqgwcycvrkGEPGLLVsrVNKKNPFFGYTGSYKQTKSKLlfdv 452
Cdd:PRK06839 312 ARRKVGSIGKPVLFCD----YELIDENKNKVEV-------------GEVGELL--IRGPNVMKEYWNRPDATEETI---- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 453 fkkGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSIILKP 532
Cdd:PRK06839 369 ---QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKW-GEIPIAFIVKKS 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 149064320 533 NKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVE 579
Cdd:PRK06839 445 SSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
71-579 |
3.28e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 130.41 E-value: 3.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 71 AFIIY-EGDVYTYEDVDKRSNRVAHaLLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIR 149
Cdd:PRK08276 2 AVIMApSGEVVTYGELEARSNRLAH-GLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 150 TSEPKAMVVGEDLLGSLEEILPSLPKHIRVWGMKDSVPEGIVSLKEKLSLASDEPVPPshhvtSSLKSTCLYifTSGTTG 229
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIAD-----ETAGADMLY--SSGTTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 230 LPKAAVISQFQV------LKGSFGLWAFGCTADDIVYI-TLPLYHSsgALLGIGGCV-ELGATCVLKKKFSASQFWNDCR 301
Cdd:PRK08276 154 RPKGIKRPLPGLdpdeapGMMLALLGFGMYGGPDSVYLsPAPLYHT--APLRFGMSAlALGGTVVVMEKFDAEEALALIE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 302 KYNVTVFQYIGELCRYLCKQPQREGEK----DHRVRLAVGNGMSSDVWRQFLDRFGNIkMCEFYGATEGN-ICFMNHT-- 374
Cdd:PRK08276 232 RYRVTHSQLVPTMFVRMLKLPEEVRARydvsSLRVAIHAAAPCPVEVKRAMIDWWGPI-IHEYYASSEGGgVTVITSEdw 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 375 -GKIGSVGRVnffynlLFSfELIKYDFQKDEplrneqgwcycVRKGEPGLLVSRVNkknpffGYTGSYKQTKSKLLFDVF 453
Cdd:PRK08276 311 lAHPGSVGKA------VLG-EVRILDEDGNE-----------LPPGEIGTVYFEMD------GYPFEYHNDPEKTAAARN 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 454 KKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVP--GYEGKAgmtsiILK 531
Cdd:PRK08276 367 PHG--WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEemGERVKA-----VVQ 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 149064320 532 PNKSLDL-----EKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVE 579
Cdd:PRK08276 440 PADGADAgdalaAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
63-580 |
5.25e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 130.01 E-value: 5.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 63 HARRQPKKAFIIYEGDVYTYEDVDKRSnRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFE 142
Cdd:PRK06145 11 HARRTPDRAALVYRDQEISYAEFHQRI-LQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 143 SLLHCIRTSEPKAMVVGEDLlgsleEILPSLPKHIRVWGmkdsvpEGIVSLKEKLSlASDEPVPPSHHVTSSLKSTCLYi 222
Cdd:PRK06145 90 EVAYILGDAGAKLLLVDEEF-----DAIVALETPKIVID------AAAQADSRRLA-QGGLEIPPQAAVAPTDLVRLMY- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 223 fTSGTTGLPKAAVISQFQVLKGSFG-LWAFGCTADDIVYITLPLYHsSGA--LLGIGGCVELGATCVLkKKFSASQFWND 299
Cdd:PRK06145 157 -TSGTTDRPKGVMHSYGNLHWKSIDhVIALGLTASERLLVVGPLYH-VGAfdLPGIAVLWVGGTLRIH-REFDPEAVLAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 300 CRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVW--RQFLDRFGNIKMCEFYGATE--GNICFMN--- 372
Cdd:PRK06145 234 IERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESriRDFTRVFTRARYIDAYGLTEtcSGDTLMEagr 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 373 HTGKIGSVGRVnffynlLFSFELikydfqkdEPLRNEQGWCYCVRKGEPGLLVSRVNKknpffGYTGSYKQTKSKLLFDv 452
Cdd:PRK06145 314 EIEKIGSTGRA------LAHVEI--------RIADGAGRWLPPNMKGEICMRGPKVTK-----GYWKDPEKTAEAFYGD- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 453 fkkgdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSIILKP 532
Cdd:PRK06145 374 ------WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRW-GERITAVVVLNP 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 149064320 533 NKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVEE 580
Cdd:PRK06145 447 GATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
64-585 |
5.97e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 130.47 E-value: 5.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFES 143
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 144 LLHCIRTSEPKAMVVGEDLLGSLEEILPSLP-KHIRVWGMKDSVPE----------------------GIVSLKEklSLA 200
Cdd:PRK08314 100 LAHYVTDSGARVAIVGSELAPKVAPAVGNLRlRHVIVAQYSDYLPAepeiavpawlraepplqalapgGVVAWKE--ALA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 201 SDEPvPPSHHVTSSlkSTCLYIFTSGTTGLPKAAVISQFQVLKGSFG--LWaFGCTADDIVYITLPLYHSSGALLGIGGC 278
Cdd:PRK08314 178 AGLA-PPPHTAGPD--DLAVLPYTSGTTGVPKGCMHTHRTVMANAVGsvLW-SNSTPESVVLAVLPLFHVTGMVHSMNAP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 279 VELGATCVLKKKfsasqfWN-----DC-RKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNG--MSSDVWRQFLD 350
Cdd:PRK08314 254 IYAGATVVLMPR------WDreaaaRLiERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGaaMPEAVAERLKE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 351 RFGnIKMCEFYGATEgNICF--MN--HTGKIGSVGRVnffynlLFSFELIKYDFQKDEPLrneqgwcycvRKGEPGLLVs 426
Cdd:PRK08314 328 LTG-LDYVEGYGLTE-TMAQthSNppDRPKLQCLGIP------TFGVDARVIDPETLEEL----------PPGEVGEIV- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 427 rVNKKNPFFGYTGSYKQT-KSKLLFDvfkkGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDF 505
Cdd:PRK08314 389 -VHGPQVFKGYWNRPEATaEAFIEID----GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 506 IQEANVYGVPVP--GYEGKAgmtSIILKPNK--SLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKL--KKLQLVE 579
Cdd:PRK08314 464 IQEACVIATPDPrrGETVKA---VVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKIlwRQLQEQE 540
|
....*.
gi 149064320 580 EGFNPL 585
Cdd:PRK08314 541 KARAAK 546
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
63-579 |
1.58e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 128.66 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 63 HARRQPKK-AFIIYE-GDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLR 140
Cdd:PRK13391 6 HAQTTPDKpAVIMAStGEVVTYRELDERSNRLAHLFRSLG-LKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 141 FESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLPkHIRVWGMKDSV--PEGIVSLKEKLSLASDEPVPpshhvTSSLKST 218
Cdd:PRK13391 85 PAEAAYIVDDSGARALITSAAKLDVARALLKQCP-GVRHRLVLDGDgeLEGFVGYAEAVAGLPATPIA-----DESLGTD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 219 CLYifTSGTTGLPKAAV-------ISQ----FQVLKgsfGLWAFGctaDDIVYI-TLPLYHsSGALLGIGGCVELGATCV 286
Cdd:PRK13391 159 MLY--SSGTTGRPKGIKrplpeqpPDTplplTAFLQ---RLWGFR---SDMVYLsPAPLYH-SAPQRAVMLVIRLGGTVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 287 LKKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEK-DH---RVRLAVGNGMSSDVWRQFLDRFGNIkMCEFYG 362
Cdd:PRK13391 230 VMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKyDLsslEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 363 ATEGN-ICFMNHT---GKIGSVGRVnffynlLFSFELIKYDFQKDEPlrneqgwcycvrKGEPGLLVSRVNKKnpfFGYT 438
Cdd:PRK13391 309 ATEGLgFTACDSEewlAHPGTVGRA------MFGDLHILDDDGAELP------------PGEPGTIWFEGGRP---FEYL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 439 GSYKQTKSKllfdvfKKGDVYFNT-GDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVP 517
Cdd:PRK13391 368 NDPAKTAEA------RHPDGTWSTvGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNE 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149064320 518 --GYEGKAgmtsiILKP----NKSLDL-EKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVE 579
Cdd:PRK13391 442 dlGEEVKA-----VVQPvdgvDPGPALaAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
80-577 |
9.88e-31 |
|
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: 125.14 E-value: 9.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVG 159
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 160 EDllgsleeilpslpkhirvwgmkdsvpegivslkeklslasdepvppshhvtsslkSTCLYIFTSGTTGLPKAAVISQF 239
Cdd:cd05972 80 AE-------------------------------------------------------DPALIYFTSGTTGLPKGVLHTHS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 240 QVLK-GSFGLWAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVL--KKKFSASQFWNDCRKYNVTVFQYIGELCR 316
Cdd:cd05972 105 YPLGhIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCGPPTAYR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 317 YLCKQPQREGEKDHrVRLAVGNG--MSSDVWRQFLDRFGnIKMCEFYGATEGNICFMNHTG---KIGSVGRVNFFYNLlf 391
Cdd:cd05972 185 MLIKQDLSSYKFSH-LRLVVSAGepLNPEVIEWWRAATG-LPIRDGYGQTETGLTVGNFPDmpvKPGSMGRPTPGYDV-- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 392 sfELIKYDFQKDEPlrneqgwcycvrkGEPGLLVSRVNKKNPFFGYTGSYKQTKSKLlfdvfkKGDVYFnTGDLMFQDHE 471
Cdd:cd05972 261 --AIIDDDGRELPP-------------GEEGDIAIKLPPPGLFLGYVGDPEKTEASI------RGDYYL-TGDRAYRDED 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 472 NFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSIILK----PNKSLDLEkMYDQVVT 547
Cdd:cd05972 319 GYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVR-GEVVKAFVVLTsgyePSEELAEE-LQGHVKK 396
|
490 500 510
....*....|....*....|....*....|
gi 149064320 548 SLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd05972 397 VLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
63-579 |
1.44e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 126.20 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 63 HARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFE 142
Cdd:PRK07788 58 AARRAPDRAALIDERGTLTYAELDEQSNALARGLLALG-VRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 143 SLLHCIRTSEPKAMVVGEDLLGSLEEILPSLPKhIRVWGM-KDSVPE---GIVSLKEKLSLASDEPVP----PSHHVtss 214
Cdd:PRK07788 137 QLAEVAAREGVKALVYDDEFTDLLSALPPDLGR-LRAWGGnPDDDEPsgsTDETLDDLIAGSSTAPLPkppkPGGIV--- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 215 lkstclyIFTSGTTGLPKAAVISQ---FQVLKGSFGLWAFGctADDIVYITLPLYHSSG---ALLGIGgcveLGATCVLK 288
Cdd:PRK07788 213 -------ILTSGTTGTPKGAPRPEpspLAPLAGLLSRVPFR--AGETTLLPAPMFHATGwahLTLAMA----LGSTVVLR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 289 KKFSASQFWNDCRKYNVT------VFqyigeLCRYLCKQPQREGEKDH---RVRLAVGNGMSSDVWRQFLDRFGNIkMCE 359
Cdd:PRK07788 280 RRFDPEATLEDIAKHKATalvvvpVM-----LSRILDLGPEVLAKYDTsslKIIFVSGSALSPELATRALEAFGPV-LYN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 360 FYGATEGNICFMNHTGKI----GSVGRVnffynlLFSFELIKYDfQKDEPlrneqgwcycVRKGEPGllvsRVNKKN--P 433
Cdd:PRK07788 354 LYGSTEVAFATIATPEDLaeapGTVGRP------PKGVTVKILD-ENGNE----------VPRGVVG----RIFVGNgfP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 434 FFGYTGS-YKQTKSKLLfdvfkkgdvyfNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVY 512
Cdd:PRK07788 413 FEGYTDGrDKQIIDGLL-----------SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVI 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 513 GVPVPGYeGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPR---FLriqDKMETTGTFKLKKLQLVE 579
Cdd:PRK07788 482 GVDDEEF-GQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRdvvFL---DELPRNPTGKVLKRELRE 547
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
56-579 |
3.79e-30 |
|
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: 124.92 E-value: 3.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 56 VLDKFlshARRQPKKAFIIYEGD-----VYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGC 130
Cdd:cd05970 22 VVDAM---AKEYPDKLALVWCDDageerIFTFAELADYSDKTANFFKAMG-IGKGDTVMLTLKRRYEFWYSLLALHKLGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 131 VVAFLNSNLRFESLLHCIRTSEPKAMVV--GEDLLGSLEEILPSLP-KHIRVWgMKDSVPEGIVSLKEKLSLASDEPVPP 207
Cdd:cd05970 98 IAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPsKPKLVW-VGDPVPEGWIDFRKLIKNASPDFERP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 208 SHHVTSSLKSTCLYIFTSGTTGLPKaAVISQF-----QVLKGSFglWAfgCTADDIVYITLPLYHSSGALLG------IG 276
Cdd:cd05970 177 TANSYPCGEDILLVYFSSGTTGMPK-MVEHDFtyplgHIVTAKY--WQ--NVREGGLHLTVADTGWGKAVWGkiygqwIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 277 GCvelgATCVLK-KKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQP-QREGEKDHRVRLAVGNGMSSDVWRQFLDRFGn 354
Cdd:cd05970 252 GA----AVFVYDyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDlSRYDLSSLRYCTTAGEALNPEVFNTFKEKTG- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 355 IKMCEFYGATEGNICFMNHTG---KIGSVGRVNFFYNLlfsfELIKYDFQKdeplrneqgwcycVRKGEPGLLVSRVNKK 431
Cdd:cd05970 327 IKLMEGFGQTETTLTIATFPWmepKPGSMGKPAPGYEI----DLIDREGRS-------------CEAGEEGEIVIRTSKG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 432 NPFFGYTGSYKQTKSKLlfDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANV 511
Cdd:cd05970 390 KPVGLFGGYYKDAEKTA--EVWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAV 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149064320 512 YGVPVPgYEGKAGMTSIIL----KPNKSLDLEKMyDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVE 579
Cdd:cd05970 466 TGVPDP-IRGQVVKATIVLakgyEPSEELKKELQ-DHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
62-579 |
2.82e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 122.19 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 62 SHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRF 141
Cdd:PRK07786 25 RHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRG-VGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 142 ESLLHCIRTSEPKAMVVgEDLLGSL----EEILPSLPKHIRVWGMKDsvpEGIVSLKEKLSlASDEPVPPshhVTSSLKS 217
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVT-EAALAPVatavRDIVPLLSTVVVAGGSSD---DSVLGYEDLLA-EAGPAHAP---VDIPNDS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 218 TCLYIFTSGTTGLPKAAVIS----QFQVLKGSFGLWAFgcTADDIVYITLPLYHSSGaLLGIGGCVELGATCVLK--KKF 291
Cdd:PRK07786 176 PALIMYTSGTTGRPKGAVLThanlTGQAMTCLRTNGAD--INSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIYplGAF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 292 SASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGeKDHRVR-LAVGNGMSSD-VWRQFLDRFGNIKMCEFYGATEGN-- 367
Cdd:PRK07786 253 DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALRvLSWGAAPASDtLLRQMAATFPEAQILAAFGQTEMSpv 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 368 ICFM---NHTGKIGSVGRVnffyNLLFSFELIkydfqkDEPLRNeqgwcycVRKGEPGLLVSRvnKKNPFFGYTGSYKQT 444
Cdd:PRK07786 332 TCMLlgeDAIRKLGSVGKV----IPTVAARVV------DENMND-------VPVGEVGEIVYR--APTLMSGYWNNPEAT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 445 KskllfDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAG 524
Cdd:PRK07786 393 A-----EAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKW-GEVP 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 149064320 525 MTSIILKP-NKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVE 579
Cdd:PRK07786 465 VAVAAVRNdDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
69-577 |
8.21e-28 |
|
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: 116.41 E-value: 8.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 69 KKAFIIYEGDVyTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCI 148
Cdd:cd05919 1 KTAFYAADRSV-TYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 149 RTSEPKAMVVGEDLLgsleeilpslpkhirvwgmkdsvpegivslkeklslasdepvppshhvtsslkstCLYIFTSGTT 228
Cdd:cd05919 79 RDCEARLVVTSADDI-------------------------------------------------------AYLLYSSGTT 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 229 GLPKAAVISQFQVLkGSFGLWA---FGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKF-SASQFWNDCRKYN 304
Cdd:cd05919 104 GPPKGVMHAHRDPL-LFADAMAreaLGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLATLARFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 305 VTVFQYIGELCRYLCKQPQREGEKDHRVRLAV--GNGMSSDVWRQFLDRFGnIKMCEFYGATE-GNICFMNHTG--KIGS 379
Cdd:cd05919 183 PTVLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFG-GPILDGIGATEvGHIFLSNRPGawRLGS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 380 VGRVNFFYNLlfsfelikydfqkdePLRNEQGwcYCVRKGEPGLLVSRvnKKNPFFGYTGSYKQTKSKLLfdvfkkgDVY 459
Cdd:cd05919 262 TGRPVPGYEI---------------RLVDEEG--HTIPPGEEGDLLVR--GPSAAVGYWNNPEKSRATFN-------GGW 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 460 FNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVygVPVPGYEGKAGMTS-IILKP---NKS 535
Cdd:cd05919 316 YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGLSRLTAfVVLKSpaaPQE 393
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 149064320 536 LDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd05919 394 SLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
81-577 |
4.57e-27 |
|
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: 114.11 E-value: 4.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 81 TYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVGe 160
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKG-VRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 161 dllgsleeilpslpkhirvwgmkdsvpegivslkeklslasdepvppshhvtSSLKSTCLYIFTSGTTGLPKAAVISQFQ 240
Cdd:cd05935 81 ----------------------------------------------------SELDDLALIPYTSGTTGLPKGCMHTHFS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 241 VLKGSFGL-WAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVTVFQYIGELCRYLC 319
Cdd:cd05935 109 AAANALQSaVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 320 KQPQREgEKDHRVRLAVGNG---MSSDVWRQFLDRFGnIKMCEFYGATEgnICFMNHTG-----KIGSVGRVNFfynllf 391
Cdd:cd05935 189 ATPEFK-TRDLSSLKVLTGGgapMPPAVAEKLLKLTG-LRFVEGYGLTE--TMSQTHTNpplrpKLQCLGIP*F------ 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 392 SFELIKYDFQKDEPLRNeqgwcycvrkGEPGLLVsrVNKKNPFFGYTGSYKQTKSKLLFDvfkKGDVYFNTGDLMFQDHE 471
Cdd:cd05935 259 GVDARVIDIETGRELPP----------NEVGEIV--VRGPQIFKGYWNRPEETEESFIEI---KGRRFFRTGDLGYMDEE 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 472 NFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgYEGKAGMTSIILKP--NKSLDLEKMYDQVVTSL 549
Cdd:cd05935 324 GYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDE-RVGEEVKAFIVLRPeyRGKVTEEDIIEWAREQM 402
|
490 500
....*....|....*....|....*...
gi 149064320 550 PAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd05935 403 AAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
80-577 |
7.02e-27 |
|
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: 113.21 E-value: 7.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHALLNHSDlKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLrfesllhcirtsepkamvvg 159
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGV-RKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRL-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 160 edllgSLEEILpslpkhirvWGMKDSvpegivslkeklslasdepvppshhvTSSLKSTCLYIFTSGTTGLPKAAVISqf 239
Cdd:cd05912 61 -----TPNELA---------FQLKDS--------------------------DVKLDDIATIMYTSGTTGKPKGVQQT-- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 240 qvlkgsFG-LWA--------FGCTADDIVYITLPLYHSSGaLLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVTVFQY 310
Cdd:cd05912 99 ------FGnHWWsaigsalnLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 311 IGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRfgNIKMCEFYGATE--GNICFMN----HTgKIGSVGRVn 384
Cdd:cd05912 172 VPTMLQRLLEILGEGYPNNLRCILLGGGPAPKPLLEQCKEK--GIPVYQSYGMTEtcSQIVTLSpedaLN-KIGSAGKP- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 385 ffynlLFSFEL-IKYDFQkdeplrneqgwcycvRKGEPGLLVsrVNKKNPFFGYTGSYKQTKSkllfdVFKKGdvYFNTG 463
Cdd:cd05912 248 -----LFPVELkIEDDGQ---------------PPYEVGEIL--LKGPNVTKGYLNRPDATEE-----SFENG--WFKTG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 464 DLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPvpgyEGKAGMTSII-LKPNKSLDLEKMY 542
Cdd:cd05912 299 DIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIP----DDKWGQVPVAfVVSERPISEEELI 374
|
490 500 510
....*....|....*....|....*....|....*
gi 149064320 543 DQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd05912 375 AYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
44-513 |
9.81e-27 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 114.81 E-value: 9.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 44 MEIYKLRGELVTVLDKFLSHARRQPKK-AFIIYEGDVY---TYEDVDKRSNRVAHALLNHsDLKRGDVVALLMSNEPDFV 119
Cdd:COG1022 1 MSEFSDVPPADTLPDLLRRRAARFPDRvALREKEDGIWqslTWAEFAERVRALAAGLLAL-GVKPGDRVAILSDNRPEWV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 120 HVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVG-EDLLGSLEEILPSLPKHIRVWGMKDSVP---EGIVSLKE 195
Cdd:COG1022 80 IADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDELPSLRHIVVLDPRGLrddPRLLSLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 196 KLSLASDEPVPPSHH---VTSSLKSTCLYIFTSGTTGLPKAAVISQFQVLKGSFGLWA-FGCTADDIVYITLPLYHSSGA 271
Cdd:COG1022 160 LLALGREVADPAELEarrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLErLPLGPGDRTLSFLPLAHVFER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 272 LLGIgGCVELGATCVlkkkFSAS--QFWNDCRKYNVTVF-------------------------QYIGELCRYLCKQ--P 322
Cdd:COG1022 240 TVSY-YALAAGATVA----FAESpdTLAEDLREVKPTFMlavprvwekvyagiqakaeeagglkRKLFRWALAVGRRyaR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 323 QREGEKDH----RVRLAVGNGMssdVWRQFLDRFGN------------------------IKMCEFYGATE-GNICFMNH 373
Cdd:COG1022 315 ARLAGKSPslllRLKHALADKL---VFSKLREALGGrlrfavsggaalgpelarffralgIPVLEGYGLTEtSPVITVNR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 374 TG--KIGSVGRvnffynllfsfelikydfqkdePLRNEQgwcycVRKGEPG-LLVsrvnkKNP--FFGYtgsYKQ---TK 445
Cdd:COG1022 392 PGdnRIGTVGP----------------------PLPGVE-----VKIAEDGeILV-----RGPnvMKGY---YKNpeaTA 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149064320 446 skllfDVFKKgDVYFNTGDLMFQDHENFLYFWDRIGDTFrwK---GENVATTEVANVLGRLDFIQEANVYG 513
Cdd:COG1022 437 -----EAFDA-DGWLHTGDIGELDEDGFLRITGRKKDLI--VtsgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
64-583 |
3.32e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 112.36 E-value: 3.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFES 143
Cdd:PRK03640 12 AFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 144 LLHCIRTSEPKAMVVGEDLLGSLEEILPSLpkhirvWGMKDSVPEGIVSLKEklslasdepvppshhvTSSLKSTCLYIF 223
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEAKLIPGISVK------FAELMNGPKEEAEIQE----------------EFDLDEVATIMY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 224 TSGTTGLPKaAVISQFQvlkgsfGLWA--------FGCTADDIVYITLPLYHSSGaLLGIGGCVELGATCVLKKKFSASQ 295
Cdd:PRK03640 149 TSGTTGKPK-GVIQTYG------NHWWsavgsalnLGLTEDDCWLAAVPIFHISG-LSILMRSVIYGMRVVLVEKFDAEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 296 FWNDCRKYNVTVFQYIGE-LCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRfgNIKMCEFYGATE--GNIC--- 369
Cdd:PRK03640 221 INKLLQTGGVTIISVVSTmLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEK--GIPVYQSYGMTEtaSQIVtls 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 370 --FMNHtgKIGSVGRVnffynlLFSFEL-IKYDFQKDEPlrNEQGwcYCVRKGePGLLVsrvnkknpffGYTGSYKQTKs 446
Cdd:PRK03640 299 peDALT--KLGSAGKP------LFPCELkIEKDGVVVPP--FEEG--EIVVKG-PNVTK----------GYLNREDATR- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 447 kllfDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPvpgyEGKAGMT 526
Cdd:PRK03640 355 ----ETFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVP----DDKWGQV 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 149064320 527 SI-ILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVEEGFN 583
Cdd:PRK03640 425 PVaFVVKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEE 482
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
70-579 |
6.05e-26 |
|
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: 110.84 E-value: 6.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 70 KAFIIYEGDVYTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIR 149
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 150 TSEPKAMVVGedllgsleeilpslpkhirvwgmkdsvpegivslkeklslasdepvppshhvtsslkstCLYIFTSGTTG 229
Cdd:cd05941 82 DSEPSLVLDP-----------------------------------------------------------ALILYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 230 LPKAAVISQFQVLKGSFGL---WAFgcTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVT 306
Cdd:cd05941 103 RPKGVVLTHANLAANVRALvdaWRW--TEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 307 VFQ-----YIGELCRYLCKQPQREGEKD---HRVRLAV-GNG-MSSDVWRQFLDRFGNiKMCEFYGATEGNI---CFMNH 373
Cdd:cd05941 181 VFMgvptiYTRLLQYYEAHFTDPQFARAaaaERLRLMVsGSAaLPVPTLEEWEAITGH-TLLERYGMTEIGMalsNPLDG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 374 TGKIGSVGRVnffynlLFSFEL-IKYDFQKDEPLRNEQGWcYCVRKgePGLlvsrvnkknpFFGYTGSYKQTKSKLlfdv 452
Cdd:cd05941 260 ERRPGTVGMP------LPGVQArIVDEETGEPLPRGEVGE-IQVRG--PSV----------FKEYWNKPEATKEEF---- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 453 fkKGDVYFNTGDLMFQDHENFLYFWDRIG-DTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSIILK 531
Cdd:cd05941 317 --TDDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDW-GERVVAVVVLR 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 149064320 532 PNK-SLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVE 579
Cdd:cd05941 394 AGAaALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
57-580 |
1.36e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 111.29 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 57 LDKFLSH-ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAhALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:PRK06178 35 LTEYLRAwARERPQRPAIIFYGHVITYAELDELSDRFA-ALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 136 NSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLP-KHIRVWGMKDSVP------------------EGIVSLkek 196
Cdd:PRK06178 114 SPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSlRHVIVTSLADVLPaeptlplpdslraprlaaAGAIDL--- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 197 LSLASDEPVPPSHHVTsSLKSTCLYIFTSGTTGLPKAAVISQFQVL--KGSFGLWAFGCTADDIVYITLPLYHSSGALLG 274
Cdd:PRK06178 191 LPALRACTAPVPLPPP-ALDALAALNYTGGTTGMPKGCEHTQRDMVytAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 275 IGGCVELGATCVLKKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPqREGEKDHRvRLAVGNGMS------SDVWRQF 348
Cdd:PRK06178 270 LLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHP-RFAEYDLS-SLRQVRVVSfvkklnPDYRQRW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 349 LDRFGNIKMCEFYGATEgnicfmNHTGKIGSVGRVNFFYNLLFS--F--------ELIKYDFQKDEPLRNEQGWCYCVRK 418
Cdd:PRK06178 348 RALTGSVLAEAAWGMTE------THTCDTFTAGFQDDDFDLLSQpvFvglpvpgtEFKICDFETGELLPLGAEGEIVVRT 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 419 gePGLLVsrvnkknpffGYTGSYKQTKskllfDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVAN 498
Cdd:PRK06178 422 --PSLLK----------GYWNKPEATA-----EALRDG--WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 499 VLGRLDFIQEANVYGVPVPGyEGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRfLRIQDKMETTGTFKLKKLQLV 578
Cdd:PRK06178 483 LLGQHPAVLGSAVVGRPDPD-KGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDLQ 560
|
..
gi 149064320 579 EE 580
Cdd:PRK06178 561 AL 562
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
223-577 |
4.15e-25 |
|
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: 106.98 E-value: 4.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 223 FTSGTTGLPKAAVISQFQVLKGSF--GLwAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVL-KKKFSASQFWND 299
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYfiGE-RLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 300 CRKYNVTVFQ-----YIGELcrylcKQPQREGEKDHRVRLAV--GNGMSSDVWRQFLDRFGNIKMCEFYGATEGN-ICFM 371
Cdd:cd05917 88 IEKEKCTALHgvptmFIAEL-----EHPDFDKFDLSSLRTGImaGAPCPPELMKRVIEVMNMKDVTIAYGMTETSpVSTQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 372 NHTG-----KIGSVGRVnffynLLFSFELIKYDFQKDEPLRNEQGWcYCVRkgepGLLVSRvnkknpffGYTGSYKQTKS 446
Cdd:cd05917 163 TRTDdsiekRVNTVGRI-----MPHTEAKIVDPEGGIVPPVGVPGE-LCIR----GYSVMK--------GYWNDPEKTAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 447 KLlfdvfkKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMT 526
Cdd:cd05917 225 AI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERY-GEEVCA 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 149064320 527 SIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd05917 298 WIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
55-556 |
7.76e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 108.33 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 55 TVLDKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALlnHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:PRK07638 2 GITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWL--NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 135 LNSNLRFESLLHCIRTSEPkAMVVGED-LLGSLEEIlpslpkHIRVWGMKDsvpegivsLKEKLSLASDEPVPpshhvTS 213
Cdd:PRK07638 80 LDIKWKQDELKERLAISNA-DMIVTERyKLNDLPDE------EGRVIEIDE--------WKRMIEKYLPTYAP-----IE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 214 SLKSTCLYI-FTSGTTGLPKAAVISQfQVLKGSFGLWA--FGCTADDIVYITLPLYHSSgALLGIGGCVELGATCVLKKK 290
Cdd:PRK07638 140 NVQNAPFYMgFTSGSTGKPKAFLRAQ-QSWLHSFDCNVhdFHMKREDSVLIAGTLVHSL-FLYGAISTLYVGQTVHLMRK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 291 FSASQFWNDCRKYNVTVFQYIGELCRYLCKQpqrEGEKDHRVRLAV-GNGMSSDVWRQFLDRFGNIKMCEFYGATEGN-I 368
Cdd:PRK07638 218 FIPNQVLDKLETENISVMYTVPTMLESLYKE---NRVIENKMKIISsGAKWEAEAKEKIKNIFPYAKLYEFYGASELSfV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 369 CFMNH---TGKIGSVGRVnfFYNLLFSfelikydfqkdepLRNEQGwcYCVRKGEPGllvsRVNKKNP--FFGYTGSykq 443
Cdd:PRK07638 295 TALVDeesERRPNSVGRP--FHNVQVR-------------ICNEAG--EEVQKGEIG----TVYVKSPqfFMGYIIG--- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 444 tkSKLLFDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgYEGKA 523
Cdd:PRK07638 351 --GVLARELNADG--WMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDS-YWGEK 425
|
490 500 510
....*....|....*....|....*....|...
gi 149064320 524 gMTSIILkpnKSLDLEKMYDQVVTSLPAYACPR 556
Cdd:PRK07638 426 -PVAIIK---GSATKQQLKSFCLQRLSSFKIPK 454
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
74-575 |
9.52e-25 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 108.25 E-value: 9.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 74 IYEGD-VYTYEDVDKRSNRVAHALlNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSE 152
Cdd:PRK12406 5 IISGDrRRSFDELAQRAARAAGGL-AALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 153 PKAMVVGEDLLGSLEEILPS--------LPKHIR-VWGMKD---SVPEGIVSLKEKLSlASDEPVPPSHHVTSSLkstcl 220
Cdd:PRK12406 84 ARVLIAHADLLHGLASALPAgvtvlsvpTPPEIAaAYRISPallTPPAGAIDWEGWLA-QQEPYDGPPVPQPQSM----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 221 yIFTSGTTGLPK-----------AAVISQFQVLkgsfglwAFGCTADDIVYITLPLYHSSGALLGIGGcVELGATCVLKK 289
Cdd:PRK12406 158 -IYTSGTTGHPKgvrraaptpeqAAAAEQMRAL-------IYGLKPGIRALLTGPLYHSAPNAYGLRA-GRLGGVLVLQP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 290 KFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQ--REGEKDHRVRLAVGNGM--SSDVWRQFLDRFGNIkMCEFYGATE 365
Cdd:PRK12406 229 RFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEevRAKYDVSSLRHVIHAAApcPADVKRAMIEWWGPV-IYEYYGSTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 366 -GNICF------MNHTGKIGSV---GRVNFFynllfsfelikydfqkDEPLRNeqgwcycVRKGEPGLLVSRVnKKNPFF 435
Cdd:PRK12406 308 sGAVTFatsedaLSHPGTVGKAapgAELRFV----------------DEDGRP-------LPQGEIGEIYSRI-AGNPDF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 436 GYTGsyKQTKSKLLfdvfkKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVP 515
Cdd:PRK12406 364 TYHN--KPEKRAEI-----DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149064320 516 VPGYeGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKM--ETTGTFKLKKL 575
Cdd:PRK12406 437 DAEF-GEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELprEDSGKIFKRRL 497
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
60-577 |
3.48e-24 |
|
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: 106.30 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 60 FLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNL 139
Cdd:cd05959 10 DLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 140 RFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLPKHIRVWGMKDSVPE--GIVSLKEKLSLASDEPVPPSHHVtsslKS 217
Cdd:cd05959 89 TPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVAAEAEQLKPAATHA----DD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 218 TCLYIFTSGTTGLPKAAV--ISQFQVLKGSFGLWAFGCTADDIVYITLPLYHSSGalLGIGGCVEL--GATCVLKKKF-S 292
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVhlHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYG--LGNSLTFPLsvGATTVLMPERpT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 293 ASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAV--GNGMSSDVWRQFLDRFGnIKMCEFYGATE-GNIC 369
Cdd:cd05959 243 PAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFG-LDILDGIGSTEmLHIF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 370 FMNHTGKI--GSVGRVNFFYNLlfsfelikydfqkdePLRNEQGwcYCVRKGEPGLLVSRVNKKNPffGYTGSYKQTKsk 447
Cdd:cd05959 322 LSNRPGRVryGTTGKPVPGYEV---------------ELRDEDG--GDVADGEPGELYVRGPSSAT--MYWNNRDKTR-- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 448 llfDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgyegkAGMTS 527
Cdd:cd05959 381 ---DTFQGE--WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDE-----DGLTK 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 149064320 528 ----IILKP---NKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd05959 451 pkafVVLRPgyeDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
81-577 |
7.74e-24 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 104.45 E-value: 7.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 81 TYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRfESLLHCIRTSEPKAMVVGE 160
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQG-IRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLT-ENERTNQLEDLDVQLLLTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 161 DLLgSLEEILpslpkhirvwgmKDSVPEGIVSLKEKLSLASDEPvppshhvtssLKSTCLYIFTSGTTGLPKAAVISQFQ 240
Cdd:TIGR01923 79 SLL-EEKDFQ------------ADSLDRIEAAGRYETSLSASFN----------MDQIATLMFTSGTTGKPKAVPHTFRN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 241 VLKGSFGL-WAFGCTADDIVYITLPLYHSSGaLLGIGGCVELGATCVLKKKFSasQFWNDCRKYNVTVFQYI-GELCRYL 318
Cdd:TIGR01923 136 HYASAVGSkENLGFTEDDNWLLSLPLYHISG-LSILFRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVpTQLNRLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 319 ckqPQREGEKDHRVRLAVGNGMSSDVWRQFLDRfgNIKMCEFYGATE--GNICFMNHTG--KIGSVGRVnffynlLFSFE 394
Cdd:TIGR01923 213 ---DEGGHNENLRKILLGGSAIPAPLIEEAQQY--GLPIYLSYGMTEtcSQVTTATPEMlhARPDVGRP------LAGRE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 395 L-IKYDFQkdeplrneqgwcycVRKGEpgLLVSrvnKKNPFFGYtgsYKQTKSKLLFDvfKKGdvYFNTGDLMFQDHENF 473
Cdd:TIGR01923 282 IkIKVDNK--------------EGHGE--IMVK---GANLMKGY---LYQGELTPAFE--QQG--WFNTGDIGELDGEGF 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 474 LYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPvpgyEGKAGMTSI-ILKPNKSLDLEKMYDQVVTSLPAY 552
Cdd:TIGR01923 336 LYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKP----DAEWGQVPVaYIVSESDISQAKLIAYLTEKLAKY 411
|
490 500
....*....|....*....|....*
gi 149064320 553 ACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:TIGR01923 412 KVPIAFEKLDELPYNASGKILRNQL 436
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
77-536 |
1.00e-23 |
|
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: 105.01 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 77 GDVYTYEDVDKRSNRVAHALlNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPK-A 155
Cdd:cd05904 30 GRALTYAELERRVRRLAAGL-AKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKlA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 156 MVVGEdllgsLEEILPSLpkHIRVWGMkDSVPEGiVSLKEKLSLASDEPVPPSHHVTSSlkSTCLYIFTSGTTGLPKAAV 235
Cdd:cd05904 109 FTTAE-----LAEKLASL--ALPVVLL-DSAEFD-SLSFSDLLFEADEAEPPVVVIKQD--DVAALLYSSGTTGRSKGVM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 236 ------ISQFQVLKGSFGLwafgCTADDIVYI-TLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVTVF 308
Cdd:cd05904 178 lthrnlIAMVAQFVAGEGS----NSDSEDVFLcVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 309 QYIGELCRYLCKQPQREGEKDHRVRlAVGNG---MSSDVWRQFLDRFGNIKMCEFYGATE-GNICFM-----NHTGKIGS 379
Cdd:cd05904 254 PVVPPIVLALVKSPIVDKYDLSSLR-QIMSGaapLGKELIEAFRAKFPNVDLGQGYGMTEsTGVVAMcfapeKDRAKYGS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 380 VGRvnffynLLFSFELIKYDFQKDEPL-RNEQGWcYCVRKgePGllvsrVNKknpffGYTGSYKQTKSKLLFDVFKKgdv 458
Cdd:cd05904 333 VGR------LVPNVEAKIVDPETGESLpPNQTGE-LWIRG--PS-----IMK-----GYLNNPEATAATIDKEGWLH--- 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149064320 459 yfnTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVygVPVPGYE-GKAGMTSIILKPNKSL 536
Cdd:cd05904 391 ---TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV--IPYPDEEaGEVPMAFVVRKPGSSL 464
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
49-579 |
1.07e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 105.24 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 49 LRGElvTVLDKFLSHARRQPKKAFIIY--EGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLA 126
Cdd:PRK12583 15 LLTQ--TIGDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALG-VQPGDRVGIWAPNCAEWLLTQFATA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 127 KLGCVVAFLNSNLRFESLLHCIRTSEPKAMVV-----GEDLLGSLEEILPSL-------------PKHIRVWGMKDSVPE 188
Cdd:PRK12583 92 RIGAILVNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLaegqpgalacerlPELRGVVSLAPAPPP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 189 GIVSLKEKLSLAsdEPVPPSHHVTSSLKSTCL----YIFTSGTTGLPKAAVISQFQVL-KGSFGLWAFGCTADDIVYITL 263
Cdd:PRK12583 172 GFLAWHELQARG--ETVSREALAERQASLDRDdpinIQYTSGTTGFPKGATLSHHNILnNGYFVAESLGLTEHDRLCVPV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 264 PLYHSSGALLGIGGCVELGATCVL-KKKFSASQFWNDCRKYNVTVFQ-----YIGELcrylcKQPQReGEKDH---RVRL 334
Cdd:PRK12583 250 PLYHCFGMVLANLGCMTVGACLVYpNEAFDPLATLQAVEEERCTALYgvptmFIAEL-----DHPQR-GNFDLsslRTGI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 335 AVGNGMSSDVWRQFLDrfgNIKMCEF---YGATEGN-ICFMNHTG-----KIGSVGRVnffynlLFSFELIKYDFQKDEP 405
Cdd:PRK12583 324 MAGAPCPIEVMRRVMD---EMHMAEVqiaYGMTETSpVSLQTTAAddlerRVETVGRT------QPHLEVKVVDPDGATV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 406 LRNEQGWcYCVRkgepGLLVSRvnkknpffGYTGSYKQTKSKLlfdvfkKGDVYFNTGDLMFQDHENFLYFWDRIGDTFR 485
Cdd:PRK12583 395 PRGEIGE-LCTR----GYSVMK--------GYWNNPEATAESI------DEDGWMHTGDLATMDEQGYVRIVGRSKDMII 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 486 WKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKME 565
Cdd:PRK12583 456 RGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY-GEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFP 534
|
570
....*....|....
gi 149064320 566 TTGTFKLKKLQLVE 579
Cdd:PRK12583 535 MTVTGKVQKFRMRE 548
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
80-577 |
1.15e-23 |
|
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: 104.10 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRfesllhcirtsePKamvvg 159
Cdd:cd05958 11 WTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLR------------PK----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 160 edllgSLEEILpslpkhirvwgmkDSVPEGIVSLKEKLSLASDepvppshhvtsslksTCLYIFTSGTTGLPKAAViSQF 239
Cdd:cd05958 74 -----ELAYIL-------------DKARITVALCAHALTASDD---------------ICILAFTSGTTGAPKATM-HFH 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 240 QVLKGSFGLWA---FGCTADDIVYITLPLYHSsgalLGIGGCV----ELGATCVLKKKFSASQFWNDCRKYNVTVFQYIG 312
Cdd:cd05958 120 RDPLASADRYAvnvLRLREDDRFVGSPPLAFT----FGLGGVLlfpfGVGASGVLLEEATPDLLLSAIARYKPTVLFTAP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 313 ELCRYLCKQPQREGEKDHRVRLAV--GNGMSSDVWRQFLDRFGnIKMCEFYGATEGNICFMNHTG---KIGSVGRVNFFY 387
Cdd:cd05958 196 TAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATG-IPIIDGIGSTEMFHIFISARPgdaRPGATGKPVPGY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 388 NLlfsfELIKyDFQKDEPlrneqgwcycvrKGEPGLLVSRvnkknpffGYTGsYKQTKSKLLFDVFKKGDVYfnTGDLMF 467
Cdd:cd05958 275 EA----KVVD-DEGNPVP------------DGTIGRLAVR--------GPTG-CRYLADKRQRTYVQGGWNI--TGDTYS 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 468 QDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGyEGKAGMTSIILKPNKSLD---LEKMYDQ 544
Cdd:cd05958 327 RDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDES-RGVVVKAFVVLRPGVIPGpvlARELQDH 405
|
490 500 510
....*....|....*....|....*....|...
gi 149064320 545 VVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd05958 406 AKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
63-586 |
1.66e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 104.12 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 63 HARRQPKK--AFIIYEGDVYTYEDVDKRSNRVAhALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLR 140
Cdd:PRK09088 4 HARLQPQRlaAVDLALGRRWTYAELDALVGRLA-AVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 141 FESLLHCIRTSEPkAMVVGEDLLGSLEEILPSLpkhirvwgmkdsvpEGIVSLKEKLSLASDEPVPPshhvtsslKSTCL 220
Cdd:PRK09088 83 ASELDALLQDAEP-RLLLGDDAVAAGRTDVEDL--------------AAFIASADALEPADTPSIPP--------ERVSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 221 YIFTSGTTGLPKAAVISQ--FQVLKGSFGLWAfGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWN 298
Cdd:PRK09088 140 ILFTSGTSGQPKGVMLSErnLQQTAHNFGVLG-RVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 299 DCRKYNVTVFQYIG--ELCRYLCKQPQREGEKDHRVRLAVGNG---MSSDVwRQFLDRfgNIKMCEFYGATEGNICF-MN 372
Cdd:PRK09088 219 RLGDPALGITHYFCvpQMAQAFRAQPGFDAAALRHLTALFTGGaphAAEDI-LGWLDD--GIPMVDGFGMSEAGTVFgMS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 373 H-----TGKIGSVGRVnffynlLFSFELIKYDFQKDEplrneqgwcycVRKGEPGLLVSRvnKKNPFFGYTGSYKQTKsk 447
Cdd:PRK09088 296 VdcdviRAKAGAAGIP------TPTVQTRVVDDQGND-----------CPAGVPGELLLR--GPNLSPGYWRRPQATA-- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 448 llfDVFKkGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTS 527
Cdd:PRK09088 355 ---RAFT-GDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQW-GEVGYLA 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 149064320 528 IILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVEEGFNPLK 586
Cdd:PRK09088 430 IVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGRK 488
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
55-580 |
1.85e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 104.44 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 55 TVLDKFLSHARRQPKKAFIIYE-GDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVA 133
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKG-IEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 134 FLNSNLRFESLLHCIRTSEPKAMVVG--------EDLLGSLEEILPSLPKHIRVWGMKDSVPEgiVSLKEklSLASDEPV 205
Cdd:PRK06087 103 PLLPSWREAELVWVLNKCQAKMFFAPtlfkqtrpVDLILPLQNQLPQLQQIVGVDKLAPATSS--LSLSQ--IIADYEPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 206 ppSHHVTSSLKSTCLYIFTSGTTGLPKAAVISQFQVLkgsFGLWAF----GCTADDIVYITLPLYHSSGALLGIGGCVEL 281
Cdd:PRK06087 179 --TTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNIL---ASERAYcarlNLTWQDVFMMPAPLGHATGFLHGVTAPFLI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 282 GATCVLKKKFSASQFWNDCRKYNVT----VFQYIGELCRYLCKQPQRegEKDHRVRLAVGNGMSSDVWRQFLDRfgNIKM 357
Cdd:PRK06087 254 GARSVLLDIFTPDACLALLEQQRCTcmlgATPFIYDLLNLLEKQPAD--LSALRFFLCGGTTIPKKVARECQQR--GIKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 358 CEFYGATEG----------NICFMNHTGKIGSVGrvnffynllfsFELIKYDFQKDEplrneqgwcycVRKGEPGLLVSR 427
Cdd:PRK06087 330 LSVYGSTESsphavvnlddPLSRFMHTDGYAAAG-----------VEIKVVDEARKT-----------LPPGCEGEEASR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 428 vnKKNPFFGYTGSYKQTkSKLLFDvfkkgDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQ 507
Cdd:PRK06087 388 --GPNVFMGYLDEPELT-ARALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIH 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149064320 508 EANVYGVPVPGYeGKAGMTSIILKPN-KSLDLEKMYDQVVTS-LPAYACPRFLRIQDKMETTGTFKLKKLQLVEE 580
Cdd:PRK06087 460 DACVVAMPDERL-GERSCAYVVLKAPhHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
62-577 |
3.49e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 100.47 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 62 SHARRQPKKAFIIYE--GDVYTYEDVDKRSNRVAHALLNhSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNL 139
Cdd:PRK13390 5 THAQIAPDRPAVIVAetGEQVSYRQLDDDSAALARVLYD-AGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 140 RFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLPKHIRVWGMKDsvpeGIVSLKEKLSLASdepvPPshhvTSSLKSTC 219
Cdd:PRK13390 84 TAPEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEID----GFGSFEAALAGAG----PR----LTEQPCGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 220 LYIFTSGTTGLPKA-----------AVISQFQVLKGSFglwaFGCTADDIVYITLPLYHSSgALLGIGGCVELGATCVLK 288
Cdd:PRK13390 152 VMLYSSGTTGFPKGiqpdlpgrdvdAPGDPIVAIARAF----YDISESDIYYSSAPIYHAA-PLRWCSMVHALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 289 KKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQpqregEKDHRVRLAVGN---------GMSSDVWRQFLDRFGNIkMCE 359
Cdd:PRK13390 227 KRFDAQATLGHVERYRITVTQMVPTMFVRLLKL-----DADVRTRYDVSSlravihaaaPCPVDVKHAMIDWLGPI-VYE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 360 FYGATEGNICFMNHTGKI----GSVGRvnffyNLLFSFELIKYDfQKDEPlRNEQGWCYCVRKGEPgllvsrvnkknpfF 435
Cdd:PRK13390 301 YYSSTEAHGMTFIDSPDWlahpGSVGR-----SVLGDLHICDDD-GNELP-AGRIGTVYFERDRLP-------------F 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 436 GYTGSYKQTKSKLlfdvFKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVP 515
Cdd:PRK13390 361 RYLNDPEKTAAAQ----HPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149064320 516 VP--GYEGKAGMTSII-LKPNKSLDLEkMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:PRK13390 437 DPemGEQVKAVIQLVEgIRGSDELARE-LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
55-580 |
7.00e-21 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 96.66 E-value: 7.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 55 TVLDKFLSHARRQPKK-AFIIYEGDV-----YTYEDVDKRSNRVAHALlnhSDL--KRGDVVALLMSNEPDFVHVWFGLA 126
Cdd:PRK13295 25 TINDDLDACVASCPDKtAVTAVRLGTgaprrFTYRELAALVDRVAVGL---ARLgvGRGDVVSCQLPNWWEFTVLYLACS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 127 KLGCVVAFLNSNLRFESLLHCIRTSEPKAMVV-----GEDLLGSLEEILPSLP--KHIRVWGmkdsvPEGIVSLKEKLSL 199
Cdd:PRK13295 102 RIGAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrGFDHAAMARRLRPELPalRHVVVVG-----GDGADSFEALLIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 200 ASDEPVPPSHHVTSSLK----STCLYIFTSGTTGLPKAavisqfqVLKGSFGLWA--------FGCTADDIVYITLPLYH 267
Cdd:PRK13295 177 PAWEQEPDAPAILARLRpgpdDVTQLIYTSGTTGEPKG-------VMHTANTLMAnivpyaerLGLGADDVILMASPMAH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 268 SSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVTvFQ-----YIGELCRYlckqpQREGEKDH---RVRLAVGNG 339
Cdd:PRK13295 250 QTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVT-FTmastpFLTDLTRA-----VKESGRPVsslRTFLCAGAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 340 MSSDVWRQFLDRFGnIKMCEFYGATEGNICFMNHTGK-----IGSVGRVnffynlLFSFELIKYDFQKDEplrneqgwcy 414
Cdd:PRK13295 324 IPGALVERARAALG-AKIVSAWGMTENGAVTLTKLDDpderaSTTDGCP------LPGVEVRVVDADGAP---------- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 415 cVRKGEPGLLVSRvnKKNPFFGYTGSYKQTKSkllfdvfkKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATT 494
Cdd:PRK13295 387 -LPAGQIGRLQVR--GCSNFGGYLKRPQLNGT--------DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 495 EVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSIILKPNKSLDLEKMYD----QVVTsLPAYacPRFLRIQDKMETTGTF 570
Cdd:PRK13295 456 EIEALLYRHPAIAQVAIVAYPDERL-GERACAFVVPRPGQSLDFEEMVEflkaQKVA-KQYI--PERLVVRDALPRTPSG 531
|
570
....*....|
gi 149064320 571 KLKKLQLVEE 580
Cdd:PRK13295 532 KIQKFRLREM 541
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
57-580 |
9.59e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 96.26 E-value: 9.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 57 LDKFLSH-ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHaLLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:PRK06710 26 LHKYVEQmASRYPEKKALHFLGKDITFSVFHDKVKRFAN-YLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 136 N---SNLRFESLLH--------CIRTSEPKAMVVGED------LLGSLEEILPsLPKHIRVWGMKDSVPEGIV------- 191
Cdd:PRK06710 105 NplyTERELEYQLHdsgakvilCLDLVFPRVTNVQSAtkiehvIVTRIADFLP-FPKNLLYPFVQKKQSNLVVkvseset 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 192 -----SLKEKLSLASDEPVPPSHHVTsslkstcLYIFTSGTTGLPKAAVISQFQVLKGSF-GL-WAFGCT-ADDIVYITL 263
Cdd:PRK06710 184 ihlwnSVEKEVNTGVEVPCDPENDLA-------LLQYTGGTTGFPKGVMLTHKNLVSNTLmGVqWLYNCKeGEEVVLGVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 264 PLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNG--MS 341
Cdd:PRK06710 257 PFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSapLP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 342 SDVWRQFlDRFGNIKMCEFYGATEGNicfmnhtgkigSVGRVNFFYNLLFSFEL-IKYDFQKDEPLRNEQGwcYCVRKGE 420
Cdd:PRK06710 337 VEVQEKF-ETVTGGKLVEGYGLTESS-----------PVTHSNFLWEKRVPGSIgVPWPDTEAMIMSLETG--EALPPGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 421 PGLLVsrVNKKNPFFGYTGSYKQTKSKLlfdvfkkGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVL 500
Cdd:PRK06710 403 IGEIV--VKGPQIMKGYWNKPEETAAVL-------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 501 GRLDFIQEANVYGVPVPgYEGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVEE 580
Cdd:PRK06710 474 YEHEKVQEVVTIGVPDP-YRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
60-577 |
1.08e-20 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 95.98 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 60 FLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSDLKRgDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNL 139
Cdd:PRK13382 49 FAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEP-RVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 140 RFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLPKHIRVWGMKDSVPEGIVslkEKLSLASDEPVPPSHHVTSSlkstc 219
Cdd:PRK13382 128 AGPALAEVVTREGVDTVIYDEEFSATVDRALADCPQATRIVAWTDEDHDLTV---EVLIAAHAGQRPEPTGRKGR----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 220 LYIFTSGTTGLPKAAVISQfqvlKGSFGL---------WafgcTADDIVYITLPLYHSSG------ALLgiggcveLGAT 284
Cdd:PRK13382 200 VILLTSGTTGTPKGARRSG----PGGIGTlkaildrtpW----RAEEPTVIVAPMFHAWGfsqlvlAAS-------LACT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 285 CVLKKKFS---ASQFWNDCRKYNVTV----FQYIGELC-----RYLCKQPqregekdhRVRLAVGNGMSSDVWRQFLDRF 352
Cdd:PRK13382 265 IVTRRRFDpeaTLDLIDRHRATGLAVvpvmFDRIMDLPaevrnRYSGRSL--------RFAAASGSRMRPDVVIAFMDQF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 353 GNIkMCEFYGATEGNICFM----------NHTGK--IGSVGRVnffynllfsfelIKYDFQKdeplrneqgwcycVRKGE 420
Cdd:PRK13382 337 GDV-IYNNYNATEAGMIATatpadlraapDTAGRpaEGTEIRI------------LDQDFRE-------------VPTGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 421 PGLLVSRVNKKnpFFGYT-GSYKQTKskllfdvfkkgDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANV 499
Cdd:PRK13382 391 VGTIFVRNDTQ--FDGYTsGSTKDFH-----------DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKT 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149064320 500 LGRLDFIQEANVYGVPVPGYeGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:PRK13382 458 LATHPDVAEAAVIGVDDEQY-GQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
68-376 |
1.71e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 95.34 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 68 PKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVafLNSNLRF--ESLL 145
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQG-LGPGDHVGIYARNRIEYVEAMLGAFKARAVP--VNVNYRYveDELR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 146 HCIRTSEPKAMVVGEDLLGSLEEILPSLPKhIRVW-----GMKDSVPEGIVSLKEKLSLASDEPVPPshhvTSSlkSTCL 220
Cdd:PRK07798 94 YLLDDSDAVALVYEREFAPRVAEVLPRLPK-LRTLvvvedGSGNDLLPGAVDYEDALAAGSPERDFG----ERS--PDDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 221 Y-IFTSGTTGLPKAAVISQFQVLKGSFGLWAFGC-----TADDIV-----------YITLPLYHSSGaLLGIGGCVELGA 283
Cdd:PRK07798 167 YlLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFATgepieDEEELAkraaagpgmrrFPAPPLMHGAG-QWAAFAALFSGQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 284 TCVL--KKKFSASQFWNDCRKYNVTVFQYIGE-LCRYLCKQPQREGEKDHRVRLAVGNG---MSSDVWRQFLDRFGNIKM 357
Cdd:PRK07798 246 TVVLlpDVRFDADEVWRTIEREKVNVITIVGDaMARPLLDALEARGPYDLSSLFAIASGgalFSPSVKEALLELLPNVVL 325
|
330
....*....|....*....
gi 149064320 358 CEFYGATEGNICFMNHTGK 376
Cdd:PRK07798 326 TDSIGSSETGFGGSGTVAK 344
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
77-577 |
1.75e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 95.33 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 77 GDVYTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAM 156
Cdd:PRK08751 48 GKTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 157 VVGEDLLGSLEEILPSLP-KHIRVWGMKDS-------------------VPE----GIVSLKEKLSLASDEPVPPSHHVT 212
Cdd:PRK08751 128 VVIDNFGTTVQQVIADTPvKQVITTGLGDMlgfpkaalvnfvvkyvkklVPEyrinGAIRFREALALGRKHSMPTLQIEP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 213 SSLkstCLYIFTSGTTGLPKAAVISQFQVLKG--SFGLWAFGC----TADDIVYITLPLYH------SSGALLGIGGCVE 280
Cdd:PRK08751 208 DDI---AFLQYTGGTTGVAKGAMLTHRNLVANmqQAHQWLAGTgkleEGCEVVITALPLYHifaltaNGLVFMKIGGCNH 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 281 LgatcvLKKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSsdVWRQFLDRFGNIK---M 357
Cdd:PRK08751 285 L-----ISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMA--VQRSVAERWKQVTgltL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 358 CEFYGATEGN-------ICFMNHTGKIGsvgrvnffYNLLFSFELIKYDFQKDEPLrneqgwcycvrkGEPGLLVSR--- 427
Cdd:PRK08751 358 VEAYGLTETSpaacinpLTLKEYNGSIG--------LPIPSTDACIKDDAGTVLAI------------GEIGELCIKgpq 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 428 VNKknpffGYTGSYKQTKSKLlfdvfkKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQ 507
Cdd:PRK08751 418 VMK-----GYWKRPEETAKVM------DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149064320 508 EANVYGVPvpgyEGKAG--MTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:PRK08751 487 EVAAVGVP----DEKSGeiVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
220-515 |
2.14e-20 |
|
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: 92.47 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 220 LYI-FTSGTTGLPKAAVISQfQVLKGSF--GLWAFGCTADDIVYITLPLYHSsGALLGIGGCVELGATCVLKKKFSASQF 296
Cdd:cd17633 3 FYIgFTSGTTGLPKAYYRSE-RSWIESFvcNEDLFNISGEDAILAPGPLSHS-LFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 297 WNDCRKYNVTVFQYIGELCRYLCkqpqREGEKDHRVR--LAVGNGMSSDVWRQFLDRFGNIKMCEFYGATEGNIC---FM 371
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALA----RTLEPESKIKsiFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFItynFN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 372 NHTGKIGSVGRVnfFYNLlfsfelikydfqkDEPLRNEQGwcycvrkGEPGLLvsRVNKKNPFFGYTGSYKQTKskllfd 451
Cdd:cd17633 157 QESRPPNSVGRP--FPNV-------------EIEIRNADG-------GEIGKI--FVKSEMVFSGYVRGGFSNP------ 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149064320 452 vfkkgDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVP 515
Cdd:cd17633 207 -----DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP 265
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
60-577 |
3.43e-20 |
|
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: 94.23 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 60 FLSHARRQPKKAFIIY---EGDV--YTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:cd12119 1 LLEHAARLHGDREIVSrthEGEVhrYTYAEVAERARRLANALRRLG-VKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 135 LNSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLPKHIRVWGMKDSVPEGIVSLKEKLS----LASDEPV---PP 207
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAyeelLAAESPEydwPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 208 SHHVTSSlkSTClyiFTSGTTGLPKAAVISQFQVLKGSFGLW---AFGCTADDIVYITLPLYHSSGALLGIgGCVELGAT 284
Cdd:cd12119 160 FDENTAA--AIC---YTSGTTGNPKGVVYSHRSLVLHAMAALltdGLGLSESDVVLPVVPMFHVNAWGLPY-AAAMVGAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 285 CVLKKKF----SASQFWndcRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAV--GNGMSSDVWRQFLDRFgnIKMC 358
Cdd:cd12119 234 LVLPGPYldpaSLAELI---EREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVigGSAVPRSLIEAFEERG--VRVI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 359 EFYGATEgnicfmnhTGKIGSVGRVNffynllfsFELIKYDFQKDEPLRNEQGW-CYCV-------------RKGEP-GL 423
Cdd:cd12119 309 HAWGMTE--------TSPLGTVARPP--------SEHSNLSEDEQLALRAKQGRpVPGVelrivdddgrelpWDGKAvGE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 424 LVSRvnkkNPFFgyTGSY-KQTKSKLLFDVfkkgDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGR 502
Cdd:cd12119 373 LQVR----GPWV--TKSYyKNDEESEALTE----DGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMA 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149064320 503 LDFIQEANVYGVPVPGYeGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd12119 443 HPAVAEAAVIGVPHPKW-GERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
55-580 |
3.94e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 94.35 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 55 TVLDKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:PRK08974 24 SLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 135 LNSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLP-KHIRVWGMKD--SVPEG-----IVSLKEKLslasdepVP 206
Cdd:PRK08974 104 VNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPvKHVILTRMGDqlSTAKGtlvnfVVKYIKRL-------VP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 207 PSH------------------HVTSSLKSTCLYI--FTSGTTGLPKAAVISQFQVLKGSF-GLWAFGCTADD---IVYIT 262
Cdd:PRK08974 177 KYHlpdaisfrsalhkgrrmqYVKPELVPEDLAFlqYTGGTTGVAKGAMLTHRNMLANLEqAKAAYGPLLHPgkeLVVTA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 263 LPLYH----SSGALLGIggcvELGATCVL-KKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVG 337
Cdd:PRK08974 257 LPLYHifalTVNCLLFI----ELGGQNLLiTNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 338 NGMSsdVWRQFLDRFGNIKMC---EFYGATEGN----ICFMNHTGKIGSVGrvnffynllfsFELIKYDFQkdepLRNEQ 410
Cdd:PRK08974 333 GGMA--VQQAVAERWVKLTGQyllEGYGLTECSplvsVNPYDLDYYSGSIG-----------LPVPSTEIK----LVDDD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 411 GwcYCVRKGEPGLLVSR---VNKknpffGYTGSYKQTKskllfDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWK 487
Cdd:PRK08974 396 G--NEVPPGEPGELWVKgpqVML-----GYWQRPEATD-----EVIKDG--WLATGDIAVMDEEGFLRIVDRKKDMILVS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 488 GENVATTEVANVLGRLDFIQEANVYGVP--VPGYEGKAgmtsIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKME 565
Cdd:PRK08974 462 GFNVYPNEIEDVVMLHPKVLEVAAVGVPseVSGEAVKI----FVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELP 537
|
570
....*....|....*
gi 149064320 566 TTGTFKLKKLQLVEE 580
Cdd:PRK08974 538 KSNVGKILRRELRDE 552
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
53-579 |
4.25e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 94.04 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 53 LVTVLDkflSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAhALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVV 132
Cdd:PRK06164 12 LASLLD---AHARARPDAVALIDEDRPLSRAELRALVDRLA-AWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 133 AFLNSNLRFESLLHCIRTSEPKAMVV-----GEDLLGSLEEI----LPSLPKHIRVWGMKDSVPEGIVSLKEKLSLASDE 203
Cdd:PRK06164 88 IAVNTRYRSHEVAHILGRGRARWLVVwpgfkGIDFAAILAAVppdaLPPLRAIAVVDDAADATPAPAPGARVQLFALPDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 204 PVPPSHHVTSSLKSTCLYIF-TSGTTGLPKAAVISQFQVLK-GSFGLWAFGCTADDIVYITLPL---YHSSGALLGIGGc 278
Cdd:PRK06164 168 APPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRhARAIARAYGYDPGAVLLAALPFcgvFGFSTLLGALAG- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 279 velGATCVLKKKFSASQfwndcrkynvTVFQYigelcrylckqpqregeKDHRVRLAVGNgmsSDVWRQFLDRFGN---- 354
Cdd:PRK06164 247 ---GAPLVCEPVFDAAR----------TARAL-----------------RRHRVTHTFGN---DEMLRRILDTAGEradf 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 355 --IKMCEFYGategnicFMNHTGKIGSVGRVNFF--YNLLFSFELIK----YDFQKDEPLRNEQGWCYC-----VR---- 417
Cdd:PRK06164 294 psARLFGFAS-------FAPALGELAALARARGVplTGLYGSSEVQAlvalQPATDPVSVRIEGGGRPAspearVRardp 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 418 -------KGEPGLLvsRVNKKNPFFGYTGSYKQTKSKLlfdvfkKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGEN 490
Cdd:PRK06164 367 qdgallpDGESGEI--EIRAPSLMRGYLDNPDATARAL------TDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 491 VATTEVANVLGRLDFIQEANVYGVPVPGYEGKAGMtsIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETT--- 567
Cdd:PRK06164 439 VNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAF--VIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesa 516
|
570
....*....|..
gi 149064320 568 GTFKLKKLQLVE 579
Cdd:PRK06164 517 NGAKIQKHRLRE 528
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
88-562 |
4.78e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 93.27 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 88 RSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGC---VVAFLNSNLRFESLLHCIRTSEPKAMVVGEDLLG 164
Cdd:cd05922 2 GVSAAASALLEAG-GVRGERVVLILPNRFTYIELSFAVAYAGGrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 165 S-LEEILPSLPKHIRVWGMkdsvpEGIVSLKeklslASDEPVPPSHhvtsslKSTCLYIFTSGTTGLPKAAVISQFQVLK 243
Cdd:cd05922 81 DrLRDALPASPDPGTVLDA-----DGIRAAR-----ASAPAHEVSH------EDLALLLYTSGSTGSPKLVRLSHQNLLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 244 GSFGLWAF-GCTADDIVYITLPLYHSSG-ALLGIGgcVELGATCVLKKKFSASQ-FWNDCRKYNVTVFQ---YIGELCRY 317
Cdd:cd05922 145 NARSIAEYlGITADDRALTVLPLSYDYGlSVLNTH--LLRGATLVLTNDGVLDDaFWEDLREHGATGLAgvpSTYAMLTR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 318 LCKQPqrEGEKDHRVRLAVGNGMSSDVWRQFLDRFGNIKMCEFYGATEgniCFMNHT--------GKIGSVGR----VNF 385
Cdd:cd05922 223 LGFDP--AKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTE---ATRRMTylpperilEKPGSIGLaipgGEF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 386 FynllfsfelikydfqkdepLRNEQGWCYCVrkGEPGLLVSRVNkknpfFGYTGsYKQTKSKLLFDVFKKGDVYfnTGDL 465
Cdd:cd05922 298 E-------------------ILDDDGTPTPP--GEPGEIVHRGP-----NVMKG-YWNDPPYRRKEGRGGGVLH--TGDL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 466 MFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYEGKAgmtSIILKPNKsLDLEKMYDQV 545
Cdd:cd05922 349 ARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLA---LFVTAPDK-IDPKDVLRSL 424
|
490
....*....|....*..
gi 149064320 546 VTSLPAYACPRFLRIQD 562
Cdd:cd05922 425 AERLPPYKVPATVRVVD 441
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
63-582 |
6.06e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 93.41 E-value: 6.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 63 HARRQPKKAFIIYEGD--VYTYEDVDKRSNRVAhALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLR 140
Cdd:PRK05852 25 AATRLPEAPALVVTADriAISYRDLARLVDDLA-GQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 141 FESllHCIRTSEPKAMVVGEDLLGSLEEILPSlpkhIRVWGMKDSVPEGIVSLKEKLSLASDEPVPPSHHVTSSL---KS 217
Cdd:PRK05852 104 IAE--QRVRSQAAGARVVLIDADGPHDRAEPT----TRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEglrPD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 218 TCLYIFTSGTTGLPKAAVISQFQVLKGSFGLWA-FGCTADDIVYITLPLYHSSG------ALLGIGGCVELGAtcvlKKK 290
Cdd:PRK05852 178 DAMIMFTGGTTGLPKMVPWTHANIASSVRAIITgYRLSPRDATVAVMPLYHGHGliaallATLASGGAVLLPA----RGR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 291 FSASQFWNDCRKYNVTVFQYIGELCRYLCKQP--QREGEKDHRVRL--AVGNGMSSDVWRQFLDRFGNIKMCEFyGATE- 365
Cdd:PRK05852 254 FSAHTFWDDIKAVGATWYTAVPTIHQILLERAatEPSGRKPAALRFirSCSAPLTAETAQALQTEFAAPVVCAF-GMTEa 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 366 ----------GNICFMNHTGKIGSVGRvnffyNLLFSFELIKYDFQKDEPLRNEQGWcycVRkgepGLLVSRvnkknpff 435
Cdd:PRK05852 333 thqvtttqieGIGQTENPVVSTGLVGR-----STGAQIRIVGSDGLPLPAGAVGEVW---LR----GTTVVR-------- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 436 GYTGSYKQTKSKllfdvFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVP 515
Cdd:PRK05852 393 GYLGDPTITAAN-----FTDG--WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVP 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149064320 516 VPGYeGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKlQLVEEGF 582
Cdd:PRK05852 466 DQLY-GEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR-RAVAEQF 530
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
54-580 |
1.02e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 92.80 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 54 VTVLDKFLSH-ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLnHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVV 132
Cdd:PRK07470 6 VMNLAHFLRQaARRFPDRIALVWGDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 133 AFLNSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLPKHIRVWGMKDsvPEGIVSLKEKLSLASDEPVPPshhVT 212
Cdd:PRK07470 85 VPTNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGG--ARAGLDYEALVARHLGARVAN---AA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 213 SSLKSTCLYIFTSGTTGLPKAAVISQFQVlkgsfglwAF-----------GCTADDIVYITLPLYHSSG--ALLGiggcV 279
Cdd:PRK07470 160 VDHDDPCWFFFTSGTTGRPKAAVLTHGQM--------AFvitnhladlmpGTTEQDASLVVAPLSHGAGihQLCQ----V 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 280 ELGATCVL--KKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGeKDH---RVRLAVGNGMSSDVWRQFLDRFGN 354
Cdd:PRK07470 228 ARGAATVLlpSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDR-YDHsslRYVIYAGAPMYRADQKRALAKLGK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 355 IkMCEFYGATE--GNICFMN---H------TGKIGSVGRVNffynllFSFELIKYDFQKDEPLRNEQGWCyCVRkgepGL 423
Cdd:PRK07470 307 V-LVQYFGLGEvtGNITVLPpalHdaedgpDARIGTCGFER------TGMEVQIQDDEGRELPPGETGEI-CVI----GP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 424 LVsrvnkknpFFGYTGSYKQTKSkllfdVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRL 503
Cdd:PRK07470 375 AV--------FAGYYNNPEANAK-----AFRDG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTH 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149064320 504 DFIQEANVYGVPVPGYeGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVEE 580
Cdd:PRK07470 440 PAVSEVAVLGVPDPVW-GEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
55-556 |
3.75e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 91.21 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 55 TVLDKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAhALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAA-AGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 135 LNSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEE--------------ILPSLPKHIRvWGMKDSVPEgIVSLKEKLSLA 200
Cdd:PRK05605 112 HNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERlrrttpletivsvnMIAAMPLLQR-LALRLPIPA-LRKARAALTGP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 201 SDEPVPPSHHVTSSL--------------KSTCLYIFTSGTTGLPKAAVIS----QFQVLKGSfgLWAFGC-TADDIVYI 261
Cdd:PRK05605 190 APGTVPWETLVDAAIggdgsdvshprptpDDVALILYTSGTTGKPKGAQLThrnlFANAAQGK--AWVPGLgDGPERVLA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 262 TLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMS 341
Cdd:PRK05605 268 ALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 342 --SDVWRQFLDRFGNiKMCEFYGATE------GNIcfMNHTGKIGSVGrvnffynLLFSFELIKY----DFQKDEPlrne 409
Cdd:PRK05605 348 lpVSTVELWEKLTGG-LLVEGYGLTEtspiivGNP--MSDDRRPGYVG-------VPFPDTEVRIvdpeDPDETMP---- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 410 qgwcycvrKGEPG-LLVsrvnkKNP--FFGYTGSYKQTKSKLLfdvfkkgDVYFNTGDLMFQDHENFLYFWDRIGDTFRW 486
Cdd:PRK05605 414 --------DGEEGeLLV-----RGPqvFKGYWNRPEETAKSFL-------DGWFRTGDVVVMEEDGFIRIVDRIKELIIT 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149064320 487 KGENVATTEVANVLGRLDFIQEANVYGVPVP-GYEGKAGmtSIILKPNKSLDLEKMYDQVVTSLPAYACPR 556
Cdd:PRK05605 474 GGFNVYPAEVEEVLREHPGVEDAAVVGLPREdGSEEVVA--AVVLEPGAALDPEGLRAYCREHLTRYKVPR 542
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
60-577 |
5.44e-19 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 90.85 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 60 FLSHARR-QPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNhSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSN 138
Cdd:PLN03102 19 FLKRASEcYPNRTSIIYGKTRFTWPQTYDRCCRLAASLIS-LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 139 LRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLPK-----HIRVWGMKDSVPEGIVSLKE---KLSLASDEPVPPS-- 208
Cdd:PLN03102 98 LDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSedsnlNLPVIFIHEIDFPKRPSSEEldyECLIQRGEPTPSLva 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 209 -------HHVTSSLKstclyiFTSGTTGLPKAAVISQ----FQVLKGSFGlWAFGCTAddiVYI-TLPLYHSSGALLGIG 276
Cdd:PLN03102 178 rmfriqdEHDPISLN------YTSGTTADPKGVVISHrgayLSTLSAIIG-WEMGTCP---VYLwTLPMFHCNGWTFTWG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 277 GCVElGATCVLKKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQRE-GEKDHRVRLAVGNGMSSDVWRQFLDRFGnI 355
Cdd:PLN03102 248 TAAR-GGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDlSPRSGPVHVLTGGSPPPAALVKKVQRLG-F 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 356 KMCEFYGATEGnicfmnhTGKIgsvgrvnffynlLFSfelikyDFQKD-EPLRNEQGWCYCVRKGEPGLLVSRVNKKN-- 432
Cdd:PLN03102 326 QVMHAYGLTEA-------TGPV------------LFC------EWQDEwNRLPENQQMELKARQGVSILGLADVDVKNke 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 433 -----PFFGYT-------------GSYKQTKSKllFDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATT 494
Cdd:PLN03102 381 tqesvPRDGKTmgeivikgssimkGYLKNPKAT--SEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 495 EVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSIILKPNKSlDLEKMYDQVVTS-----------LPAYACPRFLRIQDK 563
Cdd:PLN03102 457 EVENVLYKYPKVLETAVVAMPHPTW-GETPCAFVVLEKGET-TKEDRVDKLVTRerdlieycrenLPHFMCPRKVVFLQE 534
|
570
....*....|....
gi 149064320 564 METTGTFKLKKLQL 577
Cdd:PLN03102 535 LPKNGNGKILKPKL 548
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
80-577 |
6.60e-19 |
|
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: 90.22 E-value: 6.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVG 159
Cdd:cd05928 42 WSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 160 EDLLGSLEEIL---PSLPKHIRVwgmKDSVPEGIVSLKEKLSLASDEpvppsHHV--TSSLKSTCLYiFTSGTTGLPKAA 234
Cdd:cd05928 122 DELAPEVDSVAsecPSLKTKLLV---SEKSRDGWLNFKELLNEASTE-----HHCveTGSQEPMAIY-FTSGTTGSPKMA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 235 VISQfqvlkGSFGLWAFGC-------TADDIVYITlplyHSSGALLGIGGCV----ELGAtCV---LKKKFSASQFWNDC 300
Cdd:cd05928 193 EHSH-----SSLGLGLKVNgrywldlTASDIMWNT----SDTGWIKSAWSSLfepwIQGA-CVfvhHLPRFDPLVILKTL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 301 RKYNVTVFQYIGELCRYLCKQP-QREGEKDHRVRLAVGNGMSSDVWRQFLDRFGnIKMCEFYGATE-GNICfMNHTG--- 375
Cdd:cd05928 263 SSYPITTFCGAPTVYRMLVQQDlSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTG-LDIYEGYGQTEtGLIC-ANFKGmki 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 376 KIGSVGRVNffynllfsfelIKYDFQkdepLRNEQGwcYCVRKGEPGLLVSRVNKKNP---FFGYTGSYKQTKSKLlfdv 452
Cdd:cd05928 341 KPGSMGKAS-----------PPYDVQ----IIDDNG--NVLPPGTEGDIGIRVKPIRPfglFSGYVDNPEKTAATI---- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 453 fkKGDVYfNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgYEGKAGMTSIILKP 532
Cdd:cd05928 400 --RGDFY-LTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-IRGEVVKAFVVLAP 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 149064320 533 N-KSLDLEKM----YDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd05928 476 QfLSHDPEQLtkelQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
54-365 |
1.07e-18 |
|
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: 90.69 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 54 VTVLDKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHsDLKRGDVVALLMSNEPDFVHVWFGLAKLGCvvA 133
Cdd:COG1020 476 ATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRAL-GVGPGDLVGVCLERSLEMVVALLAVLKAGA--A 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 134 F--LNSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEilpslpkhirvwgmkDSVPegIVSLkEKLSLASDEPVPPSHHV 211
Cdd:COG1020 553 YvpLDPAYPAERLAYMLEDAGARLVLTQSALAARLPE---------------LGVP--VLAL-DALALAAEPATNPPVPV 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 212 TSSlkSTClY-IFTSGTTGLPKAAVISQFQVLkgSFGLW---AFGCTADDIVyitlpLYHSS-----------GALLGig 276
Cdd:COG1020 615 TPD--DLA-YvIYTSGSTGRPKGVMVEHRALV--NLLAWmqrRYGLGPGDRV-----LQFASlsfdasvweifGALLS-- 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 277 gcvelGATCVL---KKKFSASQFWNDCRKYNVTVFQ----YIGELCRYLCKQPqregekdHRVRLAV--GNGMSSDVWRQ 347
Cdd:COG1020 683 -----GATLVLappEARRDPAALAELLARHRVTVLNltpsLLRALLDAAPEAL-------PSLRLVLvgGEALPPELVRR 750
|
330
....*....|....*...
gi 149064320 348 FLDRFGNIKMCEFYGATE 365
Cdd:COG1020 751 WRARLPGARLVNLYGPTE 768
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
80-572 |
1.27e-18 |
|
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: 88.71 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAhALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVG 159
Cdd:cd05969 1 YTFAQLKVLSARFA-NVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 160 EdllgsleeilpslpkhirvwgmkdsvpegivSLKEKLslasdEPVPPShhvtsslkstcLYIFTSGTTGLPKA------ 233
Cdd:cd05969 80 E-------------------------------ELYERT-----DPEDPT-----------LLHYTSGTTGTPKGvlhvhd 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 234 AVISQFQVLKGSFGLWA---FGCTADDiVYITLPLYHSSGALLGiggcvelGATCVL-KKKFSASQFWNDCRKYNVTVFQ 309
Cdd:cd05969 113 AMIFYYFTGKYVLDLHPddiYWCTADP-GWVTGTVYGIWAPWLN-------GVTNVVyEGRFDAESWYGIIERVKVTVWY 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 310 YIGELCRYLCK---QPQREGEKDH-RVRLAVGNGMSSDVWRQFLDRFgNIKMCEFYGATE-GNICFMNHTG---KIGSVG 381
Cdd:cd05969 185 TAPTAIRMLMKegdELARKYDLSSlRFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTEtGSIMIANYPCmpiKPGSMG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 382 RVnffynlLFSFELIKYDFQKDEplrneqgwcycVRKGEPGLLVSRVNKKNPFFGYTGSYKQTKSKllfdvFKKGdvYFN 461
Cdd:cd05969 264 KP------LPGVKAAVVDENGNE-----------LPPGTKGILALKPGWPSMFRGIWNDEERYKNS-----FIDG--WYL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 462 TGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVP--GYEGKAgmtSIILKPNKSLDlE 539
Cdd:cd05969 320 TGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPlrGEIIKA---FISLKEGFEPS-D 395
|
490 500 510
....*....|....*....|....*....|....*..
gi 149064320 540 KMYDQVVT----SLPAYACPRFLRIQDKMETTGTFKL 572
Cdd:cd05969 396 ELKEEIINfvrqKLGAHVAPREIEFVDNLPKTRSGKI 432
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
79-579 |
1.78e-18 |
|
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: 88.21 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 79 VYTYEDVDKRSNRVAHaLLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVV 158
Cdd:cd05903 1 RLTYSELDTRADRLAA-GLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 159 gedllgsleeilpslpkhIRVWGMKDSVPEGivslkeklslasdepvppshhvtsslKSTCLYIFTSGTTGLPKAAVISQ 238
Cdd:cd05903 80 ------------------PERFRQFDPAAMP--------------------------DAVALLLFTSGTTGEPKGVMHSH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 239 FQVLKGSFGLWA-FGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWNDCRKYNVTVFQYIGELCRY 317
Cdd:cd05903 116 NTLSASIRQYAErLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 318 LCKQPQREGEKDHRVRLAVGNGMS--SDVWRQFLDRFGnIKMCEFYGATEgnicfmnHTGKIGSVgrvnffynllfsfel 395
Cdd:cd05903 196 LLNAVEEAGEPLSRLRTFVCGGATvpRSLARRAAELLG-AKVCSAYGSTE-------CPGAVTSI--------------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 396 ikydfqkdEPLRNEQGWC------------------YCVRKGEPGLLVSRvnKKNPFFGYTgsykqTKSKLLFDVFKKGd 457
Cdd:cd05903 253 --------TPAPEDRRLYtdgrplpgveikvvddtgATLAPGVEGELLSR--GPSVFLGYL-----DRPDLTADAAPEG- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 458 vYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPvPGYEGKAGMTSIILKPNKSLD 537
Cdd:cd05903 317 -WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALP-DERLGERACAVVVTKSGALLT 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 149064320 538 LEKM---YDQVVTSLPAYacPRFLRIQDKMETTGTFKLKKLQLVE 579
Cdd:cd05903 395 FDELvayLDRQGVAKQYW--PERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
80-545 |
5.06e-18 |
|
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: 87.58 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVV- 158
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYG-LKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCs 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 159 --GEDLLGSLEEILPSLPKHIrvwgmkdsVPEGIVSLKEKLSLAS--DEPVPPSHHVTSSL-------KSTCLYIFTSGT 227
Cdd:cd17642 124 kkGLQKVLNVQKKLKIIKTII--------ILDSKEDYKGYQCLYTfiTQNLPPGFNEYDFKppsfdrdEQVALIMNSSGS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 228 TGLPKAAVISQFQVL-------KGSFGLWAFGCTAddiVYITLPLYHSSGALLGIGGCVeLGATCVLKKKFSASQFWNDC 300
Cdd:cd17642 196 TGLPKGVQLTHKNIVarfsharDPIFGNQIIPDTA---ILTVIPFHHGFGMFTTLGYLI-CGFRVVLMYKFEEELFLRSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 301 RKYNVTVFQYIGELCRYLCKQPQREG-EKDHRVRLAVGNG-MSSDVWRQFLDRFGNIKMCEFYGATEGN--ICFMNHTG- 375
Cdd:cd17642 272 QDYKVQSALLVPTLFAFFAKSTLVDKyDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETTsaILITPEGDd 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 376 KIGSVGRVNFFynllFSFELIKYDFQKDEPLrNEQGWcYCVrKGePGLLVsrvnkknpffGYTGSYKQTKSklLFDvfKK 455
Cdd:cd17642 352 KPGAVGKVVPF----FYAKVVDLDTGKTLGP-NERGE-LCV-KG-PMIMK----------GYVNNPEATKA--LID--KD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 456 GdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGyEGKAGMTSIILKPNKS 535
Cdd:cd17642 410 G--WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDED-AGELPAAVVVLEAGKT 486
|
490
....*....|
gi 149064320 536 LDLEKMYDQV 545
Cdd:cd17642 487 MTEKEVMDYV 496
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
68-556 |
1.06e-17 |
|
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: 86.20 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 68 PKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHC 147
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALG-ISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 148 IRTSEPKAMVVGEDLLGslEEILPSlpkhirvwGMKDSVPEGIVSLKEKLSLAsdepvppshhvtsslkstclyiFTSGT 227
Cdd:cd12118 97 LRHSEAKVLFVDREFEY--EDLLAE--------GDPDFEWIPPADEWDPIALN----------------------YTSGT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 228 TGLPKAAVISQfqvlKGSFgLWAFGCTA-----DDIVYI-TLPLYHSSGaLLGIGGCVELGATCVLKKKFSASQFWNDCR 301
Cdd:cd12118 145 TGRPKGVVYHH----RGAY-LNALANILewemkQHPVYLwTLPMFHCNG-WCFPWTVAAVGGTNVCLRKVDAKAIYDLIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 302 KYNVTVFQYIGELCRYLCKQPQREGEK-DHRVRLAVG---------NGMSSdvwrqfldrfGNIKMCEFYGATE----GN 367
Cdd:cd12118 219 KHKVTHFCGAPTVLNMLANAPPSDARPlPHRVHVMTAgapppaavlAKMEE----------LGFDVTHVYGLTEtygpAT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 368 ICFMN-------HTGKIGSVGRVNFFYNLLFSFELIKYDFQKDEPlrneqgwcycvRKGEP-GLLVSRVNkkNPFFGYTG 439
Cdd:cd12118 289 VCAWKpewdelpTEERARLKARQGVRYVGLEEVDVLDPETMKPVP-----------RDGKTiGEIVFRGN--IVMKGYLK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 440 SYKQTKskllfDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgy 519
Cdd:cd12118 356 NPEATA-----EAFRGG--WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDE-- 426
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 149064320 520 egKAGMTS---IILKPNKSLDLEKMYDQVVTSLPAYACPR 556
Cdd:cd12118 427 --KWGEVPcafVELKEGAKVTEEEIIAFCREHLAGFMVPK 464
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
79-578 |
1.28e-17 |
|
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: 85.56 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 79 VYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVV 158
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIG-LEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 159 GEdllgsleeilpslpkhirvwgmkdsvpegivslkeklslaSDEPVppshhvtsslkstcLYIFTSGTTGLPKAAVISQ 238
Cdd:cd05971 85 DG----------------------------------------SDDPA--------------LIIYTSGTTGPPKGALHAH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 239 fQVLKGSFGlwafgctaddIVYITLPLYHSSGALL-------GIGGCVEL-------GATCVLKK--KFSASQFWNDCRK 302
Cdd:cd05971 111 -RVLLGHLP----------GVQFPFNLFPRDGDLYwtpadwaWIGGLLDVllpslyfGVPVLAHRmtKFDPKAALDLMSR 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 303 YNVT-VFqyigeLCRYLCKQPQREGE--KDHRVRL-AVGNGMSSD-----VWRQflDRFGnIKMCEFYGATEGNICFMNH 373
Cdd:cd05971 180 YGVTtAF-----LPPTALKMMRQQGEqlKHAQVKLrAIATGGESLgeellGWAR--EQFG-VEVNEFYGQTECNLVIGNC 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 374 TG----KIGSVGRVNFFYNLlfsfELIKydfQKDEPL-RNEQGWCyCVRKGEPgllvsrvnkkNPFFGYTGSYKQTKSKL 448
Cdd:cd05971 252 SAlfpiKPGSMGKPIPGHRV----AIVD---DNGTPLpPGEVGEI-AVELPDP----------VAFLGYWNNPSATEKKM 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 449 lfdvfkKGDvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVP--GYEGKAgmt 526
Cdd:cd05971 314 ------AGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPirGEIVKA--- 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 149064320 527 SIILKPNKSLDLE---KMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLV 578
Cdd:cd05971 384 FVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
81-369 |
6.90e-17 |
|
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: 83.08 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 81 TYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNL---RFESLLhciRTSEPKAMV 157
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYpaeRLAFIL---EDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 158 VGEDLLGSLEEIlpslpkhirvwgmkdsVPEGIVSLKEKLSLASDEPVPPSHHVTSSLKSTCLYIFTSGTTGLPKAAVIS 237
Cdd:TIGR01733 78 TDSALASRLAGL----------------VLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 238 QFQVLkgSFGLWA---FGCTADDIVyitlpLYHSS-----------GALLGiGGCVELGATCVLKKKFSASQFWNdcRKY 303
Cdd:TIGR01733 142 HRSLV--NLLAWLarrYGLDPDDRV-----LQFASlsfdasveeifGALLA-GATLVVPPEDEERDDAALLAALI--AEH 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 304 NVTVFQ---YIGELCrylckQPQREGEKDH-RVRLAVGNGMSSDVWRQFLDRFGNIKMCEFYGATEGNIC 369
Cdd:TIGR01733 212 PVTVLNltpSLLALL-----AAALPPALASlRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVW 276
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
64-515 |
9.79e-17 |
|
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: 83.33 E-value: 9.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKK-AFIIYEGDV-YTYEDVDKRSNRVAhALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRF 141
Cdd:cd05923 11 ASRAPDAcAIADPARGLrLTYSELRARIEAVA-ARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 142 ESLLHCIRTSEPKAMVVGEDLLGSLEEILpslpKHIRVWGMKDSVPEGIvslkekLSLASDEPVPPSHHVtsslKSTCLY 221
Cdd:cd05923 90 AELAELIERGEMTAAVIAVDAQVMDAIFQ----SGVRVLALSDLVGLGE------PESAGPLIEDPPREP----EQPAFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 222 IFTSGTTGLPKAAVISQ--------FQVLKGSFglwAFGctADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSA 293
Cdd:cd05923 156 FYTSGTTGLPKGAVIPQraaesrvlFMSTQAGL---RHG--RHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 294 SQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAV--GNGMSSDVwrqfLDRFGNIKMCEF---YGATEGNI 368
Cdd:cd05923 231 ADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTfaGATMPDAV----LERVNQHLPGEKvniYGTTEAMN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 369 CFMNHTGKIGSVGRVNFFYNLLFsfelikydfqkdepLRNEQGWCYCVRKGEPGLLVSRVNKKNPFFGYTGSYKQTKSKL 448
Cdd:cd05923 307 SLYMRDARTGTEMRPGFFSEVRI--------------VRIGGSPDEALANGEEGELIVAAAADAAFTGYLNQPEATAKKL 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149064320 449 LfdvfkkgDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVP 515
Cdd:cd05923 373 Q-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVA 432
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
57-572 |
1.40e-16 |
|
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: 83.40 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 57 LDKflsHARRQPKKAFIIYEGD------VYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGC 130
Cdd:cd17634 59 LDR---HLRENGDRTAIIYEGDdtsqsrTISYRELHREVCRFAGTLLDLG-VKKGDRVAIYMPMIPEAAVAMLACARIGA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 131 VVAFLNSNLRFESLLHCIRTSEPKAMVVGEDLL--GSLEEILPSLPKHIRVWGMkdSVPEGIVSLKEKLSLASD------ 202
Cdd:cd17634 135 VHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVraGRSVPLKKNVDDALNPNVT--SVEHVIVLKRTGSDIDWQegrdlw 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 203 -----EPVPPSHH-VTSSLKSTCLYIFTSGTTGLPKAAVISQfqvlkGSFGLWA-------FGCTADDIVYITLPLYHSS 269
Cdd:cd17634 213 wrdliAKASPEHQpEAMNAEDPLFILYTSGTTGKPKGVLHTT-----GGYLVYAattmkyvFDYGPGDIYWCTADVGWVT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 270 GALLGIGGCVELGATCVLKKKF----SASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRL----AVGNGMS 341
Cdd:cd17634 288 GHSYLLYGPLACGATTLLYEGVpnwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLrilgSVGEPIN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 342 SDVWRQFLDRFGNIK--MCEFYGATE-GNICFMNHTGKIGSVGRVNFfyNLLFSFELIKYDfqkdeplrnEQGwcycvrK 418
Cdd:cd17634 368 PEAYEWYWKKIGKEKcpVVDTWWQTEtGGFMITPLPGAIELKAGSAT--RPVFGVQPAVVD---------NEG------H 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 419 GEPGLLVSRVNKKNPFFGYTGSYKQTKSKLLFDVFKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVAN 498
Cdd:cd17634 431 PQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIES 510
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149064320 499 VLGRLDFIQEANVYGVPVPgYEGKAGMTSIILKPNKSlDLEKMYDQVVT----SLPAYACPRFLRIQDKMETTGTFKL 572
Cdd:cd17634 511 VLVAHPKVAEAAVVGIPHA-IKGQAPYAYVVLNHGVE-PSPELYAELRNwvrkEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
64-577 |
1.81e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 83.08 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKKAFIIY--------EGDVYTYEDVDKRSNRVAHALlnHS-DLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAf 134
Cdd:PRK07529 35 AARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLL--HSlGVGPGDVVAFLLPNLPETHFALWGGEAAGIANP- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 135 LNSNLRFESLLHCIRTSEPKAMVV-----GEDLLGSLEEILPSLP--KHIRVWGMKDSVP---------------EGIVS 192
Cdd:PRK07529 112 INPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEVLAALPelRTVVEVDLARYLPgpkrlavplirrkahARILD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 193 LKEKLSLASDE----PVPPSHHVTSSlkstclYIFTSGTTGLPKAAVISQF-QVLKGSFGLWAFGCTADDIVYITLPLYH 267
Cdd:PRK07529 192 FDAELARQPGDrlfsGRPIGPDDVAA------YFHTGGTTGMPKLAQHTHGnEVANAWLGALLLGLGPGDTVFCGLPLFH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 268 SSGALLGIGGCVELGATCVL------KKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPqREGEKDHRVRLAVGNG-- 339
Cdd:PRK07529 266 VNALLVTGLAPLARGAHVVLatpqgyRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVP-VDGHDISSLRYALCGAap 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 340 MSSDVWRQFLDRFGnIKMCEFYGATEGN-ICFMN---HTGKIGSVGrvnffynLLFSFELIKYdFQKDEPLRNEQGwcyC 415
Cdd:PRK07529 345 LPVEVFRRFEAATG-VRIVEGYGLTEATcVSSVNppdGERRIGSVG-------LRLPYQRVRV-VILDDAGRYLRD---C 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 416 VrKGEPGLLVsrVNKKNPFFGYTgsyKQTKSKLLFdvfkKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTE 495
Cdd:PRK07529 413 A-VDEVGVLC--IAGPNVFSGYL---EAAHNKGLW----LEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 496 VANVLGRLDFIQEANVYGVPvPGYEGKAGMTSIILKPNKSLDLEKMYDQVVTSLP--AyACPRFLRIQDKMETTGTFKLK 573
Cdd:PRK07529 483 IEEALLRHPAVALAAAVGRP-DAHAGELPVAYVQLKPGASATEAELLAFARDHIAerA-AVPKHVRILDALPKTAVGKIF 560
|
....
gi 149064320 574 KLQL 577
Cdd:PRK07529 561 KPAL 564
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
59-589 |
1.88e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 82.55 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 59 KFLSH-ARRQPKKAFIIY-EGDV-YTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:PRK08315 20 QLLDRtAARYPDREALVYrDQGLrWTYREFNEEVDALAKGLLALG-IEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 136 NSNLRFESLLHCIRTSEPKAMVVGE-----DLLGSLEEILP-------------SLPKHIRVWGMKDSVPEGIVSLKEKL 197
Cdd:PRK08315 99 NPAYRLSELEYALNQSGCKALIAADgfkdsDYVAMLYELAPelatcepgqlqsaRLPELRRVIFLGDEKHPGMLNFDELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 198 SLASDEPVPPSHHVTSSLKST-CLYI-FTSGTTGLPKAAVISQFQVLKGsfGLW---AFGCTADDIVYITLPLYHSSGAL 272
Cdd:PRK08315 179 ALGRAVDDAELAARQATLDPDdPINIqYTSGTTGFPKGATLTHRNILNN--GYFigeAMKLTEEDRLCIPVPLYHCFGMV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 273 LGIGGCVELGATCVlkkkFSASQFwnDCRK-------------YNV-TVFqyIGELcrylckqpqregekDHRvRLAVGN 338
Cdd:PRK08315 257 LGNLACVTHGATMV----YPGEGF--DPLAtlaaveeerctalYGVpTMF--IAEL--------------DHP-DFARFD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 339 gMSS-------------DVWRQFLDRFGnikMCEF---YGATEGNIcFMNHTG-------KIGSVGRVnfFYNLlfsfEL 395
Cdd:PRK08315 314 -LSSlrtgimagspcpiEVMKRVIDKMH---MSEVtiaYGMTETSP-VSTQTRtddplekRVTTVGRA--LPHL----EV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 396 IKYDfqkdePLRNEQgwcycVRKGEPGLLVSRvnkknpffGYT---GSYKqtkskllfDVFKKGDV-----YFNTGDLMF 467
Cdd:PRK08315 383 KIVD-----PETGET-----VPRGEQGELCTR--------GYSvmkGYWN--------DPEKTAEAidadgWMHTGDLAV 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 468 QDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSIILKPNKSLDLEKMYDQVVT 547
Cdd:PRK08315 437 MDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKY-GEEVCAWIILRPGATLTEEDVRDFCRG 515
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 149064320 548 SLPAYACPRFLRIQDKMETTGTFKLKKLQLVEEGFNPLKIAD 589
Cdd:PRK08315 516 KIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELGLQA 557
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
56-533 |
3.62e-16 |
|
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: 82.15 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 56 VLDKFLSHARRQPKkafIIYEGD-----VYTYEDVDKRSNRVAHALlNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGC 130
Cdd:cd05968 66 LLDKWLADTRTRPA---LRWEGEdgtsrTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 131 VVAFLNSNLRFESLLHCIRTSEPKAMVVGE---------DLLGSLEEIL---PSLPKHIRVWGMKDSVPegiVSLKEKLS 198
Cdd:cd05968 142 IVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACaqcPTVEKVVVVRHLGNDFT---PAKGRDLS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 199 LASDEPVPPSHHVTSSLKSTCLYIFTSGTTGLPKAAVISQFQV-LKGSFGLW-AFGCTADDIVYITLPLYHSSGALLGIG 276
Cdd:cd05968 219 YDEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYfQFDLKPGDLLTWFTDLGWMMGPWLIFG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 277 GCVeLGATCVLKKKF----SASQFWNDCRKYNVTVFQYIGELCRYL----CKQPQREGEKDHRVRLAVGNGMSSDVWRQF 348
Cdd:cd05968 299 GLI-LGATMVLYDGApdhpKADRLWRMVEDHEITHLGLSPTLIRALkprgDAPVNAHDLSSLRVLGSTGEPWNPEPWNWL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 349 LDRFG--NIKMCEFYGATE--GNICFMNHTGKIGSVGrvnfFYNLLFSFELIKYDfQKDEPLRNEQGWcYCVRKgepgll 424
Cdd:cd05968 378 FETVGkgRNPIINYSGGTEisGGILGNVLIKPIKPSS----FNGPVPGMKADVLD-ESGKPARPEVGE-LVLLA------ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 425 vsrvnkknPFFGYTGSYKQTKSKLLFDVFKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLD 504
Cdd:cd05968 446 --------PWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHP 517
|
490 500
....*....|....*....|....*....
gi 149064320 505 FIQEANVYGVPVPgYEGKAGMTSIILKPN 533
Cdd:cd05968 518 AVLESAAIGVPHP-VKGEAIVCFVVLKPG 545
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
88-579 |
3.73e-16 |
|
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: 81.27 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 88 RSNRVAHALLNHSDLKRG--DVVALLMSNEPDFVHVWFGLaklGCVVAFLNSNLRFESLLHCIRTSEPKAMVVGEDLLGS 165
Cdd:cd05929 4 RDLDRAQVFHQRRLLLLDvySIALNRNARAAAAEGVWIAD---GVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 166 LEEIL-----PSLPKHIRVWGmkdsVPEGIVSLKEKLSLASDEPVPPSHHVTSSLKStclyiftSGTTGLPKaaVISQfq 240
Cdd:cd05929 81 ACAIIeikaaALVCGLFTGGG----ALDGLEDYEAAEGGSPETPIEDEAAGWKMLYS-------GGTTGRPK--GIKR-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 241 vlKGSFGL--------WAFGC--TADDIVYITLPLYHSSGALLGIGGCVeLGATCVLKKKFSASQFWNDCRKYNVTVFQY 310
Cdd:cd05929 146 --GLPGGPpdndtlmaAALGFgpGADSVYLSPAPLYHAAPFRWSMTALF-MGGTLVLMEKFDPEEFLRLIERYRVTFAQF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 311 IGELCRYLCKQPqreGEKDHRVRLA-------VGNGMSSDVWRQFLDRFGNIkMCEFYGATEGN-ICFMNHTGKI---GS 379
Cdd:cd05929 223 VPTMFVRLLKLP---EAVRNAYDLSslkrvihAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGQgLTIINGEEWLthpGS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 380 VGRVnffynllfsfelikydFQKDEPLRNEQGwcYCVRKGEPGLLVSRvnkKNPFFGYTGSYKQTKSKllfdVFKKGdvy 459
Cdd:cd05929 299 VGRA----------------VLGKVHILDEDG--NEVPPGEIGEVYFA---NGPGFEYTNDPEKTAAA----RNEGG--- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 460 FNT-GDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVP--GYEGKAGMTSIILKPNKSL 536
Cdd:cd05929 351 WSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEelGQRVHAVVQPAPGADAGTA 430
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 149064320 537 DLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVE 579
Cdd:cd05929 431 LAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
77-365 |
3.89e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 81.57 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 77 GDVYTYEDVDKRSNRVAhALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKaM 156
Cdd:PLN02246 48 GRVYTYADVELLSRRVA-AGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAK-L 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 157 VVGEdllGSLEEILPSLPKHIRVWGMK-DSVPEGIVSLKEkLSLASDEPVPPshhVTSSLKSTCLYIFTSGTTGLPKAA- 234
Cdd:PLN02246 126 IITQ---SCYVDKLKGLAEDDGVTVVTiDDPPEGCLHFSE-LTQADENELPE---VEISPDDVVALPYSSGTTGLPKGVm 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 235 ------VISQFQVLKG---SFGLwafgcTADDIVYITLPLYH----SSGALLGIggcvELGATCVLKKKFSASQFWNDCR 301
Cdd:PLN02246 199 lthkglVTSVAQQVDGenpNLYF-----HSDDVILCVLPMFHiyslNSVLLCGL----RVGAAILIMPKFEIGALLELIQ 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149064320 302 KYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLaVGNG---MSSDVWRQFLDRFGNIKMCEFYGATE 365
Cdd:PLN02246 270 RHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRM-VLSGaapLGKELEDAFRAKLPNAVLGQGYGMTE 335
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
80-577 |
4.18e-16 |
|
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: 81.03 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVG 159
Cdd:cd05973 1 LTFGELRALSARFANALQELG-VGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 160 EDLLGSLEEilpslpkhirvwgmkdsvpegivslkeklslasdepvppshhvtsslkSTCLYIFTSGTTGLPKAAVISQF 239
Cdd:cd05973 80 AANRHKLDS------------------------------------------------DPFVMMFTSGTTGLPKGVPVPLR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 240 QVLK-GSFGLWAFGCTADDIVY-ITLP-----LYHSSGALLGIGgcvelGATCVLKKKFSASQFWNDCRKYNVTVFQYIG 312
Cdd:cd05973 112 ALAAfGAYLRDAVDLRPEDSFWnAADPgwaygLYYAITGPLALG-----HPTILLEGGFSVESTWRVIERLGVTNLAGSP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 313 ELCRYLCKQPQrEGEKDHRVRLAV----GNGMSSDVWRQFLDRFGnIKMCEFYGATEGNICFMNHTG-----KIGSVGRV 383
Cdd:cd05973 187 TAYRLLMAAGA-EVPARPKGRLRRvssaGEPLTPEVIRWFDAALG-VPIHDHYGQTELGMVLANHHAlehpvHAGSAGRA 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 384 nffynlLFSFELIKYDFQKDEPLrneqgwcycvrKGEPGLLVSRVnKKNPFFGYTGSYKQTKSKLlfdvfkKGDvYFNTG 463
Cdd:cd05973 265 ------MPGWRVAVLDDDGDELG-----------PGEPGRLAIDI-ANSPLMWFRGYQLPDTPAI------DGG-YYLTG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 464 DLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgYEGKAGMTSIILKPNK--SLDLEKM 541
Cdd:cd05973 320 DTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDP-ERTEVVKAFVVLRGGHegTPALADE 398
|
490 500 510
....*....|....*....|....*....|....*..
gi 149064320 542 YDQVV-TSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd05973 399 LQLHVkKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
103-572 |
6.04e-16 |
|
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: 80.84 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 103 KRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVGEDLLGSL-EEILPSLPKHIRVWG 181
Cdd:cd05909 29 KEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKLkLHHLFDVEYDARIVY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 182 MKDsVPEGIvSLKEKLSLASDEPVPPSHH------VTSSLKSTCLYIFTSGTTGLPKAAVISQFQVLKGSFGLWA-FGCT 254
Cdd:cd05909 109 LED-LRAKI-SKADKCKAFLAGKFPPKWLlrifgvAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAiFDPN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 255 ADDIVYITLPLYHSsgalLGIGGCVELGATCVLKKKFSAS-----QFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKD 329
Cdd:cd05909 187 PEDVVFGALPFFHS----FGLTGCLWLPLLSGIKVVFHPNpldykKIPELIYDKKATILLGTPTFLRGYARAAHPEDFSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 330 HRVRLAVGNGMSSDVWRQFLDRFGnIKMCEFYGATEG------NICFMNHtgKIGSVGRVnffynllfsfeLIKYDFQKD 403
Cdd:cd05909 263 LRLVVAGAEKLKDTLRQEFQEKFG-IRILEGYGTTECspvisvNTPQSPN--KEGTVGRP-----------LPGMEVKIV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 404 EPlrneQGWCYcVRKGEPGLLVSRVNkkNPFFGYTGSYKQTkskllfdVFKKGDVYFNTGDLMFQDHENFLYFWDRIGDT 483
Cdd:cd05909 329 SV----ETHEE-VPIGEGGLLLVRGP--NVMLGYLNEPELT-------SFAFGDGWYDTGDIGKIDGEGFLTITGRLSRF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 484 FRWKGENVATTEVANVLGRLDFIQeANVYGVPVPgyEGKAGMTSIILKPNKSLDLEKMYDQVVTS-LPAYACPRFLRIQD 562
Cdd:cd05909 395 AKIAGEMVSLEAIEDILSEILPED-NEVAVVSVP--DGRKGEKIVLLTTTTDTDPSSLNDILKNAgISNLAKPSYIHQVE 471
|
490
....*....|
gi 149064320 563 KMETTGTFKL 572
Cdd:cd05909 472 EIPLLGTGKP 481
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
93-515 |
7.84e-16 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 80.61 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 93 AHALLnHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVGE------DLLGSL 166
Cdd:PLN02860 46 AAGLL-RLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDEtcsswyEELQND 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 167 EeiLPSLPKHIRvwgMKDSVPEGIVSLkekLSLASDEPVPPSHHVTSSL------KSTCLYIFTSGTTGLPKAAVISQFQ 240
Cdd:PLN02860 125 R--LPSLMWQVF---LESPSSSVFIFL---NSFLTTEMLKQRALGTTELdyawapDDAVLICFTSGTTGRPKGVTISHSA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 241 VLKGSFGLWAF-GCTADDIVYITLPLYHSSG-----ALLGIGGCVelgatcVLKKKFSASQFWNDCRKYNVTVF----QY 310
Cdd:PLN02860 197 LIVQSLAKIAIvGYGEDDVYLHTAPLCHIGGlssalAMLMVGACH------VLLPKFDAKAALQAIKQHNVTSMitvpAM 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 311 IGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGNIKMCEFYGATEG--NICFMnhtgkigsvgRVNFFYN 388
Cdd:PLN02860 271 MADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcsSLTFM----------TLHDPTL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 389 LLFSFELIKYDFQKDEPLRNEQGwcYCVRKGEP------GLLVS----RVNKKNP--FFGYTGSYKQTKSKLlfdvfkKG 456
Cdd:PLN02860 341 ESPKQTLQTVNQTKSSSVHQPQG--VCVGKPAPhvelkiGLDESsrvgRILTRGPhvMLGYWGQNSETASVL------SN 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 149064320 457 DVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVP 515
Cdd:PLN02860 413 DGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVP 471
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
80-307 |
1.78e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 79.55 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHALLNHsDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVG 159
Cdd:PRK04319 74 YTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 160 EDLLGSL-EEILPSLpKHIRVWGMKDSVPEGIVSLKEKLSLASDE-PVPPSHhvtssLKSTCLYIFTSGTTGLPKA---- 233
Cdd:PRK04319 153 PALLERKpADDLPSL-KHVLLVGEDVEEGPGTLDFNALMEQASDEfDIEWTD-----REDGAILHYTSGSTGKPKGvlhv 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 234 --AVISQFQVlkgsfGLWA--------FGCTAD-----DIVY-ITLPLYHssgallgiggcvelGAT-CVLKKKFSASQF 296
Cdd:PRK04319 227 hnAMLQHYQT-----GKYVldlheddvYWCTADpgwvtGTSYgIFAPWLN--------------GATnVIDGGRFSPERW 287
|
250
....*....|.
gi 149064320 297 WNDCRKYNVTV 307
Cdd:PRK04319 288 YRILEDYKVTV 298
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
80-573 |
5.14e-15 |
|
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: 77.64 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVG 159
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALG-VEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 160 EdllgsleeilpslpkhirvwgmkdsvPEGIVSLkeklslasdepvppshhvtsslkstclyIFTSGTTGLPKAAVISQ- 238
Cdd:cd05907 85 D--------------------------PDDLATI----------------------------IYTSGTTGRPKGVMLSHr 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 239 --FQVLKGSFGLWAFgcTADDIVYITLPLYHSSGALLGIGGCVELGATCVLkkKFSASQFWNDCRKYNVTVFQYIGELCR 316
Cdd:cd05907 111 niLSNALALAERLPA--TEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYF--ASSAETLLDDLSEVRPTVFLAVPRVWE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 317 YLCKQPQREGEKDH-----------RVRLAVGNG--MSSDVWRQFLdRFGnIKMCEFYGATE-GNICFMNH--TGKIGSV 380
Cdd:cd05907 187 KVYAAIKVKAVPGLkrklfdlavggRLRFAASGGapLPAELLHFFR-ALG-IPVYEGYGLTEtSAVVTLNPpgDNRIGTV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 381 GRvnffynllfsfelikydfqkdePLRNEQgwcycVRKGEPGLLVsrVNKKNPFFGYTGSYKQTKSKLLfdvfkkGDVYF 460
Cdd:cd05907 265 GK----------------------PLPGVE-----VRIADDGEIL--VRGPNVMLGYYKNPEATAEALD------ADGWL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 461 NTGDLMFQDHENFLYFWDRIGDTFRW-KGENVATTEVANVLGRLDFIQEANVYG----------VPVPGY-EGKAGMTSI 528
Cdd:cd05907 310 HTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIGdgrpflvaliVPDPEAlEAWAEEHGI 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 149064320 529 ILKPNKSL--------DLEKMYDQVVTSLPAYACPRFLRIQDKMET------TGTFKLK 573
Cdd:cd05907 390 AYTDVAELaanpavraEIEAAVEAANARLSRYEQIKKFLLLPEPFTiengelTPTLKLK 448
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
57-284 |
7.66e-15 |
|
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: 77.49 E-value: 7.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 57 LDKFLS-HARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHsDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:COG1021 27 LGDLLRrRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 136 NSNLRFESLLHCIRTSEPKAMVVGEDLLG--------SLEEILPSLpKHIRVWGmkDsvPEGIVSLKEKLS--LASDEPV 205
Cdd:COG1021 106 LPAHRRAEISHFAEQSEAVAYIIPDRHRGfdyralarELQAEVPSL-RHVLVVG--D--AGEFTSLDALLAapADLSEPR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 206 PPSHHVtsslkstCLYIFTSGTTGLPKaaVISQFQ-----VLKGSFGLWAFgcTADDIVYITLPLYH----SSGALLGI- 275
Cdd:COG1021 181 PDPDDV-------AFFQLSGGTTGLPK--LIPRTHddylySVRASAEICGL--DADTVYLAALPAAHnfplSSPGVLGVl 249
|
250
....*....|.
gi 149064320 276 --GGCVELGAT 284
Cdd:COG1021 250 yaGGTVVLAPD 260
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
218-574 |
1.12e-14 |
|
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: 75.76 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 218 TCLYIFTSGTTGLPKAAVISQFQVLKGSFGLWAFG--CTADDIVYITLPLYHSsGALLGIGGCVELGATCVLKKKF-SAS 294
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGlnWVVGDVTYLPLPATHI-GGLWWILTCLIHGGLCVTGGENtTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 295 QFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRL-AVGNGMSSDVWRQFLDRFGNIKMCEFYGATE-GNICFM- 371
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLiGYGGSRAIAADVRFIEATGLTNTAQVYGLSEtGTALCLp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 372 --NHTGKIGSVGRvnffynllfsfELIKYDFQkdepLRNEQGwcYCVRKGEPGLLVSrvnkKNPFF--GYTGSYKQTKSK 447
Cdd:cd17635 162 tdDDSIEINAVGR-----------PYPGVDVY----LAATDG--IAGPSASFGTIWI----KSPANmlGYWNNPERTAEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 448 LLfdvfkkgDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVP------------ 515
Cdd:cd17635 221 LI-------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISdeefgelvglav 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 516 -VPGYEGKAGMTSIILKPNKsldlekmydqvvtSLPAYACPRFLRIQDKMETTGTFKLKK 574
Cdd:cd17635 294 vASAELDENAIRALKHTIRR-------------ELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
73-567 |
2.55e-14 |
|
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: 75.64 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 73 IIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCvvAFLNSNLRF--ESLLHCIRT 150
Cdd:cd05930 6 VVDGDQSLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGA--AYVPLDPSYpaERLAYILED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 151 SEPKAMVVGEDllgsleeilpslpkhirvwgmkdsvpegivslkeklSLAsdepvppshHVtsslkstclyIFTSGTTGL 230
Cdd:cd05930 83 SGAKLVLTDPD------------------------------------DLA---------YV----------IYTSGSTGK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 231 PKAAVISQFQVLkgSFGLW---AFGCTADDIVyitlpLYHSS----GALLGIGGCVELGATCVL---KKKFSASQFWNDC 300
Cdd:cd05930 108 PKGVMVEHRGLV--NLLLWmqeAYPLTPGDRV-----LQFTSfsfdVSVWEIFGALLAGATLVVlpeEVRKDPEALADLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 301 RKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGNIKMCEFYGATEGNICfmnhtgkigsv 380
Cdd:cd05930 181 AEEGITVLHLTPSLLRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVD----------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 381 grvnffynllFSFELIKYDFQKDE------PLRNEQgwCY-------CVRKGEPGLL------VSRvnkknpffGYTGSY 441
Cdd:cd05930 250 ----------ATYYRVPPDDEEDGrvpigrPIPNTR--VYvldenlrPVPPGVPGELyiggagLAR--------GYLNRP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 442 KQTKSKLLFDVFKKGDVYFNTGDLMFQDHENFLYFWDRIgDT------FRwkgenVATTEVANVLGRLDFIQEANVygVP 515
Cdd:cd05930 310 ELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRI-DDqvkirgYR-----IELGEIEAALLAHPGVREAAV--VA 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 149064320 516 vpgYEGKAGMTS----IILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETT 567
Cdd:cd05930 382 ---REDGDGEKRlvayVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLT 434
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
60-237 |
6.24e-14 |
|
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: 74.30 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 60 FLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNhSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNL 139
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRA-RGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 140 RFESLLHCIRTSEPKAMVVGEDLLGSLEEilpslpkhIRVWGMKDSVPEGivslkekLSLASDEPVPPSHhvtsslKSTC 219
Cdd:cd17651 80 PAERLAFMLADAGPVLVLTHPALAGELAV--------ELVAVTLLDQPGA-------AAGADAEPDPALD------ADDL 138
|
170
....*....|....*....
gi 149064320 220 LY-IFTSGTTGLPKAAVIS 237
Cdd:cd17651 139 AYvIYTSGSTGRPKGVVMP 157
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-577 |
1.48e-13 |
|
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: 72.51 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 221 YIFTSGTTGLPKAAVISQF-QVLKGSFGLWAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVL------KKKFSA 293
Cdd:cd05944 7 YFHTGGTTGTPKLAQHTHSnEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRNPGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 294 SQFWNDCRKYNVTVFQYIGELCRYLCkqpQREGEKD-HRVRLAVGNG--MSSDVWRQFLDRFGnIKMCEFYGATEGN--- 367
Cdd:cd05944 87 DNFWKLVERYRITSLSTVPTVYAALL---QVPVNADiSSLRFAMSGAapLPVELRARFEDATG-LPVVEGYGLTEATclv 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 368 -ICFMNHTGKIGSVGrvnffynLLFSFELIKydfqkdepLRNEQGWCYCVRKGEPGlLVSRVNKKNPffGYTGSYKQTKS 446
Cdd:cd05944 163 aVNPPDGPKRPGSVG-------LRLPYARVR--------IKVLDGVGRLLRDCAPD-EVGEICVAGP--GVFGGYLYTEG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 447 KLLFDVfkkGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgYEGKAGMT 526
Cdd:cd05944 225 NKNAFV---ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDA-HAGELPVA 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 149064320 527 SIILKPNKSLDLEKMYDQVVTSLPAYAC-PRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd05944 301 YVQLKPGAVVEEEELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
63-287 |
1.91e-13 |
|
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: 73.04 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 63 HARRQPKKA---FIIYEGDV---YTYEDVDKRSNRVAHALLNHsdLKRGDVVALLMSNEPDFVHVWFG--LAKLGCVVAF 134
Cdd:cd05931 2 RAAARPDRPaytFLDDEGGReetLTYAELDRRARAIAARLQAV--GKPGDRVLLLAPPGLDFVAAFLGclYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 135 L-NSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLPKHIRVWGMkdsvpegIVSLKEKLSLASDEPVPPSHHvts 213
Cdd:cd05931 80 PpTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLL-------VVDLLPDTSAADWPPPSPDPD--- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149064320 214 slkSTCLYIFTSGTTGLPKAAVISQFQVL---KGSFGlwAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVL 287
Cdd:cd05931 150 ---DIAYLQYTSGSTGTPKGVVVTHRNLLanvRQIRR--AYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVL 221
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
58-562 |
2.01e-13 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 72.99 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 58 DKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLnHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNS 137
Cdd:PRK07514 7 DALRAAFADRDAPFIETPDGLRYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 138 NLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLP-KHIRVWGmkdsvPEGIVSLKEKLSLASD--EPVPPShhvTSS 214
Cdd:PRK07514 86 AYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGaPHVETLD-----ADGTGSLLEAAAAAPDdfETVPRG---ADD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 215 LKSTcLYifTSGTTGLPKAAVISQFQVLKGSFGL---WAFgcTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKF 291
Cdd:PRK07514 158 LAAI-LY--TSGTTGRSKGAMLSHGNLLSNALTLvdyWRF--TPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 292 SASQFWNDCRKynVTVFQYIGELCRYLCKQPQREGEKDHRVRLAV-GNG-MSSDVWRQFLDRFGNiKMCEFYGATEGNic 369
Cdd:PRK07514 233 DPDAVLALMPR--ATVMMGVPTFYTRLLQEPRLTREAAAHMRLFIsGSApLLAETHREFQERTGH-AILERYGMTETN-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 370 fMNHTG------KIGSVGRVnffynlLFSFELIKYDFQKDEPLrneqgwcycvRKGEPGLLvsRVNKKNPFFGYTGSYKQ 443
Cdd:PRK07514 308 -MNTSNpydgerRAGTVGFP------LPGVSLRVTDPETGAEL----------PPGEIGMI--EVKGPNVFKGYWRMPEK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 444 TKSKLlfdvfkKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKA 523
Cdd:PRK07514 369 TAEEF------RADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDF-GEG 441
|
490 500 510
....*....|....*....|....*....|....*....
gi 149064320 524 GMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQD 562
Cdd:PRK07514 442 VTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVD 480
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
55-528 |
3.63e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 72.35 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 55 TVLDKFLSHARRQPKkAFIIYEGD---VYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCV 131
Cdd:PRK05857 15 TVLDRVFEQARQQPE-AIALRRCDgtsALRYRELVAEVGGLAADLRAQS-VSRGSRVLVISDNGPETYLSVLACAKLGAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 132 VAFLNSNLRFESLLHCIRTSEPKAMVVGEDL---LGSLEEILPSLPKhIRVWGMKDSVPEG----IVSLKEKLSLASDEP 204
Cdd:PRK05857 93 AVMADGNLPIAAIERFCQITDPAAALVAPGSkmaSSAVPEALHSIPV-IAVDIAAVTRESEhsldAASLAGNADQGSEDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 205 VPpshhvtsslkstclYIFTSGTTGLPKAAVISQ---FQV---LKGSfGLWAFGCTADDIVYITLPLYHsSGALLGIGGC 278
Cdd:PRK05857 172 LA--------------MIFTSGTTGEPKAVLLANrtfFAVpdiLQKE-GLNWVTWVVGETTYSPLPATH-IGGLWWILTC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 279 VELGATCVLKKKFSAS--QFWNDcRKYNVTVFqyIGELCRYLCKQPQREGEKDHRVRLAVGNG---MSSDVwrQFLDRFG 353
Cdd:PRK05857 236 LMHGGLCVTGGENTTSllEILTT-NAVATTCL--VPTLLSKLVSELKSANATVPSLRLVGYGGsraIAADV--RFIEATG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 354 nIKMCEFYGATEGN---ICFMNHTGKI-----GSVGR----VNFFynllfsfelikydfqkdepLRNEQGWCYCVRKGEP 421
Cdd:PRK05857 311 -VRTAQVYGLSETGctaLCLPTDDGSIvkieaGAVGRpypgVDVY-------------------LAATDGIGPTAPGAGP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 422 GLLVSRVNKKNP--FFGYTGSYKQTKSKLLfdvfkkgDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANV 499
Cdd:PRK05857 371 SASFGTLWIKSPanMLGYWNNPERTAEVLI-------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRI 443
|
490 500
....*....|....*....|....*....
gi 149064320 500 LGRLDFIQEANVYGVPVPGYEGKAGMTSI 528
Cdd:PRK05857 444 AEGVSGVREAACYEIPDEEFGALVGLAVV 472
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
64-287 |
4.86e-13 |
|
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: 71.46 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFES 143
Cdd:cd12117 7 AARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 144 LLHCIRTSEPKAMVVGEDLLGSLEEILPslpkhiRVWGMKDSVPEgivslkeklslasDEPVPPshhVTSSLKSTCLYIF 223
Cdd:cd12117 86 LAFMLADAGAKVLLTDRSLAGRAGGLEV------AVVIDEALDAG-------------PAGNPA---VPVSPDDLAYVMY 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 224 TSGTTGLPKAAVISQFQVLKGSFGLWAFGCTADDIVYITLPL------YHSSGALLGiggcvelGATCVL 287
Cdd:cd12117 144 TSGSTGRPKGVAVTHRGVVRLVKNTNYVTLGPDDRVLQTSPLafdastFEIWGALLN-------GARLVL 206
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
222-574 |
6.11e-13 |
|
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: 70.22 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 222 IFTSGTTGLPKAAVISQFQVLkGSFGLWA--FGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSASQFWND 299
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTL-RAAAAWAdcADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 300 CRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNgmSSDVWRQFLDR------FGNIKMCefYGATEGNICFMNH 373
Cdd:cd17638 85 IERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTG--AATVPVELVRRmrselgFETVLTA--YGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 374 TGKigsvgrvnffynllfSFELIKYDFQKDEPlrneqgwCYCVRKGEPGLLVSRvnKKNPFFGYTGSYKQTKSKLlfdvf 453
Cdd:cd17638 161 PGD---------------DAETVATTCGRACP-------GFEVRIADDGEVLVR--GYNVMQGYLDDPEATAEAI----- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 454 kKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPvPGYEGKAGMTSIILKPN 533
Cdd:cd17638 212 -DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVP-DERMGEVGKAFVVARPG 289
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 149064320 534 KSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKK 574
Cdd:cd17638 290 VTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
81-287 |
9.75e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 71.08 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 81 TYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMV--- 157
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIgip 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 158 ---VGEDLLGSLEeilPSLPKHIRV-----WGMKDsvpegIVSLKEKLSLASDEPVPPSHHvtsslkSTCLYIFTSGTTG 229
Cdd:PRK09274 122 kahLARRLFGWGK---PSVRRLVTVggrllWGGTT-----LATLLRDGAAAPFPMADLAPD------DMAAILFTSGSTG 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149064320 230 LPKAAVIS------QFQVLKGSFGLwafgcTADDIVYITLPLYhssgALLGIGgcveLGATCVL 287
Cdd:PRK09274 188 TPKGVVYThgmfeaQIEALREDYGI-----EPGEIDLPTFPLF----ALFGPA----LGMTSVI 238
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
60-572 |
1.18e-12 |
|
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: 70.38 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 60 FLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNhSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNL 139
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRA-RGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 140 RFESLLHCIRTSEPKAMVVGEDLLGSLeeilpslpkhirvwgmkdsVPEGIVSLKEKLSLASDEPVPPShhVTSSLKSTC 219
Cdd:cd17646 83 PADRLAYMLADAGPAVVLTTADLAARL-------------------PAGGDVALLGDEALAAPPATPPL--VPPRPDNLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 220 LYIFTSGTTGLPK------AAVISQFQVLKGSFGLwafgcTADDIVY-------------ITLPLyhSSGALLGI---GG 277
Cdd:cd17646 142 YVIYTSGSTGRPKgvmvthAGIVNRLLWMQDEYPL-----GPGDRVLqktplsfdvsvweLFWPL--VAGARLVVarpGG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 278 CVELGATCVLkkkfsasqfwndCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGnIKM 357
Cdd:cd17646 215 HRDPAYLAAL------------IREHGVTTCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPG-AEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 358 CEFYGATEGNI------CFMNHTGKIGSVGRVNF---FYNLlfsfelikydfqkDEPLRNeqgwcycVRKGEPGLL---- 424
Cdd:cd17646 282 HNLYGPTEAAIdvthwpVRGPAETPSVPIGRPVPntrLYVL-------------DDALRP-------VPVGVPGELylgg 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 425 --VSRvnkknpffGYTGSYKQTKSKLLFDVFKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGR 502
Cdd:cd17646 342 vqLAR--------GYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAA 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 503 LDFIQEANV--------------YGVPVPGYEGkagmtsiilkpnksLDLEKMYDQVVTSLPAYACP-RFLRIqDKMETT 567
Cdd:cd17646 414 HPAVTHAVVvaraapagaarlvgYVVPAAGAAG--------------PDTAALRAHLAERLPEYMVPaAFVVL-DALPLT 478
|
....*
gi 149064320 568 GTFKL 572
Cdd:cd17646 479 ANGKL 483
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
495-571 |
1.81e-12 |
|
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: 62.95 E-value: 1.81e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149064320 495 EVANVLGRLDFIQEANVYGVPVPgYEGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFK 571
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
64-275 |
3.19e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 69.13 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLnHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLrFES 143
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFA-QQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQL-PQP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 144 LLHcirtsepkamvvgedllgsleEILPSLpkHIRVwgMKDSVPEGIVSLKEKLSLAsdePVPPSHHVTSSLKSTCLYIF 223
Cdd:PRK09029 91 LLE---------------------ELLPSL--TLDF--ALVLEGENTFSALTSLHLQ---LVEGAHAVAWQPQRLATMTL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 149064320 224 TSGTTGLPKAAVISQFQVL---KGSFGLWAFgcTADDIVYITLPLYHSSGalLGI 275
Cdd:PRK09029 143 TSGSTGLPKAAVHTAQAHLasaEGVLSLMPF--TAQDSWLLSLPLFHVSG--QGI 193
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
63-567 |
1.04e-11 |
|
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: 67.59 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 63 HARRQPKKAFIIYEGD------VYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCV--VAF 134
Cdd:cd05966 62 HLKERGDKVAIIWEGDepdqsrTITYRELLREVCRFANVLKSLG-VKKGDRVAIYMPMIPELVIAMLACARIGAVhsVVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 135 lnSNLRFESLLHCIRTSEPKAMVV------GEDLLGsLEEI-------LPSlPKHIRVW---GMKDSVPEGI-VSLKEKL 197
Cdd:cd05966 141 --AGFSAESLADRINDAQCKLVITadggyrGGKVIP-LKEIvdealekCPS-VEKVLVVkrtGGEVPMTEGRdLWWHDLM 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 198 SLASDEpVPP----SHHVtsslkstcLYI-FTSGTTGLPKAAVISQfqvlkGSFGLWA---------------FGCTAdD 257
Cdd:cd05966 217 AKQSPE-CEPewmdSEDP--------LFIlYTSGSTGKPKGVVHTT-----GGYLLYAattfkyvfdyhpddiYWCTA-D 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 258 IVYITLPLYHSSGALLgiggcveLGATCVLkkkF-------SASQFWNDCRKYNVTVFqY-----IGELCRYLCKQPQRE 325
Cdd:cd05966 282 IGWITGHSYIVYGPLA-------NGATTVM---FegtptypDPGRYWDIVEKHKVTIF-YtaptaIRALMKFGDEWVKKH 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 326 GEKDHRVRLAVGNGMSSDVWRQFLDRFGNIK--MCEFYGATE-GNICFMNHTG----KIGSVGRVnffynlLFSFELIKY 398
Cdd:cd05966 351 DLSSLRVLGSVGEPINPEAWMWYYEVIGKERcpIVDTWWQTEtGGIMITPLPGatplKPGSATRP------FFGIEPAIL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 399 DfQKDEPLRNEQGWCYCVRKGEPGLLVSrvnkknpFFGYTGSYKQTksklLFDVFKkgDVYFnTGDLMFQDHENflYFW- 477
Cdd:cd05966 425 D-EEGNEVEGEVEGYLVIKRPWPGMART-------IYGDHERYEDT----YFSKFP--GYYF-TGDGARRDEDG--YYWi 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 478 -DRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgYEGKAGMTSIILKPN--KSLDLEK-MYDQVVTSLPAYA 553
Cdd:cd05966 488 tGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHD-IKGEAIYAFVTLKDGeePSDELRKeLRKHVRKEIGPIA 566
|
570
....*....|....
gi 149064320 554 CPRFLRIQDKMETT 567
Cdd:cd05966 567 TPDKIQFVPGLPKT 580
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
77-580 |
1.11e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 67.70 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 77 GDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAM 156
Cdd:PLN02330 53 GKAVTYGEVVRDTRRFAKALRSLG-LRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 157 VVGEDLLGSLEEIlpSLPkhirVWGMKDSVPEGIVSLKEKLSlASDEPVPPSHHVTSSLKSTCLYIFTSGTTGLPKAAVI 236
Cdd:PLN02330 132 VTNDTNYGKVKGL--GLP----VIVLGEEKIEGAVNWKELLE-AADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVML 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 237 SQfQVLKGSFGLWAFGCTADDIVYIT----LPLYHssgaLLGIGG--CVEL--GATCVLKKKFSASQFWNDCRKYNVTVF 308
Cdd:PLN02330 205 TH-RNLVANLCSSLFSVGPEMIGQVVtlglIPFFH----IYGITGicCATLrnKGKVVVMSRFELRTFLNALITQEVSFA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 309 QYIGELCRYLCKQPQREGEKDHRVRL----AVGNGMSSDVWRQFLDRFGNIKMCEFYGATEGNICFMNH--------TGK 376
Cdd:PLN02330 280 PIVPPIILNLVKNPIVEEFDLSKLKLqaimTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHgdpekghgIAK 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 377 IGSVGRVnfFYNLLFSFelIKYDFQKDEPlrneqgwcycvrKGEPGLLVSRvnKKNPFFGYTGSYKQTKSKLlfdvfkKG 456
Cdd:PLN02330 360 KNSVGFI--LPNLEVKF--IDPDTGRSLP------------KNTPGELCVR--SQCVMQGYYNNKEETDRTI------DE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 457 DVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVygVPVPGYE-GKAGMTSIILKPNKS 535
Cdd:PLN02330 416 DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV--VPLPDEEaGEIPAACVVINPKAK 493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 149064320 536 LDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVEE 580
Cdd:PLN02330 494 ESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
57-580 |
1.18e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 67.47 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 57 LDKFLSHARRQPKKAFII---YEGDVY--TYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCV 131
Cdd:PRK06018 12 CHRIIDHAARIHGNREVVtrsVEGPIVrtTYAQIHDRALKVSQALDRDG-IKLGDRVATIAWNTWRHLEAWYGIMGIGAI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 132 VAFLNSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLP--KHIRVWGMKDSVPE----GIVSLKEKLSLAS---- 201
Cdd:PRK06018 91 CHTVNPRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLPsvERYVVLTDAAHMPQttlkNAVAYEEWIAEADgdfa 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 202 ----DEpvppshhvtsslKSTCLYIFTSGTTGLPKAAVIS-QFQVLKG--SFGLWAFGCTADDIVYITLPLYH------- 267
Cdd:PRK06018 171 wktfDE------------NTAAGMCYTSGTTGDPKGVLYShRSNVLHAlmANNGDALGTSAADTMLPVVPLFHanswgia 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 268 ----SSGALLGIGGCVELGATC--VL---KKKFSASQfwndcrkynVTVFQYigeLCRYLckqpQREGEKDHRVRLAV-- 336
Cdd:PRK06018 239 fsapSMGTKLVMPGAKLDGASVyeLLdteKVTFTAGV---------PTVWLM---LLQYM----EKEGLKLPHLKMVVcg 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 337 GNGMSSDVWRQFLDRfgNIKMCEFYGATEgnicfmnhTGKIGSVGRvnffynLLFSFELIKYDFQKDEPLrneqgwcycv 416
Cdd:PRK06018 303 GSAMPRSMIKAFEDM--GVEVRHAWGMTE--------MSPLGTLAA------LKPPFSKLPGDARLDVLQ---------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 417 RKGEPGL-----LVSRVNKKNPFFGYT------------GSYKQTKSKLLFDvfkkgDVYFNTGDLMFQDHENFLYFWDR 479
Cdd:PRK06018 357 KQGYPPFgvemkITDDAGKELPWDGKTfgrlkvrgpavaAAYYRVDGEILDD-----DGFFDTGDVATIDAYGYMRITDR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 480 IGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLR 559
Cdd:PRK06018 432 SKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKW-DERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVA 510
|
570 580
....*....|....*....|.
gi 149064320 560 IQDKMETTGTFKLKKLQLVEE 580
Cdd:PRK06018 511 FVDAIPHTATGKILKTALREQ 531
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
76-590 |
1.44e-11 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 67.12 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 76 EGDVYTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKA 155
Cdd:PRK05620 35 EQEQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 156 MVVGEDLLGSLEEILPSLP--KHIRVWGMKDS------VPEGIV-----SLKEKLSLASDEPVPPSHhvtsSLKSTClyi 222
Cdd:PRK05620 115 IVADPRLAEQLGEILKECPcvRAVVFIGPSDAdsaaahMPEGIKvysyeALLDGRSTVYDWPELDET----TAAAIC--- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 223 FTSGTTGLPKAAVISQFQVLKGSFGLWA---FGCTADDIVYITLPLYH-----------SSGALLGIGG-------CVEL 281
Cdd:PRK05620 188 YSTGTTGAPKGVVYSHRSLYLQSLSLRTtdsLAVTHGESFLCCVPIYHvlswgvplaafMSGTPLVFPGpdlsaptLAKI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 282 GATCVLKKKFSASQFWndcrkynvtvfqyIGELCRYLCKQPQREGEKDhrvrLAVGNGMSS----DVWRQfldRFGnIKM 357
Cdd:PRK05620 268 IATAMPRVAHGVPTLW-------------IQLMVHYLKNPPERMSLQE----IYVGGSAVPpiliKAWEE---RYG-VDV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 358 CEFYGATEgnicfmnhTGKIGSVGRvnffynllfsfelikydfqkdeP---LRNEQGWCYCVRKGE-PGLLVSR-VNKKN 432
Cdd:PRK05620 327 VHVWGMTE--------TSPVGTVAR----------------------PpsgVSGEARWAYRVSQGRfPASLEYRiVNDGQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 433 PFFGY--------------TGSYKQTKSKL---LFDVFKKGDV-----------YFNTGDLMFQDHENFLYFWDRIGDTF 484
Cdd:PRK05620 377 VMESTdrnegeiqvrgnwvTASYYHSPTEEgggAASTFRGEDVedandrftadgWLRTGDVGSVTRDGFLTIHDRARDVI 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 485 RWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYeGKAGMTSIILKPNKSLDLE---KMYDQVVTSLPAYACPRFLRIQ 561
Cdd:PRK05620 457 RSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKW-GERPLAVTVLAPGIEPTREtaeRLRDQLRDRLPNWMLPEYWTFV 535
|
570 580 590
....*....|....*....|....*....|...
gi 149064320 562 DKMETT--GTFKLKKL-QLVEEG-FNPLKIADP 590
Cdd:PRK05620 536 DEIDKTsvGKFDKKDLrQHLADGdFEIIKLKGP 568
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
56-588 |
1.66e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.67 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 56 VLDKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALlnhsdLKRGDV----VALLMSNEPDFVHVWFGLAKLGCV 131
Cdd:PRK12316 2005 VHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRL-----RARGVGpevrVAIAAERSFELVVALLAVLKAGGA 2079
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 132 VAFLNSNLRFESLLHCIRTSepkamvvGEDLLGSLEEILPSLPkhirvwgmkdsVPEGIVSLkeKLSLASDEPVPPSHHV 211
Cdd:PRK12316 2080 YVPLDPNYPAERLAYMLEDS-------GAALLLTQRHLLERLP-----------LPAGVARL--PLDRDAEWADYPDTAP 2139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 212 TSSLKSTCL--YIFTSGTTGLPKAAVISQFQVLkgSFGLWA---FGCTADDIVYITLP---------LYHS--SGALLGI 275
Cdd:PRK12316 2140 AVQLAGENLayVIYTSGSTGLPKGVAVSHGALV--AHCQAAgerYELSPADCELQFMSfsfdgaheqWFHPllNGARVLI 2217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 276 GGcvelgatcvlKKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDH-RVRLAVGNGMSSDVWRQFLDRFGN 354
Cdd:PRK12316 2218 RD----------DELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAvRVYCFGGEAVPAASLRLAWEALRP 2287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 355 IKMCEFYGATEGNICFMNHTGK-----------IGSVGRVNFFYNLLFSFELIKydfqkdeplrneQGWCYCVRKGEPGL 423
Cdd:PRK12316 2288 VYLFNGYGPTEAVVTPLLWKCRpqdpcgaayvpIGRALGNRRAYILDADLNLLA------------PGMAGELYLGGEGL 2355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 424 lvSRvnkknpffGYTGSYKQTKSKLLFDVF-KKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGR 502
Cdd:PRK12316 2356 --AR--------GYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQA 2425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 503 LDFIQEANVygVPVPGYEGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVEEGF 582
Cdd:PRK12316 2426 HPAVREAVV--VAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDV 2503
|
....*.
gi 149064320 583 NPLKIA 588
Cdd:PRK12316 2504 SQLRQA 2509
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
64-575 |
1.71e-11 |
|
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: 66.50 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLnHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFES 143
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALA-SLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 144 LLHCIRTSEPKAMVVGEDllgsleeilpslpkhirvwgmkdsvpegivslkeklSLAsdepvppshhvtsslkstclYI- 222
Cdd:cd05945 80 IREILDAAKPALLIADGD------------------------------------DNA--------------------YIi 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 223 FTSGTTGLPKAAVISQFQVLkgSFGLWA---FGCTADDIVYITLPlYHSSGALLGIGGCVELGATCV-----LKKKFsaS 294
Cdd:cd05945 104 FTSGSTGRPKGVQISHDNLV--SFTNWMlsdFPLGPGDVFLNQAP-FSFDLSVMDLYPALASGATLVpvprdATADP--K 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 295 QFWNDCRKYNVTVF---QYIGELCRylcKQPQREGEKDHRVRLAV--GNGMSSDVWRQFLDRFGNIKMCEFYGATEGNI- 368
Cdd:cd05945 179 QLFRFLAEHGITVWvstPSFAAMCL---LSPTFTPESLPSLRHFLfcGEVLPHKTARALQQRFPDARIYNTYGPTEATVa 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 369 CFMNHTGK--IGSVGRVNffynllfsfelIKYDFqKDEPLR--NEQGwcYCVRKGEPGLLVSR---VNKknpffGYTGSY 441
Cdd:cd05945 256 VTYIEVTPevLDGYDRLP-----------IGYAK-PGAKLVilDEDG--RPVPPGEKGELVISgpsVSK-----GYLNNP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 442 KQTKSKLLFDvfkKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVygVPVPGYEG 521
Cdd:cd05945 317 EKTAAAFFPD---EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV--VPKYKGEK 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 149064320 522 KAGMTS-IILKPNKSLDLEKMYDQVV-TSLPAYACPRFLRIQDKMETTGTFKL--KKL 575
Cdd:cd05945 392 VTELIAfVVPKPGAEAGLTKAIKAELaERLPPYMIPRRFVYLDELPLNANGKIdrKAL 449
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
65-577 |
1.86e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 66.93 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 65 RRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALlnHS-DLKRGDVVALLMSNEPDfvhVWFGLAK---LGCVVAFLNSNLR 140
Cdd:PRK06188 23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAF--EAlGLGTGDAVALLSLNRPE---VLMAIGAaqlAGLRRTALHPLGS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 141 FESLLHCIRTSEPKAMVVG----EDLLGSLEEILPSLpKHIRVWGmkdSVPEGiVSLkeklsLASDEPVPPSHHVTSSLK 216
Cdd:PRK06188 98 LDDHAYVLEDAGISTLIVDpapfVERALALLARVPSL-KHVLTLG---PVPDG-VDL-----LAAAAKFGPAPLVAAALP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 217 STCLYIF-TSGTTGLPKAAVIS------QFQVLKGSFGLwafgctADDIVY-ITLPLYHSSGALlgIGGCVELGATCVLK 288
Cdd:PRK06188 168 PDIAGLAyTGGTTGKPKGVMGThrsiatMAQIQLAEWEW------PADPRFlMCTPLSHAGGAF--FLPTLLRGGTVIVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 289 KKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQregekDHRVRLAV-------GNGMSSDVWRQFLDRFGNIKMcEFY 361
Cdd:PRK06188 240 AKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPD-----LRTRDLSSletvyygASPMSPVRLAEAIERFGPIFA-QYY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 362 GATEG--NICFM---NHTGK----IGSVGRVNFFYN--LLfsfelikydfqkDEPLRNeqgwcycVRKGEPGLLVSRvnk 430
Cdd:PRK06188 314 GQTEApmVITYLrkrDHDPDdpkrLTSCGRPTPGLRvaLL------------DEDGRE-------VAQGEVGEICVR--- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 431 kNPFF--GYTGSYKQTKskllfDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQE 508
Cdd:PRK06188 372 -GPLVmdGYWNRPEETA-----EAFRDG--WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQ 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149064320 509 ANVYGVPVPGYeGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:PRK06188 444 VAVIGVPDEKW-GEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-368 |
4.42e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.52 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 60 FLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALlnhsdLKRG---DV-VALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:PRK12316 4557 VAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHAL-----IARGvgpEVlVGIAMERSAEMMVGLLAVLKAGGAYVPL 4631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 136 NSNLRFESLLHCIRTSepkamvvGEDLLGSLEEILPSLPkhirvwgmkdsVPEGIVSLkeKLSLASDEPVPPSHHVTSSL 215
Cdd:PRK12316 4632 DPEYPRERLAYMMEDS-------GAALLLTQSHLLQRLP-----------IPDGLASL--ALDRDEDWEGFPAHDPAVRL 4691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 216 KSTCL--YIFTSGTTGLPKAAVISQFQVLkgSFGLW---AFGCTADDIVyITLPLYHSSGALLGIGGCVELGATCVLKKk 290
Cdd:PRK12316 4692 HPDNLayVIYTSGSTGRPKGVAVSHGSLV--NHLHAtgeRYELTPDDRV-LQFMSFSFDGSHEGLYHPLINGASVVIRD- 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 291 fsaSQFWNDCRKY------NVTVFQYIGELCRYLCKQPQREGEKDH-RVRLAVGNGMSSDVWRQFLDRFGNIKMCEFYGA 363
Cdd:PRK12316 4768 ---DSLWDPERLYaeihehRVTVLVFPPVYLQQLAEHAERDGEPPSlRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGP 4844
|
....*
gi 149064320 364 TEGNI 368
Cdd:PRK12316 4845 TETTV 4849
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
62-552 |
5.23e-11 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 65.25 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 62 SHARRQPKKAFIIY-EGDVYTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLN-SNL 139
Cdd:PLN02574 48 SHHNHNGDTALIDSsTGFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNpSSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 140 RFESLLHCIRTSEPKAMVVGEDLlgsleEILPSLpkhirvwgmkdSVPegIVSLKEKLSLASDEPVPPSHHVTSSLKSTC 219
Cdd:PLN02574 128 LGEIKKRVVDCSVGLAFTSPENV-----EKLSPL-----------GVP--VIGVPENYDFDSKRIEFPKFYELIKEDFDF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 220 L------------YIFTSGTTGLPKAAVISQFQVLKG-----SFGLWAFGCTADDIVYIT-LPLYHSSGALLGIGGCVEL 281
Cdd:PLN02574 190 VpkpvikqddvaaIMYSSGTTGASKGVVLTHRNLIAMvelfvRFEASQYEYPGSDNVYLAaLPMFHIYGLSLFVVGLLSL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 282 GATCVLKKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNG---MSSDVWRQFLDRFGNIKMC 358
Cdd:PLN02574 270 GSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGaapLSGKFIQDFVQTLPHVDFI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 359 EFYGATEgnicfmnhTGKIGSVGRVNFFYNLLFSFELIKYDFQKdEPLRNEQGwcYCVRKGEPGLLVSR---VNKknpff 435
Cdd:PLN02574 350 QGYGMTE--------STAVGTRGFNTEKLSKYSSVGLLAPNMQA-KVVDWSTG--CLLPPGNCGELWIQgpgVMK----- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 436 GYTGSYKQTKSKLLfdvfkkGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVygVP 515
Cdd:PLN02574 414 GYLNNPKATQSTID------KDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAV--TA 485
|
490 500 510
....*....|....*....|....*....|....*...
gi 149064320 516 VPGYE-GKAGMTSIILKPNKSLDLEKMYDQVVTSLPAY 552
Cdd:PLN02574 486 VPDKEcGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPY 523
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
76-287 |
5.71e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.96 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 76 EGDVYTYEDVDKRSNRVAHALLNHSDLkrGDVVALLMSNEPDFVHVWFG--LAKLGCVVAFLNSNLR---FESLLHCIRT 150
Cdd:PRK05691 37 EGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGclYAGVIAVPAYPPESARrhhQERLLSIIAD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 151 SEPKAMVVGEDLLGSLEEIlpslpKHIRVwgmkDSVPE--GIVSLKEKLSLASDEPVPPSHHVTsslkstcLYIFTSGTT 228
Cdd:PRK05691 115 AEPRLLLTVADLRDSLLQM-----EELAA----ANAPEllCVDTLDPALAEAWQEPALQPDDIA-------FLQYTSGST 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149064320 229 GLPKAAVISQF------QVLKGSFGLWAfgcTADDIVYITLPLYHSSGAllgIGGCVE---LGATCVL 287
Cdd:PRK05691 179 ALPKGVQVSHGnlvaneQLIRHGFGIDL---NPDDVIVSWLPLYHDMGL---IGGLLQpifSGVPCVL 240
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
61-267 |
6.27e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 65.11 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 61 LSHARRQPKKAFII---YEGDV--YTYEDVDKRSNRVAHAlLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:PRK07008 16 IAHAARHAGDTEIVsrrVEGDIhrYTYRDCERRAKQLAQA-LAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 136 NSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLPkHIRVWGM---KDSVPEGIVSLK--EKLSLASDEPV--PPS 208
Cdd:PRK07008 95 NPRLFPEQIAYIVNHAEDRYVLFDLTFLPLVDALAPQCP-NVKGWVAmtdAAHLPAGSTPLLcyETLVGAQDGDYdwPRF 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149064320 209 HHVTSSlkSTClyiFTSGTTGLPKAAVISQFQVLKGSFGLW---AFGCTADDIVYITLPLYH 267
Cdd:PRK07008 174 DENQAS--SLC---YTSGTTGNPKGALYSHRSTVLHAYGAAlpdAMGLSARDAVLPVVPMFH 230
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
53-577 |
2.59e-10 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 63.12 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 53 LVTVLDKflSHARRQPKKAFIIYeGDVYTYEDVDKRSNRVAhALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVV 132
Cdd:PRK07059 25 LADLLEE--SFRQYADRPAFICM-GKAITYGELDELSRALA-AWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 133 AFLNSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLP-KHIRVWGMKD-----------------------SVPe 188
Cdd:PRK07059 101 VNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAvKHVVVASMGDllgfkghivnfvvrrvkkmvpawSLP- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 189 GIVSLKEKLSL---ASDEPVPPSHHVTSSLKstclyiFTSGTTGLPKAAVISQFQVL--KGSFGLW---AFGCTADDIVY 260
Cdd:PRK07059 180 GHVRFNDALAEgarQTFKPVKLGPDDVAFLQ------YTGGTTGVSKGATLLHRNIVanVLQMEAWlqpAFEKKPRPDQL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 261 IT---LPLYH----SSGALLGIggcvELGATCVL-KKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRV 332
Cdd:PRK07059 254 NFvcaLPLYHifalTVCGLLGM----RTGGRNILiPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 333 RLAVGNGMSsdVWRQFLDRFGNIKMC---EFYGATEGNICFM-------NHTGKIGSVgrvnffynlLFSFEL-IKYDFQ 401
Cdd:PRK07059 330 IVANGGGMA--VQRPVAERWLEMTGCpitEGYGLSETSPVATcnpvdatEFSGTIGLP---------LPSTEVsIRDDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 402 KDEPLrneqgwcycvrkGEPGLLVSRvnkkNP--FFGYTGSYKQTkSKLLFDvfkkgDVYFNTGDLMFQDHENFLYFWDR 479
Cdd:PRK07059 399 NDLPL------------GEPGEICIR----GPqvMAGYWNRPDET-AKVMTA-----DGFFRTGDVGVMDERGYTKIVDR 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 480 IGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgYEGKAgMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLR 559
Cdd:PRK07059 457 KKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDE-HSGEA-VKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVE 534
|
570
....*....|....*...
gi 149064320 560 IQDKMETTGTFKLKKLQL 577
Cdd:PRK07059 535 FRTELPKTNVGKILRREL 552
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
77-292 |
4.45e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 62.31 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 77 GDVYTYEDVDKRSNRVAHallnhsDLKRGDVVALLMSNEPDFVhvwfgLAKLGCVVAF-----LNSNLRFESLLHCIRTS 151
Cdd:PRK07787 23 GRVLSRSDLAGAATAVAE------RVAGARRVAVLATPTLATV-----LAVVGALIAGvpvvpVPPDSGVAERRHILADS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 152 EPKAmvvgedLLGSLEEILPSLPkhirvwgmkdSVPegiVSLKEKLSLASDEPVPpshhvtsslKSTCLYIFTSGTTGLP 231
Cdd:PRK07787 92 GAQA------WLGPAPDDPAGLP----------HVP---VRLHARSWHRYPEPDP---------DAPALIVYTSGTTGPP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149064320 232 KAAVISQFQVLKGSFGLW-AFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFS 292
Cdd:PRK07787 144 KGVVLSRRAIAADLDALAeAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPT 205
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
55-577 |
9.30e-10 |
|
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: 61.19 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 55 TVLDKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAhALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLA-AGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 135 LNSNLRFESLLHCIRTSEPKAMVVGedllgsleeilpslpkhiRVWGMKDSVPegivslkeklsLAsdepvppsHHVTSS 214
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIVP------------------DRHAGFDHRA-----------LA--------RELAES 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 215 LKSTCLYIFTSGTTGLPKAavISQFQ-----VLKGSFGLWAFGctaDDIVYIT-LPLYH-----SSGAL--LGIGGCVEL 281
Cdd:cd05920 138 IPEVALFLLSGGTTGTPKL--IPRTHndyayNVRASAEVCGLD---QDTVYLAvLPAAHnfplaCPGVLgtLLAGGRVVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 282 GATCVLKKKFSAsqfwndCRKYNVT--------VFQYIGELCRYlckqpqREGEKDHRVRLAVGNGMSSDVWRQFLDRFG 353
Cdd:cd05920 213 APDPSPDAAFPL------IEREGVTvtalvpalVSLWLDAAASR------RADLSSLRLLQVGGARLSPALARRVPPVLG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 354 nIKMCEFYGATEGNICFMN----HTGKIGSVGRvnffynllfsfELIKYDFQK--DEPLRNeqgwcycVRKGEPGLLVSR 427
Cdd:cd05920 281 -CTLQQVFGMAEGLLNYTRlddpDEVIIHTQGR-----------PMSPDDEIRvvDEEGNP-------VPPGEEGELLTR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 428 vnkkNPffgYT--GSYK----QTKSkllFDvfkkGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLG 501
Cdd:cd05920 342 ----GP---YTirGYYRapehNARA---FT----PDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLL 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149064320 502 RLDFIQEANVYGVPVPgYEGKAGMTSIILKPN--KSLDLEKMYDQVvtSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd05920 408 RHPAVHDAAVVAMPDE-LLGERSCAFVVLRDPppSAAQLRRFLRER--GLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
64-572 |
1.47e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 61.33 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 64 ARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSDLKrGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFES 143
Cdd:PRK12467 522 ARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGP-DVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDR 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 144 LLHCIRTSepkamvvGEDLLGSLEEILPSLPkhirvwgmkdsVPEGIVSLKekLSLASDEPVPPSHHVTS---SLKSTCL 220
Cdd:PRK12467 601 LAYMLDDS-------GVRLLLTQSHLLAQLP-----------VPAGLRSLC--LDEPADLLCGYSGHNPEvalDPDNLAY 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 221 YIFTSGTTGLPKAAVISQ------FQVLKGSFGLwafgcTADDIVYITLPlYHSSGALLGIGGCVELGATCVLKKK---F 291
Cdd:PRK12467 661 VIYTSGSTGQPKGVAISHgalanyVCVIAERLQL-----AADDSMLMVST-FAFDLGVTELFGALASGATLHLLPPdcaR 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 292 SASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDV---WRQFLDRFGNIKMcefYGATEGNI 368
Cdd:PRK12467 735 DAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLlarVRALGPGARLINH---YGPTETTV 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 369 CFMnhTGKIGSVGRVNFFYNLlfsfelikydfqkDEPLRNeQGWcYC-------VRKGEPGLL------VSRvnkknpff 435
Cdd:PRK12467 812 GVS--TYELSDEERDFGNVPI-------------GQPLAN-LGL-YIldhylnpVPVGVVGELyiggagLAR-------- 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 436 GYTGSYKQTKSKLLFDVF-KKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANV--- 511
Cdd:PRK12467 867 GYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVlaq 946
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149064320 512 ----------YGVPVPGYEGKAgmtsiilkpnKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKL 572
Cdd:PRK12467 947 pgdaglqlvaYLVPAAVADGAE----------HQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
222-558 |
1.90e-09 |
|
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: 59.59 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 222 IFTSGTTGLPKAAVISQFQVLKGSFGL-WAFGCTADDIVYITLPLYHSSGalLGIGGCV-ELGATCVLKKKFSASQFWND 299
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIAANLQLiHAMGLTEADVYLNMLPLFHIAG--LNLALATfHAGGANVVMEKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 300 CRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRqfLDRFGNIKMCEFYGATE--GNICFMNHTGKI 377
Cdd:cd17637 84 IEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAPETIQR--FEETTGATFWSLYGQTEtsGLVTLSPYRERP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 378 GSVGRVNffynLLFSFELIKydfQKDEPlrneqgwcycVRKGEPGLLVSRvnkkNP--FFGYTGSYKQTKSkllfdVFKK 455
Cdd:cd17637 162 GSAGRPG----PLVRVRIVD---DNDRP----------VPAGETGEIVVR----GPlvFQGYWNLPELTAY-----TFRN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 456 GdvYFNTGDLMFQDHENFLYFWDRIGDTFRWK--GENVATTEVANVLGRLDFIQEANVYGVPVPGY-EG-KAgmtSIILK 531
Cdd:cd17637 216 G--WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWgEGiKA---VCVLK 290
|
330 340
....*....|....*....|....*..
gi 149064320 532 PNKSLDLEKMYDQVVTSLPAYACPRFL 558
Cdd:cd17637 291 PGATLTADELIEFVGSRIARYKKPRYV 317
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
61-286 |
2.47e-09 |
|
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: 59.99 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 61 LSHARRQPKKAFIIYEGDV-----YTYEDVDKRSNRVAHALLNhSDLKRGDVVALLMSNEPDFVhVWFGLAKL-GCVVAF 134
Cdd:cd05906 16 LLRAAERGPTKGITYIDADgseefQSYQDLLEDARRLAAGLRQ-LGLRPGDSVILQFDDNEDFI-PAFWACVLaGFVPAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 135 L-------NSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILpslpkhiRVWGMKDSVpegIVSLKEKLSLASDEPVPP 207
Cdd:cd05906 94 LtvpptydEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLE-------TLSGLPGIR---VLSIEELLDTAADHDLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 208 ShhvtsSLKSTCLYIFTSGTTGLPKAAVISQFQVLKGSFG-LWAFGCTADDIVYITLPLYHssgallgIGGCVELGATCV 286
Cdd:cd05906 164 S-----RPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGkIQHNGLTPQDVFLNWVPLDH-------VGGLVELHLRAV 231
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
80-517 |
5.86e-09 |
|
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: 58.63 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAhALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVG 159
Cdd:cd05932 7 FTWGEVADKARRLA-AALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 160 EdlLGSLEEILPSLPKH-IRVWGMKDSVP---EGIVSLKEKLSLASDEPVPPSHHVTSslkstclYIFTSGTTGLPKAAV 235
Cdd:cd05932 86 K--LDDWKAMAPGVPEGlISISLPPPSAAncqYQWDDLIAQHPPLEERPTRFPEQLAT-------LIYTSGTTGQPKGVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 236 ISqFqvlkGSFGlWA-------FGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKkfSASQFWNDCRKYNVTVF 308
Cdd:cd05932 157 LT-F----GSFA-WAaqagiehIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE--SLDTFVEDVQRARPTLF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 309 QYIGELC-----RYLCKQPQRE--------------GEKDHR------VRLAvGNGmSSDVWRQFLDRFGNI--KMCEFY 361
Cdd:cd05932 229 FSVPRLWtkfqqGVQDKIPQQKlnlllkipvvnslvKRKVLKglgldqCRLA-GCG-SAPVPPALLEWYRSLglNILEAY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 362 GATEgnicfmnhtgkigsvgrvNFFYNLLfsfelikydfqkDEPLRNEQGWcycVRKGEPGLLVS-------RVNKKNPF 434
Cdd:cd05932 307 GMTE------------------NFAYSHL------------NYPGRDKIGT---VGNAGPGVEVRisedgeiLVRSPALM 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 435 FGYtgsYKQ-TKSKLLFDvfkkGDVYFNTGDLMFQDHENFLYFWDRIGDTFRW-KGENVATTEVANVLGRLDFIQEANVY 512
Cdd:cd05932 354 MGY---YKDpEATAEAFT----ADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
....*
gi 149064320 513 GVPVP 517
Cdd:cd05932 427 GSGLP 431
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
56-238 |
6.08e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 58.75 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 56 VLDKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHaLLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFL 135
Cdd:PRK04813 4 IIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAA-FIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 136 NSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEIlpslpkhirvwgmkdsvpeGIVSLKE-KLSLASDEPVPPSHHVtsS 214
Cdd:PRK04813 83 DVSSPAERIEMIIEVAKPSLIIATEELPLEILGI-------------------PVITLDElKDIFATGNPYDFDHAV--K 141
|
170 180
....*....|....*....|....
gi 149064320 215 LKSTCLYIFTSGTTGLPKAAVISQ 238
Cdd:PRK04813 142 GDDNYYIIFTSGTTGKPKGVQISH 165
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
68-306 |
6.58e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 58.81 E-value: 6.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 68 PKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHC 147
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRG-IGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 148 IRTSEPKAMVVGEDLLGSLEEILPSLP-KHIRVWGMKDSVPEG---IVSLKEKLSLASDEP----VPPSHHVTS-SLKst 218
Cdd:PRK08162 111 LRHGEAKVLIVDTEFAEVAREALALLPgPKPLVIDVDDPEYPGgrfIGALDYEAFLASGDPdfawTLPADEWDAiALN-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 219 clyiFTSGTTGLPK--------AAVISQFQVLKgsfglWAFGCTAddiVYI-TLPLYHSSG-----ALLGIGGcvelgaT 284
Cdd:PRK08162 189 ----YTSGTTGNPKgvvyhhrgAYLNALSNILA-----WGMPKHP---VYLwTLPMFHCNGwcfpwTVAARAG------T 250
|
250 260
....*....|....*....|..
gi 149064320 285 CVLKKKFSASQFWNDCRKYNVT 306
Cdd:PRK08162 251 NVCLRKVDPKLIFDLIREHGVT 272
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
67-308 |
8.14e-09 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 58.32 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 67 QPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLH 146
Cdd:PLN02479 33 HPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRS-IGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 147 CIRTSEPKAMVVGEDLLGSLEEILPSL---------PKHIRVWGMKDSVPEgivSLKEKLS---------LASDEP---- 204
Cdd:PLN02479 112 LLEHSKSEVVMVDQEFFTLAEEALKILaekkkssfkPPLLIVIGDPTCDPK---SLQYALGkgaieyekfLETGDPefaw 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 205 VPPShhvtSSLKSTCLYiFTSGTTGLPKAAVISQfqvlKGSFgLWAFGCTA-----DDIVYI-TLPLYHSSG-------- 270
Cdd:PLN02479 189 KPPA----DEWQSIALG-YTSGTTASPKGVVLHH----RGAY-LMALSNALiwgmnEGAVYLwTLPMFHCNGwcftwtla 258
|
250 260 270
....*....|....*....|....*....|....*...
gi 149064320 271 ALLGIGGCVelgatcvlkKKFSASQFWNDCRKYNVTVF 308
Cdd:PLN02479 259 ALCGTNICL---------RQVTAKAIYSAIANYGVTHF 287
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
44-353 |
1.42e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 57.71 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 44 MEIYKLRGELVtvldkflsharrqpkkafiiyegDVYTYEDVDKRSNRVAHALLNHsDLKRGDVVALLMSNEPDFVHVWF 123
Cdd:PRK09192 37 MNFYDRRGQLE-----------------------EALPYQTLRARAEAGARRLLAL-GLKPGDRVALIAETDGDFVEAFF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 124 GLAKLGCV-------VAFLNSNLRFESLLHCIRTSEPKAMVVGEDLLGSLEEILPSLP-KHIRVWGMKDSVPEGIVSLKe 195
Cdd:PRK09192 93 ACQYAGLVpvplplpMGFGGRESYIAQLRGMLASAQPAAIITPDELLPWVNEATHGNPlLHVLSHAWFKALPEADVALP- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 196 klslasdepvPPSHHVTSSLKstclyiFTSGTTGLPKAAVISQFQVLKGSFGLWAFGCT--ADDIVYITLPLYHSsgalL 273
Cdd:PRK09192 172 ----------RPTPDDIAYLQ------YSSGSTRFPRGVIITHRALMANLRAISHDGLKvrPGDRCVSWLPFYHD----M 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 274 GIGGCVELGATCVLKKKFSASQ-F------WNDCRKYN---VTVFQYIG-ELCrylckqPQREGEKDH------RVRLAv 336
Cdd:PRK09192 232 GLVGFLLTPVATQLSVDYLPTRdFarrplqWLDLISRNrgtISYSPPFGyELC------ARRVNSKDLaeldlsCWRVA- 304
|
330 340
....*....|....*....|
gi 149064320 337 GNG---MSSDVWRQFLDRFG 353
Cdd:PRK09192 305 GIGadmIRPDVLHQFAEAFA 324
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
77-270 |
1.79e-08 |
|
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: 57.44 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 77 GDV-YTYEDVDKRSNRVAHALlnhSDL--KRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEP 153
Cdd:cd05915 21 EVHrTTYAEVYQRARRLMGGL---RALgvGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAED 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 154 KAMVVGEDLLGSLEEILpSLPKHIRVWGMKDSVPEgivSLKEKLSLASD--EPVPPSHHVTSSLKStclyiFTSGTTGLP 231
Cdd:cd05915 98 KVLLFDPNLLPLVEAIR-GELKTVQHFVVMDEKAP---EGYLAYEEALGeeADPVRVPERAACGMA-----YTTGTTGLP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 149064320 232 KAAVISQfqvlKGSF-GLWAFGCTADDI-----VYI-TLPLYHSSG 270
Cdd:cd05915 169 KGVVYSH----RALVlHSLAASLVDGTAlsekdVVLpVVPMFHVNA 210
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
74-294 |
2.50e-08 |
|
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: 56.68 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 74 IYEGDVYTYEDVDKRSNRVaHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEP 153
Cdd:cd05914 2 YYGGEPLTYKDLADNIAKF-ALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 154 KAMVVGEdllgsleeilpslpkhirvwgmkdsvpegivslKEKLSlasdepvppshhvtsslkstcLYIFTSGTTGLPKA 233
Cdd:cd05914 81 KAIFVSD---------------------------------EDDVA---------------------LINYTSGTTGNSKG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149064320 234 AVISQFQVLKGSFGLWAFG-CTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKKKFSAS 294
Cdd:cd05914 107 VMLTYRNIVSNVDGVKEVVlLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSA 168
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-556 |
2.79e-08 |
|
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: 56.24 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 220 LYI-FTSGTTGLPKAAVISQFQVLKGSFGLWAFGCTADDIVYITL---------------PLYHSSGALLGIGGCVELGA 283
Cdd:cd05924 6 LYIlYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHkaaaaaagtvmfpapPLMHGTGSWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 284 TCVLKKKFSASQFWNDCRKYNVTVFQYIGE-LCRYLCKQPQREGEKDHRVRLAVGNG---MSSDVWRQFLDRFGNIKMCE 359
Cdd:cd05924 86 VVLPDDRFDPEEVWRTIEKHKVTSMTIVGDaMARPLIDALRDAGPYDLSSLFAISSGgalLSPEVKQGLLELVPNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 360 FYGATE-GNICFMNHTGKIGSVGrvnFFYNLLFSFELIKYDFQKDEPLRNEQGWcyCVRKGEPGLlvsrvnkknpffGYT 438
Cdd:cd05924 166 AFGSSEtGFTGSGHSAGSGPETG---PFTRANPDTVVLDDDGRVVPPGSGGVGW--IARRGHIPL------------GYY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 439 GSYKQTKSKLlfdvFKKGDV-YFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVP 517
Cdd:cd05924 229 GDEAKTAETF----PEVDGVrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDE 304
|
330 340 350
....*....|....*....|....*....|....*....
gi 149064320 518 GYeGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPR 556
Cdd:cd05924 305 RW-GQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPK 342
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
80-517 |
3.02e-08 |
|
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: 56.42 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHaLLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAflnsnlrfesllhcirtsePKAMVVG 159
Cdd:cd05974 1 VSFAEMSARSSRVAN-FLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVI-------------------PATTLLT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 160 EDLLgsleeilpslpkhirvwgmKDSVPEG--IVSLKEKLSLASDePVppshhvtsslkstcLYIFTSGTTGLPKAAVIS 237
Cdd:cd05974 61 PDDL-------------------RDRVDRGgaVYAAVDENTHADD-PM--------------LLYFTSGTTSKPKLVEHT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 238 QFQVLKGSFG-LWAFGCTADDIVY-ITLP-----LYHSSGALLGIGGCVELgatcVLKKKFSASQFWNDCRKYNVTVFQY 310
Cdd:cd05974 107 HRSYPVGHLStMYWIGLKPGDVHWnISSPgwakhAWSCFFAPWNAGATVFL----FNYARFDAKRVLAALVRYGVTTLCA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 311 IGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQfLDRFGNIKMCEFYGATEGNICFMNHTG---KIGSVGRvnffy 387
Cdd:cd05974 183 PPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQ-VRRAWGLTIRDGYGQTETTALVGNSPGqpvKAGSMGR----- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 388 nllfsfELIKYDFQKDEPLRNEqgwcycVRKGEPGLLVSRVNKKNPFFGYTGSYKQTKSKLlfdvfkkGDVYFNTGDLMF 467
Cdd:cd05974 257 ------PLPGYRVALLDPDGAP------ATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAM 317
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 149064320 468 QDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVygVPVP 517
Cdd:cd05974 318 RDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV--VPSP 365
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
81-572 |
6.97e-08 |
|
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: 55.17 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 81 TYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVvge 160
Cdd:cd17650 14 TYRELNERANQLARTLRGLG-VAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 161 dllgsleeILPSLPKHIrvwgmkdsvpegivslkeklslasdepvppshhvtsslkstclyIFTSGTTGLPKAAVISQFQ 240
Cdd:cd17650 90 --------TQPEDLAYV--------------------------------------------IYTSGTTGKPKGVMVEHRN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 241 VL------KGSFGLWAFGCTADDIVYITLPLYHSSGAL-LGIGGCVelgATCVLKKKFSASQFWNDCRKYNVTVFQYIGE 313
Cdd:cd17650 118 VAhaahawRREYELDSFPVRLLQMASFSFDVFAGDFARsLLNGGTL---VICPDEVKLDPAALYDLILKSRITLMESTPA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 314 LCRYLCKQPQREGEKDHRVR-LAVGNGMSSDVW-RQFLDRFG-NIKMCEFYGATEGNICFMNHTGKIGSVGRVNF----- 385
Cdd:cd17650 195 LIRPVMAYVYRNGLDLSAMRlLIVGSDGCKAQDfKTLAARFGqGMRIINSYGVTEATIDSTYYEEGRDPLGDSANvpigr 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 386 ------FYNLlfsfelikydfqkdEPLRNEQ-----GWCYCVRKGepgllVSRvnkknpffGYTGSYKQTKSKLLFDVFK 454
Cdd:cd17650 275 plpntaMYVL--------------DERLQPQpvgvaGELYIGGAG-----VAR--------GYLNRPELTAERFVENPFA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 455 KGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVygVPVPGYEGKAGMTSIILkPNK 534
Cdd:cd17650 328 PGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVV--AVREDKGGEARLCAYVV-AAA 404
|
490 500 510
....*....|....*....|....*....|....*...
gi 149064320 535 SLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKL 572
Cdd:cd17650 405 TLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
219-579 |
4.65e-07 |
|
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: 51.95 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 219 CLYIFTSGTTGLPKAAVISQFQVLKGSFGLWAF-GCTADDIVYITLPLYHssgallgIGG------CVELGATCVLKKKF 291
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRlGFGGGDSWLLSLPLYH-------VGGlailvrSLLAGAELVLLERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 292 SASQfwNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNG-MSSDVWRQFLDRfgNIKMCEFYGATE--GNI 368
Cdd:cd17630 76 QALA--EDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGApIPPELLERAADR--GIPLYTTYGMTEtaSQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 369 CfmnhTG-----KIGSVGRVnffynllfsFELIKYDFQKDEplrneqgwcyCVRKGEPGLlvsrvnkknpFFGYtgsykq 443
Cdd:cd17630 152 A----TKrpdgfGRGGVGVL---------LPGRELRIVEDG----------EIWVGGASL----------AMGY------ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 444 TKSKLLFDVFKKGdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPGYegka 523
Cdd:cd17630 193 LRGQLVPEFNEDG--WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEEL---- 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 149064320 524 GMTSI-ILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQLVE 579
Cdd:cd17630 267 GQRPVaVIVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
80-513 |
5.26e-07 |
|
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: 52.36 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHALLnHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVg 159
Cdd:cd17640 6 ITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 160 edllgsleeilpslpkhirvwgmkDSVPEGIVSLkeklslasdepvppshhvtsslkstclyIFTSGTTGLPKAAVISQF 239
Cdd:cd17640 84 ------------------------ENDSDDLATI----------------------------IYTSGTTGNPKGVMLTHA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 240 QVLKGSFGLWAFGCT-ADDIVYITLPLYHSSGALlgiggCVELGATCVLKKKFSA-SQFWNDCRKYNVTVFQYIGELCRY 317
Cdd:cd17640 112 NLLHQIRSLSDIVPPqPGDRFLSILPIWHSYERS-----AEYFIFACGCSQAYTSiRTLKDDLKRVKPHYIVSVPRLWES 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 318 LCKQPQREGEKDHRVR------LAVGN-------GMSSDVwrQFLDRFGN---IKMCEFYGATEgnicfmnhTGKIGSVG 381
Cdd:cd17640 187 LYSGIQKQVSKSSPIKqflflfFLSGGifkfgisGGGALP--PHVDTFFEaigIEVLNGYGLTE--------TSPVVSAR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 382 RvnFFYNLLFSFELIKYD--FQKDEPLRNEqgwcyCVRKGEPGLLVSR---VNKknpffGYtgsYKQ--TKSKLLFDvfk 454
Cdd:cd17640 257 R--LKCNVRGSVGRPLPGteIKIVDPEGNV-----VLPPGEKGIVWVRgpqVMK-----GY---YKNpeATSKVLDS--- 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 455 kgDVYFNTGDLMFQDHENFLYFWDRIGDTFRWK-GENVATTEVANVLGRLDFIQEANVYG 513
Cdd:cd17640 319 --DGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
60-572 |
6.29e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.04 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 60 FLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLnHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNL 139
Cdd:PRK12316 3063 FEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLI-ERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 140 RFESLLHCIRTSepkamvvGEDLLGSLEEILPSLPKHIRVWgMKDSVPEGIvslkeklslasDEPVPPSHHVTSSLKSTc 219
Cdd:PRK12316 3142 PEERLAYMLEDS-------GAQLLLSQSHLRLPLAQGVQVL-DLDRGDENY-----------AEANPAIRTMPENLAYV- 3201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 220 lyIFTSGTTGLPKAAVISQFQVLKGSFGLW-AFGCTADDIVyITLPLYHSSGALLGIGGCVELGATCVLkkkfSASQFWN 298
Cdd:PRK12316 3202 --IYTSGSTGKPKGVGIRHSALSNHLCWMQqAYGLGVGDRV-LQFTTFSFDVFVEELFWPLMSGARVVL----AGPEDWR 3274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 299 DCRKY-------NVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFldrFGNIKMCEFYGATEGNICFM 371
Cdd:PRK12316 3275 DPALLvelinseGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQV---FAGLPLYNLYGPTEATITVT 3351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 372 NHTGKIGSVGRVNFFYNLLFSFELIKYDFQKDEPlrneQGWCYCVRKGEPGLLVsrvnkknpffGYTGSYKQTKSKLLFD 451
Cdd:PRK12316 3352 HWQCVEEGKDAVPIGRPIANRACYILDGSLEPVP----VGALGELYLGGEGLAR----------GYHNRPGLTAERFVPD 3417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 452 VFKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVpvpgyEGKAGMTSIILK 531
Cdd:PRK12316 3418 PFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV-----DGRQLVAYVVPE 3492
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 149064320 532 PNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKL 572
Cdd:PRK12316 3493 DEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKL 3533
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
81-238 |
7.21e-07 |
|
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: 52.36 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 81 TYEDVDKRSNRVAHALLnHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVVGE 160
Cdd:cd05933 10 TYKEYYEACRQAAKAFL-KLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 161 D-LLGSLEEILPSLPKHIRVWGMKDSVPE---GIVSLKEKLSLASDEPVPPSHHVTSSLKST--CLYIFTSGTTGLPKAA 234
Cdd:cd05933 89 QkQLQKILQIQDKLPHLKAIIQYKEPLKEkepNLYSWDEFMELGRSIPDEQLDAIISSQKPNqcCTLIYTSGTTGMPKGV 168
|
....
gi 149064320 235 VISQ 238
Cdd:cd05933 169 MLSH 172
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
81-275 |
8.69e-07 |
|
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: 51.69 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 81 TYEDVDKRSNRVAHALlNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVvge 160
Cdd:cd05910 4 SFRELDERSDRIAQGL-TAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 161 dllgsleeilpSLPKhirvwgmkdsvpegivslkeklslaSDEPVppshhvtsslkstcLYIFTSGTTGLPKAAVIS--- 237
Cdd:cd05910 80 -----------GIPK-------------------------ADEPA--------------AILFTSGSTGTPKGVVYRhgt 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 149064320 238 ---QFQVLKGSFGLwafgcTADDIVYITLPLYHSSGALLGI 275
Cdd:cd05910 110 faaQIDALRQLYGI-----RPGEVDLATFPLFALFGPALGL 145
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
56-237 |
9.04e-07 |
|
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: 51.77 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 56 VLDKFLSHARRQP-KKAFIIYEGDVyTYEDVDKRSNRVAHaLLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAF 134
Cdd:cd05918 1 VHDLIEERARSQPdAPAVCAWDGSL-TYAELDRLSSRLAH-HLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 135 LNsnlrfesllhcirtsepkamvvgedllgsleeilPSLPKHiRVWGMkdsvpegIVSLKEKLSLASDepvpPSHHvtss 214
Cdd:cd05918 79 LD----------------------------------PSHPLQ-RLQEI-------LQDTGAKVVLTSS----PSDA---- 108
|
170 180
....*....|....*....|....
gi 149064320 215 lkstcLY-IFTSGTTGLPKAAVIS 237
Cdd:cd05918 109 -----AYvIFTSGSTGKPKGVVIE 127
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
76-132 |
1.19e-06 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 51.58 E-value: 1.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 149064320 76 EGDVYTYEDVDKRSNRVAHALLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVV 132
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVP 67
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
68-238 |
2.42e-06 |
|
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: 50.37 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 68 PKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHC 147
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 148 IRTSEPKAMVVGEDLLGSLEEILPSLPkhIRVWGMKDSVPegivslkeklslASDEPVPPSHhvtsslksTCLYIFTSGT 227
Cdd:cd12116 80 LEDAEPALVLTDDALPDRLPAGLPVLL--LALAAAAAAPA------------APRTPVSPDD--------LAYVIYTSGS 137
|
170
....*....|.
gi 149064320 228 TGLPKAAVISQ 238
Cdd:cd12116 138 TGRPKGVVVSH 148
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
58-577 |
3.16e-06 |
|
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: 50.01 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 58 DKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHAlLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNS 137
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAAR-LRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 138 NLRFESLLHCIRTSEPKAMVVGEDLLGSLeeilpslpkhirvwgmkdsvpegivslkeklslasdepvppshhvtsslks 217
Cdd:cd12115 82 AYPPERLRFILEDAQARLVLTDPDDLAYV--------------------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 218 tclyIFTSGTTGLPKAAVISQFQVlkGSFGLWAFG-CTADDI--------------VY-ITLPLYHssgallgiGGCVEL 281
Cdd:cd12115 111 ----IYTSGSTGRPKGVAIEHRNA--AAFLQWAAAaFSAEELagvlastsicfdlsVFeLFGPLAT--------GGKVVL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 282 GATCVLKKKFSASQfwndcrkyNVTVFQYIGELCRYLCKQ---PQregekdhRVR---LAvGNGMSSDVWRQFLDRFGNI 355
Cdd:cd12115 177 ADNVLALPDLPAAA--------EVTLINTVPSAAAELLRHdalPA-------SVRvvnLA-GEPLPRDLVQRLYARLQVE 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 356 KMCEFYGATE----GNICFMN-HTGKIGSVGRvnffynllfsfelikydfqkdePLRNEQGWCY-----CVRKGEPGLL- 424
Cdd:cd12115 241 RVVNLYGPSEdttySTVAPVPpGASGEVSIGR----------------------PLANTQAYVLdralqPVPLGVPGELy 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 425 -----VSRvnkknpffGYTGSYKQTKSKLLFDVFKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANV 499
Cdd:cd12115 299 iggagVAR--------GYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAA 370
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149064320 500 LGRLDFIQEAnVYGVPVPGYEGKAGMTSIILKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd12115 371 LRSIPGVREA-VVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
125-267 |
3.42e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 50.10 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 125 LAKLGCVVAFLNSNLRFESLLHCIRTsepkaMVVgedlLGSLEEILPSLPKHIRVwgmkdsvpeGIVSLKEKLSLASDEP 204
Cdd:PLN02736 151 VAAIFCVPQTLNTLLSCLSEIPSVRL-----IVV----VGGADEPLPSLPSGTGV---------EIVTYSKLLAQGRSSP 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 205 VPPSHHVTSSLKSTClyiFTSGTTGLPKAAVISQFQVLKGSFGlwafgcTADDI------VYIT-LPLYH 267
Cdd:PLN02736 213 QPFRPPKPEDVATIC---YTSGTTGTPKGVVLTHGNLIANVAG------SSLSTkfypsdVHISyLPLAH 273
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
55-273 |
1.30e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 48.42 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 55 TVLDKFLSHARRQPKKAFII--YEGDVYTYEDVDKRSNrVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVV 132
Cdd:PRK06814 632 TLFEALIEAAKIHGFKKLAVedPVNGPLTYRKLLTGAF-VLGRKLKKN-TPPGENVGVMLPNANGAAVTFFALQSAGRVP 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 133 AFLNSNLRFESLLHCIRTSEPKAMVVGEDLL--GSLEEILPSLPKHIRVWGMKDsVPEGIvSLKEKL--SLASDEPVPPS 208
Cdd:PRK06814 710 AMINFSAGIANILSACKAAQVKTVLTSRAFIekARLGPLIEALEFGIRIIYLED-VRAQI-GLADKIkgLLAGRFPLVYF 787
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 209 HHVtsSLKSTCLYIFTSGTTGLPKAAVISQFQVLKGSFGLWA-FGCTADDIVYITLPLYHS----SGALL 273
Cdd:PRK06814 788 CNR--DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAArIDFSPEDKVFNALPVFHSfgltGGLVL 855
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
58-576 |
1.31e-05 |
|
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: 48.07 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 58 DKFLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNS 137
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLG-VVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 138 NLRFESLLHCIRTSEPKAMVvgedllgsleeilpslpkhirvwgmkdsvpegivslkeklslasdepvppshhVTSSLKS 217
Cdd:cd17653 80 KLPSARIQAILRTSGATLLL-----------------------------------------------------TTDSPDD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 218 TCLYIFTSGTTGLPKAAVISQFQVLK-------------GS-----FGLwAFGCTADDIVyitlplyhssgallgigGCV 279
Cdd:cd17653 107 LAYIIFTSGSTGIPKGVMVPHRGVLNyvsqpparldvgpGSrvaqvLSI-AFDACIGEIF-----------------STL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 280 ELGATCVLKKkfSASQFWNDCRKYNVT-------------VFQYIgelcrylckqpqregekdHRVRLAvGNGMSSDVwr 346
Cdd:cd17653 169 CNGGTLVLAD--PSDPFAHVARTVDALmstpsilstlspqDFPNL------------------KTIFLG-GEAVPPSL-- 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 347 qfLDRFG-NIKMCEFYGATEGNI-CFMNHT--GKIGSVGRV--NFFYNLLfsfelikyDFQKDEPLRNEQGWCYCVrkge 420
Cdd:cd17653 226 --LDRWSpGRRLYNAYGPTECTIsSTMTELlpGQPVTIGKPipNSTCYIL--------DADLQPVPEGVVGEICIS---- 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 421 pGLLVSRvnkknpffGYTGSYKQTKSKLLFDVFKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVL 500
Cdd:cd17653 292 -GVQVAR--------GYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVV 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 501 GRLD--------FIQEANVYGVPVPgyegkagmtsiilkpnKSLDLEKMYDQVVTSLPAYACP-RFLRIqDKMETTGTFK 571
Cdd:cd17653 363 LQSQpevtqaaaIVVNGRLVAFVTP----------------ETVDVDGLRSELAKHLPSYAVPdRIIAL-DSFPLTANGK 425
|
....*..
gi 149064320 572 L--KKLQ 576
Cdd:cd17653 426 VdrKALR 432
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
68-365 |
1.67e-05 |
|
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: 47.69 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 68 PKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCvvAFLNSNLRF--ESLL 145
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGG--AYVPIDPAYpvERIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 146 HCIRTSEPkAMVVGEdllgsleeilPSLPKHIrvwgmkdsvpegivslkeklslasdepvppshhvtsslkstclyIFTS 225
Cdd:cd17643 78 FILADSGP-SLLLTD----------PDDLAYV--------------------------------------------IYTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 226 GTTGLPKAAVISQFQVLkgsfGL-----WAFGCTADDIVYitlpLYHSS----------GALLGiggcvelGATCVLKKK 290
Cdd:cd17643 103 GSTGRPKGVVVSHANVL----ALfaatqRWFGFNEDDVWT----LFHSYafdfsvweiwGALLH-------GGRLVVVPY 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 291 F---SASQFWNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAV--GNGMSSDVWRQFLDRFGN-----IKMcef 360
Cdd:cd17643 168 EvarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLdrpqlVNM--- 244
|
....*
gi 149064320 361 YGATE 365
Cdd:cd17643 245 YGITE 249
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
80-279 |
2.13e-05 |
|
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: 47.60 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHALLNHS-DLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFESLLHCIRTSEPKAMVV 158
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGgKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 159 GEDLlgsleeilpslpkhirvwgmkdsvpeGIVSLKEKLSLASDEPVPpshHVTSSLKSTCLYIFTSGTTGLPKAAVISQ 238
Cdd:cd05927 86 DAGV--------------------------KVYSLEEFEKLGKKNKVP---PPPPKPEDLATICYTSGTTGNPKGVMLTH 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 149064320 239 FQVLKGSFGLWAFG-----CTADDiVYIT-LPLYHS-----SGALLGIGGCV 279
Cdd:cd05927 137 GNIVSNVAGVFKILeilnkINPTD-VYISyLPLAHIfervvEALFLYHGAKI 187
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
24-243 |
2.24e-05 |
|
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: 47.65 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 24 FPYFWDDLWFLLKLVRYgiqmeiyklRGELVTVLDK-------------------FLSHARRQPKKAFIIYEG---DVYT 81
Cdd:cd05943 30 PGAFWAAVWDFSGVRGS---------KPYDVVVVSGrimpgarwfpgarlnyaenLLRHADADDPAAIYAAEDgerTEVT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 82 YEDVDKRSNRVAHALLnHSDLKRGDVVALLMSNEPDFVHVWFGLAKLG-----CVVAF-LNSNL-RFESLlhcirtsEPK 154
Cdd:cd05943 101 WAELRRRVARLAAALR-ALGVKPGDRVAGYLPNIPEAVVAMLATASIGaiwssCSPDFgVPGVLdRFGQI-------EPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 155 AMVVGE---------DLLGSLEEI---LPSLPKHIRVWGMKDSVPEGIVSLKEKLSLASD-----------EPVPPSHHv 211
Cdd:cd05943 173 VLFAVDaytyngkrhDVREKVAELvkgLPSLLAVVVVPYTVAAGQPDLSKIAKALTLEDFlatgaagelefEPLPFDHP- 251
|
250 260 270
....*....|....*....|....*....|....*..
gi 149064320 212 tsslkstcLYI-FTSGTTGLPKAAVISQ----FQVLK 243
Cdd:cd05943 252 --------LYIlYSSGTTGLPKCIVHGAggtlLQHLK 280
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
60-577 |
3.25e-05 |
|
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: 46.78 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 60 FLSHARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHaLLNHSDLKRGDVVALLMSNEPDFVHVWFGLAKLGcvvaflnsnl 139
Cdd:cd17645 4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLAR-HLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAG---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 140 rfesllhcirtsepkamvvgedllGSLEEILPSLPKHIRVWGMKDSVPEGIVSLKEKLSLAsdepvppshhvtsslkstc 219
Cdd:cd17645 73 ------------------------GAYVPIDPDYPGERIAYMLADSSAKILLTNPDDLAYV------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 220 lyIFTSGTTGLPKAAVISQFQVLkgSFGLW---AFGCTADD--IVYITLPLyhsSGALLGIGGCVELGATCVL---KKKF 291
Cdd:cd17645 110 --IYTSGSTGLPKGVMIEHHNLV--NLCEWhrpYFGVTPADksLVYASFSF---DASAWEIFPHLTAGAALHVvpsERRL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 292 SASQFWNDCRKYNVTvfqyIGELCRYLCKQPQREGEKDHRVRLAVGngmssDVWRQFLDRfgNIKMCEFYGATEGNIcfm 371
Cdd:cd17645 183 DLDALNDYFNQEGIT----ISFLPTGAAEQFMQLDNQSLRVLLTGG-----DKLKKIERK--GYKLVNNYGPTENTV--- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 372 nhtgkigsvgrvnffynLLFSFELIK--YDFQKDEPLRNEQgwCYCVRKGepgLLVSRVNKKNPFF--------GYTGSY 441
Cdd:cd17645 249 -----------------VATSFEIDKpyANIPIGKPIDNTR--VYILDEA---LQLQPIGVAGELCiageglarGYLNRP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 442 KQTKSKLLFDVFKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVpvpgyEG 521
Cdd:cd17645 307 ELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAK-----ED 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 149064320 522 KAGMTSII--LKPNKSLDLEKMYDQVVTSLPAYACPRFLRIQDKMETTGTFKLKKLQL 577
Cdd:cd17645 382 ADGRKYLVayVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
81-381 |
5.14e-05 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 46.27 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 81 TYEDVDKRSNRVAHALLNHsDLKRGDVVALLMSNEPDFVHVWFGLAKLG---CVV--AFLNSNLRFESLLHCIRTSEPkA 155
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDL-GLSAERPLLILSGNSIEHALMALAAMYAGvpaAPVspAYSLMSQDLAKLKHLFELLKP-G 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 156 MVVGED---LLGSLEEILPSLPKHIRVWGMKDSvpEGIVSLKEKLSLASDEPVPPSHHVTSSlKSTCLYIFTSGTTGLPK 232
Cdd:cd05921 105 LVFAQDaapFARALAAIFPLGTPLVVSRNAVAG--RGAISFAELAATPPTAAVDAAFAAVGP-DTVAKFLFTSGSTGLPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 233 AAVISQFQ---VLKGSFGLWAFGCTADDIVYITLPLYHSSGALLGIGGCVELGATCVLKK-KFSASQFWNDCRK------ 302
Cdd:cd05921 182 AVINTQRMlcaNQAMLEQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDDgKPMPGGFEETLRNlreisp 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 303 -YNVTVFQYIGELCRYLCKQP--QREGEKDHRVRLAVGNGMSSDVWRQfLDRFG------NIKMCEFYGATE-GNICFMN 372
Cdd:cd05921 262 tVYFNVPAGWEMLVAALEKDEalRRRFFKRLKLMFYAGAGLSQDVWDR-LQALAvatvgeRIPMMAGLGATEtAPTATFT 340
|
330
....*....|.
gi 149064320 373 H--TGKIGSVG 381
Cdd:cd05921 341 HwpTERSGLIG 351
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
204-491 |
1.42e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 44.73 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 204 PVPPSHHvtsslkstcLYI-FTSGTTGLPKAAVISQFQVLKGSFGLWAFgCTADDIVyiTLPLYHSS-GAL---LGIGGC 278
Cdd:PTZ00237 250 PVESSHP---------LYIlYTSGTTGNSKAVVRSNGPHLVGLKYYWRS-IIEKDIP--TVVFSHSSiGWVsfhGFLYGS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 279 VELGATCVL------KKKFSASQFWNDCRKYNVTVFQYIGELCRYLCKQpQREGEKDHR-------VRLAVGNGMSSDVW 345
Cdd:PTZ00237 318 LSLGNTFVMfeggiiKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKT-DPEATIIRSkydlsnlKEIWCGGEVIEESI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 346 RQFLDRFGNIKMCEFYGATEGNICFmnhtgkIGSVGRVNFFYNLL-FSFELIKYD-FQKDEPLRNEQgwcycvrkgEPGL 423
Cdd:PTZ00237 397 PEYIENKLKIKSSRGYGQTEIGITY------LYCYGHINIPYNATgVPSIFIKPSiLSEDGKELNVN---------EIGE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149064320 424 LVSRVnKKNPFFGYTGSYKQTKSKLLFDVFKKgdvYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENV 491
Cdd:PTZ00237 462 VAFKL-PMPPSFATTFYKNDEKFKQLFSKFPG---YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKV 525
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
222-514 |
1.43e-04 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 44.89 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 222 IFTSGTTGLPKAAVISQ--FQVLKGSFGLWAFG--------CTAdDIVYITLPLYHSSGALLGiggcvelGATCVLKKKF 291
Cdd:PLN02654 281 LYTSGSTGKPKGVLHTTggYMVYTATTFKYAFDykptdvywCTA-DCGWITGHSYVTYGPMLN-------GATVLVFEGA 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 292 ----SASQFWNDCRKYNVTVFQYIGELCRYLCKQP----QREGEKDHRVRLAVGNGMSSDVWRQFLDRFGNIK--MCEFY 361
Cdd:PLN02654 353 pnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyvTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRcpISDTW 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 362 GATE-GNICFMNHTG----KIGSVgrvnffynlLFSFelikYDFQK---DEPLRNEQGWC---YCVRKGEPGLLVSrvnk 430
Cdd:PLN02654 433 WQTEtGGFMITPLPGawpqKPGSA---------TFPF----FGVQPvivDEKGKEIEGECsgyLCVKKSWPGAFRT---- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 431 knpFFGYTGSYKQTkskllfdVFKKGDVYFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEAN 510
Cdd:PLN02654 496 ---LYGDHERYETT-------YFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAA 565
|
....
gi 149064320 511 VYGV 514
Cdd:PLN02654 566 VVGI 569
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
224-365 |
2.70e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 43.60 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 224 TSGTTGLPKAAVISQ--FQVLKGSF--GLWAFGCTADDIVYITLPlYH-SSGALLGIGGCVELGATCVlkkkfSAS---- 294
Cdd:COG1541 91 SSGTTGKPTVVGYTRkdLDRWAELFarSLRAAGVRPGDRVQNAFG-YGlFTGGLGLHYGAERLGATVI-----PAGggnt 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 295 ----QFwndCRKYNVTVFqyigeLC-----RYLCKQPQREGE--KDHRVRLAV-GNGMSSDVWRQFL-DRFGnIKMCEFY 361
Cdd:COG1541 165 erqlRL---MQDFGPTVL-----VGtpsylLYLAEVAEEEGIdpRDLSLKKGIfGGEPWSEEMRKEIeERWG-IKAYDIY 235
|
....
gi 149064320 362 GATE 365
Cdd:COG1541 236 GLTE 239
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
73-236 |
3.97e-04 |
|
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: 43.40 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 73 IIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGcvVAFLnsnlrfesllhcirtse 152
Cdd:cd17652 6 VVFGDETLTYAELNARANRLARLLAARG-VGPERLVALALPRSAELVVAILAVLKAG--AAYL----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 153 PkamvvgedllgsleeILPSLPKHiRVWGM-KDSVPEGIVSLKEKLSlasdepvppshhvtsslkstclY-IFTSGTTGL 230
Cdd:cd17652 66 P---------------LDPAYPAE-RIAYMlADARPALLLTTPDNLA----------------------YvIYTSGSTGR 107
|
....*.
gi 149064320 231 PKAAVI 236
Cdd:cd17652 108 PKGVVV 113
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
66-232 |
5.39e-04 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 43.05 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 66 RQPKKAFIIYEGDVYTYEDVDKRSNRVAHALLNHSdLKRGDVVALLMSNEPDFVHVWFGLAKLGCV-VAFLNSNLRFEsL 144
Cdd:PRK10946 35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQG-IKPGDTALVQLGNVAEFYITFFALLKLGVApVNALFSHQRSE-L 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 145 LHCIRTSEPKAMVV--------GEDLLGSLEEILPSLpkhiRVWGMKDSvpEGIVSLKEKLSLASDEPVP---PSHHVTs 213
Cdd:PRK10946 113 NAYASQIEPALLIAdrqhalfsDDDFLNTLVAEHSSL----RVVLLLND--DGEHSLDDAINHPAEDFTAtpsPADEVA- 185
|
170
....*....|....*....
gi 149064320 214 slkstcLYIFTSGTTGLPK 232
Cdd:PRK10946 186 ------FFQLSGGSTGTPK 198
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
63-368 |
9.15e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 63 HARRQPKKAFIIYEGDVYTYEDVDKRSNRVAHALlnhSDLKRG-DV-VALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLR 140
Cdd:PRK05691 1140 QARQTPERIALVWDGGSLDYAELHAQANRLAHYL---RDKGVGpDVcVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYP 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 141 FESLLHCIRTSepkamvvGEDLLGSLEEILPSLPKhirvwgmkdsvPEGIVSLK-EKLSLASDEPVPPSHHVTSSlkSTC 219
Cdd:PRK05691 1217 AERLAYMLADS-------GVELLLTQSHLLERLPQ-----------AEGVSAIAlDSLHLDSWPSQAPGLHLHGD--NLA 1276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 220 LYIFTSGTTGLPK------AAVISQFQVLKGSFGLwafgcTADDIVYITLPLYHSSGA----LLGIGGC-VELGATCVLK 288
Cdd:PRK05691 1277 YVIYTSGSTGQPKgvgnthAALAERLQWMQATYAL-----DDSDVLMQKAPISFDVSVwecfWPLITGCrLVLAGPGEHR 1351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 289 KKFSASQFwndCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRLAVGNGMSSDVWRQFLDRFGNIKMCEFYGATEGNI 368
Cdd:PRK05691 1352 DPQRIAEL---VQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAI 1428
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
81-276 |
1.45e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 41.64 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 81 TYEDVDKRSNRVAHAL--LNHsdlKRGDVVALLMSNEPDfvhvWFgLAKLGC-----VVAFLNSNLRFESLLHCIRTSEP 153
Cdd:PLN02387 108 TYGQVFERVCNFASGLvaLGH---NKEERVAIFADTRAE----WL-IALQGCfrqniTVVTIYASLGEEALCHSLNETEV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 154 KAMVVGEDLLGSLEEILPSLPKHIRVWGMKDSVPEG-----------IVSLKEKLSLASDEPVPPShhvTSSLKSTCLYI 222
Cdd:PLN02387 180 TTVICDSKQLKKLIDISSQLETVKRVIYMDDEGVDSdsslsgssnwtVSSFSEVEKLGKENPVDPD---LPSPNDIAVIM 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149064320 223 FTSGTTGLPKAAVISQFQVLKGSFGLWAF--GCTADDIVYITLPLYH-----------SSGALLGIG 276
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNIVATVAGVMTVvpKLGKNDVYLAYLPLAHilelaaesvmaAVGAAIGYG 323
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
222-368 |
2.27e-03 |
|
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: 40.88 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 222 IFTSGTTGLPKAAVISQFQVLKGSFGLWAfgctaddIVYITLPLYHSSGALLGIGGCVE-------LGATCVL---KKKF 291
Cdd:cd17644 112 IYTSGSTGKPKGVMIEHQSLVNLSHGLIK-------EYGITSSDRVLQFASIAFDVAAEeiyvtllSGATLVLrpeEMRS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 292 SASQFWNDCRKYNVTVF--------QYIGELCRYLCKQPqregekdHRVRLAV--GNGMSSDVWRQFLDRFGN-IKMCEF 360
Cdd:cd17644 185 SLEDFVQYIQQWQLTVLslppaywhLLVLELLLSTIDLP-------SSLRLVIvgGEAVQPELVRQWQKNVGNfIQLINV 257
|
....*...
gi 149064320 361 YGATEGNI 368
Cdd:cd17644 258 YGPTEATI 265
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
80-129 |
3.85e-03 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 40.43 E-value: 3.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 149064320 80 YTYEDVDKRSNRVAHALLNhSDLKRGDVVALLMSNEPDFVHVWFGLAKLG 129
Cdd:TIGR03443 271 FTYKQINEASNILAHYLLK-TGIKRGDVVMIYAYRGVDLVVAVMGVLKAG 319
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
459-556 |
3.89e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 39.98 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 459 YFNTGDLMFQDHENFLYFWDRIGDTFRWKGENVATTEVANVLGRLDFIQEANVYGVPVPgYEGKAgMTSIILKPNKSLDL 538
Cdd:PRK07445 325 IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDP-HWGEV-VTAIYVPKDPSISL 402
|
90
....*....|....*...
gi 149064320 539 EKMYDQVVTSLPAYACPR 556
Cdd:PRK07445 403 EELKTAIKDQLSPFKQPK 420
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
224-365 |
5.72e-03 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 39.53 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064320 224 TSGTTGLPK-----AAVISQFQVLKgSFGLWAFGCTADDIVYITlPLYHSSGALLGI-GGCVELGATCVlkkKFSASQF- 296
Cdd:cd05913 86 SSGTTGKPTvvgytKNDLDVWAELV-ARCLDAAGVTPGDRVQNA-YGYGLFTGGLGFhYGAERLGALVI---PAGGGNTe 160
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149064320 297 --WNDCRKYNVTVFQYIGELCRYLCKQPQREGEKDHRVRL---AVGNGMSSDVWRQFLDRFGNIKMCEFYGATE 365
Cdd:cd05913 161 rqLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRELSLkvgIFGAEPWTEEMRKRIERRLGIKAYDIYGLTE 234
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
211-267 |
8.43e-03 |
|
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: 39.12 E-value: 8.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149064320 211 VTSSLKST-CLYIFTSGTTGLPKAAVISQFQVLKGSFGL--WAFGCTADDIVYIT-LPLYH 267
Cdd:cd17639 82 FTDGKPDDlACIMYTSGSTGNPKGVMLTHGNLVAGIAGLgdRVPELLGPDDRYLAyLPLAH 142
|
|
| |
