|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
138-679 |
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: 980.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 138 EGSSITNSQLDARSCQAAWVLKaklkDAVIQNTRDAAAILVLPSKTisALSVFLGLAKLGCPVAWINPHSRGMPLLHSVR 217
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALL----AHAGLRPGDTVALLLGNEPA--FLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 218 SSGASVLIVDPDLQENLEEVLPKLLAENIHCFYLGHSSPTPGVEALGASLDAAPSDPVPASLRATIKWKSPAIFIFTSGT 297
Cdd:cd05938 76 CCGAKVLVVAPELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 298 TGLPKPAILSHERVIQVSNVLSFCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTV 377
Cdd:cd05938 156 TGLPKAARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 378 ILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANVWKNFQQRFGPIRIWEFYGSTEGNVGLMNYVGHCGAVGRTSCIL 457
Cdd:cd05938 236 IQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 458 RMLTPFELVQFDIETAEPLRDKQGFCIPVEPGKPGLLLTKVRKNQPFLGYRGSQAESNRKLVANVRRVGDLYFNTGDVLT 537
Cdd:cd05938 316 KLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSPFLGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 538 LDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEGKVGMAAVKLAPGKTFDGQKLYQHVRS 617
Cdd:cd05938 396 QDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVRE 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 228008365 618 WLPAYATPHFIRIQDSLEITNTYKLVKSRLVREGFDVGIIADPLYILDNKAQTFRSLMPDVY 679
Cdd:cd05938 476 YLPAYARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
100-685 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 628.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 100 GLKFRRRLNKHPPETFVDALERQALAWPDRVALVctgSEGSSITNSQLDARSCQAAWVLKAK-LK--DAV---IQNTRDA 173
Cdd:PRK08279 24 GLKRTALITPDSKRSLGDVFEEAAARHPDRPALL---FEDQSISYAELNARANRYAHWAAARgVGkgDVVallMENRPEY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 174 AAILvlpsktisalsvfLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAENIHCFYLG- 252
Cdd:PRK08279 101 LAAW-------------LGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGd 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 253 HSSPTPGVEALGASLDAAPSDPvPASlRATIKWKSPAIFIFTSGTTGLPKPAILSHERVIQVSNVLS-FCGCRADDVVYD 331
Cdd:PRK08279 168 TLDDPEGYEDLAAAAAGAPTTN-PAS-RSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGgLLRLTPDDVLYC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 332 VLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLR 411
Cdd:PRK08279 246 CLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGLR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 412 ANVWKNFQQRFGPIRIWEFYGSTEGNVGLMNYVGHCGAVGRtsCILRMLTPFELVQFDIETAEPLRDKQGFCIPVEPGKP 491
Cdd:PRK08279 326 PDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGR--VPLWLAHPYAIVKYDVDTGEPVRDADGRCIKVKPGEV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 492 GLLLTKVRKNQPFLGYRgSQAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLS 571
Cdd:PRK08279 404 GLLIGRITDRGPFDGYT-DPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 572 SLDFLEEVNVYGVPVPGCEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVREG 651
Cdd:PRK08279 483 GFPGVEEAVVYGVEVPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRKEG 562
|
570 580 590
....*....|....*....|....*....|....
gi 228008365 652 FDVGIIADPLYILDNKAQTFRSLMPDVYQAVCEG 685
Cdd:PRK08279 563 FDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAG 596
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
139-653 |
1.22e-179 |
|
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: 518.83 E-value: 1.22e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 139 GSSITNSQLDARSCQAAWVLKA---KLKDAVIqntrdaaaiLVLPSKtISALSVFLGLAKLGCPVAWINPHSRGMPLLHS 215
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSlglKPGDVVA---------LFMENR-PEYVLLWLGLVKIGAVAALINYNLRGESLAHC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 216 VRSSGASVLIVDPdlqenleevlpkllaenihCFYlghssptpgvealgasldaapsdpvpaslratikwkspaifIFTS 295
Cdd:cd05940 71 LNVSSAKHLVVDA-------------------ALY-----------------------------------------IYTS 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 296 GTTGLPKPAILSHERVIQVSNVLSFCGCRAD-DVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQHG 374
Cdd:cd05940 91 GTTGLPKAAIISHRRAWRGGAFFAGSGGALPsDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQ 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 375 VTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANVWKNFQQRFGPIRIWEFYGSTEGNVGLMNYVGHCGAVGRTS 454
Cdd:cd05940 171 ATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 455 CILRMLTPFELVQFDIETAEPLRDKQGFCIPVEPGKPGLLLTKVRKNQPFLGYRGSQAeSNRKLVANVRRVGDLYFNTGD 534
Cdd:cd05940 251 SLLRKVAPLALVKYDLESGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFDGYTDPAA-TEKKILRDVFKKGDAWFNTGD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 535 VLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEGKVGMAAVKLAPGKTFDGQKLYQH 614
Cdd:cd05940 330 LMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEEFDLSALAAH 409
|
490 500 510
....*....|....*....|....*....|....*....
gi 228008365 615 VRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVREGFD 653
Cdd:cd05940 410 LEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFD 448
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
189-653 |
2.71e-152 |
|
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: 449.95 E-value: 2.71e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 189 VFLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVD--PDLQENLEEVLPKllaenihcfylghsspTPGVEAlgas 266
Cdd:cd05939 44 LWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFNllDPLLTQSSTEPPS----------------QDDVNF---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 267 ldaapsdpvpaslratikwKSPAIFIFTSGTTGLPKPAILSHERVIQVSNVLSFC-GCRADDVVYDVLPLYHTIGLVLGF 345
Cdd:cd05939 104 -------------------RDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAfGMRPEDVVYDCLPLYHSAGGIMGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 346 LGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANVWKNFQQRFGPI 425
Cdd:cd05939 165 GQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 426 RIWEFYGSTEGNVGLMNYVGHCGAVGRTSCILRMLTPFELVQFDIETAEPLRDKQGFCIPVEPGKPGLLLTKVRKNQP-- 503
Cdd:cd05939 245 QIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRLIKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPlr 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 504 -FLGYRgSQAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVY 582
Cdd:cd05939 325 rFDGYV-NEGATNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVY 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228008365 583 GVPVPGCEGKVGMAAVkLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVREGFD 653
Cdd:cd05939 404 GVEVPGVEGRAGMAAI-VDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGYD 473
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
138-653 |
2.18e-128 |
|
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: 388.33 E-value: 2.18e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 138 EGSSITNSQLDARSCQ-AAWVLKA---KLKDAVIQNTRDAAAILVLpsktisalsvFLGLAKLGCPVAWINPHSRGMPLL 213
Cdd:cd05937 2 EGKTWTYSETYDLVLRyAHWLHDDlgvQAGDFVAIDLTNSPEFVFL----------WLGLWSIGAAPAFINYNLSGDPLI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 214 HSVRSSGASVLIVDPDlqenleevlpkllaenihcfylghssptpgvealgasldaapsdpvpaslratikwkSPAIFIF 293
Cdd:cd05937 72 HCLKLSGSRFVIVDPD---------------------------------------------------------DPAILIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 294 TSGTTGLPKPAILSHERVIQVSNVLS-FCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQ 372
Cdd:cd05937 95 TSGTTGLPKAAAISWRRTLVTSNLLShDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 373 HGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANVWKNFQQRFGPIRIWEFYGSTEGNVGLMNY-VGH--CGA 449
Cdd:cd05937 175 SGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnVGDfgAGA 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 450 VGRTSCILRMLTPFE--LVQFDIETAEPLRD-KQGFCIPVEPGKPGLLLTKVRKN--QPFLGYRGSQAESNRKLVANVRR 524
Cdd:cd05937 255 IGHHGLIRRWKFENQvvLVKMDPETDDPIRDpKTGFCVRAPVGEPGEMLGRVPFKnrEAFQGYLHNEDATESKLVRDVFR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 525 VGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEGKVGMAAVKL---- 600
Cdd:cd05937 335 KGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLeess 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 228008365 601 APGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVREGFD 653
Cdd:cd05937 415 AVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVD 467
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
115-650 |
7.38e-85 |
|
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: 274.38 E-value: 7.38e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 115 FVDALERQALAWPDRVALVCtgsEGSSITNSQLDARSCQ-AAWVLKAKLKdaviqnTRDAAAILVLPSktISALSVFLGL 193
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF---GGRRLTYAELDARARRlAAALRALGVG------PGDRVALLLPNS--PEFVVAFLAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 194 AKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVdpdlqenleevlpkllaenihcfylghssptpgvealgasldaapsd 273
Cdd:COG0318 70 LRAGAVVVPLNPRLTAEELAYILEDSGARALVT----------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 274 pvpaslratikwkspAIFIFTSGTTGLPKPAILSHERViqVSNVLSFC---GCRADDVVYDVLPLYHTIGLVLGFLGCLQ 350
Cdd:COG0318 103 ---------------ALILYTSGTTGRPKGVMLTHRNL--LANAAAIAaalGLTPGDVVLVALPLFHVFGLTVGLLAPLL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 351 VGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM--GNGLRANVWKNFQQRFGpIRIW 428
Cdd:COG0318 166 AGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFG-VRIV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 429 EFYGSTEGN-VGLMNYVGHC----GAVGRtscilrmltPFELVQFDIetaeplRDKQGfcIPVEPGKPGLLLtkVRKNQP 503
Cdd:COG0318 245 EGYGLTETSpVVTVNPEDPGerrpGSVGR---------PLPGVEVRI------VDEDG--RELPPGEVGEIV--VRGPNV 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 504 FLGYRGSQAESNRKLVanvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYG 583
Cdd:COG0318 306 MKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVG 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 228008365 584 VPVPGcEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVRE 650
Cdd:COG0318 379 VPDEK-WGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
119-652 |
1.73e-80 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 265.85 E-value: 1.73e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 119 LERQALAWPDRVALVCTGSEgssITNSQLDARSCQAAwvlkAKLKDAVIQNTrDAAAILVlpSKTISALSVFLGLAKLGC 198
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTR---WTYAEAARAAAAAA----HALAAAGVKRG-DRVALMC--GNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 199 PVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAenIHCFYLGHSSPTPGVEALGASLDAAPSD-PVPA 277
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLP--LPAVWLLDAPASVSVPAGWSTAPLPPLDaPAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 278 slrATIKWKSPAIFIFTSGTTGLPKPAILSHERV----IQVSNVLsfcGCRADDVVYDVLPLYHTIGLVLgFLGCLQVGA 353
Cdd:PRK06155 175 ---AAVQPGDTAAILYTSGTTGPSKGVCCPHAQFywwgRNSAEDL---EIGADDVLYTTLPLFHTNALNA-FFQALLAGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 354 TCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANVWKNFQQRFGpIRIWEFYGS 433
Cdd:PRK06155 248 TYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFG-VDLLDGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 434 TEGNVGLmnYVGH----CGAVGRtscilrmLTPfelvQFDIETAeplrDKQGfcIPVEPGKPGLLLtkVRKNQPFL---G 506
Cdd:PRK06155 327 TETNFVI--AVTHgsqrPGSMGR-------LAP----GFEARVV----DEHD--QELPDGEPGELL--LRADEPFAfatG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 507 YRGSQAesnrKLVANVRrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPV 586
Cdd:PRK06155 386 YFGMPE----KTVEAWR---NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPS 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 228008365 587 PGCEGKVgMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVREGF 652
Cdd:PRK06155 459 ELGEDEV-MAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGV 523
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-647 |
8.74e-78 |
|
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: 254.91 E-value: 8.74e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 139 GSSITNSQLDARSCQAAWVLKAKlkdAVIQNTRdaaaILVLPSKTISALSVFLGLAKLGCPVAWINPHSRGMPLLHSVRS 218
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAAL---GIRPGDR----VALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 219 SGASVLIVDPdlqenleevlpkllaenihcfylghssptpgvealgasldaapsdpvpaslratikwkspAIFIFTSGTT 298
Cdd:cd05934 74 SGAQLVVVDP------------------------------------------------------------ASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 299 GLPKPAILSHERVIQVSNVLS-FCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTV 377
Cdd:cd05934 94 GPPKGVVITHANLTFAGYYSArRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 378 ILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANVWKNFQQRFGpIRIWEFYGSTEGNVGLMNYVGHCGAVGrtscil 457
Cdd:cd05934 174 TNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG-VRLLEGYGMTETIVGVIGPRDEPRRPG------ 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 458 rmltPFELVQFDIETAepLRDKQGFciPVEPGKPG-LLLTKVRKNQPFLGYRGsQAESNRKLVANvrrvgdLYFNTGDVL 536
Cdd:cd05934 247 ----SIGRPAPGYEVR--IVDDDGQ--ELPAGEPGeLVIRGLRGWGFFKGYYN-MPEATAEAMRN------GWFHTGDLG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 537 TLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEGKVgMAAVKLAPGKTFDGQKLYQHVR 616
Cdd:cd05934 312 YRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEV-KAVVVLRPGETLDPEELFAFCE 390
|
490 500 510
....*....|....*....|....*....|.
gi 228008365 617 SWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd05934 391 GQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
188-662 |
4.85e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 221.48 E-value: 4.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 188 SVFLGLAKL-GCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAENIhcfylghSSPtPGVEALGAS 266
Cdd:PRK07867 68 SLLLGAAALsGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINV-------DSP-AWADELAAH 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 267 LDAAPSDPVPASlratikwKSPAIFIFTSGTTGLPKPAILSHERVIQVSNVLS--FcGCRADDVVYDVLPLYHTIGLVLG 344
Cdd:PRK07867 140 RDAEPPFRVADP-------DDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAqrF-GLGPDDVCYVSMPLFHSNAVMAG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 345 FLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANVWKNFQQRFGp 424
Cdd:PRK07867 212 WAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIARFARRFG- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 425 IRIWEFYGSTEGNVGLMNYVGH-CGAVGRTSCILRMLtpfelvqfDIETAEPlrdkqgfCIPVEPGKPGLL--------L 495
Cdd:PRK07867 291 CVVVDGFGSTEGGVAITRTPDTpPGALGPLPPGVAIV--------DPDTGTE-------CPPAEDADGRLLnadeaigeL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 496 TKVRKNQPFLGY-RGSQAESnrklvanvRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLD 574
Cdd:PRK07867 356 VNTAGPGGFEGYyNDPEADA--------ERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYP 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 575 FLEEVNVYGVPVPGCEGKVgMAAVKLAPGKTFDGQKL--YQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVREGF 652
Cdd:PRK07867 428 DATEVAVYAVPDPVVGDQV-MAALVLAPGAKFDPDAFaeFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGV 506
|
490
....*....|
gi 228008365 653 DVgiiADPLY 662
Cdd:PRK07867 507 DC---ADPVW 513
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
288-641 |
5.66e-63 |
|
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: 212.92 E-value: 5.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAILSHERVI-QVSNVLSFCGCRADDVVYDVLPLYHtIGLVLGFLGCLQVGATCVLAPKFSASRF 366
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLaAAAALAASGGLTEGDVFLSTLPLFH-IGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 367 WAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNG--LRANVWKNFQQRFGpIRIWEFYGSTEGNVGLMNYV 444
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPG-IKLVNGYGLTETGGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 445 GHCGAVGRTSCilrmLTPFELVQFDIetaeplRDKQGfcIPVEPGKPGLLLtkVRKNQPFLGYRGsqaesNRKLVANVRR 524
Cdd:cd04433 160 PDDDARKPGSV----GRPVPGVEVRI------VDPDG--GELPPGEIGELV--VRGPSVMKGYWN-----NPEATAAVDE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 525 vgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGcEGKVGMAAVKLAPGK 604
Cdd:cd04433 221 --DGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPE-WGERVVAVVVLRPGA 297
|
330 340 350
....*....|....*....|....*....|....*..
gi 228008365 605 TFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYK 641
Cdd:cd04433 298 DLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGK 334
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
191-655 |
7.36e-57 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 202.18 E-value: 7.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 191 LGLAKL-GCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEV-LPKLLaenihcfYLGHSSPTpGVEALGASLD 268
Cdd:PRK13388 69 LAAAALgGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGLdLPGVR-------VLDVDTPA-YAELVAAAGA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 269 AAPSDPVPAslratikwKSPAIFIFTSGTTGLPKPAILSHERVIQVSNVLSF-CGCRADDVVYDVLPLYHTIGLVLGFLG 347
Cdd:PRK13388 141 LTPHREVDA--------MDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTErFGLTRDDVCYVSMPLFHSNAVMAGWAP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 348 CLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANVWKNFQQRFGpIRI 427
Cdd:PRK13388 213 AVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFG-CQV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 428 WEFYGSTEGNVGLMNYVGH-CGAVGRtscilrmltPFE-LVQFDIETAEPlrdkqgfCIPVEPGKPGLL---------LT 496
Cdd:PRK13388 292 EDGYGSSEGAVIVVREPGTpPGSIGR---------GAPgVAIYNPETLTE-------CAVARFDAHGALlnadeaigeLV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 497 KVRKNQPFLGYRGSQAesnrklvANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFL 576
Cdd:PRK13388 356 NTAGAGFFEGYYNNPE-------ATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 577 EEVNVYGVPVPgcegKVG---MAAVKLAPGKTFDGQKL--YQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVREG 651
Cdd:PRK13388 429 NRVAVYAVPDE----RVGdqvMAALVLRDGATFDPDAFaaFLAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQG 504
|
....
gi 228008365 652 FDVG 655
Cdd:PRK13388 505 WATG 508
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
119-557 |
1.47e-55 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 195.22 E-value: 1.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 119 LERQALAWPDRVALVCtgSEGSSITNSQLDARSCQAAWVLKAK-LKDAviqntrDAAAILVLPSktISALSVFLGLAKLG 197
Cdd:pfam00501 1 LERQAARTPDKTALEV--GEGRRLTYRELDERANRLAAGLRALgVGKG------DRVAILLPNS--PEWVVAFLACLKAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 198 CPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQ-ENLEEVLPKLlaENIHCFYLGHSSPTPGVEALGASLDAAPSDPVP 276
Cdd:pfam00501 71 AVYVPLNPRLPAEELAYILEDSGAKVLITDDALKlEELLEALGKL--EVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 277 AslrATIKWKSPAIFIFTSGTTGLPKPAILSHERViqVSNVLSFCGCR-------ADDVVYDVLPLYHTIGLVLGFLGCL 349
Cdd:pfam00501 149 P---PPPDPDDLAYIIYTSGTTGKPKGVMLTHRNL--VANVLSIKRVRprgfglgPDDRVLSTLPLFHDFGLSLGLLGPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 350 QVGATCVLAPKFSA---SRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM--GNGLRANVWKNFQQRFGP 424
Cdd:pfam00501 224 LAGATVVLPPGFPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLsgGAPLPPELARRFRELFGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 425 iRIWEFYGSTEGNVGLMNYVGHCGAVGRTSCILRmltPFELVQFDIETAEPLRdkqgfciPVEPGKPGLLLtkVRKNQPF 504
Cdd:pfam00501 304 -ALVNGYGLTETTGVVTTPLPLDEDLRSLGSVGR---PLPGTEVKIVDDETGE-------PVPPGEPGELC--VRGPGVM 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 228008365 505 LGYRGSQAESNRKLVANVrrvgdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWK 557
Cdd:pfam00501 371 KGYLNDPELTAEAFDEDG------WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
115-648 |
7.88e-54 |
|
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: 192.01 E-value: 7.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 115 FVDALERQALAWPDRVALVCTGSegsSITNSQLDARS-CQAAWVLKAKLK--DAVIqntrdaaaiLVLPsKTISALSVFL 191
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGR---KLTYRELDALAeAFAAGLQNLGVQpgDRVA---------LMLP-NCPQFPIAYF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 192 GLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEevlpkllaenihcfylghssptpgvealgasldaap 271
Cdd:cd05936 68 GALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAVSFTDLLA------------------------------------ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 272 sDPVPASLRATIKWKSPAIFIFTSGTTGLPKPAILSHERViqVSNVLSfcgCRA--------DDVVYDVLPLYHTIGLVL 343
Cdd:cd05936 112 -AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNL--VANALQ---IKAwledllegDDVVLAALPLFHVFGLTV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 344 GFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNG--LRANVWKNFQQR 421
Cdd:cd05936 186 ALLLPLALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEEL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 422 FGpIRIWEFYGSTE----GNVGLMNYVGHCGAVGrtscilrmlTPFELVQFDIetaeplRDKQGfcIPVEPGKPGLLLtk 497
Cdd:cd05936 266 TG-VPIVEGYGLTEtspvVAVNPLDGPRKPGSIG---------IPLPGTEVKI------VDDDG--EELPPGEVGELW-- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 498 VRKNQPFLGYRGSQAESNRKLVanvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLE 577
Cdd:cd05936 326 VRGPQVMKGYWNRPEETAEAFV-------DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVA 398
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228008365 578 EVNVYGVPVPGcEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLV 648
Cdd:cd05936 399 EAAVVGVPDPY-SGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
136-622 |
6.84e-48 |
|
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: 175.86 E-value: 6.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 136 GSEGSSITNSQLDARSCQAAWVLKAklkdavIQNTRDAAAILVLPSkTISALSVFLGLAKLGCPVAWINPHSRGMPLLHS 215
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAAGLRK------LGLKKGDVVGIISPN-STYYPPVFLGCLFAGGIFSAANPIYTADELAHQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 216 VRSSGASVLIVDPDLQENLEEVLPKLLA-ENIHCFYlGHSSPTPGVEALGASLDAAPSDPVPASLRATIKwkSPAIFIFT 294
Cdd:cd05911 78 LKISKPKVIFTDPDGLEKVKEAAKELGPkDKIIVLD-DKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKD--DTAAILYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 295 SGTTGLPKPAILSHERVI----QVSNVLSFCGCRaDDVVYDVLPLYHTIGLvLGFLGCLQVGATCVLAPKFSASRFWAEC 370
Cdd:cd05911 155 SGTTGLPKGVCLSHRNLIanlsQVQTFLYGNDGS-NDVILGFLPLYHIYGL-FTTLASLLNGATVIIMPKFDSELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 371 RQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGlrANVWKNFQQRFGPIR-IWEF---YGSTE-GNVGLMN--Y 443
Cdd:cd05911 233 EKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGG--APLSKELQELLAKRFpNATIkqgYGMTEtGGILTVNpdG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 444 VGHCGAVGRtscilrmLTP-FELVQFDIETAEPLrdkqgfcipvEPGKPGLLLtkVRKNQPFLGYRGSQAESNRKLVAnv 522
Cdd:cd05911 311 DDKPGSVGR-------LLPnVEAKIVDDDGKDSL----------GPNEPGEIC--VRGPQVMKGYYNNPEATKETFDE-- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 523 rrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAP 602
Cdd:cd05911 370 ----DGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVS-GELPRAYVVRKP 444
|
490 500
....*....|....*....|
gi 228008365 603 GKTFDGQKLYQHVRSWLPAY 622
Cdd:cd05911 445 GEKLTEKEVKDYVAKKVASY 464
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
119-644 |
3.43e-47 |
|
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: 172.79 E-value: 3.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 119 LERQALAWPDRVALVCtgsEGSSITNSQLDARSCQAAWVLKAKLkdaVIQNTRdaaaILVLPSKTISALSVFLGLAKLGC 198
Cdd:cd17631 1 LRRRARRHPDRTALVF---GGRSLTYAELDERVNRLAHALRALG---VAKGDR----VAVLSKNSPEFLELLFAAARLGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 199 PVAWINPHSRGMPLLHSVRSSGASVLIVDPdlqenleevlpkllaenihcfylghssptpgvealgasldaapsdpvpas 278
Cdd:cd17631 71 VFVPLNFRLTPPEVAYILADSGAKVLFDDL-------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 279 lratikwkspAIFIFTSGTTGLPKPAILSHERVI-QVSNVLSFCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVL 357
Cdd:cd17631 101 ----------ALLMYTSGTTGRPKGAMLTHRNLLwNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVI 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 358 APKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNG-------LRAnvWknfqQRFGPiRIWEF 430
Cdd:cd17631 171 LRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapmperlLRA--L----QARGV-KFVQG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 431 YGSTE--GNVGLM---NYVGHCGAVGRtscilrmltPFELVQFDIetaeplRDKQGfcIPVEPGKPGLLLtkVRKNQPFL 505
Cdd:cd17631 244 YGMTEtsPGVTFLspeDHRRKLGSAGR---------PVFFVEVRI------VDPDG--REVPPGEVGEIV--VRGPHVMA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 506 GYRgsqaesnRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVP 585
Cdd:cd17631 305 GYW-------NRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVP 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 228008365 586 VPGCeGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVK 644
Cdd:cd17631 378 DEKW-GEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
111-647 |
3.61e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 171.63 E-value: 3.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 111 PPETFVDALERQALAWPDRVALVctgSEGSSITNSQLDARSCQAAwvlkAKLKDAVIQnTRDAAAILV--LPSKTISALs 188
Cdd:PRK07656 3 EWMTLPELLARAARRFGDKEAYV---FGDQRLTYAELNARVRRAA----AALAALGIG-KGDRVAIWApnSPHWVIAAL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 189 vflGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLA-ENIHCFYLGHSSPTPGVEALGASL 267
Cdd:PRK07656 74 ---GALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPAlEHVVICETEEDDPHTEKMKTFTDF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 268 DAAPSDPVPAslrATIKWKSPAIFIFTSGTTGLPKPAILSHERVIqvSNVLSFCGC---RADDVVYDVLPLYHTIGLVLG 344
Cdd:PRK07656 151 LAAGDPAERA---PEVDPDDVADILFTSGTTGRPKGAMLTHRQLL--SNAADWAEYlglTEGDRYLAANPFFHVFGYKAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 345 FLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGlrANV----WKNFQQ 420
Cdd:PRK07656 226 VNAPLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGA--ASMpvalLERFES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 421 RFGPIRIWEFYGSTEGN-VGLMNYVGHCGAVGRTSCilrmLTPFELVQFDIEtaeplrDKQGfcIPVEPGKPGLLLtkVR 499
Cdd:PRK07656 304 ELGVDIVLTGYGLSEASgVTTFNRLDDDRKTVAGTI----GTAIAGVENKIV------NELG--EEVPVGEVGELL--VR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 500 KNQPFLGYRGSQAESnrklVANVRRVGDLYfnTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEV 579
Cdd:PRK07656 370 GPNVMKGYYDDPEAT----AAAIDADGWLH--TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEA 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 580 NVYGVPvpgCE--GKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:PRK07656 444 AVIGVP---DErlGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
127-650 |
2.43e-41 |
|
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: 157.47 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVCTGSegssitnsqldarscqAAWVLKAKLKDAVIQNTRDAAAILVLPSKTIS-AL-------SVFLGLAKLGC 198
Cdd:cd05926 1 PDAPALVVPGS----------------TPALTYADLAELVDDLARQLAALGIKKGDRVAiALpnglefvVAFLAAARAGA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 199 PVAWINPHSRG--MPLLHSvrSSGASVLIVDPDlqeNLEEVLPKLLAENIHCFYLGHSSPTPGVEALGASLDAAPSDPVP 276
Cdd:cd05926 65 VVAPLNPAYKKaeFEFYLA--DLGSKLVLTPKG---ELGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 277 ASLRATIKWKSPAIFIFTSGTTGLPKPAILSHE------RVIQVSNVLSFcgcraDDVVYDVLPLYHTIGLVLGFLGCLQ 350
Cdd:cd05926 140 AKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRnlaasaTNITNTYKLTP-----DDRTLVVMPLFHVHGLVASLLSTLA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 351 VGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPE-QPEDKIHTVRLAM--GNGLRANVWKNFQQRFGpIRI 427
Cdd:cd05926 215 AGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRPEpNPESPPPKLRFIRscSASLPPAVLEALEATFG-APV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 428 WEFYGSTE-----------------GNVGLmnyvghcgAVGRTSCILRmltpfelvqfdiETAEPLrdkqgfcipvEPGK 490
Cdd:cd05926 294 LEAYGMTEaahqmtsnplppgprkpGSVGK--------PVGVEVRILD------------EDGEIL----------PPGV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 491 PGLLLtkVRKNQPFLGYRGSQAESNrklvANVRRVGdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVL 570
Cdd:cd05926 344 VGEIC--LRGPNVTRGYLNNPEANA----EAAFKDG--WFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVL 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 571 SSLDFLEEVNVYGVPVPgCEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKlVKSRLVRE 650
Cdd:cd05926 416 LSHPAVLEAVAFGVPDE-KYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGK-IQRRKVAE 493
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
110-660 |
3.34e-41 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 158.35 E-value: 3.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 110 HPPETF---VDALERQALAWPDRVALVCTGSEGS--SITNSQLDARSCQAAWVLKAK-LK--DAVIqntrdaaaiLVLPs 181
Cdd:COG0365 3 FVGGRLniaYNCLDRHAEGRGDKVALIWEGEDGEerTLTYAELRREVNRFANALRALgVKkgDRVA---------IYLP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 182 KTISALSVFLGLAKLGCPvawinpHSRGMPLL--HSVRS----SGASVLIVDP---------DLQENLEEVLPKLlaENI 246
Cdd:COG0365 73 NIPEAVIAMLACARIGAV------HSPVFPGFgaEALADriedAEAKVLITADgglrggkviDLKEKVDEALEEL--PSL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 247 -HCF---YLGHSSPTPGVEALGASLDAAPSDPVPASLRATikwkSPAIFIFTSGTTGLPKPAILSHeRVIQVSNVLSF-- 320
Cdd:COG0365 145 eHVIvvgRTGADVPMEGDLDWDELLAAASAEFEPEPTDAD----DPLFILYTSGTTGKPKGVVHTH-GGYLVHAATTAky 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 321 -CGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVL---APKF-SASRFWAECRQHGVTVILYVGEILRYLCNVPEQP 395
Cdd:COG0365 220 vLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLyegRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 396 EDK--IHTVRLAMGNGLRAN--VWKNFQQRFGpIRIWEFYGSTEgnvglmnyVGHC------------GAVGRtscilrm 459
Cdd:COG0365 300 LKKydLSSLRLLGSAGEPLNpeVWEWWYEAVG-VPIVDGWGQTE--------TGGIfisnlpglpvkpGSMGK------- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 460 ltPFELVQFDIetaeplRDKQGfcIPVEPGKPGLLLtkVRKNQP--FLGYRGsQAESNRKLVANvrRVGDLYFnTGDVLT 537
Cdd:COG0365 364 --PVPGYDVAV------VDEDG--NPVPPGEEGELV--IKGPWPgmFRGYWN-DPERYRETYFG--RFPGWYR-TGDGAR 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 538 LDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVygVPVPGCEGKVGMAA-VKLAPGKTFDG---QKLYQ 613
Cdd:COG0365 428 RDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV--VGVPDEIRGQVVKAfVVLKPGVEPSDelaKELQA 505
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 228008365 614 HVRSWLPAYATPHFIRIQDSLEITNTYKLVKsRLVR---EGFDVGI---IADP 660
Cdd:COG0365 506 HVREELGPYAYPREIEFVDELPKTRSGKIMR-RLLRkiaEGRPLGDtstLEDP 557
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
117-652 |
6.06e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 151.24 E-value: 6.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 117 DALERQALAWPDRVALVCtgsEGSSITNSQLDARSCQAAWVLKA---KLKDAVIQNTRDAAAILVLpsktisalsvFLGL 193
Cdd:PRK08316 15 DILRRSARRYPDKTALVF---GDRSWTYAELDAAVNRVAAALLDlglKKGDRVAALGHNSDAYALL----------WLAC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 194 AKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAEnihcfYLGHSSPTPGVEALGASLD----- 268
Cdd:PRK08316 82 ARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVD-----TLILSLVLGGREAPGGWLDfadwa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 269 -AAPSDPVPASLRATikwkSPAIFIFTSGTTGLPKPAILSHERVIQ--VSNVLSfCGCRADDVVYDVLPLYHTIGLVLGF 345
Cdd:PRK08316 157 eAGSVAEPDVELADD----DLAQILYTSGTESLPKGAMLTHRALIAeyVSCIVA-GDMSADDIPLHALPLYHCAQLDVFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 346 LGCLQVGATCVLAPKFSASRFWAECRQHGVTVI-----LYVGeilryLCNVPEqpedkIHTVRLAmgnGLR--------- 411
Cdd:PRK08316 232 GPYLYVGATNVILDAPDPELILRTIEAERITSFfapptVWIS-----LLRHPD-----FDTRDLS---SLRkgyygasim 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 412 -ANVWKNFQQRFGPIRIWEFYGSTEgnVGLMNYV-------GHCGAVGRTScilrmltpfelvqFDIETAepLRDKQGfc 483
Cdd:PRK08316 299 pVEVLKELRERLPGLRFYNCYGQTE--IAPLATVlgpeehlRRPGSAGRPV-------------LNVETR--VVDDDG-- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 484 IPVEPGKPGLLLTkvRKNQPFLGYRGSQAESnrklvANVRRVGdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVST 563
Cdd:PRK08316 360 NDVAPGEVGEIVH--RSPQLMLGYWDDPEKT-----AEAFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVAS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 564 GEVECVLSSLDFLEEVNVYGVPVPGCEGKVgMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLV 643
Cdd:PRK08316 431 REVEEALYTHPAVAEVAVIGLPDPKWIEAV-TAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKIL 509
|
....*....
gi 228008365 644 KsRLVREGF 652
Cdd:PRK08316 510 K-RELRERY 517
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
112-655 |
7.97e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 148.03 E-value: 7.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 112 PETFVDALERQALAWPDRVALVCTGSEgssITNSQLDARSCQAAWVLKAKlkdAVIQNTRDAaailVLPSKTISALSVFL 191
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYFDGRR---TTYAELDERVNRLANALRAL---GVKKGDRVA----VFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 192 GLAKLGC---PVAWinphsRGMP--LLHSVRSSGASVLIVDPDLQENLEEVLPKLlaENIHCFYLGHSSPTPGVEALGAS 266
Cdd:PRK06187 75 AVPKIGAvlhPINI-----RLKPeeIAYILNDAEDRVVLVDSEFVPLLAAILPQL--PTVRTVIVEGDGPAAPLAPEVGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 267 ----LDAAPSDPVPAslraTIKWKSPAIFIFTSGTTGLPKPAILSHeRVIqVSNVLSFC---GCRADDVVYDVLPLYHTI 339
Cdd:PRK06187 148 yeelLAAASDTFDFP----DIDENDAAAMLYTSGTTGHPKGVVLSH-RNL-FLHSLAVCawlKLSRDDVYLVIVPMFHVH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 340 GLVLGFLGcLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM--GNGLRANVWKN 417
Cdd:PRK06187 222 AWGLPYLA-LMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLRE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 418 FQQRFGpIRIWEFYGSTE-GNVGLMNY--------VGHCGAVGRtscilrmltPFELVQFDIetaeplRDKQGFCIPVEP 488
Cdd:PRK06187 301 FKEKFG-IDLVQGYGMTEtSPVVSVLPpedqlpgqWTKRRSAGR---------PLPGVEARI------VDDDGDELPPDG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 489 GKPGLLLtkVRKNQPFLGYRGSQAESNRKLVANvrrvgdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVEC 568
Cdd:PRK06187 365 GEVGEII--VRGPWLMQGYWNRPEATAETIDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELED 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 569 VLSSLDFLEEVNVYGVPVPgcegKVG---MAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKs 645
Cdd:PRK06187 436 ALYGHPAVAEVAVIGVPDE----KWGerpVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILK- 510
|
570
....*....|
gi 228008365 646 RLVREGFDVG 655
Cdd:PRK06187 511 RVLREQYAEG 520
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
171-681 |
4.70e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 149.10 E-value: 4.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 171 RDAAAILVLPSKTISALSVFLGLAKLGCPVAWINPhsrGMPLLHSVRSSGASVLIVDPdlqENLEEVLpkllAENIHCFY 250
Cdd:PRK07868 495 RQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPP---DTDLAAAVRLGGVTEIITDP---TNLEAAR----QLPGRVLV 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 251 LGhssptpGVEALGasLDAAPS---------DPVPASLRAtikWKSP--------AIFIF-TSGTTGLPKPaILSHERVI 312
Cdd:PRK07868 565 LG------GGESRD--LDLPDDadvidmekiDPDAVELPG---WYRPnpglardlAFIAFsTAGGELVAKQ-ITNYRWAL 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 313 QVSNVLSFCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVP 392
Cdd:PRK07868 633 SAFGTASAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDP 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 393 EQPEDKIHTVRLAMGNGLRANVWKNFQQRFGPIRIWEFYGSTEGNVGLMNYVGH-CGAVGRTsciLRMLTPFELVQFDIE 471
Cdd:PRK07868 713 AFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGAkIGSKGRP---LPGAGRVELAAYDPE 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 472 TAEPLRDKQGFCIPVEPGKPGLLLTKVRKNqpflgyrgsqAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLG 551
Cdd:PRK07868 790 HDLILEDDRGFVRRAEVNEVGVLLARARGP----------IDPTASVKRGVFAPADTWISTEYLFRRDDDGDYWLVDRRG 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 552 DTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEgkVGMAAVKLAPGKTFDGQKLYQHVRSwLPAYATPHFIRIQ 631
Cdd:PRK07868 860 SVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQ--LAVAAVTLRPGAAITAADLTEALAS-LPVGLGPDIVHVV 936
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 228008365 632 DSLEITNTYKLVKSRLVREGfdvgiIADP---LYILDNKAQTFRSLMPDVYQA 681
Cdd:PRK07868 937 PEIPLSATYRPTVSALRAAG-----IPKPgrqAWYFDPETNRYRRLTPAVRAE 984
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-649 |
8.82e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 144.62 E-value: 8.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 119 LERQALAWPDRVALVctgSEGSSITNSQLDARSCQAAWVLKAKLkdaviqNTRDAAAILVLPSKTISALSVFLGLAKLGC 198
Cdd:PRK06839 8 IEKRAYLHPDRIAII---TEEEEMTYKQLHEYVSKVAAYLIYEL------NVKKGERIAILSQNSLEYIVLLFAIAKVEC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 199 PVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAEnihcfylghssPTPGVEALGASLDAAPSDPVPAS 278
Cdd:PRK06839 79 IAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQ-----------RVISITSLKEIEDRKIDNFVEKN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 279 LRAtikwksPAIFIFTSGTTGLPKPAILSHERVI--QVSNVLSFcGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCV 356
Cdd:PRK06839 148 ESA------SFIICYTSGTTGKPKGAVLTQENMFwnALNNTFAI-DLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 357 LAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANV--WKNFQQRfgPIRIWEFYGST 434
Cdd:PRK06839 221 VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEelMREFIDR--GFLFGQGFGMT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 435 EGNVGLM-----NYVGHCGAVGRTscilrmlTPFElvqfDIETAEPLRDKqgfcipVEPGKPGLLLtkVRKNQPFLGYRg 509
Cdd:PRK06839 299 ETSPTVFmlseeDARRKVGSIGKP-------VLFC----DYELIDENKNK------VEVGEVGELL--IRGPNVMKEYW- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 510 sqaeSNRKLVANVRRVGdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGC 589
Cdd:PRK06839 359 ----NRPDATEETIQDG--WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKW 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 590 eGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVR 649
Cdd:PRK06839 433 -GEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
127-642 |
3.58e-36 |
|
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: 142.89 E-value: 3.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVctgSEGSSITNSQLDARSCQAAWVLKAKLkdaVIQNTRdaaaILVLPSKTISALSVFLGLAKLGC-PVAwINP 205
Cdd:cd05959 18 GDKTAFI---DDAGSLTYAELEAEARRVAGALRALG---VKREER----VLLIMLDTVDFPTAFLGAIRAGIvPVP-VNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 206 HSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAENIHCFYLGHSSPTPGVEALGASLDAAPSDPVPASLRAtikw 285
Cdd:cd05959 87 LLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPAATHA---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 286 KSPAIFIFTSGTTGLPKPAILSHERVIQVS-----NVLsfcGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPK 360
Cdd:cd05959 163 DDPAFWLYSSGSTGRPKGVVHLHADIYWTAelyarNVL---GIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 361 F-SASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM--GNGLRANVWKNFQQRFGpIRIWEFYGSTE-G 436
Cdd:cd05959 240 RpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFG-LDILDGIGSTEmL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 437 NVGLMNYVG--HCGAVGRTscilrmlTPFELVQfdietaepLRDKQGfcIPVEPGKPGLLLtkVRKNQPFLGYRGSQAES 514
Cdd:cd05959 319 HIFLSNRPGrvRYGTTGKP-------VPGYEVE--------LRDEDG--GDVADGEPGELY--VRGPSSATMYWNNRDKT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 515 NRKLVANVRRVGDLYFNtgdvltlDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEGKVg 594
Cdd:cd05959 380 RDTFQGEWTRTGDKYVR-------DDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKP- 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 228008365 595 MAAVKLAPGKTFDG---QKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:cd05959 452 KAFVVLRPGYEDSEaleEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKI 502
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
276-647 |
8.51e-34 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 135.97 E-value: 8.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 276 PASLRATIKWKS--PAIFIFTSGTTGLPKPAILSHERvIQVSNVLSF--CGCRADDVVYDVLPLYHTIGLVLGFLGCLQV 351
Cdd:PRK08008 161 PATLCYAPPLSTddTAEILFTSGTTSRPKGVVITHYN-LRFAGYYSAwqCALRDDDVYLTVMPAFHIDCQCTAAMAAFSA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 352 GATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANVWKN-FQQRFGpIRIWEF 430
Cdd:PRK08008 240 GATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLREVMFYLNLSDQEKDaFEERFG-VRLLTS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 431 YGSTEGNVGLmnyVG-------HCGAVGRtscilrmltpfelVQFDIEtAEpLRDKQGfcIPVEPGKPGLLLTK-VRKNQ 502
Cdd:PRK08008 319 YGMTETIVGI---IGdrpgdkrRWPSIGR-------------PGFCYE-AE-IRDDHN--RPLPAGEIGEICIKgVPGKT 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 503 PFLGYRGSQAESNRKLVANvrrvGDLYfnTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVY 582
Cdd:PRK08008 379 IFKEYYLDPKATAKVLEAD----GWLH--TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVV 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 228008365 583 GVPVPGCEGKVgMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:PRK08008 453 GIKDSIRDEAI-KAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
288-649 |
1.57e-32 |
|
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: 130.87 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAILSHERVIQVSNVL-SFCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRF 366
Cdd:cd05941 91 PALILYTSGTTGRPKGVVLTHANLAANVRALvDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 367 WAECRQHGVTVILYVGEI----LRYLCNVPEQPEDKI----HTVRLAM-GNG-LRANVWKNFQQRFGPiRIWEFYGSTEG 436
Cdd:cd05941 171 AISRLMPSITVFMGVPTIytrlLQYYEAHFTDPQFARaaaaERLRLMVsGSAaLPVPTLEEWEAITGH-TLLERYGMTEI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 437 NVGLMN-YVG--HCGAVGRtscilrmltPFELVQFDIetAEPLRDKqgfciPVEPGKPGLLLtkVRKNQPFLGY---RGS 510
Cdd:cd05941 250 GMALSNpLDGerRPGTVGM---------PLPGVQARI--VDEETGE-----PLPRGEVGEIQ--VRGPSVFKEYwnkPEA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 511 QAESNRklvanvrrvGDLYFNTGDVLTLDQEGFFYFQDRLG-DTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGc 589
Cdd:cd05941 312 TKEEFT---------DDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPD- 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228008365 590 EGKVGMAAVKLAPGK-TFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVR 649
Cdd:cd05941 382 WGERVVAVVVLRAGAaALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
141-647 |
4.09e-30 |
|
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: 123.73 E-value: 4.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 141 SITNSQLDARSCQAAWVLKAKLK---DAVIQNTRDAAAILVLpsktisalsvFLGLAKLGCPVAWINPHSRGMPLLHSVR 217
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVssgDRVLLLMLDSPELVQL----------FLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 218 SSGASVLIVDpdlqenleevlpkllAENIhCFYLghssptpgvealgasldaapsdpvpaslratikwkspaifiFTSGT 297
Cdd:cd05919 80 DCEARLVVTS---------------ADDI-AYLL-----------------------------------------YSSGT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 298 TGLPKPAILSHerviqvSNVLSFC--------GCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKF-SASRFWA 368
Cdd:cd05919 103 TGPPKGVMHAH------RDPLLFAdamarealGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 369 ECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM--GNGLRANVWKNFQQRFGpIRIWEFYGSTE-GNVGLMNYVG 445
Cdd:cd05919 177 TLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFG-GPILDGIGATEvGHIFLSNRPG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 446 --HCGAVGRTscilrmLTPFELvqfdietaePLRDKQGFCIPvePGKPGLLLtkVRKNQPFLGYRGSQAESnrklvanVR 523
Cdd:cd05919 256 awRLGSTGRP------VPGYEI---------RLVDEEGHTIP--PGEEGDLL--VRGPSAAVGYWNNPEKS-------RA 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 524 RVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVygVPVPGCEGKVGMAA-VKLAP 602
Cdd:cd05919 310 TFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAV--VAVPESTGLSRLTAfVVLKS 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 228008365 603 GKTFDG---QKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd05919 388 PAAPQEslaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
111-650 |
3.95e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 122.80 E-value: 3.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 111 PPETFVDALERQALAWPDRVALVCTGSEgssITNSQLDARSCQAAWVLKAKlkdAVIQNTRDAaaiLVLPSkTISALSVF 190
Cdd:PRK05605 30 GDTTLVDLYDNAVARFGDRPALDFFGAT---TTYAELGKQVRRAAAGLRAL---GVRPGDRVA---IVLPN-CPQHIVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 191 LGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIV-D---PDLQE-------------NLEEVLPKL--LA-------- 243
Cdd:PRK05605 100 YAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVwDkvaPTVERlrrttpletivsvNMIAAMPLLqrLAlrlpipal 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 244 ----ENIHcfylghsSPTPGVEALGASLDAAPSDPVPASLRATIKWKSPAIFIFTSGTTGLPKPAILSHERViqVSNVLS 319
Cdd:PRK05605 180 rkarAALT-------GPAPGTVPWETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNL--FANAAQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 320 fcgCRA--------DDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNV 391
Cdd:PRK05605 251 ---GKAwvpglgdgPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 392 PEQPEDKIHTVRLAMGNG--LRANVWKNFQQRFGPiRIWEFYGSTE------GNVglMNYVGHCGAVGrtscilrmlTPF 463
Cdd:PRK05605 328 AEERGVDLSGVRNAFSGAmaLPVSTVELWEKLTGG-LLVEGYGLTEtspiivGNP--MSDDRRPGYVG---------VPF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 464 ELVqfDIETAEPlrDKQGFCIPvePGKPGLLLtkVRKNQPFLGYRGsQAESNRKLVAnvrrvgDLYFNTGDVLTLDQEGF 543
Cdd:PRK05605 396 PDT--EVRIVDP--EDPDETMP--DGEEGELL--VRGPQVFKGYWN-RPEETAKSFL------DGWFRTGDVVVMEEDGF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 544 FYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVP-GCEGKVgmAAVKLAPGKTFDGQKLYQHVRSWLPAY 622
Cdd:PRK05605 461 IRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREdGSEEVV--AAVVLEPGAALDPEGLRAYCREHLTRY 538
|
570 580
....*....|....*....|....*...
gi 228008365 623 ATPHFIRIQDSLEITNTYKlVKSRLVRE 650
Cdd:PRK05605 539 KVPRRFYHVDELPRDQLGK-VRRREVRE 565
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
123-603 |
4.60e-29 |
|
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: 121.57 E-value: 4.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 123 ALAWPDRVALVcTGSEGSSITNSQLDARSCQAAWVLKAKLkdaVIQNtrDAAAILvLPSkTISALSVFLGLAKLGCPVAW 202
Cdd:cd05904 15 ASAHPSRPALI-DAATGRALTYAELERRVRRLAAGLAKRG---GRKG--DVVLLL-SPN-SIEFPVAFLAVLSLGAVVTT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 203 INPHSRGMPLLHSVRSSGASVLIVDPDLQENLEE-VLPKLLAENIHCFYLGHSSPtpgvealgasLDAAPSDPVPaslRA 281
Cdd:cd05904 87 ANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASlALPVVLLDSAEFDSLSFSDL----------LFEADEAEPP---VV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 282 TIKWKSPAIFIFTSGTTGLPKPAILSHERVIqvSNVLSFCGCRA-----DDVVYDVLPLYHTIGLVLGFLGCLQVGATCV 356
Cdd:cd05904 154 VIKQDDVAALLYSSGTTGRSKGVMLTHRNLI--AMVAQFVAGEGsnsdsEDVFLCVLPMFHIYGLSSFALGLLRLGATVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 357 LAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNG--LRANVWKNFQQRFGPIRIWEFYGST 434
Cdd:cd05904 232 VMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAapLGKELIEAFRAKFPNVDLGQGYGMT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 435 E-GNVGLMNYVGHCGAVGRTSCilRMLTP-FELVQFDIETAEPLrdkqgfciPvePGKPGLLLtkVRKNQPFLGYRGSQA 512
Cdd:cd05904 312 EsTGVVAMCFAPEKDRAKYGSV--GRLVPnVEAKIVDPETGESL--------P--PNQTGELW--IRGPSIMKGYLNNPE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 513 ESNRKLvanvrrVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVygVPVPGCE-G 591
Cdd:cd05904 378 ATAATI------DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV--IPYPDEEaG 449
|
490
....*....|..
gi 228008365 592 KVGMAAVKLAPG 603
Cdd:cd05904 450 EVPMAFVVRKPG 461
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
288-647 |
8.60e-29 |
|
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: 119.75 E-value: 8.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAILSHE----RVIQVSNVLsfcGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVL--APKF 361
Cdd:cd05972 83 PALIYFTSGTTGLPKGVLHTHSyplgHIPTAAYWL---GLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 362 SASRFWAECRQHGVTVILYVGEILRYLCNvPEQPEDKIHTVRLAMGNG--LRANVWKNFQQRFG-PIRiwEFYGSTEGNV 438
Cdd:cd05972 160 DAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSYKFSHLRLVVSAGepLNPEVIEWWRAATGlPIR--DGYGQTETGL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 439 GLMNYVG---HCGAVGRTscilrmlTPfelvQFDIEtaepLRDKQGfcIPVEPGKPGLLLTKVRKNQPFLGYRGSQaesn 515
Cdd:cd05972 237 TVGNFPDmpvKPGSMGRP-------TP----GYDVA----IIDDDG--RELPPGEEGDIAIKLPPPGLFLGYVGDP---- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 516 RKLVANVRrvGDlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPgCEGKVGM 595
Cdd:cd05972 296 EKTEASIR--GD-YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP-VRGEVVK 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 228008365 596 AAVKLAPGKTFD---GQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd05972 372 AFVVLTSGYEPSeelAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
111-649 |
1.14e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 121.60 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 111 PPETFVDALERQALAWPDRVALVCT-----GSEGSSITNSQLDARSCQAAWVLKAklkdavIQNTRDAAAILVLP--SKT 183
Cdd:PRK07529 23 LPASTYELLSRAAARHPDAPALSFLldadpLDRPETWTYAELLADVTRTANLLHS------LGVGPGDVVAFLLPnlPET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 184 ISALsvfLG--LAKLGCPvawINPHSRGMPLLHSVRSSGASVLIV-----DPDLQENLEEVLPKLLA-ENIHCFYLGHSS 255
Cdd:PRK07529 97 HFAL---WGgeAAGIANP---INPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEVLAALPElRTVVEVDLARYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 256 PTP--------------GVEALGASLDAAPSDpvpASLRAT-IKWKSPAIFIFTSGTTGLPKPAILSHERviQVSNVLS- 319
Cdd:PRK07529 171 PGPkrlavplirrkahaRILDFDAELARQPGD---RLFSGRpIGPDDVAAYFHTGGTTGMPKLAQHTHGN--EVANAWLg 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 320 --FCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSA------SRFWAECRQHGVTVILYVGEILRYLCNV 391
Cdd:PRK07529 246 alLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGYrgpgviANFWKIVERYRINFLSGVPTVYAALLQV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 392 PEQPEDkIHTVRLAMGNG--LRANVWKNFQQRFGpIRIWEFYGSTEGN-VGLMNYVGH---CGAVGrtsciLRMltPFEL 465
Cdd:PRK07529 326 PVDGHD-ISSLRYALCGAapLPVEVFRRFEAATG-VRIVEGYGLTEATcVSSVNPPDGerrIGSVG-----LRL--PYQR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 466 VQfdietAEPLRDKQGFCIPVEPGKPGLLLtkVRKNQPFLGYrgSQAESNRKLvanvrRVGDLYFNTGDVLTLDQEGFFY 545
Cdd:PRK07529 397 VR-----VVILDDAGRYLRDCAVDEVGVLC--IAGPNVFSGY--LEAAHNKGL-----WLEDGWLNTGDLGRIDADGYFW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 546 FQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPGKTFDGQKLYQHVRSWLP--AyA 623
Cdd:PRK07529 463 LTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHA-GELPVAYVQLKPGASATEAELLAFARDHIAerA-A 540
|
570 580
....*....|....*....|....*.
gi 228008365 624 TPHFIRIQDSLEITNTYKLVKSRLVR 649
Cdd:PRK07529 541 VPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
154-622 |
2.41e-28 |
|
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: 119.36 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 154 AAWVLKAKLKDAVIQNTRDAaaiLVLPSKTISALsVFLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQEN 233
Cdd:cd05909 16 GAIALARKLAKMTKEGENVG---VMLPPSAGGAL-ANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 234 LEEVLPKLLAENIHCFYLghssptpgvEALGASLD--------AAPSDPVPASLR----ATIKWKSPAIFIFTSGTTGLP 301
Cdd:cd05909 92 LKLHHLFDVEYDARIVYL---------EDLRAKISkadkckafLAGKFPPKWLLRifgvAPVQPDDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 302 KPAILSHERVIQ-VSNVLSFCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAE-CRQHGVTVIL 379
Cdd:cd05909 163 KGVVLSHKNLLAnVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPLDYKKIPElIYDKKATILL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 380 YVGEILRYLCNVpEQPEDkIHTVRLAM--GNGLRANVWKNFQQRFGpIRIWEFYGSTEG----NVGLMNYVGHCGAVGRt 453
Cdd:cd05909 243 GTPTFLRGYARA-AHPED-FSSLRLVVagAEKLKDTLRQEFQEKFG-IRILEGYGTTECspviSVNTPQSPNKEGTVGR- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 454 scilrmltPFELVQFDIETAEPLrdkqgfcIPVEPGKPGLLLtkVRKNQPFLGYRGSQAESNRKlvanvrrVGDLYFNTG 533
Cdd:cd05909 319 --------PLPGMEVKIVSVETH-------EEVPIGEGGLLL--VRGPNVMLGYLNEPELTSFA-------FGDGWYDTG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 534 DVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLdFLEEVNVYGVPVPgCEGKvGMAAVKLAPGKTFDGQKLYQ 613
Cdd:cd05909 375 DIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEI-LPEDNEVAVVSVP-DGRK-GEKIVLLTTTTDTDPSSLND 451
|
490
....*....|....*
gi 228008365 614 HVRS------WLPAY 622
Cdd:cd05909 452 ILKNagisnlAKPSY 466
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
121-650 |
3.54e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 119.38 E-value: 3.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 121 RQALA-WPDRVALVctgsEGS-SITNSQLDARSCQAAWVLKAK-LK--DAVIQNTRDAAAILVlpsktiSALSVFlglaK 195
Cdd:PRK07470 14 RQAARrFPDRIALV----WGDrSWTWREIDARVDALAAALAARgVRkgDRILVHSRNCNQMFE------SMFAAF----R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 196 LGCpvAWINPHSRGMP--LLHSVRSSGASVLIVDPDLQENLEEVLPKLLAENiHCFYLGHSSPTPGVEALgasLDAAPSD 273
Cdd:PRK07470 80 LGA--VWVPTNFRQTPdeVAYLAEASGARAMICHADFPEHAAAVRAASPDLT-HVVAIGGARAGLDYEAL---VARHLGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 274 PVPAslrATIKWKSPAIFIFTSGTTGLPKPAILSHERV-IQVSNVLS--FCGCRADDVVYDVLPLYHTIGLvlgfLGCLQ 350
Cdd:PRK07470 154 RVAN---AAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMaFVITNHLAdlMPGTTEQDASLVVAPLSHGAGI----HQLCQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 351 V--GATCVLAP--KFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGlrANVWKNFQQR----F 422
Cdd:PRK07470 227 VarGAATVLLPseRFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAG--APMYRADQKRalakL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 423 GPIrIWEFYGSTE--GNV------------GLMNYVGHCGaVGRTScilrmltpfelVQFDIEtaeplrDKQGfcIPVEP 488
Cdd:PRK07470 305 GKV-LVQYFGLGEvtGNItvlppalhdaedGPDARIGTCG-FERTG-----------MEVQIQ------DDEG--RELPP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 489 GKPGLLLtkVRKNQPFLGYRGSQAesnrklvANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVEC 568
Cdd:PRK07470 364 GETGEIC--VIGPAVFAGYYNNPE-------ANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 569 VLSSLDFLEEVNVYGVPVPgCEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKsRLV 648
Cdd:PRK07470 435 KLLTHPAVSEVAVLGVPDP-VWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITK-KMV 512
|
..
gi 228008365 649 RE 650
Cdd:PRK07470 513 RE 514
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
292-644 |
5.01e-28 |
|
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: 115.29 E-value: 5.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 292 IFTSGTTGLPKPAILSHERVIQVSNVLSFCG-CRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAEC 370
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCAdLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 371 RQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNG--LRANVWKNFQQRFGPIRIWEFYGSTEGNVGLMnyvghcg 448
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAatVPVELVRRMRSELGFETVLTAYGLTEAGVATM------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 449 avgrtsCilRMLTPFELVQFDIETAEPlrdkqGFciPVEPGKPGLLLtkVRKNQPFLGYRGSQAESNRKLVAnvrrvgDL 528
Cdd:cd17638 159 ------C--RPGDDAETVATTCGRACP-----GF--EVRIADDGEVL--VRGYNVMQGYLDDPEATAEAIDA------DG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 529 YFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPGKTFDG 608
Cdd:cd17638 216 WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERM-GEVGKAFVVARPGVTLTE 294
|
330 340 350
....*....|....*....|....*....|....*.
gi 228008365 609 QKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVK 644
Cdd:cd17638 295 EDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
120-647 |
8.99e-27 |
|
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: 114.61 E-value: 8.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 120 ERQALAWPDRVALVCtgsEGSSITNSQLDARSCQAAWVLKAKlkdAVIQNtrDAAAILVlpSKTISALSVFLGLAKLGCP 199
Cdd:cd12117 4 EEQAARTPDAVAVVY---GDRSLTYAELNERANRLARRLRAA---GVGPG--DVVGVLA--ERSPELVVALLAVLKAGAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 200 VAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLaenihcfylghssptpgveaLGASLDAAPSDPVPASL 279
Cdd:cd12117 74 YVPLDPELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVV--------------------IDEALDAGPAGNPAVPV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 280 RATikwkSPAIFIFTSGTTGLPKPAILSH------------------ERVIQVSNvLSFcgcraDDVVYDVlplyhtigl 341
Cdd:cd12117 134 SPD----DLAYVMYTSGSTGRPKGVAVTHrgvvrlvkntnyvtlgpdDRVLQTSP-LAF-----DASTFEI--------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 342 vlgfLGCLQVGATCVLAPK---FSASRFWAECRQHGVTVILYVGEILRYLcnVPEQPEdKIHTVRLAMGNGLRANV--WK 416
Cdd:cd12117 195 ----WGALLNGARLVLAPKgtlLDPDALGALIAEEGVTVLWLTAALFNQL--ADEDPE-CFAGLRELLTGGEVVSPphVR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 417 NFQQRFGPIRIWEFYGSTEGNVGLMNYVGHCGAVGRTSciLRMLTPfelvqFDIETAEPLrDKQGfcIPVEPGKPGLL-- 494
Cdd:cd12117 268 RVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGS--IPIGRP-----IANTRVYVL-DEDG--RPVPPGVPGELyv 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 495 ----LTKvrknqpflGYRGSQAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVL 570
Cdd:cd12117 338 ggdgLAL--------GYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAAL 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 228008365 571 SSLDFLEEVNVygVPVPGCEGKVGMAAVkLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd12117 410 RAHPGVREAVV--VVREDAGGDKRLVAY-VVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
127-642 |
1.49e-26 |
|
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: 113.39 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVCtgsEGSSITNSQLDARSCQAAWVLKAKLkdaVIQNTRdaAAILVLPS-KTISALsvfLGLAKLGC---PVAW 202
Cdd:cd05930 1 PDAVAVVD---GDQSLTYAELDARANRLARYLRERG---VGPGDL--VAVLLERSlEMVVAI---LAVLKAGAayvPLDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 203 INPHSRgmpLLHSVRSSGASVLIVDPDlqenleevlpkllaenihcfylghssptpgvealgasldaapsdpvpaslrat 282
Cdd:cd05930 70 SYPAER---LAYILEDSGAKLVLTDPD----------------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 283 ikwkSPAIFIFTSGTTGLPKPAILSH-------------------ERVIQVSNvLSFcgcraDDVVYDvlplyhtiglvl 343
Cdd:cd05930 94 ----DLAYVIYTSGSTGKPKGVMVEHrglvnlllwmqeaypltpgDRVLQFTS-FSF-----DVSVWE------------ 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 344 gFLGCLQVGATCVLAPK---FSASRFWAECRQHGVTVILYVGEILRYLcnVPEQPEDKIHTVRLAM--GNGLRANVWKNF 418
Cdd:cd05930 152 -IFGALLAGATLVVLPEevrKDPEALADLLAEEGITVLHLTPSLLRLL--LQELELAALPSLRLVLvgGEALPPDLVRRW 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 419 QQRFGPIRIWEFYGSTEGNVG-LMNYVGHCGAVGRTSCILRmltpfelvqfdietaePLRDKQGF-----CIPVEPGKPG 492
Cdd:cd05930 229 RELLPGARLVNLYGPTEATVDaTYYRVPPDDEEDGRVPIGR----------------PIPNTRVYvldenLRPVPPGVPG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 493 -LLLTKVrknQPFLGYRGSQAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLgDT------FRwkgenVSTGE 565
Cdd:cd05930 293 eLYIGGA---GLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRI-DDqvkirgYR-----IELGE 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008365 566 VECVLSSLDFLEEVNVygVPVP-GCEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:cd05930 364 IEAALLAHPGVREAAV--VAREdGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKV 439
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
289-650 |
1.81e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 114.36 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 289 AIFIFTSGTTGLPKPAILSHERViqVSNVLS----FCGCR-ADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSA 363
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMLTHKNL--VSNTLMgvqwLYNCKeGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDM 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 364 SRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNG--LRANVWKNFQQRFGPiRIWEFYGSTEGN-VGL 440
Cdd:PRK06710 287 KMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSapLPVEVQEKFETVTGG-KLVEGYGLTESSpVTH 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 441 MNYVGH---CGAVGrtscilrmlTPF---ELVQFDIETAEPLRdkqgfcipvePGKPGLLLtkVRKNQPFLGYRGSQAES 514
Cdd:PRK06710 366 SNFLWEkrvPGSIG---------VPWpdtEAMIMSLETGEALP----------PGEIGEIV--VKGPQIMKGYWNKPEET 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 515 NRKLvanvrrvGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPgCEGKVG 594
Cdd:PRK06710 425 AAVL-------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDP-YRGETV 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 228008365 595 MAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVRE 650
Cdd:PRK06710 497 KAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
112-647 |
2.24e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 113.68 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 112 PETFVDALERQALAWPDRVALVctgSEGSSITNSQLDARSCQ-AAWVLKAklkdAVIQNTRDAaaiLVLPSKtISALSVF 190
Cdd:PRK06164 9 ADTLASLLDAHARARPDAVALI---DEDRPLSRAELRALVDRlAAWLAAQ----GVRRGDRVA---VWLPNC-IEWVVLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 191 LGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDP-----DLQENLEEVLPKLLAenihcfylghssPTPGVEALGA 265
Cdd:PRK06164 78 LACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPgfkgiDFAAILAAVPPDALP------------PLRAIAVVDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 266 SLDAAPSD-----------PVPASLRATIKWKS----PAIFIFTSGTTGLPK------PAILSHERVIQVSnvlsfCGCR 324
Cdd:PRK06164 146 AADATPAPapgarvqlfalPDPAPPAAAGERAAdpdaGALLFTTSGTTSGPKlvlhrqATLLRHARAIARA-----YGYD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 325 ADDVVYDVLPLYHTIGLVlGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRL 404
Cdd:PRK06164 221 PGAVLLAALPFCGVFGFS-TLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 405 AMGNGLRA--NVWKNFQQRFGPIRiwEFYGSTEgNVGLMNyvghcgavgrtscILRMLTPfelVQFDIE----TAEP--- 475
Cdd:PRK06164 300 GFASFAPAlgELAALARARGVPLT--GLYGSSE-VQALVA-------------LQPATDP---VSVRIEgggrPASPear 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 476 --LRDKQGFCIpVEPGKPGLLltKVRKNQPFLGYRGSQAESNRKLVAnvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDT 553
Cdd:PRK06164 361 vrARDPQDGAL-LPDGESGEI--EIRAPSLMRGYLDNPDATARALTD------DGYFRTGDLGYTRGDGQFVYQTRMGDS 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 554 FRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVpgcEGK-VGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQD 632
Cdd:PRK06164 432 LRLGGFLVNPAEIEHALEALPGVAAAQVVGATR---DGKtVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVE 508
|
570
....*....|....*...
gi 228008365 633 SLEIT---NTYKLVKSRL 647
Cdd:PRK06164 509 AFPVTesaNGAKIQKHRL 526
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
123-650 |
2.52e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 113.87 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 123 ALAWPDRVALVctgSEGSSITNSQLDARSCQAAWVLKAKlkdaviqNTRDAAAILVLPSKTISALSVFLGLAKLGCPVAW 202
Cdd:PRK07788 59 ARRAPDRAALI---DERGTLTYAELDEQSNALARGLLAL-------GVRAGDGVAVLARNHRGFVLALYAAGKVGARIIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 203 INPHSRGMPLLHSVRSSGASVLIVDP---DLQENLEEVLPKLLAENIHCfyLGHSSPTPGVEALGASLDAAPSDPVPasl 279
Cdd:PRK07788 129 LNTGFSGPQLAEVAAREGVKALVYDDeftDLLSALPPDLGRLRAWGGNP--DDDEPSGSTDETLDDLIAGSSTAPLP--- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 280 ratiKWKSPA-IFIFTSGTTGLPKPAILSHERVIQ-VSNVLSFCGCRADDVVYDVLPLYHTIGLVLGFLGcLQVGATCVL 357
Cdd:PRK07788 204 ----KPPKPGgIVILTSGTTGTPKGAPRPEPSPLApLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 358 APKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM----GNGLRANVWKNFQQRFGPIrIWEFYGS 433
Cdd:PRK07788 279 RRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIifvsGSALSPELATRALEAFGPV-LYNLYGS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 434 TEGNVGLM----NYVGHCGAVGR--TSCILRMLtpfelvqfdietaeplrDKQGfcIPVEPGKPGLLLtkVRKNQPFLGY 507
Cdd:PRK07788 358 TEVAFATIatpeDLAEAPGTVGRppKGVTVKIL-----------------DENG--NEVPRGVVGRIF--VGNGFPFEGY 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 508 RGSqaesnrklvANVRRVGDLyFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVP 587
Cdd:PRK07788 417 TDG---------RDKQIIDGL-LSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDE 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 228008365 588 gcE-GKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATP---HFIriqDSLEITNTYKLVKsRLVRE 650
Cdd:PRK07788 487 --EfGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPrdvVFL---DELPRNPTGKVLK-RELRE 547
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
127-653 |
2.87e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 113.06 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVCTGSEgssITNSQLDARSCQAAWVLKAK---LKDAVIQNTRDAAAILVLPSKTISALSVFLGLA-KLGCP-VA 201
Cdd:PRK06145 16 PDRAALVYRDQE---ISYAEFHQRILQAAGMLHARgigQGDVVALLMKNSAAFLELAFAASYLGAVFLPINyRLAADeVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 202 WINPHSrgmpllhsvrssGASVLIVDPDLQENLEEVLPKLLAEnihcfylGHSSPTPGVEALGAsLDAAPSDPV-PASLR 280
Cdd:PRK06145 93 YILGDA------------GAKLLLVDEEFDAIVALETPKIVID-------AAAQADSRRLAQGG-LEIPPQAAVaPTDLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 281 AtikwkspaiFIFTSGTTGLPKPAILSHERVIQVS-NVLSFCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAP 359
Cdd:PRK06145 153 R---------LMYTSGTTDRPKGVMHSYGNLHWKSiDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 360 KFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRA--NVWKNFQQRFGPIRIWEFYGSTEGN 437
Cdd:PRK06145 224 EFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTpeSRIRDFTRVFTRARYIDAYGLTETC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 438 VG--LMNYVGHCGAVGRTScilRMLTPFELvqfdietaePLRDKQGFCIPvePGKPGLLLtkVRKNQPFLGYRGSQAESN 515
Cdd:PRK06145 304 SGdtLMEAGREIEKIGSTG---RALAHVEI---------RIADGAGRWLP--PNMKGEIC--MRGPKVTKGYWKDPEKTA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 516 RKLvanvrrVGDlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGM 595
Cdd:PRK06145 368 EAF------YGD-WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRW-GERIT 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 228008365 596 AAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKsRLVREGFD 653
Cdd:PRK06145 440 AVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLK-RVLRDELN 496
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
127-647 |
4.76e-26 |
|
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: 111.96 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVCtgsEGSSITNSQLDARSCQAAwvlkAKLKDaviQNTRDAAAILVLPSKTISALSVFLGLAKLGCPVAWINPH 206
Cdd:cd05945 5 PDRPAVVE---GGRTLTYRELKERADALA----AALAS---LGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 207 SRGMPLLHSVRSSGASVLIVDPDlqenleevlpkllaenihcfylghssptpgvealgasldaapsdpvpaslratikwk 286
Cdd:cd05945 75 SPAERIREILDAAKPALLIADGD--------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 287 SPAIFIFTSGTTGLPKPAILSHERVIQVSNV-LSFCGCRADDVVYDVLPLyhTIGL-VLGFLGCLQVGATCVLAPK---F 361
Cdd:cd05945 98 DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWmLSDFPLGPGDVFLNQAPF--SFDLsVMDLYPALASGATLVPVPRdatA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 362 SASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM--GNGLRANVWKNFQQRFGPIRIWEFYGSTEGNVg 439
Cdd:cd05945 176 DPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLfcGEVLPHKTARALQQRFPDARIYNTYGPTEATV- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 440 lmnyvghcgAVgrtscilrmlTPFELVQFDIETAEPL---RDKQGFCI--------PVEPGKPGLLLtkVRKNQPFLGYR 508
Cdd:cd05945 255 ---------AV----------TYIEVTPEVLDGYDRLpigYAKPGAKLvildedgrPVPPGEKGELV--ISGPSVSKGYL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 509 GSQAESNRklvANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVygVPVPG 588
Cdd:cd05945 314 NNPEKTAA---AFFPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV--VPKYK 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228008365 589 CEGKVGMAA-VKLAPGKTFDGQK-LYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd05945 389 GEKVTELIAfVVPKPGAEAGLTKaIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
288-637 |
6.44e-26 |
|
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: 111.38 E-value: 6.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAILSHERVIQVSN-VLSFCGCRADDVVYDVLPLYHTIGLVLgFLGCLQVGATCVLAPKFSASR- 365
Cdd:cd05922 119 LALLLYTSGSTGSPKLVRLSHQNLLANARsIAEYLGITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDDa 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 366 FWAECRQHGVT---VILYVGEILRYLCNVPEqpedKIHTVRL--AMGNGLRANVWKNFQQRFGPIRIWEFYGSTEGNvGL 440
Cdd:cd05922 198 FWEDLREHGATglaGVPSTYAMLTRLGFDPA----KLPSLRYltQAGGRLPQETIARLRELLPGAQVYVMYGQTEAT-RR 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 441 MNYV------GHCGAVGRtscilrmltPFELVQFDIetaepLRDKQGFCIPVEPGKPGllltkVRKNQPFLGYRGSQAEs 514
Cdd:cd05922 273 MTYLpperilEKPGSIGL---------AIPGGEFEI-----LDDDGTPTPPGEPGEIV-----HRGPNVMKGYWNDPPY- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 515 nrkLVANVRRVGDLYfnTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEgkvG 594
Cdd:cd05922 333 ---RRKEGRGGGVLH--TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGE---K 404
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 228008365 595 MAAVKLAPGKTfDGQKLYQHVRSWLPAYATPHFIRIQDSLEIT 637
Cdd:cd05922 405 LALFVTAPDKI-DPKDVLRSLAERLPPYKVPATVRVVDELPLT 446
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
288-634 |
1.18e-25 |
|
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: 108.51 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAILSHERVIQVS-NVLSFCGCRADDVVYDVLPLYHTIGLVLGfLGCLQVGATCVLAPKFSASRF 366
Cdd:cd17637 2 PFVIIHTAAVAGRPRGAVLSHGNLIAANlQLIHAMGLTEADVYLNMLPLFHIAGLNLA-LATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 367 WAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANVwknfqQRF---GPIRIWEFYGSTE--GNVGLM 441
Cdd:cd17637 81 LELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAPETI-----QRFeetTGATFWSLYGQTEtsGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 442 NYVGHCGAVGRTScilrMLTPFELV-QFDIetaeplrdkqgfciPVEPGKPGLLLtkVRKNQPFLGYRGSQAESNRKLva 520
Cdd:cd17637 156 PYRERPGSAGRPG----PLVRVRIVdDNDR--------------PVPAGETGEIV--VRGPLVFQGYWNLPELTAYTF-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 521 nvrRVGdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWK--GENVSTGEVECVLSSLDFLEEVNVYGVPVPgcEGKVGMAAV 598
Cdd:cd17637 214 ---RNG--WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIGVPDP--KWGEGIKAV 286
|
330 340 350
....*....|....*....|....*....|....*..
gi 228008365 599 -KLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSL 634
Cdd:cd17637 287 cVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEAL 323
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
116-647 |
7.23e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 109.36 E-value: 7.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 116 VDALERQALAWPDRVALVCTGSEgssITNSQLDARSCQAAWVLKAKlkdAVIQNTRDAAAILVLPSKTIsalsVFLGLAK 195
Cdd:PRK06178 36 TEYLRAWARERPQRPAIIFYGHV---ITYAELDELSDRFAALLRQR---GVGAGDRVAVFLPNCPQFHI----VFFGILK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 196 LGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAENIHcfylghssptpgVEALGASLDAAPSDPV 275
Cdd:PRK06178 106 LGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVI------------VTSLADVLPAEPTLPL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 276 PASLRA-------------------------TIKWKSPAIFIFTSGTTGLPKPAILSHERVI--QVSNVLSFCGCRADDV 328
Cdd:PRK06178 174 PDSLRAprlaaagaidllpalractapvplpPPALDALAALNYTGGTTGMPKGCEHTQRDMVytAAAAYAVAVVGGEDSV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 329 VYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGN 408
Cdd:PRK06178 254 FLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 409 GLRANVWKNFQQRF----GPIRIWEFYGSTEGN----------VGLMNYVGHCGAVGrtscilrmL----TPFELVQFdi 470
Cdd:PRK06178 334 SFVKKLNPDYRQRWraltGSVLAEAAWGMTETHtcdtftagfqDDDFDLLSQPVFVG--------LpvpgTEFKICDF-- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 471 ETAEPLrdkqgfciPVepGKPGLLLtkVRKNQPFLGYRGsqaesNRKLVANVRRVGdlYFNTGDVLTLDQEGFFYFQDRL 550
Cdd:PRK06178 404 ETGELL--------PL--GAEGEIV--VRTPSLLKGYWN-----KPEATAEALRDG--WLHTGDIGKIDEQGFLHYLGRR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 551 GDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGcEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHfIRI 630
Cdd:PRK06178 465 KEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPD-KGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRI 542
|
570
....*....|....*..
gi 228008365 631 QDSLEITNTYKLVKSRL 647
Cdd:PRK06178 543 VDALPMTATGKVRKQDL 559
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
293-647 |
1.19e-24 |
|
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: 105.82 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 293 FTSGTTGLPKPAILSHERVIQVSNVLSFC-GCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVL-APKFSASRFWAEC 370
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERlGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 371 RQ------HGVTVIlYVGEIlrylcNVPEQPEDKIHTVR--LAMGNGLRANVWKNFQQRFGPIRIWEFYGSTEGN-VGLM 441
Cdd:cd05917 89 EKekctalHGVPTM-FIAEL-----EHPDFDKFDLSSLRtgIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSpVSTQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 442 NYVG-----HCGAVGRtscilrmLTPF-ELVQFDIETaeplrdkqgfCIPVEPGKPGLLLtkVRKNQPFLGYRGSQaESN 515
Cdd:cd05917 163 TRTDdsiekRVNTVGR-------IMPHtEAKIVDPEG----------GIVPPVGVPGELC--IRGYSVMKGYWNDP-EKT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 516 RKLVAnvrrvGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGM 595
Cdd:cd05917 223 AEAID-----GDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERY-GEEVC 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 228008365 596 AAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd05917 297 AWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
136-652 |
1.36e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 108.07 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 136 GSEGSSITNSQLDARSCQAAWVLKAK-LKDAviqntrDAAAILVlpSKTISALSVFLGLAKLG---CPVAWinpHSRGMP 211
Cdd:PRK08276 6 APSGEVVTYGELEARSNRLAHGLRALgLREG------DVVAILL--ENNPEFFEVYWAARRSGlyyTPINW---HLTAAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 212 LLHSVRSSGASVLIVDPDLQENLEEvLPKLLAENIHCFYLGhSSPTPGVEALGASLDAAPSDPVPA-SLRATikwkspai 290
Cdd:PRK08276 75 IAYIVDDSGAKVLIVSAALADTAAE-LAAELPAGVPLLLVV-AGPVPGFRSYEEALAAQPDTPIADeTAGAD-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 291 FIFTSGTTGLPK---PAiLSHERVIQVSNVLSFCGCR-----ADDVVYDVLPLYHTIGLVLGfLGCLQVGATCVLAPKFS 362
Cdd:PRK08276 145 MLYSSGTTGRPKgikRP-LPGLDPDEAPGMMLALLGFgmyggPDSVYLSPAPLYHTAPLRFG-MSALALGGTVVVMEKFD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 363 ASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDK---------IHT-------VRLAMGNglranvWknfqqrFGPIr 426
Cdd:PRK08276 223 AEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARydvsslrvaIHAaapcpveVKRAMID------W------WGPI- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 427 IWEFYGSTEGN-VGLMN---YVGHCGAVGRT-SCILRMLtpfelvqfdietaeplrDKQGfcIPVEPGKPGLLLtkVRKN 501
Cdd:PRK08276 290 IHEYYASSEGGgVTVITsedWLAHPGSVGKAvLGEVRIL-----------------DEDG--NELPPGEIGTVY--FEMD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 502 QPFLGYRGSQAesnrKLVANVRRVGdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNV 581
Cdd:PRK08276 349 GYPFEYHNDPE----KTAAARNPHG--WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAV 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 228008365 582 YGVPvpgCE--GKVGMAAVKLAPGKTFD---GQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLvREGF 652
Cdd:PRK08276 423 FGVP---DEemGERVKAVVQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL-RDRY 494
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
289-647 |
1.54e-24 |
|
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: 107.18 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 289 AIFIFTSGTTGLPKPAILSHERVIQVS-----NVLsfcGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSA 363
Cdd:cd05958 100 CILAFTSGTTGAPKATMHFHRDPLASAdryavNVL---RLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 364 SRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM--GNGLRANVWKNFQQRFGpIRIWEFYGSTEG-NVGL 440
Cdd:cd05958 177 DLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATG-IPIIDGIGSTEMfHIFI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 441 MNYVGHCgAVGRTScilrmlTPFELVqfdieTAEpLRDKQGFciPVEPGKPGLLLTKvrknQPfLGYRGSQAESNRKLVa 520
Cdd:cd05958 256 SARPGDA-RPGATG------KPVPGY-----EAK-VVDDEGN--PVPDGTIGRLAVR----GP-TGCRYLADKRQRTYV- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 521 nvrrvGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGcEGKVGMAAVKL 600
Cdd:cd05958 315 -----QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDES-RGVVVKAFVVL 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 228008365 601 APGKTFDGQ---KLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd05958 389 RPGVIPGPVlarELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
112-435 |
2.42e-24 |
|
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: 109.18 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 112 PETFVDALERQALAWPDRVALVCtgsEGSSITNSQLDARSCQAAWVLKAKlkdAVIQNTRDAaaiLVLPsKTISALSVFL 191
Cdd:COG1020 475 DATLHELFEAQAARTPDAVAVVF---GDQSLTYAELNARANRLAHHLRAL---GVGPGDLVG---VCLE-RSLEMVVALL 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 192 GLAKLGCpvAWI-----NPHSRgmpLLHSVRSSGASVLIVDPDLQENLeevlpkllaenihcfylghssPTPGVEAL--- 263
Cdd:COG1020 545 AVLKAGA--AYVpldpaYPAER---LAYMLEDAGARLVLTQSALAARL---------------------PELGVPVLald 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 264 GASLDAAPSDPVPASLRATikwkSPAIFIFTSGTTGLPKPAILSHERVIQ-VSNVLSFCGCRADDVVydvlPLYHTIGL- 341
Cdd:COG1020 599 ALALAAEPATNPPVPVTPD----DLAYVIYTSGSTGRPKGVMVEHRALVNlLAWMQRRYGLGPGDRV----LQFASLSFd 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 342 --VLGFLGCLQVGATCVLAPK---FSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVrLAMGNGLRANVWK 416
Cdd:COG1020 671 asVWEIFGALLSGATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLV-LVGGEALPPELVR 749
|
330
....*....|....*....
gi 228008365 417 NFQQRFGPIRIWEFYGSTE 435
Cdd:COG1020 750 RWRARLPGARLVNLYGPTE 768
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
113-650 |
2.71e-24 |
|
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: 107.54 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 113 ETFVDALERQALAWPDRVALVCtgsEGSSITNSQLDARSCQAAwvlkAKLKDAVIQntRDAAAILVLPSkTISALSVFLG 192
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVD---GERRLSYAELDRRADRLA----AGLLALGLR--PGDRVVVQLPN-VAEFVIVFFA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 193 LAKLGC-PVAWINPHsRGMPLLHSVRSSGASVLIVdPDLQE--NLEEVLPKLLAENI---HCFYLGHSSPtpgvealGAS 266
Cdd:COG1021 95 LFRAGAiPVFALPAH-RRAEISHFAEQSEAVAYII-PDRHRgfDYRALARELQAEVPslrHVLVVGDAGE-------FTS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 267 LDAAPSDPVPASLRATIKWkSPAIFIFTSGTTGLPK-------PAILSHERVIQVsnvlsfCGCRADDVVYDVLPLYHTI 339
Cdd:COG1021 166 LDALLAAPADLSEPRPDPD-DVAFFQLSGGTTGLPKliprthdDYLYSVRASAEI------CGLDADTVYLAALPAAHNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 340 GLVL-GFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLaMGNG---LRANVW 415
Cdd:COG1021 239 PLSSpGVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRV-LQVGgakLSPELA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 416 KNFQQRFGpIRIWEFYGSTEgnvGLMNYVghcgavgrtscilRMLTPFELVqfdIET-------AEPLR--DKQGfcIPV 486
Cdd:COG1021 318 RRVRPALG-CTLQQVFGMAE---GLVNYT-------------RLDDPEEVI---LTTqgrpispDDEVRivDEDG--NPV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 487 EPGKPGLLLTKvrknQP--FLGYRGSqAESNrklvanvRRV--GDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVS 562
Cdd:COG1021 376 PPGEVGELLTR----GPytIRGYYRA-PEHN-------ARAftPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 563 TGEVECVLSSLDFLEEVNVYGVPVP--G---CegkvgmaAVKLAPGKTFDGQKLYQHVRSW-LPAYATPHFIRIQDSLEI 636
Cdd:COG1021 444 AEEVENLLLAHPAVHDAAVVAMPDEylGersC-------AFVVPRGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPL 516
|
570
....*....|....
gi 228008365 637 TNTYKLVKSRLVRE 650
Cdd:COG1021 517 TAVGKIDKKALRAA 530
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
172-647 |
3.18e-24 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 107.09 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 172 DAAAILVlpSKTISALSVFLGLAKLGC---PVAWinpHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLL------ 242
Cdd:PRK12406 37 DCVALLM--RNDFAFFEAAYAAMRLGAyavPVNW---HFKPEEIAYILEDSGARVLIAHADLLHGLASALPAGVtvlsvp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 243 --AENIHCFYL--GHSSPTPGVEALGASLDA-APSDPVPAslratikwKSPAIFIFTSGTTGLPK----PAILSHERVIQ 313
Cdd:PRK12406 112 tpPEIAAAYRIspALLTPPAGAIDWEGWLAQqEPYDGPPV--------PQPQSMIYTSGTTGHPKgvrrAAPTPEQAAAA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 314 VSNVLSFCGCRADDVVYDVLPLYHTIGLVLGfLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPE 393
Cdd:PRK12406 184 EQMRALIYGLKPGIRALLTGPLYHSAPNAYG-LRAGRLGGVLVLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 394 QPEDK---------IHT-------VRLAMGNglranvWknfqqrFGPIrIWEFYGSTE-GNVGLMN---YVGHCGAVGRt 453
Cdd:PRK12406 263 EVRAKydvsslrhvIHAaapcpadVKRAMIE------W------WGPV-IYEYYGSTEsGAVTFATsedALSHPGTVGK- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 454 scilrmLTPFELVQFDIETAEPLrdkqgfcipvEPGKPGLLLTKVRKNQPFLgYRGSQAESnrklvANVRRVGdlYFNTG 533
Cdd:PRK12406 329 ------AAPGAELRFVDEDGRPL----------PQGEIGEIYSRIAGNPDFT-YHNKPEKR-----AEIDRGG--FITSG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 534 DVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPGKTFDGQKLYQ 613
Cdd:PRK12406 385 DVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEF-GEALMAVVEPQPGATLDEADIRA 463
|
490 500 510
....*....|....*....|....*....|....
gi 228008365 614 HVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:PRK12406 464 QLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
293-642 |
5.57e-24 |
|
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: 103.25 E-value: 5.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 293 FTSGTTGLPKPAILSHERVIQ--VSNVLSFcGCRADDVVYDVLPLYHTIGLvLGFLGCLQVGATCVLAPKFSASRFWAEC 370
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIEsfVCNEDLF-NISGEDAILAPGPLSHSLFL-YGAISALYLGGTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 371 RQHGVTVILYVGEILRYLCNVpEQPEDKIHTVrLAMGNGLRANVWKNFQQRFGPIRIWEFYGSTEGNVGLMNYVGHC--- 447
Cdd:cd17633 85 NQYNATVIYLVPTMLQALART-LEPESKIKSI-FSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESrpp 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 448 GAVGRtscilrmltPFELVQFDIETAEPlrdkqgfcipvepGKPGLLltKVRKNQPFLGYRGSQAESNrklvanvrrvgD 527
Cdd:cd17633 163 NSVGR---------PFPNVEIEIRNADG-------------GEIGKI--FVKSEMVFSGYVRGGFSNP-----------D 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 528 LYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPvpgcEGKVGMAAVKLAPGKTFD 607
Cdd:cd17633 208 GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP----DARFGEIAVALYSGDKLT 283
|
330 340 350
....*....|....*....|....*....|....*
gi 228008365 608 GQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:cd17633 284 YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
119-650 |
1.68e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 104.27 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 119 LERQALAWPDRVALVctgSEGSSITNSQLDarscQAAWVLKAKLKDAVIQNTrDAAAILVlpSKTISALSVFLGLAKLGC 198
Cdd:PRK03640 8 LKQRAFLTPDRTAIE---FEEKKVTFMELH----EAVVSVAGKLAALGVKKG-DRVALLM--KNGMEMILVIHALQQLGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 199 PVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAEnihcfylghssptpgVEALGASlDAAPSDPVPAS 278
Cdd:PRK03640 78 VAVLLNTRLSREELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAE---------------LMNGPKE-EAEIQEEFDLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 279 LRATIkwkspaifIFTSGTTGLPKPailsherVIQ---------VSNVLSFcGCRADDVVYDVLPLYHTIGLVLGFLGcL 349
Cdd:PRK03640 142 EVATI--------MYTSGTTGKPKG-------VIQtygnhwwsaVGSALNL-GLTEDDCWLAAVPIFHISGLSILMRS-V 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 350 QVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLcnVPEQPEDKIH-TVR-LAMGNG------LRANVWKNfqqr 421
Cdd:PRK03640 205 IYGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRL--LERLGEGTYPsSFRcMLLGGGpapkplLEQCKEKG---- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 422 fgpIRIWEFYGSTEGN---VGL-----MNYVGhcgAVGRTscilrmLTPfelVQFDIEtaeplrDKQGFCIPVEPGK--- 490
Cdd:PRK03640 279 ---IPVYQSYGMTETAsqiVTLspedaLTKLG---SAGKP------LFP---CELKIE------KDGVVVPPFEEGEivv 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 491 PGLLLTKvrknqpflGYRgSQAESNRKLVANvrrvGdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVL 570
Cdd:PRK03640 338 KGPNVTK--------GYL-NREDATRETFQD----G--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVL 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 571 SSLDFLEEVNVYGVPvPGCEGKVGMAAVKLapGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVRE 650
Cdd:PRK03640 403 LSHPGVAEAGVVGVP-DDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
122-647 |
1.69e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 104.50 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 122 QALAWPDRVALVCTGSeGSSITNSQLDARSCQAAWVLKaklKDAVIQNTRDAaailVLPSKTISALSVFLGLAKLGC--- 198
Cdd:PRK09088 4 HARLQPQRLAAVDLAL-GRRWTYAELDALVGRLAAVLR---RRGCVDGERLA----VLARNSVWLVALHFACARVGAiyv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 199 PVAWinphsrgmpllhsvRSSGasvlivdPDLQENLEEVLPKLLaenihcfyLGHSSPTPG------VEALGASLDAAPS 272
Cdd:PRK09088 76 PLNW--------------RLSA-------SELDALLQDAEPRLL--------LGDDAVAAGrtdvedLAAFIASADALEP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 273 DPVPASLRatikwKSPAIFIFTSGTTGLPKPAILSHERVIQVSNVLSFCG-CRADDVVYDVLPLYHTIGLVLGFLGCLQV 351
Cdd:PRK09088 127 ADTPSIPP-----ERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGrVDAHSSFLCDAPMFHIIGLITSVRPVLAV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 352 GATCVLAPKFSASRFWAECRQHGVTVILYVGeilrylcnVPEQPEdkihtvRLAMGNGLRANVWKNFQQRF---GP---- 424
Cdd:PRK09088 202 GGSILVSNGFEPKRTLGRLGDPALGITHYFC--------VPQMAQ------AFRAQPGFDAAALRHLTALFtggAPhaae 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 425 -IRIW--------EFYGSTE-GNVGLMNY-----VGHCGAVGrtscilrmlTPFELVQFDIETAEPlRDkqgfcipVEPG 489
Cdd:PRK09088 268 dILGWlddgipmvDGFGMSEaGTVFGMSVdcdviRAKAGAAG---------IPTPTVQTRVVDDQG-ND-------CPAG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 490 KPGLLLtkVRKNQPFLGYRGSQAESNRKLVAnvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECV 569
Cdd:PRK09088 331 VPGELL--LRGPNLSPGYWRRPQATARAFTG------DGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAV 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008365 570 LSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:PRK09088 403 LADHPGIRECAVVGMADAQW-GEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
127-650 |
1.94e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 104.39 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVCTGSeGSSITNSQLDARSCQAAWVL-KAKLKDAviqntrDAAAILVlpSKTISALSVFLGLAKLGCPVAWINP 205
Cdd:PRK13391 11 PDKPAVIMAST-GEVVTYRELDERSNRLAHLFrSLGLKRG------DHVAIFM--ENNLRYLEVCWAAERSGLYYTCVNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 206 HSRGMPLLHSVRSSGASVLIVDP---DLQENLEEVLPKLLaeniHCFYLGHSSPTPGVEALGASLDAAPSDPVPASLRAT 282
Cdd:PRK13391 82 HLTPAEAAYIVDDSGARALITSAaklDVARALLKQCPGVR----HRLVLDGDGELEGFVGYAEAVAGLPATPIADESLGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 283 IkwkspaiFIFTSGTTGLPKP--AILSHERVIQVSNVLSFC----GCRADDVVYDVLPLYHTIGLvlGFLGCLQ-VGATC 355
Cdd:PRK13391 158 D-------MLYSSGTTGRPKGikRPLPEQPPDTPLPLTAFLqrlwGFRSDMVYLSPAPLYHSAPQ--RAVMLVIrLGGTV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 356 VLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDK--IHTVRLAMGNG--LRANVWKNFQQRFGPIrIWEFY 431
Cdd:PRK13391 229 IVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKydLSSLEVAIHAAapCPPQVKEQMIDWWGPI-IHEYY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 432 GSTEGN----VGLMNYVGHCGAVGRTSC-ILRMLtpfelvqfdietaeplrDKQGFCIPvePGKPGLLLTKVRKNQPFLG 506
Cdd:PRK13391 308 AATEGLgftaCDSEEWLAHPGTVGRAMFgDLHIL-----------------DDDGAELP--PGEPGTIWFEGGRPFEYLN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 507 YRGSQAESnrklvanvrRVGDLYFNT-GDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVP 585
Cdd:PRK13391 369 DPAKTAEA---------RHPDGTWSTvGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVP 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 586 VP--GCEGKvgmAAVKLAPGKTFD---GQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKsRLVRE 650
Cdd:PRK13391 440 NEdlGEEVK---AVVQPVDGVDPGpalAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYK-RLLRD 505
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
113-603 |
3.23e-23 |
|
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: 103.74 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 113 ETFVDALERQALAWPDRVALVCTGSeGSSITNSQLDAR-SCQAAWVLKAKLKDA-----VIQNTRDAAAILvlpsktisa 186
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPAR-GLRLTYSELRARiEAVAARLHARGLRPGqrvavVLPNSVEAVIAL--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 187 lsvfLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDlqenlEEVLPKLLAENIHCFYLGHSSPTPGVEALGAS 266
Cdd:cd05923 71 ----LALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVD-----AQVMDAIFQSGVRVLALSDLVGLGEPESAGPL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 267 LDAAPSDPvpaslratikwKSPAIFIFTSGTTGLPKPAILSH----ERVIQVSNVlsfCGCR--ADDVVYDVLPLYHTIG 340
Cdd:cd05923 142 IEDPPREP-----------EQPAFVFYTSGTTGLPKGAVIPQraaeSRVLFMSTQ---AGLRhgRHNVVLGLMPLYHVIG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 341 LVLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVR------LAMGNGLRANV 414
Cdd:cd05923 208 FFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRhvtfagATMPDAVLERV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 415 wknfqQRFGPIRIWEFYGSTEGNVGLMNYVGHCGAVGRTSCilrmltpFELVQFdietaepLRDKQGFCIPVEPGKPGLL 494
Cdd:cd05923 288 -----NQHLPGEKVNIYGTTEAMNSLYMRDARTGTEMRPGF-------FSEVRI-------VRIGGSPDEALANGEEGEL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 495 LTKVRKNQPFLGYRGSQAESNRKLVanvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLD 574
Cdd:cd05923 349 IVAAAADAAFTGYLNQPEATAKKLQ-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHP 421
|
490 500
....*....|....*....|....*....
gi 228008365 575 FLEEVNVYGVPVPGCeGKVGMAAVKLAPG 603
Cdd:cd05923 422 GVTEVVVIGVADERW-GQSVTACVVPREG 449
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
256-648 |
3.86e-23 |
|
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: 103.23 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 256 PTPGVEALGASLDAAPSDPVPASLRAtikWKspaiFIFTSGTTGLPKpAILSH--ERVIQVSNVLSF---CGCRADDVVY 330
Cdd:cd05929 102 ALDGLEDYEAAEGGSPETPIEDEAAG---WK----MLYSGGTTGRPK-GIKRGlpGGPPDNDTLMAAalgFGPGADSVYL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 331 DVLPLYHTIGLVLGFLGcLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDK--IHTVRLAMGN 408
Cdd:cd05929 174 SPAPLYHAAPFRWSMTA-LFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAydLSSLKRVIHA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 409 GLRANVW-KNFQQRFGPIRIWEFYGSTEGNvGLM-----NYVGHCGAVGRTscilrmltpfelVQFDIEtaepLRDKQGf 482
Cdd:cd05929 253 AAPCPPWvKEQWIDWGGPIIWEYYGGTEGQ-GLTiingeEWLTHPGSVGRA------------VLGKVH----ILDEDG- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 483 cIPVEPGKPGLLLtkVRKNQPFL---GYRGSQAESNRKLVANVrrvgdlyfntGDVLTLDQEGFFYFQDRLGDTFRWKGE 559
Cdd:cd05929 315 -NEVPPGEIGEVY--FANGPGFEytnDPEKTAAARNEGGWSTL----------GDVGYLDEDGYLYLTDRRSDMIISGGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 560 NVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPG---KTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEI 636
Cdd:cd05929 382 NIYPQEIENALIAHPKVLDAAVVGVPDEEL-GQRVHAVVQPAPGadaGTALAEELIAFLRDRLSRYKCPRSIEFVAELPR 460
|
410
....*....|..
gi 228008365 637 TNTYKLVKSRLV 648
Cdd:cd05929 461 DDTGKLYRRLLR 472
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
103-567 |
1.56e-22 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 103.47 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 103 FRRRLNKHPP--ETFVDALERqalaWPDRVALVCTGseGSSITNSQLDArscqAAWVLKAKLKDAviqnTRDAAAI-LVL 179
Cdd:PRK08633 607 WKSRKEALPPlaEAWIDTAKR----NWSRLAVADST--GGELSYGKALT----GALALARLLKRE----LKDEENVgILL 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 180 PSKTISALsVFLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKL-LAENIHCFYLGHSSPTP 258
Cdd:PRK08633 673 PPSVAGAL-ANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLeLPENVKVIYLEDLKAKI 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 259 G-VEALGASLDA--APSDPVPASLRATIKWKSPAIFIFTSGTTGLPKPAILSHERVI----QVSNVLSFcgcRADDVVYD 331
Cdd:PRK08633 752 SkVDKLTALLAArlLPARLLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILsnieQISDVFNL---RNDDVILS 828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 332 VLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAE-CRQHGVTVILYVGEILR-YLCNVPEQPEDkIHTVRLAMGNG 409
Cdd:PRK08633 829 SLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKlVAKHRATILLGTPTFLRlYLRNKKLHPLM-FASLRLVVAGA 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 410 --LRANVWKNFQQRFGpIRIWEFYGSTE----GNVGLMNY--------VGH-CGAVGRT--SCILRMLTPfelvqfdiET 472
Cdd:PRK08633 908 ekLKPEVADAFEEKFG-IRILEGYGATEtspvASVNLPDVlaadfkrqTGSkEGSVGMPlpGVAVRIVDP--------ET 978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 473 AEPLrdkqgfcipvEPGKPGLLLtkVRKNQPFLGYRGsQAESNRKLVANVRRVGdlYFNTGDVLTLDQEGFFYFQDRLGD 552
Cdd:PRK08633 979 FEEL----------PPGEDGLIL--IGGPQVMKGYLG-DPEKTAEVIKDIDGIG--WYVTGDKGHLDEDGFLTITDRYSR 1043
|
490
....*....|....*
gi 228008365 553 TFRWKGENVSTGEVE 567
Cdd:PRK08633 1044 FAKIGGEMVPLGAVE 1058
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
116-647 |
5.40e-22 |
|
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: 100.04 E-value: 5.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 116 VDALERQALAWPDRVALVctgSEGSSITNSQLDARSCQAAWVLKAKlkdAVIQNTRdaAAILVLPSktiSALSV-FLGLA 194
Cdd:cd17646 1 HALVAEQAARTPDAPAVV---DEGRTLTYRELDERANRLAHLLRAR---GVGPEDR--VAVLLPRS---ADLVVaLLAVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 195 KLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQenleevlpkllaenihcfylGHSSPTPGVEALGASLDAAPSDP 274
Cdd:cd17646 70 KAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTADLA--------------------ARLPAGGDVALLGDEALAAPPAT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 275 VPAslrATIKWKSPAIFIFTSGTTGLPKPAILSHERViqVSNVLSFC---GCRADDVVYDVLPLYHTIGlVLGFLGCLQV 351
Cdd:cd17646 130 PPL---VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGI--VNRLLWMQdeyPLGPGDRVLQKTPLSFDVS-VWELFWPLVA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 352 GATCVLA-------PKFSASRFwaecRQHGVTVILYVGEILRYLCNVPEQPEdkIHTVRLAM--GNGLRANVWKNFQQRF 422
Cdd:cd17646 204 GARLVVArpgghrdPAYLAALI----REHGVTTCHFVPSMLRVFLAEPAAGS--CASLRRVFcsGEALPPELAARFLALP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 423 GpIRIWEFYGSTEGNVGLMNYVGHCGAVGRTSCILRMLTPFELVQFDietaEPLRdkqgfciPVEPGKPG-LLLTKVrkn 501
Cdd:cd17646 278 G-AELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLD----DALR-------PVPVGVPGeLYLGGV--- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 502 QPFLGYRGSQAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNV 581
Cdd:cd17646 343 QLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008365 582 YGVPVPGcEGKVGMAAVKLAPGKT-FDGQKLYQHVRSWLPAYATP-HFIRIqDSLEITNTYKLVKSRL 647
Cdd:cd17646 423 VARAAPA-GAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPaAFVVL-DALPLTANGKLDRAAL 488
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
113-650 |
8.26e-22 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 99.74 E-value: 8.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 113 ETFVDALERQALAWPDRVALVctgSEGSSITNSQLDARS-CQAAWV---LKAKLKDAVIqntrdaaaiLVLPSKTISALS 188
Cdd:PRK08974 23 QSLVDMFEQAVARYADQPAFI---NMGEVMTFRKLEERSrAFAAYLqngLGLKKGDRVA---------LMMPNLLQYPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 189 VFlGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAENIHCFYLGHSSPTPG--------- 259
Cdd:PRK08974 91 LF-GILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDQLSTAKgtlvnfvvk 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 260 -VEALgasldaAPSDPVPASL---------------RATIKWKSPAIFIFTSGTTGLPKPAILSHERVIqvSNVLSFCGC 323
Cdd:PRK08974 170 yIKRL------VPKYHLPDAIsfrsalhkgrrmqyvKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNML--ANLEQAKAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 324 ------RADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLA--PKfSASRFWAECRQHGVTVILYVGEILRYLCNVPEQP 395
Cdd:PRK08974 242 ygpllhPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLItnPR-DIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 396 EDKIHTVRLAMGNGLR-----ANVWKNFQQRfgpiRIWEFYGSTEGN----VGLMNYVGHCGAVGrtscilrmltpFELV 466
Cdd:PRK08974 321 ELDFSSLKLSVGGGMAvqqavAERWVKLTGQ----YLLEGYGLTECSplvsVNPYDLDYYSGSIG-----------LPVP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 467 QFDIEtaepLRDKQGFCIPvePGKPGLLLtkVRKNQPFLGYRGSQAESnrklvANVrrVGDLYFNTGDVLTLDQEGFFYF 546
Cdd:PRK08974 386 STEIK----LVDDDGNEVP--PGEPGELW--VKGPQVMLGYWQRPEAT-----DEV--IKDGWLATGDIAVMDEEGFLRI 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 547 QDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEGKVGMAAVKLAPGKTFDgqKLYQHVRSWLPAYATPH 626
Cdd:PRK08974 451 VDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEE--ELITHCRRHLTGYKVPK 528
|
570 580
....*....|....*....|....
gi 228008365 627 FIRIQDSLEITNTYKLVKsRLVRE 650
Cdd:PRK08974 529 LVEFRDELPKSNVGKILR-RELRD 551
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
289-642 |
1.26e-21 |
|
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: 98.32 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 289 AIFIFTSGTTGLPKPAILSHeRVIQVSNVLSFCGCRAD--DVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRF 366
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTH-FSAAANALQSAVWTGLTpsDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 367 WAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNG--LRANVWKNFQQRFGpIRIWEFYGSTEGnvglMNYV 444
Cdd:cd05935 166 LELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTG-LRFVEGYGLTET----MSQT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 445 gHCGAVGR--TSCILRMLTPFELVQFDIETAEPLrdkqgfcipvEPGKPGLLLtkVRKNQPFLGYrGSQAESNRKLVANV 522
Cdd:cd05935 241 -HTNPPLRpkLQCLGIP*FGVDARVIDIETGREL----------PPNEVGEIV--VRGPQIFKGY-WNRPEETEESFIEI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 523 RrvGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGcEGKVGMAAVKLAP 602
Cdd:cd05935 307 K--GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDER-VGEEVKAFIVLRP 383
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 228008365 603 GK--TFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:cd05935 384 EYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
288-649 |
1.48e-21 |
|
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: 97.89 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAILSHERVIQVSNVLSFC---GCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATcVLA---PKF 361
Cdd:cd05971 90 PALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPfnlFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVP-VLAhrmTKF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 362 SASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVR-LAMGN---GLRANVWKnfQQRFGpIRIWEFYGSTEGN 437
Cdd:cd05971 169 DPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRaIATGGeslGEELLGWA--REQFG-VEVNEFYGQTECN 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 438 VglmnYVGHC--------GAVGRTscilrmlTPFELVQfdietaepLRDKQGfcIPVEPGKPGLLLTKVRKNQPFLGY-R 508
Cdd:cd05971 246 L----VIGNCsalfpikpGSMGKP-------IPGHRVA--------IVDDNG--TPLPPGEVGEIAVELPDPVAFLGYwN 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 509 GSQAesnrklvANVRRVGDlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPg 588
Cdd:cd05971 305 NPSA-------TEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDP- 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 228008365 589 CEGKVGMAAVKLAPGKTFDGQ---KLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVR 649
Cdd:cd05971 376 IRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
112-647 |
2.88e-21 |
|
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: 97.40 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 112 PETFVDALERQALAWPDRVALVCtgsEGSSITNSQLDARSCQAAwvlkAKLKDAVIQntRDAAAILVLPSkTISALSVFL 191
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVD---GDRRLTYRELDRRADRLA----AGLRGLGIR--PGDRVVVQLPN-VAEFVVLFF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 192 GLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDpdlqENLEEVLPKLLAENIHcfylgHSSPTPgvealgasldaap 271
Cdd:cd05920 84 ALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVP----DRHAGFDHRALARELA-----ESIPEV------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 272 sdpvpaslratikwkspAIFIFTSGTTGLPKPAILSHERVI-QVSNVLSFCGCRADDVVYDVLPLYHTIGLVL-GFLGCL 349
Cdd:cd05920 142 -----------------ALFLLSGGTTGTPKLIPRTHNDYAyNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 350 QVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRL--AMGNGLRANVWKNFQQRFGPiRI 427
Cdd:cd05920 205 LAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLlqVGGARLSPALARRVPPVLGC-TL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 428 WEFYGSTEGnvgLMNYVghcgavgrtscilRMLTPFELVqfdIET-AEPLR--------DKQGfcIPVEPGKPGLLLTkv 498
Cdd:cd05920 284 QQVFGMAEG---LLNYT-------------RLDDPDEVI---IHTqGRPMSpddeirvvDEEG--NPVPPGEEGELLT-- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 499 RKNQPFLGYRGSQAESNRKLVAnvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEE 578
Cdd:cd05920 341 RGPYTIRGYYRAPEHNARAFTP------DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHD 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 579 VNVYGVPVPGCEGKVgmAAVKLAPGKTFDGQKLYQHVRSW-LPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd05920 415 AAVVAMPDELLGERS--CAFVVLRDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
127-647 |
7.33e-21 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 96.75 E-value: 7.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVctgSEGSSITNSQLDARSCQAAWVLKAklkdaVIQNTRDAAAILVLPSKT-ISALsvfLGLAKLGCPVAWINP 205
Cdd:PRK13382 57 PDRPGLI---DELGTLTWRELDERSDALAAALQA-----LPIGEPRVVGIMCRNHRGfVEAL---LAANRIGADILLLNT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 206 HSRGMPLLHSVRSSGASVLIVDpdlqENLEEVLPKLLAENIHCFYLGHSSPTPGvEALGASLDAAPSDPVPasLRATIKW 285
Cdd:PRK13382 126 SFAGPALAEVVTREGVDTVIYD----EEFSATVDRALADCPQATRIVAWTDEDH-DLTVEVLIAAHAGQRP--EPTGRKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 286 KspaIFIFTSGTTGLPKPAILSHERVIQV-SNVLSFCGCRADDVVYDVLPLYHTIG---LVL-GFLGClqvgaTCVLAPK 360
Cdd:PRK13382 199 R---VILLTSGTTGTPKGARRSGPGGIGTlKAILDRTPWRAEEPTVIVAPMFHAWGfsqLVLaASLAC-----TIVTRRR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 361 FSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKI--HTVRLAMGNG--LRANVWKNFQQRFGPIrIWEFYGSTEg 436
Cdd:PRK13382 271 FDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYsgRSLRFAAASGsrMRPDVVIAFMDQFGDV-IYNNYNATE- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 437 nVGLMNyvghcgavgrtscilrMLTPFELvQFDIETA-EP-----LR--DKQGFCIPvePGKPGLLLtkVRKNQPFLGYR 508
Cdd:PRK13382 349 -AGMIA----------------TATPADL-RAAPDTAgRPaegteIRilDQDFREVP--TGEVGTIF--VRNDTQFDGYT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 509 -GSQAESNRKLVAnvrrvgdlyfnTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVP 587
Cdd:PRK13382 407 sGSTKDFHDGFMA-----------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDE 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 588 GCeGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:PRK13382 476 QY-GQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
137-647 |
1.27e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 96.10 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 137 SEGSSITNSQLDARSCQ-AAWVL-KAKLKDAviqntrDAAAiLVLPSKTISALSVFlGLAKLGCPVAWINPHSRGMPLLH 214
Cdd:PRK08751 46 SFGKTITYREADQLVEQfAAYLLgELQLKKG------DRVA-LMMPNCLQYPIATF-GVLRAGLTVVNVNPLYTPRELKH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 215 SVRSSGASVLIVDPDLQENLEEVLPKLLAENIHCFYLGHSSPTPGVEALGASLD----AAPSDPVPASLR------ATIK 284
Cdd:PRK08751 118 QLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGFPKAALVNFVVKyvkkLVPEYRINGAIRfrealaLGRK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 285 WKSPAIFI---------FTSGTTGLPKPAILSHERVI----QVSNVLSFCGC--RADDVVYDVLPLYHTIGLVLGFLGCL 349
Cdd:PRK08751 198 HSMPTLQIepddiaflqYTGGTTGVAKGAMLTHRNLVanmqQAHQWLAGTGKleEGCEVVITALPLYHIFALTANGLVFM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 350 QVGATCVLapkFSASR----FWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLR-----ANVWKnfqq 420
Cdd:PRK08751 278 KIGGCNHL---ISNPRdmpgFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAvqrsvAERWK---- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 421 RFGPIRIWEFYGSTEGN----VGLMNYVGHCGAVGrtscilrMLTPfelvqfdiETAEPLRDKQGFCIPVepGKPGLLLt 496
Cdd:PRK08751 351 QVTGLTLVEAYGLTETSpaacINPLTLKEYNGSIG-------LPIP--------STDACIKDDAGTVLAI--GEIGELC- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 497 kVRKNQPFLGYRGSQAESNRKLVAnvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFL 576
Cdd:PRK08751 413 -IKGPQVMKGYWKRPEETAKVMDA------DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGV 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228008365 577 EEVNVYGVPVPGCEGKVGMAAVKLAPGKTFDGQKlyQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:PRK08751 486 LEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVK--AHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
286-649 |
1.69e-20 |
|
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: 94.88 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 286 KSPAIFIFTSGTTGLPKPAILSHERVIQ--VSNVLSFcGCRADDVvydvlpLYHT------IGLVLGFLGCLQVGATCVL 357
Cdd:cd05969 89 EDPTLLHYTSGTTGTPKGVLHVHDAMIFyyFTGKYVL-DLHPDDI------YWCTadpgwvTGTVYGIWAPWLNGVTNVV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 358 -APKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDK--IHTVRL--AMGNGLRANVWKNFQQRFGpIRIWEFYG 432
Cdd:cd05969 162 yEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKydLSSLRFihSVGEPLNPEAIRWGMEVFG-VPIHDTWW 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 433 STE-GNVGLMNYVGH---CGAVGRtscilrmltPFElvqfDIETAepLRDKQGFciPVEPGKPGLLltKVRKNQP--FLG 506
Cdd:cd05969 241 QTEtGSIMIANYPCMpikPGSMGK---------PLP----GVKAA--VVDENGN--ELPPGTKGIL--ALKPGWPsmFRG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 507 YRGSQAESNRKLVanvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPV 586
Cdd:cd05969 302 IWNDEERYKNSFI-------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPD 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008365 587 PgCEGKVGMAAVKLAPGktFD-----GQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKsRLVR 649
Cdd:cd05969 375 P-LRGEIIKAFISLKEG--FEpsdelKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMR-RVLK 438
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
127-647 |
2.07e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 95.08 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVcTGSEGSSITNSQLDARSCQAAWVLKaklkDAVIqntRDAAAILVLPSKTISALSVFLGLAKLGCPVAWINPH 206
Cdd:PRK13390 11 PDRPAVI-VAETGEQVSYRQLDDDSAALARVLY----DAGL---RTGDVVALLSDNSPEALVVLWAALRSGLYITAINHH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 207 SRGMPLLHSVRSSGASVLIVDPDLQENLEEVlpkllaenihcfylghSSPTPGVEALGASLDAApsdpvpASLRATIKWK 286
Cdd:PRK13390 83 LTAPEADYIVGDSGARVLVASAALDGLAAKV----------------GADLPLRLSFGGEIDGF------GSFEAALAGA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 287 SP--------AIFIFTSGTTGLPK---PAIlsHERVIQ------VSNVLSFCGCRADDVVYDVLPLYHTIGLV-LGFLGC 348
Cdd:PRK13390 141 GPrlteqpcgAVMLYSSGTTGFPKgiqPDL--PGRDVDapgdpiVAIARAFYDISESDIYYSSAPIYHAAPLRwCSMVHA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 349 LqvGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDK---------IHT-------VRLAMGNGLra 412
Cdd:PRK13390 219 L--GGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRydvsslravIHAaapcpvdVKHAMIDWL-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 413 nvwknfqqrfGPIrIWEFYGSTEGN----VGLMNYVGHCGAVGRTscilrmltpfelVQFDIETAeplrDKQGFCIPVep 488
Cdd:PRK13390 295 ----------GPI-VYEYYSSTEAHgmtfIDSPDWLAHPGSVGRS------------VLGDLHIC----DDDGNELPA-- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 489 GKPGLLLTKvRKNQPFlgyrgSQAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVEC 568
Cdd:PRK13390 346 GRIGTVYFE-RDRLPF-----RYLNDPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETEN 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 569 VLSSLDFLEEVNVYGVPVPGCEGKVgMAAVKLAPGktFDG-----QKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLV 643
Cdd:PRK13390 420 ALTMHPAVHDVAVIGVPDPEMGEQV-KAVIQLVEG--IRGsdelaRELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLV 496
|
....
gi 228008365 644 KSRL 647
Cdd:PRK13390 497 KGLL 500
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
119-642 |
3.39e-20 |
|
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: 94.33 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 119 LERQALAWPDRVALVCtgsEGSSITNSQLDARSCQAAWVLKAklkDAViqNTRDAAAILVLPS-KTISALsvfLGLAKLG 197
Cdd:cd17651 1 FERQAARTPDAPALVA---EGRRLTYAELDRRANRLAHRLRA---RGV--GPGDLVALCARRSaELVVAL---LAILKAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 198 CPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPkllaenihcfylghssptPGVEALGASLDAAPSDPVPA 277
Cdd:cd17651 70 AAYVPLDPAYPAERLAFMLADAGPVLVLTHPALAGELAVELV------------------AVTLLDQPGAAAGADAEPDP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 278 SLRAtikwKSPAIFIFTSGTTGLPKPAILSHerviqvSNVLSFcgCRADDVVYDVLPLYHTIGLV-LGF-------LGCL 349
Cdd:cd17651 132 ALDA----DDLAYVIYTSGSTGRPKGVVMPH------RSLANL--VAWQARASSLGPGARTLQFAgLGFdvsvqeiFSTL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 350 QVGATCVLAP---KFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVR--------LAMGNGLRAnvwknF 418
Cdd:cd17651 200 CAGATLVLPPeevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRylltggeqLVLTEDLRE-----F 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 419 QQRFGPIRIWEFYGSTEGNVGLMNYV-GHCGAVGRTSCILRMLTPFELVQFDietaEPLRdkqgfciPVEPGKPGLLLtk 497
Cdd:cd17651 275 CAGLPGLRLHNHYGPTETHVVTALSLpGDPAAWPAPPPIGRPIDNTRVYVLD----AALR-------PVPPGVPGELY-- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 498 VRKNQPFLGYRGSQAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLE 577
Cdd:cd17651 342 IGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVR 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 228008365 578 EVNVYGVPVPGCEGKVgMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:cd17651 422 EAVVLAREDRPGEKRL-VAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
116-652 |
4.42e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 94.28 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 116 VDALERqalaWPDRVALVCTGSegsSITNSQLDARSCQAAWVLKAklkdaVIQNTRDAAAILVLPSktisALSVFLGLAK 195
Cdd:PRK06188 19 VSALKR----YPDRPALVLGDT---RLTYGQLADRISRYIQAFEA-----LGLGTGDAVALLSLNR----PEVLMAIGAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 196 --LGCPVAWINP------HsrgmplLHSVRSSGASVLIVDP----DLQENLEEVLPKLLaeniHCFYLGhssPTPGVEAL 263
Cdd:PRK06188 83 qlAGLRRTALHPlgslddH------AYVLEDAGISTLIVDPapfvERALALLARVPSLK----HVLTLG---PVPDGVDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 264 GASLDAAPSDP-VPASLRATIKWkspaiFIFTSGTTGLPKPAILSH-ERVIQVSNVLSFCGCRADDVVYDVLPLYHTIGL 341
Cdd:PRK06188 150 LAAAAKFGPAPlVAAALPPDIAG-----LAYTGGTTGKPKGVMGTHrSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 342 VlgFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPE-------------DKIHTVRLAMGn 408
Cdd:PRK06188 225 F--FLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTrdlssletvyygaSPMSPVRLAEA- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 409 glranvwknfQQRFGPIrIWEFYGSTEG--NVGLMNYVGHCGA-VGR-TSCilRMLTPFELVQfdietaepLRDKQGfcI 484
Cdd:PRK06188 302 ----------IERFGPI-FAQYYGQTEApmVITYLRKRDHDPDdPKRlTSC--GRPTPGLRVA--------LLDEDG--R 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 485 PVEPGKPGLLLtkVRKnqPFL--GYRGSQAESnrklvANVRRVGDLYfnTGDVLTLDQEGFFYFQDRLGDTFRWKGENVS 562
Cdd:PRK06188 359 EVAQGEVGEIC--VRG--PLVmdGYWNRPEET-----AEAFRDGWLH--TGDVAREDEDGFYYIVDRKKDMIVTGGFNVF 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 563 TGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:PRK06188 428 PREVEDVLAEHPAVAQVAVIGVPDEKW-GEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKP 506
|
570
....*....|
gi 228008365 643 VKsRLVREGF 652
Cdd:PRK06188 507 DK-KALRARY 515
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
113-650 |
5.91e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 94.07 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 113 ETFVDALERQALAWPDRVALVctgsegssitNSQLDARscqAAWvlkAKLKDAVIQNTRDAAAILVLP--------SKTI 184
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALV----------VRHQALR---YTW---RQLADAVDRLARGLLALGVQPgdrvgiwaPNCA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 185 SALSVFLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDP-----DLQENLEEVLPKLL---AENIHCFYLGH--- 253
Cdd:PRK12583 82 EWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADafktsDYHAMLQELLPGLAegqPGALACERLPElrg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 254 -----SSPTPGVEALGASLDAAP--SDPVPASLRATIKWKSPAIFIFTSGTTGLPKPAILSHERVIqvsNVLSFCGCRAD 326
Cdd:PRK12583 162 vvslaPAPPPGFLAWHELQARGEtvSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNIL---NNGYFVAESLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 327 DVVYDVL----PLYHTIGLVLGFLGCLQVGAtCVLAPK-----FSASRFWAECRQ---HGVTViLYVGEIlrylcNVPEQ 394
Cdd:PRK12583 239 LTEHDRLcvpvPLYHCFGMVLANLGCMTVGA-CLVYPNeafdpLATLQAVEEERCtalYGVPT-MFIAEL-----DHPQR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 395 PEDKIHTVRLAMGNG------LRANVWKnfQQRFGPIRIweFYGSTEGN-VGLMNyvghcgavGRTSCILRMLTPFELVQ 467
Cdd:PRK12583 312 GNFDLSSLRTGIMAGapcpieVMRRVMD--EMHMAEVQI--AYGMTETSpVSLQT--------TAADDLERRVETVGRTQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 468 FDIETAepLRDKQGFCIPvePGKPGLLLTkvRKNQPFLGYRGsQAESNRKLVAnvrrvGDLYFNTGDVLTLDQEGFFYFQ 547
Cdd:PRK12583 380 PHLEVK--VVDPDGATVP--RGEIGELCT--RGYSVMKGYWN-NPEATAESID-----EDGWMHTGDLATMDEQGYVRIV 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 548 DRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPvpgCE--GKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATP 625
Cdd:PRK12583 448 GRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVP---DEkyGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVP 524
|
570 580
....*....|....*....|....*
gi 228008365 626 HFIRIQDSLEITNTYKLVKSRLvRE 650
Cdd:PRK12583 525 RYFRFVDEFPMTVTGKVQKFRM-RE 548
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
187-650 |
6.27e-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: 93.85 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 187 LSVFLGLAKLGCPVAWINPhsRGMP--LLHSVRSSGASVLIVDPDLQENLEEVLPKLlaENIHCFYL------GHSSPTP 258
Cdd:cd12119 64 LELYYAVPGMGAVLHTINP--RLFPeqIAYIINHAEDRVVFVDRDFLPLLEAIAPRL--PTVEHVVVmtddaaMPEPAGV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 259 GVEALGASLDAAPsdpvpaslrATIKW-----KSPAIFIFTSGTTGLPKPAILSHERVI----QVSNVLSFcGCRADDVV 329
Cdd:cd12119 140 GVLAYEELLAAES---------PEYDWpdfdeNTAAAICYTSGTTGNPKGVVYSHRSLVlhamAALLTDGL-GLSESDVV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 330 YDVLPLYHTIGLVLGFlGCLQVGATCVLAPKFSASRFWAEC-RQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM-- 406
Cdd:cd12119 210 LPVVPMFHVNAWGLPY-AAAMVGAKLVLPGPYLDPASLAELiEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVig 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 407 GNGLRANVWKNFQQRFgpIRIWEFYGSTEgnvglmnyVGHCGAVGRTscilrmltPFELVQFDIETAEPLRDKQGFCIP- 485
Cdd:cd12119 289 GSAVPRSLIEAFEERG--VRVIHAWGMTE--------TSPLGTVARP--------PSEHSNLSEDEQLALRAKQGRPVPg 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 486 -----VEPG---KP------GLLltKVRKnqPFL--GYRGSQAESNRKLVanvrrvgDLYFNTGDVLTLDQEGFFYFQDR 549
Cdd:cd12119 351 velriVDDDgreLPwdgkavGEL--QVRG--PWVtkSYYKNDEESEALTE-------DGWLRTGDVATIDEDGYLTITDR 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 550 LGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPgcegKVG---MAAVKLAPGKTFDGQKLYQHVRSWLPAYATPH 626
Cdd:cd12119 420 SKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHP----KWGerpLAVVVLKEGATVTAEELLEFLADKVAKWWLPD 495
|
490 500
....*....|....*....|....
gi 228008365 627 FIRIQDSLEITNTYKLVKSRLvRE 650
Cdd:cd12119 496 DVVFVDEIPKTSTGKIDKKAL-RE 518
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
274-650 |
1.08e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 93.32 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 274 PVPASLRATIKW--KSPAIFIFTSGTTGLPKPAILSHER-VIQVSNVLSFCGCRADDVVYDVLPLYHtIGLVLGFLGCLQ 350
Cdd:PLN02860 158 RALGTTELDYAWapDDAVLICFTSGTTGRPKGVTISHSAlIVQSLAKIAIVGYGEDDVYLHTAPLCH-IGGLSSALAMLM 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 351 VGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPE--DKIHTVR--LAMGNGLRANVWKNFQQRFGPIR 426
Cdd:PLN02860 237 VGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMtwKVFPSVRkiLNGGGSLSSRLLPDAKKLFPNAK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 427 IWEFYGSTEGnvglmnyvghCGAVgrTSCILRMLTPFELVQFDIETAEPLRD----KQGFCI------------PVEPGK 490
Cdd:PLN02860 317 LFSAYGMTEA----------CSSL--TFMTLHDPTLESPKQTLQTVNQTKSSsvhqPQGVCVgkpaphvelkigLDESSR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 491 PGLLLTkvRKNQPFLGYRGSQAESnrklvANVrRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVL 570
Cdd:PLN02860 385 VGRILT--RGPHVMLGYWGQNSET-----ASV-LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 571 SSLDFLEEVNVYGVPvpgcEGKVG---MAAVKLAPG--------------KTFDGQKLYQHVRSW-LPAYATPH-FIRIQ 631
Cdd:PLN02860 457 SQHPGVASVVVVGVP----DSRLTemvVACVRLRDGwiwsdnekenakknLTLSSETLRHHCREKnLSRFKIPKlFVQWR 532
|
410
....*....|....*....
gi 228008365 632 DSLEITNTYKLVKSRLVRE 650
Cdd:PLN02860 533 KPFPLTTTGKIRRDEVRRE 551
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
111-583 |
1.19e-19 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 93.24 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 111 PPETFVDALERQALAWPDRVALVC-TGSEGSSITNSQLDARSCQAAWVLKA---KLKDAViqntrdaaAILvlpSKTISA 186
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREkEDGIWQSLTWAEFAERVRALAAGLLAlgvKPGDRV--------AIL---SDNRPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 187 LSVF-LGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIV-DPDLQENLEEV---LPKLlaENIHCFYLGHSSPTPGV- 260
Cdd:COG1022 78 WVIAdLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVrdeLPSL--RHIVVLDPRGLRDDPRLl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 261 -----EALGAsldAAPSDPVPASLRATIKWKSPAIFIFTSGTTGLPKPAILSHERVI-QVSNVLSFCGCRADDVVYDVLP 334
Cdd:COG1022 156 sldelLALGR---EVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLsNARALLERLPLGPGDRTLSFLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 335 LYHTIGLVLGFlGCLQVGATCVLAPkfSASRFWAECRQHGVTvilyvgeilrYLCNVPEQPEdKIHT------------- 401
Cdd:COG1022 233 LAHVFERTVSY-YALAAGATVAFAE--SPDTLAEDLREVKPT----------FMLAVPRVWE-KVYAgiqakaeeagglk 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 402 ---VRLAMGNGLRAN-----------------------VWKNFQQRFGP------------------------IRIWEFY 431
Cdd:COG1022 299 rklFRWALAVGRRYArarlagkspslllrlkhaladklVFSKLREALGGrlrfavsggaalgpelarffralgIPVLEGY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 432 GSTE-GNVGLMNYVGHC--GAVGRtscilrmltPFELVQFDIetaeplrdkqgfcipvepGKPGLLLtkVRKNQPFLGYR 508
Cdd:COG1022 379 GLTEtSPVITVNRPGDNriGTVGP---------PLPGVEVKI------------------AEDGEIL--VRGPNVMKGYY 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008365 509 GSQAESNRKLVAnvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFrwK---GENVSTGEVECVLSSLDFLEEVNVYG 583
Cdd:COG1022 430 KNPEATAEAFDA------DGWLHTGDIGELDEDGFLRITGRKKDLI--VtsgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
117-652 |
1.64e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 92.25 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 117 DALeRQALAWPDRVALvcTGSEGSSITNSQLDARSCQAAWVLKA-KLK--DAVIQNTRDAAAILVLPSKTISALSVFLGL 193
Cdd:PRK07514 7 DAL-RAAFADRDAPFI--ETPDGLRYTYGDLDAASARLANLLVAlGVKpgDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 194 aklgcpvawiNPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAenIHCFYL---GHSSPTPGVEALGASLDAA 270
Cdd:PRK07514 84 ----------NTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGA--PHVETLdadGTGSLLEAAAAAPDDFETV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 271 PSDPvpaslratikwKSPAIFIFTSGTTGLPKPAILSHERVIqvSNVLS---FCGCRADDVVYDVLPLYHTIGLVLGFLG 347
Cdd:PRK07514 152 PRGA-----------DDLAAILYTSGTTGRSKGAMLSHGNLL--SNALTlvdYWRFTPDDVLIHALPIFHTHGLFVATNV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 348 CLQVGATCVLAPKFSASRFWAECRQhgVTVI-----LYVgeilRYLCNvPEQPEDKIHTVRLAM-GNG-LRANVWKNFQQ 420
Cdd:PRK07514 219 ALLAGASMIFLPKFDPDAVLALMPR--ATVMmgvptFYT----RLLQE-PRLTREAAAHMRLFIsGSApLLAETHREFQE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 421 RFGPiRIWEFYGSTEGNvglMN----YVGH--CGAVGRTscilrmLTPFELVQFDIETAEPLrdkqgfcipvEPGKPGLL 494
Cdd:PRK07514 292 RTGH-AILERYGMTETN---MNtsnpYDGErrAGTVGFP------LPGVSLRVTDPETGAEL----------PPGEIGMI 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 495 ltKVRKNQPFLGY-R--GSQAESNRklvanvrrvGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLS 571
Cdd:PRK07514 352 --EVKGPNVFKGYwRmpEKTAEEFR---------ADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEID 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 572 SLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEiTNTYKLVKSRLVREG 651
Cdd:PRK07514 421 ELPGVVESAVIGVPHPDF-GEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELP-RNTMGKVQKNLLREQ 498
|
.
gi 228008365 652 F 652
Cdd:PRK07514 499 Y 499
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
120-642 |
3.77e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 92.92 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 120 ERQALAWPDRVALVctgSEGSSITNSQLDARSCQAAWVLKAKlkdAVIQNTRDAAAIlvlpSKTISALSVFLGLAKLGCP 199
Cdd:PRK12467 519 EAQARQHPERPALV---FGEQVLSYAELNRQANRLAHVLIAA---GVGPDVLVGIAV----ERSIEMVVGLLAVLKAGGA 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 200 VAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLE-----EVLPKLLAENIHCFYLGHSSPTPgvealgasLDaapsdp 274
Cdd:PRK12467 589 YVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPvpaglRSLCLDEPADLLCGYSGHNPEVA--------LD------ 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 275 vPASLratikwkspAIFIFTSGTTGLPKPAILSHERVIQVSNVLS-FCGCRADDVVYDVLPLYHTIGlVLGFLGCLQVGA 353
Cdd:PRK12467 655 -PDNL---------AYVIYTSGSTGQPKGVAISHGALANYVCVIAeRLQLAADDSMLMVSTFAFDLG-VTELFGALASGA 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 354 TCVLAPK---FSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRanvWKNFQQ--RFGP-IRI 427
Cdd:PRK12467 724 TLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQ---VDLLARvrALGPgARL 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 428 WEFYGSTEGNVGLMNY-VGHCGAVGRTSCILRMLTPFELVQFDIETAeplrdkqgfciPVEPGKPGLLLtkVRKNQPFLG 506
Cdd:PRK12467 801 INHYGPTETTVGVSTYeLSDEERDFGNVPIGQPLANLGLYILDHYLN-----------PVPVGVVGELY--IGGAGLARG 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 507 YRGSQAESNRKLVAN-VRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVygVP 585
Cdd:PRK12467 868 YHRRPALTAERFVPDpFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV--LA 945
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 228008365 586 VPGCEGKVGMAAvkLAPGKTFDGQK-------LYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:PRK12467 946 QPGDAGLQLVAY--LVPAAVADGAEhqatrdeLKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
288-642 |
6.45e-19 |
|
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: 89.88 E-value: 6.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAIlshervIQVSNVLSF-------CGCRADDVVYDVLPLYHTIGLVLGFLGCLQVG-ATCVLAP 359
Cdd:cd05973 90 PFVMMFTSGTTGLPKGVP------VPLRALAAFgaylrdaVDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLEG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 360 KFSASRFWAECRQHGVTVILYVGEILRYL----CNVPEQPEDKIHTVRLAmGNGLRANVWKNFQQRFGpIRIWEFYGSTE 435
Cdd:cd05973 164 GFSVESTWRVIERLGVTNLAGSPTAYRLLmaagAEVPARPKGRLRRVSSA-GEPLTPEVIRWFDAALG-VPIHDHYGQTE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 436 GNVGLMNYVG-----HCGAVGRTscilrmLTPFELVQFDIETAEPLrdkqgfcipvePGKPGLLLTKVRkNQPFLGYRGS 510
Cdd:cd05973 242 LGMVLANHHAlehpvHAGSAGRA------MPGWRVAVLDDDGDELG-----------PGEPGRLAIDIA-NSPLMWFRGY 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 511 QAESNRKLVANvrrvgdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPgCE 590
Cdd:cd05973 304 QLPDTPAIDGG-------YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDP-ER 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 228008365 591 GKVGMAAVKLAPGktFDG-----QKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:cd05973 376 TEVVKAFVVLRGG--HEGtpalaDELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI 430
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
117-643 |
7.40e-19 |
|
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: 90.71 E-value: 7.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 117 DALERQALAWPDRVALVCTGSEGS---SITNSQLDARSCQAAWVLKAKlkdAVIQNTRDAAAILVLPSKTISALSVflgl 193
Cdd:cd17634 57 NALDRHLRENGDRTAIIYEGDDTSqsrTISYRELHREVCRFAGTLLDL---GVKKGDRVAIYMPMIPEAAVAMLAC---- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 194 AKLGCPVAWINPHSRGMPLLHSVRSSGASVLI-----VDPDLQENLEEVLPKLLAENI----HCFYLGHS-SPTPGVEAL 263
Cdd:cd17634 130 ARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLItadggVRAGRSVPLKKNVDDALNPNVtsveHVIVLKRTgSDIDWQEGR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 264 GASLDAAPSDPVPASLRATIKWKSPAIFIFTSGTTGLPKPAILSHE-RVIQVSNVLSFCgcraddvvYDVLP--LYHT-- 338
Cdd:cd17634 210 DLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGgYLVYAATTMKYV--------FDYGPgdIYWCta 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 339 -IGLVLG----FLGCLQVGATCVL---APKF-SASRFWAECRQHGVTVILYVGEILRYLcnVPEQPE----DKIHTVRLA 405
Cdd:cd17634 282 dVGWVTGhsylLYGPLACGATTLLyegVPNWpTPARMWQVVDKHGVNILYTAPTAIRAL--MAAGDDaiegTDRSSLRIL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 406 MGNGLRAN--VWKNFQQRFGPIR--IWEFYGSTEGNvglmnyvGHCGAVGRTSCILRMLTPFELVqfdIETAEPLRDKQG 481
Cdd:cd17634 360 GSVGEPINpeAYEWYWKKIGKEKcpVVDTWWQTETG-------GFMITPLPGAIELKAGSATRPV---FGVQPAVVDNEG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 482 FciPVEPGKPG-LLLTKVRKNQPFLGYRgsqaESNRKLVANVRRVGDLYFnTGDVLTLDQEGFFYFQDRLGDTFRWKGEN 560
Cdd:cd17634 430 H--PQPGGTEGnLVITDPWPGQTRTLFG----DHERFEQTYFSTFKGMYF-SGDGARRDEDGYYWITGRSDDVINVAGHR 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 561 VSTGEVECVLSSLDFLEEVNVYGVPVPgCEGKVGMAAVKLAPGKTfDGQKLYQHVRSW----LPAYATPHFIRIQDSLEI 636
Cdd:cd17634 503 LGTAEIESVLVAHPKVAEAAVVGIPHA-IKGQAPYAYVVLNHGVE-PSPELYAELRNWvrkeIGPLATPDVVHWVDSLPK 580
|
....*..
gi 228008365 637 TNTYKLV 643
Cdd:cd17634 581 TRSGKIM 587
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
113-650 |
3.03e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 88.57 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 113 ETFVDALERQALAWPDRVALVCTGSEGSS---ITNSQLDARSCQAAWVLkaklkdaviqntrdaAAILVLPSKTISA--- 186
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTAVRLGTGAprrFTYRELAALVDRVAVGL---------------ARLGVGRGDVVSCqlp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 187 -----LSVFLGLAKLGcpvAWINPHsrgMP------LLHSVRSSGASVLIVD--------PDLQENLEEVLPKLLaeniH 247
Cdd:PRK13295 89 nwwefTVLYLACSRIG---AVLNPL---MPifrereLSFMLKHAESKVLVVPktfrgfdhAAMARRLRPELPALR----H 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 248 CFYLGHSSPTpGVEAL--GASLDAAPSDPVP-ASLRAtikwkSP---AIFIFTSGTTGLPKPAILSHERViqVSNVLSF- 320
Cdd:PRK13295 159 VVVVGGDGAD-SFEALliTPAWEQEPDAPAIlARLRP-----GPddvTQLIYTSGTTGEPKGVMHTANTL--MANIVPYa 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 321 --CGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDK 398
Cdd:PRK13295 231 erLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 399 IHTVR--LAMGNGLRANVWKNFQQRFGpIRIWEFYGSTEgnvglmnyvghCGAVgrTSCIL-----RMLT----PFELVQ 467
Cdd:PRK13295 311 VSSLRtfLCAGAPIPGALVERARAALG-AKIVSAWGMTE-----------NGAV--TLTKLddpdeRASTtdgcPLPGVE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 468 FDIetaeplRDKQGfcIPVEPGKPGLLLtkVRKNQPFLGYRGsQAESNRKLvanvrrvGDLYFNTGDVLTLDQEGFFYFQ 547
Cdd:PRK13295 377 VRV------VDADG--APLPAGQIGRLQ--VRGCSNFGGYLK-RPQLNGTD-------ADGWFDTGDLARIDADGYIRIS 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 548 DRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPGKTFDgqklYQHVRSWLPAYAT--- 624
Cdd:PRK13295 439 GRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERL-GERACAFVVPRPGQSLD----FEEMVEFLKAQKVakq 513
|
570 580
....*....|....*....|....*...
gi 228008365 625 --PHFIRIQDSLEITNTYKLVKSRLvRE 650
Cdd:PRK13295 514 yiPERLVVRDALPRTPSGKIQKFRL-RE 540
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
165-651 |
3.18e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 88.12 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 165 AVIQNTRDAAAILVLPSKTISALSVFLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVD-PDLQENLEEVLPKLLA 243
Cdd:PRK07787 37 AVAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPaPDDPAGLPHVPVRLHA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 244 ENIHcfylghssptpgvealgasldaAPSDPVPASlratikwksPAIFIFTSGTTGLPKPAILSHERVIQVSNVLSFC-G 322
Cdd:PRK07787 117 RSWH----------------------RYPEPDPDA---------PALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAwQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 323 CRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQHGvTVILYVGEILRYLCNVPEQPEdKIHTV 402
Cdd:PRK07787 166 WTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQALSEGG-TLYFGVPTVWSRIAADPEAAR-ALRGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 403 RLAMGNG--LRANVWKNFQQRFGpIRIWEFYGSTEgnvGLMNYVGHC------GAVGrtscilrmlTPFELVQFDietae 474
Cdd:PRK07787 244 RLLVSGSaaLPVPVFDRLAALTG-HRPVERYGMTE---TLITLSTRAdgerrpGWVG---------LPLAGVETR----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 475 pLRDKQGFCIPVEPGKPGLLltKVRKNQPFLGYRG---SQAESnrklvanvrRVGDLYFNTGDVLTLDQEGFFYFQDRLG 551
Cdd:PRK07787 306 -LVDEDGGPVPHDGETVGEL--QVRGPTLFDGYLNrpdATAAA---------FTADGWFRTGDVAVVDPDGMHRIVGRES 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 552 -DTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVklAPGKTFDGQKLYQHVRSWLPAYATPHFIRI 630
Cdd:PRK07787 374 tDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDL-GQRIVAYV--VGADDVAADELIDFVAQQLSVHKRPREVRF 450
|
490 500
....*....|....*....|.
gi 228008365 631 QDSLEITNTYKLVKSRLVREG 651
Cdd:PRK07787 451 VDALPRNAMGKVLKKQLLSEG 471
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
143-581 |
3.48e-18 |
|
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: 87.32 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 143 TNSQLDARSCQAAWVLKA----KLKDAViqntrdaaAILVlpSKTISALSVFLGLAKLGC---PVAWINPHSRgmpLLHS 215
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaggvGPGDRV--------AVLL--ERSAELVVAILAVLKAGAayvPLDPAYPAER---LAFI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 216 VRSSGASVLIVDPDLQENLEEVLPkllaenihcfylghsSPTPGVEALGASLDAAPSDPVPASLRATIkwkSPAIFIFTS 295
Cdd:TIGR01733 68 LEDAGARLLLTDSALASRLAGLVL---------------PVILLDPLELAALDDAPAPPPPDAPSGPD---DLAYVIYTS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 296 GTTGLPKPAILSHERViqVSNVLSFCGC---RADDVVYDVLPLYHTIGlVLGFLGCLQVGATCVLAPK---FSASRFWAE 369
Cdd:TIGR01733 130 GSTGRPKGVVVTHRSL--VNLLAWLARRyglDPDDRVLQFASLSFDAS-VEEIFGALLAGATLVVPPEdeeRDDAALLAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 370 C-RQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAmGNGLRANVWKNFQQRFGPIRIWEFYGSTEGNVGLMNYVGHCG 448
Cdd:TIGR01733 207 LiAEHPVTVLNLTPSLLALLAAALPPALASLRLVILG-GEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 449 AVGRTS--CILRmltPFELVQFDIETAEpLRdkqgfciPVEPGKPGLLLtkVRKNQPFLGYRGSQAESNRKLVANVRRVG 526
Cdd:TIGR01733 286 DAPRESpvPIGR---PLANTRLYVLDDD-LR-------PVPVGVVGELY--IGGPGVARGYLNRPELTAERFVPDPFAGG 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 228008365 527 D---LYFnTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNV 581
Cdd:TIGR01733 353 DgarLYR-TGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
287-585 |
3.55e-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: 87.82 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 287 SPAIFIFTSGTTGLPKPAILSHERVIqvSNVLSFC---GCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSA 363
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHNTLS--ASIRQYAerlGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 364 SRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVR--LAMGNGLRANVWKNFQQRFGPIrIWEFYGSTEgnvglm 441
Cdd:cd05903 172 DKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRtfVCGGATVPRSLARRAAELLGAK-VCSAYGSTE------ 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 442 nyvgHCGAVGRTS---CILRMLT---PFELVQFDIEtaeplrDKQGFCIPvePGKPGLLLtkVRKNQPFLGYrgsqaeSN 515
Cdd:cd05903 245 ----CPGAVTSITpapEDRRLYTdgrPLPGVEIKVV------DDTGATLA--PGVEGELL--SRGPSVFLGY------LD 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 516 RKLvANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVP 585
Cdd:cd05903 305 RPD-LTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALP 373
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
288-642 |
6.91e-18 |
|
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: 85.39 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAILSHERVIQVSNVLSFCGCR--ADDVVYDVLPLYHTIGLvLGFLGCLQVGATCVLAPKFSASR 365
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNwvVGDVTYLPLPATHIGGL-WWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 366 -FWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRA-NVWKNFQQRFGPIRIWEFYGSTE-GNVGLMN 442
Cdd:cd17635 82 sLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAiAADVRFIEATGLTNTAQVYGLSEtGTALCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 443 Y---VGHCGAVGRTscilrmLTPFELVQFDIETAEPLRDKQGFCIpvepgkpgllltkVRKNQPFLGYRGSQAESNRKLV 519
Cdd:cd17635 162 TdddSIEINAVGRP------YPGVDVYLAATDGIAGPSASFGTIW-------------IKSPANMLGYWNNPERTAEVLI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 520 anvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEGKVGMAAVK 599
Cdd:cd17635 223 -------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA 295
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 228008365 600 LAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:cd17635 296 SAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
281-647 |
8.13e-18 |
|
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: 86.25 E-value: 8.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 281 ATIKWKSPAIFIFTSGTTGLPKPAILSHERVI--QVSNVLSFcGCRADDVVYDVLPLYHTIGLVLGFLGcLQVGATCVLA 358
Cdd:cd05912 72 SDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWwsAIGSALNL-GLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 359 PKFSASRFWAECRQHGVTVILYVGEILRYLCNV-PEQPEDKIHTVRLAmGNGLRANVWKNFQQRfgPIRIWEFYGSTEGN 437
Cdd:cd05912 150 DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEIlGEGYPNNLRCILLG-GGPAPKPLLEQCKEK--GIPVYQSYGMTETC 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 438 ---VGL-----MNYVGhcgAVGRtscilrmltPFELVQFDIETAEplrdkqgfcipVEPGKPGLLLTK---VRKnqpflG 506
Cdd:cd05912 227 sqiVTLspedaLNKIG---SAGK---------PLFPVELKIEDDG-----------QPPYEVGEILLKgpnVTK-----G 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 507 YRGsQAESNRKLVANVrrvgdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPV 586
Cdd:cd05912 279 YLN-RPDATEESFENG------WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPD 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228008365 587 PGCeGKVGMAAVKLApgKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd05912 352 DKW-GQVPVAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
114-650 |
1.60e-17 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 86.34 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 114 TFVDALERQALAWPDRVALVctGSEGSSITNSQLD-ARSCQAAWVLKAKLKDAviqntrDAAAiLVLPSKTISALsVFLG 192
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVV--DNHGASYTYSALDhAASRLANWLLAKGIEPG------DRVA-FQLPGWCEFTI-IYLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 193 LAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVdPDLQEN---LEEVLPklLAENIHcfYLGH----SSPTPGVEALga 265
Cdd:PRK06087 94 CLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA-PTLFKQtrpVDLILP--LQNQLP--QLQQivgvDKLAPATSSL-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 266 SLDAAPSDPVPASLRATIKWKSPAIFIFTSGTTGLPKPAILSHerviqvSNVL----SFC---GCRADDVVYDVLPLYHT 338
Cdd:PRK06087 167 SLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTH------NNILaserAYCarlNLTWQDVFMMPAPLGHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 339 IGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILyvGE---ILRYLCNVPEQPEDkIHTVRLAMGNG--LRAN 413
Cdd:PRK06087 241 TGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCML--GAtpfIYDLLNLLEKQPAD-LSALRFFLCGGttIPKK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 414 VWKNFQQRfgPIRIWEFYGSTEGnvglmnyVGHCgAVGRTSCILRML----TPFELVQFDIEtaeplrDKQGFCIPvePG 489
Cdd:PRK06087 318 VARECQQR--GIKLLSVYGSTES-------SPHA-VVNLDDPLSRFMhtdgYAAAGVEIKVV------DEARKTLP--PG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 490 KPGLLLTkvRKNQPFLGYRGSQAESNRKLVAnvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECV 569
Cdd:PRK06087 380 CEGEEAS--RGPNVFMGYLDEPELTARALDE------EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDI 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 570 LSSLDFLEEVNVYGVPVPGCEGKVGMAAVKLAPGKTFDGQKLYQHV-RSWLPAYATPHFIRIQDSLEITNTYKLVKSRLV 648
Cdd:PRK06087 452 LLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLR 531
|
..
gi 228008365 649 RE 650
Cdd:PRK06087 532 KD 533
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
105-659 |
3.58e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 85.21 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 105 RRLNkhppetFVDALERQALAWPDRVALVCTGSegsSITNSQLDARSCQAAWVLKAKlkdAVIQNTRdaaaILVLPSKTI 184
Cdd:PRK07786 15 RRQN------WVNQLARHALMQPDAPALRFLGN---TTTWRELDDRVAALAGALSRR---GVGFGDR----VLILMLNRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 185 SALSVFLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVlpKLLAENIHCFYLGHSSPTPGVEALG 264
Cdd:PRK07786 79 EFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAV--RDIVPLLSTVVVAGGSSDDSVLGYE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 265 ASLDAAPSDPVPASlratIKWKSPAIFIFTSGTTGLPKPAILSHERVIQVSNVLSFcGCRAD---DVVYDVLPLYHTIGL 341
Cdd:PRK07786 157 DLLAEAGPAHAPVD----IPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLR-TNGADinsDVGFVGVPLFHIAGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 342 --VLGFlgcLQVGATCVLAP--KFSASRFWAECRQHGVTVILYVGEILRYLCNVPE-QPEDkihtvrLAmgngLRANVW- 415
Cdd:PRK07786 232 gsMLPG---LLLGAPTVIYPlgAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQaRPRD------LA----LRVLSWg 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 416 ---------KNFQQRFGPIRIWEFYGSTEGN-VGLM----NYVGHCGAVGRtscilrmltPFELVQFDIeTAEPLRDkqg 481
Cdd:PRK07786 299 aapasdtllRQMAATFPEAQILAAFGQTEMSpVTCMllgeDAIRKLGSVGK---------VIPTVAARV-VDENMND--- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 482 fcipVEPGKPGLLLtkvrknqpflgYRGSQAES----NRKLVANVRRVGdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWK 557
Cdd:PRK07786 366 ----VPVGEVGEIV-----------YRAPTLMSgywnNPEATAEAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 558 GENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPG-KTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEI 636
Cdd:PRK07786 429 GENIYCAEVENVLASHPDIVEVAVIGRADEKW-GEVPVAVAAVRNDdAALTLEDLAEFLTDRLARYKHPKALEIVDALPR 507
|
570 580
....*....|....*....|...
gi 228008365 637 TNTYKLVKSRLvREGFDVGIIAD 659
Cdd:PRK07786 508 NPAGKVLKTEL-RERYGACVNVE 529
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
127-647 |
4.22e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 84.83 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVcTGSEgsSITNSQLDARSCQAAWVLKAKLKdaviQNTRDAaaiLVLPSKtISALSVFLGLAKLGCPVAWINPH 206
Cdd:PRK07638 15 PNKIAIK-ENDR--VLTYKDWFESVCKVANWLNEKES----KNKTIA---ILLENR-IEFLQLFAGAAMAGWTCVPLDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 207 SRGMPLLHSVRSSGASVLIVD---------------------PDLQENLEEVLPKLLAENIHcFYLGhssptpgvealga 265
Cdd:PRK07638 84 WKQDELKERLAISNADMIVTEryklndlpdeegrvieidewkRMIEKYLPTYAPIENVQNAP-FYMG------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 266 sldaapsdpvpaslratikwkspaifiFTSGTTGLPKPAILSHErviqvSNVLSF-C-----GCRADDVVYDVLPLYHTI 339
Cdd:PRK07638 150 ---------------------------FTSGSTGKPKAFLRAQQ-----SWLHSFdCnvhdfHMKREDSVLIAGTLVHSL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 340 GLvLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCN---VPEQPeDKIhtvrLAMGNGLRANVWK 416
Cdd:PRK07638 198 FL-YGAISTLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKenrVIENK-MKI----ISSGAKWEAEAKE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 417 NFQQRFGPIRIWEFYGSTEgnVGLMNYVGHC------GAVGRtscilrmltPFELVQFDIETAEPLRdkqgfcipVEPGK 490
Cdd:PRK07638 272 KIKNIFPYAKLYEFYGASE--LSFVTALVDEeserrpNSVGR---------PFHNVQVRICNEAGEE--------VQKGE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 491 PGLLLtkVRKNQPFLGYRGSQAESNRKLVANVRRVGDLYFntgdvltLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVL 570
Cdd:PRK07638 333 IGTVY--VKSPQFFMGYIIGGVLARELNADGWMTVRDVGY-------EDEEGFIYIVGREKNMILFGGINIFPEEIESVL 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 228008365 571 SSLDFLEEVNVYGVPVPgCEGKVGMAAVKlapGKTfDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:PRK07638 404 HEHPAVDEIVVIGVPDS-YWGEKPVAIIK---GSA-TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
110-599 |
9.94e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 83.86 E-value: 9.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 110 HPPET-FVDALERQALAWPDRVALVCTGSEgssITNSQLDARSCQAAWVLKAKLK----DAVI---QNTrdaaailvlPS 181
Cdd:PRK08314 6 TLPETsLFHNLEVSARRYPDKTAIVFYGRA---ISYRELLEEAERLAGYLQQECGvrkgDRVLlymQNS---------PQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 182 KTISALSVFlglaKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKL-LAENIHCFYLGHSSPTPGV 260
Cdd:PRK08314 74 FVIAYYAIL----RANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLrLRHVIVAQYSDYLPAEPEI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 261 eALGASLDAAPSDPVPASLRATiKWKSP-----------------AIFIFTSGTTGLPKPAILSHERVIqvSNVLSFC-- 321
Cdd:PRK08314 150 -AVPAWLRAEPPLQALAPGGVV-AWKEAlaaglappphtagpddlAVLPYTSGTTGVPKGCMHTHRTVM--ANAVGSVlw 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 322 -GCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKfsasrfW-----AEC-RQHGVTVILYVGEILRYLCNVPEQ 394
Cdd:PRK08314 226 sNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPR------WdreaaARLiERYRVTHWTNIPTMVVDFLASPGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 395 PEDKIHTVRLAMGNG--LRANVWKNFQQRFGpIRIWEFYGSTE-GNVGLMNYVGHcgavGRTSCilrMLTPFELVQ---F 468
Cdd:PRK08314 300 AERDLSSLRYIGGGGaaMPEAVAERLKELTG-LDYVEGYGLTEtMAQTHSNPPDR----PKLQC---LGIPTFGVDarvI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 469 DIETAEPLrdkqgfcipvEPGKPGLLLtkVRKNQPFLGYRGsQAESNRKlvANVRRVGDLYFNTGDVLTLDQEGFFYFQD 548
Cdd:PRK08314 372 DPETLEEL----------PPGEVGEIV--VHGPQVFKGYWN-RPEATAE--AFIEIDGKRFFRTGDLGRMDEEGYFFITD 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 228008365 549 RLGDTFRWKGENVSTGEVE------------CVLSSLDFL--EEVNVYGVPVPGCEGKVG-----------MAAVK 599
Cdd:PRK08314 437 RLKRMINASGFKVWPAEVEnllykhpaiqeaCVIATPDPRrgETVKAVVVLRPEARGKTTeeeiiawarehMAAYK 512
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
105-649 |
1.74e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 84.24 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 105 RRLNKHPPETFVDAL-ERQALAWPDRVALVCTGSEGSSitnSQLDARSCQAAWVLKAKlkdAVIQNTRDAAAILVLPSKT 183
Cdd:PRK12316 1994 RTPEAYPRGPGVHQRiAEQAARAPEAIAVVFGDQHLSY---AELDSRANRLAHRLRAR---GVGPEVRVAIAAERSFELV 2067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 184 ISalsvFLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLeevlpkLLAENIHCFYLghssptpgvEAL 263
Cdd:PRK12316 2068 VA----LLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERL------PLPAGVARLPL---------DRD 2128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 264 GASLDAAPSDPVPASLRATIkwkspAIFIFTSGTTGLPKPAILSHERVIQvsnvlsfcGCRADDVVYDVLP---LYHTI- 339
Cdd:PRK12316 2129 AEWADYPDTAPAVQLAGENL-----AYVIYTSGSTGLPKGVAVSHGALVA--------HCQAAGERYELSPadcELQFMs 2195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 340 ----GLVLGFLGCLQVGATCVLAPK--FSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM-GNGLRA 412
Cdd:PRK12316 2196 fsfdGAHEQWFHPLLNGARVLIRDDelWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFgGEAVPA 2275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 413 NVWKNFQQRFGPIRIWEFYGSTEGNVG-LMNYVGH---CGAV---------GRTSCILRmltpfelvqfdiETAEPLrdK 479
Cdd:PRK12316 2276 ASLRLAWEALRPVYLFNGYGPTEAVVTpLLWKCRPqdpCGAAyvpigralgNRRAYILD------------ADLNLL--A 2341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 480 QGFCIPVEPGKPGLlltkVRknqpflGYRGSQAESNRKLVAN-VRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKG 558
Cdd:PRK12316 2342 PGMAGELYLGGEGL----AR------GYLNRPGLTAERFVPDpFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRG 2411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 559 ENVSTGEVECVLSSLDFLEEVNVygVPVPGCEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITN 638
Cdd:PRK12316 2412 FRIELGEIEARLQAHPAVREAVV--VAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNP 2489
|
570
....*....|.
gi 228008365 639 TYKLVKSRLVR 649
Cdd:PRK12316 2490 NGKLDRKALPK 2500
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
118-617 |
2.53e-16 |
|
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: 82.57 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 118 ALERQALaWPDRVALVcTGSEGSSITNSQLDARSCQAAWVLKaklKDAVIQNTRdaaaILVLPSKTIS-ALSVFLGLAkL 196
Cdd:cd17642 23 AMKRYAS-VPGTIAFT-DAHTGVNYSYAEYLEMSVRLAEALK---KYGLKQNDR----IAVCSENSLQfFLPVIAGLF-I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 197 GCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKL-LAENI------------HCFYLGHSSPTPgveal 263
Cdd:cd17642 93 GVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLkIIKTIiildskedykgyQCLYTFITQNLP----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 264 gASLDAAPSDPVPASLRATIkwkspAIFIFTSGTTGLPKPAILSHERViqvsnVLSFCGCR---------ADDVVYDVLP 334
Cdd:cd17642 168 -PGFNEYDFKPPSFDRDEQV-----ALIMNSSGSTGLPKGVQLTHKNI-----VARFSHARdpifgnqiiPDTAILTVIP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 335 LYHTIGLvLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVP-EQPEDKIHTVRLAMGNG-LRA 412
Cdd:cd17642 237 FHHGFGM-FTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGApLSK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 413 NVWKNFQQRFGPIRIWEFYGSTEGNVG-LMNYVGHC--GAVGRtscilrmLTPFELVQ-FDIETAEPLrdkqgfcipvEP 488
Cdd:cd17642 316 EVGEAVAKRFKLPGIRQGYGLTETTSAiLITPEGDDkpGAVGK-------VVPFFYAKvVDLDTGKTL----------GP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 489 GKPGLLLtkVRKNQPFLGYRGSQaESNRKLVANvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVEC 568
Cdd:cd17642 379 NERGELC--VKGPMIMKGYVNNP-EATKALIDK-----DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELES 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 228008365 569 VLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPGKTFDGQKLYQHVRS 617
Cdd:cd17642 451 ILLQHPKIFDAGVAGIPDEDA-GELPAAVVVLEAGKTMTEKEVMDYVAS 498
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
143-647 |
2.95e-16 |
|
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: 81.73 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 143 TNSQLDarsCQAAWVLKAkLKDAVIQNTRDAAaiLVLPSKTISALSVFLGLAkLGCPVAWINPHSRGMPLLHSVRSSGAS 222
Cdd:TIGR01923 1 TWQDLD---CEAAHLAKA-LKAQGIRSGSRVA--LVGQNSIEMVLLLHACLL-LGAEIAMLNTRLTENERTNQLEDLDVQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 223 VLIVDPDLQENleevlpKLLAENIHcfylghssptpgvealgaslDAAPSDPVPASLRATIKWKSPAIFIFTSGTTGLPK 302
Cdd:TIGR01923 74 LLLTDSLLEEK------DFQADSLD--------------------RIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 303 PAILSH----ERVIQVSNVLSFcgcRADDVVYDVLPLYHTIGLVLgFLGCLQVGATCVLAPKFSAsrfWAECRQHG-VTV 377
Cdd:TIGR01923 128 AVPHTFrnhyASAVGSKENLGF---TEDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDKFNQ---LLEMIANErVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 378 ILYVGEIL-RYLcnvpEQ--PEDKIHTVRLAmGNGLRANVWKNFQQRFGPIriWEFYGSTEgnvglmnyvghcgavgRTS 454
Cdd:TIGR01923 201 ISLVPTQLnRLL----DEggHNENLRKILLG-GSAIPAPLIEEAQQYGLPI--YLSYGMTE----------------TCS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 455 CILRMLTPFELVQFDIETAEPLRDKQgfcIPVePGKPGLLLTKVRKNQPFLGYRGsqaesNRKLVANVRRVGdlYFNTGD 534
Cdd:TIGR01923 258 QVTTATPEMLHARPDVGRPLAGREIK---IKV-DNKEGHGEIMVKGANLMKGYLY-----QGELTPAFEQQG--WFNTGD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 535 VLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVygVPVPGCE-GKVGMAAVKLApgKTFDGQKLYQ 613
Cdd:TIGR01923 327 IGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVV--VPKPDAEwGQVPVAYIVSE--SDISQAKLIA 402
|
490 500 510
....*....|....*....|....*....|....*
gi 228008365 614 HVRSWLPAYATP-HFIRIqDSLEITNTYKLVKSRL 647
Cdd:TIGR01923 403 YLTEKLAKYKVPiAFEKL-DELPYNASGKILRNQL 436
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
289-647 |
2.98e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 80.99 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 289 AIFIFTSGTTGLPKPAILSHERVIQVSNVLSFCGC-RADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAP------KF 361
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLfDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyrnPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 362 SASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEdkIHTVRLAMGNG--LRANVWKNFQQRFGpIRIWEFYGSTEGNVG 439
Cdd:cd05944 85 LFDNFWKLVERYRITSLSTVPTVYAALLQVPVNAD--ISSLRFAMSGAapLPVELRARFEDATG-LPVVEGYGLTEATCL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 440 L-MNYVG---HCGAVGrtsciLRMltPFELVQFDIETAE--PLRDkqgfCIPVEPGK-----PGLlltkvrknqpFLGYr 508
Cdd:cd05944 162 VaVNPPDgpkRPGSVG-----LRL--PYARVRIKVLDGVgrLLRD----CAPDEVGEicvagPGV----------FGGY- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 509 gSQAESNRKLVanvrrVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPG 588
Cdd:cd05944 220 -LYTEGNKNAF-----VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAH 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 589 CeGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYAT-PHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd05944 294 A-GELPVAYVQLKPGAVVEEEELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
103-572 |
6.34e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 81.18 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 103 FRRRL------NKHPPETFVdaLERQAlAWPDRVALVcTGSEGSSITNSQLDARSCQAAWVLkAKL---KDAVIqntrda 173
Cdd:PLN02246 10 FRSKLpdiyipNHLPLHDYC--FERLS-EFSDRPCLI-DGATGRVYTYADVELLSRRVAAGL-HKLgirQGDVV------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 174 aaILVLPSKTISALSvFLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVdpdlQENLEEVLPKLLAEN---IHCF- 249
Cdd:PLN02246 79 --MLLLPNCPEFVLA-FLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT----QSCYVDKLKGLAEDDgvtVVTId 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 250 -----YLGHSSPTPGVEALGASLDAAPSDPV--PaslratikwkspaifiFTSGTTGLPKPAILSHERVI-----QVSNV 317
Cdd:PLN02246 152 dppegCLHFSELTQADENELPEVEISPDDVValP----------------YSSGTTGLPKGVMLTHKGLVtsvaqQVDGE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 318 LSFCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPED 397
Cdd:PLN02246 216 NPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 398 KIHTVRLAMGNG--LRANVWKNFQQRFGPIRIWEFYGSTE-GNVGLMNYV----------GHCGAVGRTScilrmltpfE 464
Cdd:PLN02246 296 DLSSIRMVLSGAapLGKELEDAFRAKLPNAVLGQGYGMTEaGPVLAMCLAfakepfpvksGSCGTVVRNA---------E 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 465 LVQFDIETAEPL-RDKQG-FCIpvepgkpgllltkvRKNQPFLGYRGSqAESNRKLVANvrrvgDLYFNTGDVLTLDQEG 542
Cdd:PLN02246 367 LKIVDPETGASLpRNQPGeICI--------------RGPQIMKGYLND-PEATANTIDK-----DGWLHTGDIGYIDDDD 426
|
490 500 510
....*....|....*....|....*....|
gi 228008365 543 FFYFQDRLGDTFRWKGENVSTGEVECVLSS 572
Cdd:PLN02246 427 ELFIVDRLKELIKYKGFQVAPAELEALLIS 456
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
116-652 |
1.10e-15 |
|
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: 80.61 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 116 VDALERQALA-WPDRVALVCTGSEGS--SITNSQLDARSCQAAWVLKA---KLKDAVIqntrdaaaiLVLPsKTISALSV 189
Cdd:cd05968 63 VEQLLDKWLAdTRTRPALRWEGEDGTsrTLTYGELLYEVKRLANGLRAlgvGKGDRVG---------IYLP-MIPEIVPA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 190 FLGLAKLGcpvAWINPHSRGM---PLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAENI--HCFYLGHSSPtpgVEALG 264
Cdd:cd05968 133 FLAVARIG---GIVVPIFSGFgkeAAATRLQDAEAKALITADGFTRRGREVNLKEEADKAcaQCPTVEKVVV---VRHLG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 265 ASLDAAPSDPV--------PASLRATIKWKSPAIFIFTSGTTGLPKPAILSHERV-IQVSNVLSFC-GCRADDVVYDVLP 334
Cdd:cd05968 207 NDFTPAKGRDLsydeeketAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQfDLKPGDLLTWFTD 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 335 LYHTIGLVLGFlGCLQVGATCVL---APKF-SASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDK--IHTVRLAMGN 408
Cdd:cd05968 287 LGWMMGPWLIF-GGLILGATMVLydgAPDHpKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAhdLSSLRVLGST 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 409 GLRANV--WKnfqqrfgpiriWEFYGSTEGNVGLMNYVGHCGAVGRTSC--ILRMLTPFELVQFDIETAEPLRDKQGFCI 484
Cdd:cd05968 366 GEPWNPepWN-----------WLFETVGKGRNPIINYSGGTEISGGILGnvLIKPIKPSSFNGPVPGMKADVLDESGKPA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 485 PVEPGKpgLLLTKvrknqPFLGY-RGSQAESNRKLVANVRRVGDLYFNtGDVLTLDQEGFFYFQDRLGDTFRWKGENVST 563
Cdd:cd05968 435 RPEVGE--LVLLA-----PWPGMtRGFWRDEDRYLETYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGP 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 564 GEVECVLSSLDFLEEVNVYGVPVPgCEGKVGMAAVKLAPGKTFDG---QKLYQHVRSWLPAYATPHFIRIQDSLEITNTY 640
Cdd:cd05968 507 AEIESVLNAHPAVLESAAIGVPHP-VKGEAIVCFVVLKPGVTPTEalaEELMERVADELGKPLSPERILFVKDLPKTRNA 585
|
570
....*....|..
gi 228008365 641 KLVKsRLVREGF 652
Cdd:cd05968 586 KVMR-RVIRAAY 596
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
179-647 |
1.50e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 80.19 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 179 LPSKTISALSVFlGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPK------LLAE--NIH--- 247
Cdd:PRK05677 82 LPNVLQYPVAVF-GAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKtgvkhvIVTEvaDMLppl 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 248 -----------------CFYLGHSSPTPGVEALGASLDAAPSDPVPASLratikwkspAIFIFTSGTTGLPKPAILSHER 310
Cdd:PRK05677 161 krllinavvkhvkkmvpAYHLPQAVKFNDALAKGAGQPVTEANPQADDV---------AVLQYTGGTTGVAKGAMLTHRN 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 311 ViqVSNVLSfcgCRA---------DDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPK---FSAsrFWAECRQHGVTVI 378
Cdd:PRK05677 232 L--VANMLQ---CRAlmgsnlnegCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNprdLPA--MVKELGKWKFSGF 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 379 LYVGEILRYLCNVPEQPEDKIHTVRLAMGNG--LRANVWKNFQQRFGpIRIWEFYGSTEGN-VGLMNYVGHC--GAVGrt 453
Cdd:PRK05677 305 VGLNTLFVALCNNEAFRKLDFSALKLTLSGGmaLQLATAERWKEVTG-CAICEGYGMTETSpVVSVNPSQAIqvGTIG-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 454 scilrMLTPFELVQfdietaepLRDKQGFCIPVepGKPGLLLtkVRKNQPFLGYRGSQAESNRKLVAnvrrvgDLYFNTG 533
Cdd:PRK05677 382 -----IPVPSTLCK--------VIDDDGNELPL--GEVGELC--VKGPQVMKGYWQRPEATDEILDS------DGWLKTG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 534 DVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPvpgcEGKVGmAAVKL----APGKTFDGQ 609
Cdd:PRK05677 439 DIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVP----DEKSG-EAIKVfvvvKPGETLTKE 513
|
490 500 510
....*....|....*....|....*....|....*...
gi 228008365 610 KLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:PRK05677 514 QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
176-622 |
2.04e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 79.89 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 176 ILVLPSkTISALSVFLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEE--VLPKLLAENIHcfylgH 253
Cdd:PLN02574 96 LLLLPN-SVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPlgVPVIGVPENYD-----F 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 254 SSPTPGVEALgASLDAAPSDPVPASLratIKWKSPAIFIFTSGTTGLPKPAILSHERVIqvSNVLSFCGCRA-------- 325
Cdd:PLN02574 170 DSKRIEFPKF-YELIKEDFDFVPKPV---IKQDDVAAIMYSSGTTGASKGVVLTHRNLI--AMVELFVRFEAsqyeypgs 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 326 DDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLcnvpeqpedkIHTVRLA 405
Cdd:PLN02574 244 DNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMAL----------TKKAKGV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 406 MGNGLRANVW-------------KNFQQRFGPIRIWEFYGSTEGNVglmnyvghCGAVGRTSCILRMLTPFELVQFDIEt 472
Cdd:PLN02574 314 CGEVLKSLKQvscgaaplsgkfiQDFVQTLPHVDFIQGYGMTESTA--------VGTRGFNTEKLSKYSSVGLLAPNMQ- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 473 AEPLRDKQGFCIPvePGKPGLLLTKvrknqpflGYRGSQAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGD 552
Cdd:PLN02574 385 AKVVDWSTGCLLP--PGNCGELWIQ--------GPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKE 454
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 553 TFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAY 622
Cdd:PLN02574 455 IIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKEC-GEIPVAFVVRRQGSTLSQEAVINYVAKQVAPY 523
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
103-642 |
2.93e-15 |
|
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: 79.08 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 103 FRRRLNKHPPETF---VDALERQALAWPDRVALVCTGSEGSS--ITNSQLDARSCQAAWVLKAKlkdaVIQntRDAAAIL 177
Cdd:cd05970 4 FHNNFSINVPENFnfaYDVVDAMAKEYPDKLALVWCDDAGEEriFTFAELADYSDKTANFFKAM----GIG--KGDTVML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 178 VLPSKtISALSVFLGLAKLGCpVAWINPHS-RGMPLLHSVRSSGASVLIVD--PDLQENLEEVLPKllAENIHCFYLGHS 254
Cdd:cd05970 78 TLKRR-YEFWYSLLALHKLGA-IAIPATHQlTAKDIVYRIESADIKMIVAIaeDNIPEEIEKAAPE--CPSKPKLVWVGD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 255 SPTPGVEALGASLDAAPSDPVPASLRATIKWKSPAIFIFTSGTTGLPKpaILSHERVIQVSNVLS---FCGCRADDVVYD 331
Cdd:cd05970 154 PVPEGWIDFRKLIKNASPDFERPTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTakyWQNVREGGLHLT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 332 VLPLYHTIGLVLGFLGCLQVGATCVL--APKFSASRFWAECRQHGVTVILYVGEILRYLcnVPEQPED-KIHTVRLAM-- 406
Cdd:cd05970 232 VADTGWGKAVWGKIYGQWIAGAAVFVydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFL--IREDLSRyDLSSLRYCTta 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 407 GNGLRANVWKNFQQRFGpIRIWEFYGSTEGNVGLMNYVG---HCGAVGRTscilrmlTPfelvQFDIEtaepLRDKQGfc 483
Cdd:cd05970 310 GEALNPEVFNTFKEKTG-IKLMEGFGQTETTLTIATFPWmepKPGSMGKP-------AP----GYEID----LIDREG-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 484 IPVEPGKPGLLLTKVRKNQPFLGYRGSQAESNRklVANVRRVGdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVST 563
Cdd:cd05970 372 RSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAEK--TAEVWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGP 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 564 GEVECVLSSLDFLEEVNVYGVPVPgCEGKVGMAAVKLA----PGKTFDgQKLYQHVRSWLPAYATPHFIRIQDSLEITNT 639
Cdd:cd05970 448 FEVESALIQHPAVLECAVTGVPDP-IRGQVVKATIVLAkgyePSEELK-KELQDHVKKVTAPYKYPRIVEFVDELPKTIS 525
|
...
gi 228008365 640 YKL 642
Cdd:cd05970 526 GKI 528
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
110-647 |
4.61e-15 |
|
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: 78.11 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 110 HPPETFVDALERQALAWPDRVALVctgSEGSSITNSQLDARSCQAAwvlkAKLKDAVIQnTRDAAAilVLPSKTISALSV 189
Cdd:cd12118 1 YVPLTPLSFLERAAAVYPDRTSIV---YGDRRYTWRQTYDRCRRLA----SALAALGIS-RGDTVA--VLAPNTPAMYEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 190 FLGLAKLGCPVAWIN----PHSRGMPLLHSvrssGASVLIVDPDLQenLEEVLpkllaenihcfylghssptpgvealga 265
Cdd:cd12118 71 HFGVPMAGAVLNALNtrldAEEIAFILRHS----EAKVLFVDREFE--YEDLL--------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 266 sldaAPSDPVPASLRATIKWKSPAIFiFTSGTTGLPKPAILSHeR---VIQVSNVLSFcGCRADDVVYDVLPLYHTIGLv 342
Cdd:cd12118 118 ----AEGDPDFEWIPPADEWDPIALN-YTSGTTGRPKGVVYHH-RgayLNALANILEW-EMKQHPVYLWTLPMFHCNGW- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 343 lGFL-GCLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKI-HTVRLAMGNGL-RANVWKNFQ 419
Cdd:cd12118 190 -CFPwTVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLpHRVHVMTAGAPpPAAVLAKME 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 420 QrfGPIRIWEFYGSTEgnvglmNYvghcGAVgrTSCI---------------------LRMLTPFELVQFDIETAEPL-R 477
Cdd:cd12118 269 E--LGFDVTHVYGLTE------TY----GPA--TVCAwkpewdelpteerarlkarqgVRYVGLEEVDVLDPETMKPVpR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 478 DkqgfcipvepGKP-GLLLtkVRKNQPFLGY-RGSQAesNRKLVAnvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFR 555
Cdd:cd12118 335 D----------GKTiGEIV--FRGNIVMKGYlKNPEA--TAEAFR------GGWFHSGDLAVIHPDGYIEIKDRSKDIII 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 556 WKGENVSTGEVECVLSSLDFLEEVNVYGVPVPgCEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDsLE 635
Cdd:cd12118 395 SGGENISSVEVEGVLYKHPAVLEAAVVARPDE-KWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LP 472
|
570
....*....|..
gi 228008365 636 ITNTYKLVKSRL 647
Cdd:cd12118 473 KTSTGKIQKFVL 484
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
127-642 |
8.49e-15 |
|
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: 77.35 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVCtgsEGSSITNSQLDARSCQAAWVLKAKlkdAVIQNTRdaAAILVLPS-KTISALsvfLGLAKLG---CPVAW 202
Cdd:cd17643 1 PEAVAVVD---EDRRLTYGELDARANRLARTLRAE---GVGPGDR--VALALPRSaELIVAL---LAILKAGgayVPIDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 203 INPHSRgmpLLHSVRSSGASVLIVDPDlqenleevlpkllaenihcfylghssptpgvealgasldaapsdpvpaslrat 282
Cdd:cd17643 70 AYPVER---IAFILADSGPSLLLTDPD----------------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 283 ikwkSPAIFIFTSGTTGLPKPAILSHerviqvSNVLS-FCGCR------ADDVVYdvlpLYHTIGL---VLGFLGCLQVG 352
Cdd:cd17643 94 ----DLAYVIYTSGSTGRPKGVVVSH------ANVLAlFAATQrwfgfnEDDVWT----LFHSYAFdfsVWEIWGALLHG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 353 ATCVLAPKF---SASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM--GNGLRANVWKNFQQRFGPIR- 426
Cdd:cd17643 160 GRLVVVPYEvarSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLDRp 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 427 -IWEFYGSTEGNVglmnYVGHcgavgrtscilRMLTPFELVQFDIET-AEPLRDKQGFCI-----PVEPGKPGLLLtkVR 499
Cdd:cd17643 240 qLVNMYGITETTV----HVTF-----------RPLDAADLPAAAASPiGRPLPGLRVYVLdadgrPVPPGVVGELY--VS 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 500 KNQPFLGYRGSQAESNRKLVAN-VRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEE 578
Cdd:cd17643 303 GAGVARGYLGRPELTAERFVANpFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRD 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 228008365 579 VNVyGVPVPGCEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:cd17643 383 AAV-IVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
111-625 |
2.21e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 77.01 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 111 PPETFVDALERQALAWPDRVALVctgSEGSSITNSQLDARSCQAAWVLKA---KLKDAViqntrdAAAilvLPSktisal 187
Cdd:PRK10252 456 PETTLSALVAQQAAKTPDAPALA---DARYQFSYREMREQVVALANLLRErgvKPGDSV------AVA---LPR------ 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 188 SVFLGLAklgcpvawinphsrgmplLHSVRSSGASVLIVDPD-----LQENLEEVLPKLL---AENIHCFylghsSPTPG 259
Cdd:PRK10252 518 SVFLTLA------------------LHAIVEAGAAWLPLDTGypddrLKMMLEDARPSLLittADQLPRF-----ADVPD 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 260 VEALGASLDAAPSDPVPASLRATikwKSPAIFIFTSGTTGLPKPAILSHERVIqvsNVLSFC----GCRADDVV------ 329
Cdd:PRK10252 575 LTSLCYNAPLAPQGAAPLQLSQP---HHTAYIIFTSGSTGRPKGVMVGQTAIV---NRLLWMqnhyPLTADDVVlqktpc 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 330 -YDVlplyhtigLVLGFLGCLQVGATCVLAPKfSASRFWAECRQ----HGVTVILYVGEILRYLCN--VPEQPEDKIHTV 402
Cdd:PRK10252 649 sFDV--------SVWEFFWPFIAGAKLVMAEP-EAHRDPLAMQQffaeYGVTTTHFVPSMLAAFVAslTPEGARQSCASL 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 403 R--LAMGNGLRANVWKNFQQRFGpIRIWEFYGSTEGNVGLMNY--VGHCGAVGRTSCI----------LRMLTpfelvqf 468
Cdd:PRK10252 720 RqvFCSGEALPADLCREWQQLTG-APLHNLYGPTEAAVDVSWYpaFGEELAAVRGSSVpigypvwntgLRILD------- 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 469 dietaEPLRdkqgfciPVEPGKPG-LLLTKVRKNQPFLGYRGSQAEsnrKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQ 547
Cdd:PRK10252 792 -----ARMR-------PVPPGVAGdLYLTGIQLAQGYLGRPDLTAS---RFIADPFAPGERMYRTGDVARWLDDGAVEYL 856
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 548 DRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGV-----PVPGCEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAY 622
Cdd:PRK10252 857 GRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaAATGGDARQLVGYLVSQSGLPLDTSALQAQLRERLPPH 936
|
...
gi 228008365 623 ATP 625
Cdd:PRK10252 937 MVP 939
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
121-362 |
2.73e-14 |
|
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: 76.12 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 121 RQALAWPDRVALVCT---GSEGSSITNSQLDARSCQAAWVLKAKLKdaviqnTRDAAAILVLPSktISALSVFLG--LAK 195
Cdd:cd05931 1 RRAAARPDRPAYTFLddeGGREETLTYAELDRRARAIAARLQAVGK------PGDRVLLLAPPG--LDFVAAFLGclYAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 196 LgCPVAWINPH-SRGMPLLHSV-RSSGASVLIVDPDLQENLEEVLpkllaenihcfylgHSSPTPGVEALgASLDAAPSD 273
Cdd:cd05931 73 A-IAVPLPPPTpGRHAERLAAIlADAGPRVVLTTAAALAAVRAFA--------------ASRPAAGTPRL-LVVDLLPDT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 274 PVPASLRATIKWKSPAIFIFTSGTTGLPKPAILSHERVI-QVSNVLSFCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVG 352
Cdd:cd05931 137 SAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLaNVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSG 216
|
250
....*....|
gi 228008365 353 ATCVLAPKFS 362
Cdd:cd05931 217 GPSVLMSPAA 226
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
116-647 |
3.50e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 75.83 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 116 VDALERQALAWPDRVALVCTGSegsSITNSQLDARSCQ-AAWVLKAKLKDA---------VIQNTRDAAAILvlpsktis 185
Cdd:PRK07059 26 ADLLEESFRQYADRPAFICMGK---AITYGELDELSRAlAAWLQSRGLAKGarvaimmpnVLQYPVAIAAVL-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 186 alsvflglaKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAENIHCFYLGH------------ 253
Cdd:PRK07059 95 ---------RAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDllgfkghivnfv 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 254 ---------SSPTPG------VEALGASLDAAPSDPVPASLratikwkspAIFIFTSGTTGLPKPAILSHERViqVSNVL 318
Cdd:PRK07059 166 vrrvkkmvpAWSLPGhvrfndALAEGARQTFKPVKLGPDDV---------AFLQYTGGTTGVSKGATLLHRNI--VANVL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 319 --------SFCGCRADDVVYDV--LPLYHTIGLVLGFLGCLQVGATCVLAPKfsaSR----FWAECRQHGVTVILYVGEI 384
Cdd:PRK07059 235 qmeawlqpAFEKKPRPDQLNFVcaLPLYHIFALTVCGLLGMRTGGRNILIPN---PRdipgFIKELKKYQVHIFPAVNTL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 385 LRYLCNVPEQPEDKIHTVRLAMGNGL--RANVWKNFQQRFG-PIRiwEFYGSTEgnvglmnyvghcgavgrTSCILrMLT 461
Cdd:PRK07059 312 YNALLNNPDFDKLDFSKLIVANGGGMavQRPVAERWLEMTGcPIT--EGYGLSE-----------------TSPVA-TCN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 462 PFELVQFDIETAEPL-------RDKQGFCIPvePGKPGLLLtkVRKNQPFLGYRGSQAESNRKLVAnvrrvgDLYFNTGD 534
Cdd:PRK07059 372 PVDATEFSGTIGLPLpstevsiRDDDGNDLP--LGEPGEIC--IRGPQVMAGYWNRPDETAKVMTA------DGFFRTGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 535 VLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEGKVGMAAVKLAPGKTfdGQKLYQH 614
Cdd:PRK07059 442 VGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALT--EEDVKAF 519
|
570 580 590
....*....|....*....|....*....|...
gi 228008365 615 VRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:PRK07059 520 CKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
252-637 |
3.75e-14 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 75.69 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 252 GHSSPTPGVEaLGASLDAAPSDPVPASLRAtikwkSPAIFIFTSGTTGLPKPAILSHERViqVSNVLSFC---GCRADDV 328
Cdd:PRK05852 148 GPSGGTLSVH-LDAATEPTPATSTPEGLRP-----DDAMIMFTGGTTGLPKMVPWTHANI--ASSVRAIItgyRLSPRDA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 329 VYDVLPLYHTIGLVLGFLGCLQVGATcVLAP---KFSASRFWAECRQHGVTVILYVGEILRYLCNVP--EQPEDKIHTVR 403
Cdd:PRK05852 220 TVAVMPLYHGHGLIAALLATLASGGA-VLLPargRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAatEPSGRKPAALR 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 404 L--AMGNGLRANVWKNFQQRFGPIRIwEFYGSTEGNvglmnyvgHCGAVGRTSCILRMLTPFELVQF-------DIETAE 474
Cdd:PRK05852 299 FirSCSAPLTAETAQALQTEFAAPVV-CAFGMTEAT--------HQVTTTQIEGIGQTENPVVSTGLvgrstgaQIRIVG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 475 PlrDKQgfciPVEPGKPGLLL----TKVRknqpflGYRGSQAESnrklVANVRrvgDLYFNTGDVLTLDQEGFFYFQDRL 550
Cdd:PRK05852 370 S--DGL----PLPAGAVGEVWlrgtTVVR------GYLGDPTIT----AANFT---DGWLRTGDLGSLSAAGDLSIRGRI 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 551 GDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEGKVGMAAVKLAPGKTfDGQKLYQHVRSWLPAYATPHFIRI 630
Cdd:PRK05852 431 KELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPP-TAEELVQFCRERLAAFEIPASFQE 509
|
....*..
gi 228008365 631 QDSLEIT 637
Cdd:PRK05852 510 ASGLPHT 516
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
127-647 |
4.43e-14 |
|
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: 75.02 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVCtgsEGSSITNSQLDARSCQAAWVLKAklkDAVIQNTRdaAAILVlpSKTISALSVFLGLAKLGCPVAWINPH 206
Cdd:cd12116 1 PDATAVRD---DDRSLSYAELDERANRLAARLRA---RGVGPGDR--VAVYL--PRSARLVAAMLAVLKAGAAYVPLDPD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 207 SRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLaenihcfylghssptPGVEALGASLDAAPSDPVPASlratikwk 286
Cdd:cd12116 71 YPADRLRYILEDAEPALVLTDDALPDRLPAGLPVLL---------------LALAAAAAAPAAPRTPVSPDD-------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 287 sPAIFIFTSGTTGLPKPAILSHerviqvSNVLSFC-------GCRADDVVYDVLPLYHTIGlVLGFLGCLQVGATCVLAP 359
Cdd:cd12116 128 -LAYVIYTSGSTGRPKGVVVSH------RNLVNFLhsmrerlGLGPGDRLLAVTTYAFDIS-LLELLLPLLAGARVVIAP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 360 K---FSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTvrLAMGNGLRANVWKNFQQRFGpiRIWEFYGSTEG 436
Cdd:cd12116 200 RetqRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGLTA--LCGGEALPPDLAARLLSRVG--SLWNLYGPTET 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 437 NVglmnyvghcgavgrTSCILRMLTPFELVQFdietAEPLRDKQGFCI-----PVEPGKPGLLL---TKVRKnqpflGYR 508
Cdd:cd12116 276 TI--------------WSTAARVTAAAGPIPI----GRPLANTQVYVLdaalrPVPPGVPGELYiggDGVAQ-----GYL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 509 GSQAESNRKLVANVRRVGD--LYfNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPV 586
Cdd:cd12116 333 GRPALTAERFVPDPFAGPGsrLY-RTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRED 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 228008365 587 PGCEGKVgmAAVKLAPGKTFDGQKLYQHVRSWLPAYATP-HFIRIqDSLEITNTYKLVKSRL 647
Cdd:cd12116 412 GGDRRLV--AYVVLKAGAAPDAAALRAHLRATLPAYMVPsAFVRL-DALPLTANGKLDRKAL 470
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
127-406 |
6.06e-14 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 74.61 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVCTGSEgssITNSQLDARSCQAAWVLKAKlkdavIQNTRDAAAILVlpSKTISALSVFLGLAKLGcpVAWInPH 206
Cdd:cd12114 1 PDATAVICGDGT---LTYGELAERARRVAGALKAA-----GVRPGDLVAVTL--PKGPEQVVAVLGILAAG--AAYV-PV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 207 SRGMP---LLHSVRSSGASVLIVDPDLQENLEEVLPkllaenihcfylghsSPTPGVEALGASLDAAPSDPVPASLrati 283
Cdd:cd12114 68 DIDQPaarREAILADAGARLVLTDGPDAQLDVAVFD---------------VLILDLDALAAPAPPPPVDVAPDDL---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 284 kwkspAIFIFTSGTTGLPKPAILSHErviQVSNVLSFCGCR----ADDVVYDVLPLYHTIGlVLGFLGCLQVGATCVLAP 359
Cdd:cd12114 129 -----AYVIFTSGSTGTPKGVMISHR---AALNTILDINRRfavgPDDRVLALSSLSFDLS-VYDIFGALSAGATLVLPD 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 228008365 360 KFSASR--FWAE-CRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM 406
Cdd:cd12114 200 EARRRDpaHWAElIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVL 249
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
118-646 |
1.23e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 74.16 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 118 ALERQALAW-PDRVALVCTG-SEGSSITNSQLDARSCQAAWVLKAKlkdAVIQNTRdaaaILVLPSKTISALSVFLGLAK 195
Cdd:PRK04319 48 AIDRHADGGrKDKVALRYLDaSRKEKYTYKELKELSNKFANVLKEL---GVEKGDR----VFIFMPRIPELYFALLGALK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 196 LGCPVAwinphsrgmPLLHS-----VRS----SGASVLIVDPDLQENL-EEVLPKLLaeniHCFYLG-HSSPTPGVEALG 264
Cdd:PRK04319 121 NGAIVG---------PLFEAfmeeaVRDrledSEAKVLITTPALLERKpADDLPSLK----HVLLVGeDVEEGPGTLDFN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 265 ASLDAAPSDpvpaslrATIKW---KSPAIFIFTSGTTGLPKPAILSHERVIQ--VSN--VLSFcgcRADDVVY---DvlP 334
Cdd:PRK04319 188 ALMEQASDE-------FDIEWtdrEDGAILHYTSGSTGKPKGVLHVHNAMLQhyQTGkyVLDL---HEDDVYWctaD--P 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 335 LYHTiGLVLGFLGCLQVGAT-CVLAPKFSASRFWAECRQHGVTV-----------------------------ILYVGEi 384
Cdd:PRK04319 256 GWVT-GTSYGIFAPWLNGATnVIDGGRFSPERWYRILEDYKVTVwytaptairmlmgagddlvkkydlsslrhILSVGE- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 385 lrylcnvPEQPEdkihtvrlamgnglrANVWKnfQQRFGpIRIWEFYGSTE-GNVGLMNYVG---HCGAVGRtscilrml 460
Cdd:PRK04319 334 -------PLNPE---------------VVRWG--MKVFG-LPIHDNWWMTEtGGIMIANYPAmdiKPGSMGK-------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 461 tPFELVQFDIetaepLRDKQGfciPVEPGKPGLLltKVRKNQP--FLGYRGSQAESNRKLvanvrrVGDLYFnTGDVLTL 538
Cdd:PRK04319 381 -PLPGIEAAI-----VDDQGN---ELPPNRMGNL--AIKKGWPsmMRGIWNNPEKYESYF------AGDWYV-SGDSAYM 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 539 DQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPgCEGKVGMAAVKLAPGKTFDGQ---KLYQHV 615
Cdd:PRK04319 443 DEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDP-VRGEIIKAFVALRPGYEPSEElkeEIRGFV 521
|
570 580 590
....*....|....*....|....*....|....*
gi 228008365 616 RSWLPAYATPHFIRIQDSLEITNTYK----LVKSR 646
Cdd:PRK04319 522 KKGLGAHAAPREIEFKDKLPKTRSGKimrrVLKAW 556
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
117-649 |
2.01e-13 |
|
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: 72.73 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 117 DALERQALAWPDRVALVctgSEGSSITNSQLDARSCQAAwvlkAKLKDAVIQnTRDAAAILVlpSKTISALSVFLGLAKL 196
Cdd:cd17653 1 DAFERIAAAHPDAVAVE---SLGGSLTYGELDAASNALA----NRLLQLGVV-PGDVVPLLS--DRSLEMLVAILAILKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 197 GCPVAWINPHSRGMPLLHSVRSSGASVLIVDPdlqenleevlpkllaenihcfylghssptpgvealgasldaAPSDPvp 276
Cdd:cd17653 71 GAAYVPLDAKLPSARIQAILRTSGATLLLTTD-----------------------------------------SPDDL-- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 277 aslratikwkspAIFIFTSGTTGLPKPAILSHervIQVSNVLSFCGCRADDVVYDVLPLYHTIGL---VLGFLGCLQVGA 353
Cdd:cd17653 108 ------------AYIIFTSGSTGIPKGVMVPH---RGVLNYVSQPPARLDVGPGSRVAQVLSIAFdacIGEIFSTLCNGG 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 354 TCVLApkfSASRFWAECRQHgVTVILYVGEILRYLcnvPEQPEDKIHTVRLAmGNGLRANV---WknfqqRFGPiRIWEF 430
Cdd:cd17653 173 TLVLA---DPSDPFAHVART-VDALMSTPSILSTL---SPQDFPNLKTIFLG-GEAVPPSLldrW-----SPGR-RLYNA 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 431 YGSTEGNVglmnyvghcgavgrtSCILRMLTPFELVQFdietAEPLR---------DKQgfciPVEPGKPGLLLtkVRKN 501
Cdd:cd17653 239 YGPTECTI---------------SSTMTELLPGQPVTI----GKPIPnstcyildaDLQ----PVPEGVVGEIC--ISGV 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 502 QPFLGYRGSQAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDflEEVNV 581
Cdd:cd17653 294 QVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQ--PEVTQ 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008365 582 YGVPVpgcegkVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLVR 649
Cdd:cd17653 372 AAAIV------VNGRLVAFVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
110-647 |
2.07e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 73.12 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 110 HPPETFVDALERQALAWPDRVALV-CTGSegSSITNSQLDARSCQAAWVLKAKlkdAVIQNTRdaaaILVLPSKTISALS 188
Cdd:PRK05857 11 QLPSTVLDRVFEQARQQPEAIALRrCDGT--SALRYRELVAEVGGLAADLRAQ---SVSRGSR----VLVISDNGPETYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 189 VFLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQ---ENLEEVLPKLLAENIHCFY-LGHSSPTPGVEALG 264
Cdd:PRK05857 82 SVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKmasSAVPEALHSIPVIAVDIAAvTRESEHSLDAASLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 265 ASLDAAPSDPVPaslratikwkspaiFIFTSGTTGLPKPAILSHERVIQVSNVLSFCGCR-----ADDVVYDVLPLYHtI 339
Cdd:PRK05857 162 GNADQGSEDPLA--------------MIFTSGTTGEPKAVLLANRTFFAVPDILQKEGLNwvtwvVGETTYSPLPATH-I 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 340 GLVLGFLGCLQVGATCVLAPKFSASrFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLR---ANVwk 416
Cdd:PRK05857 227 GGLWWILTCLMHGGLCVTGGENTTS-LLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRaiaADV-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 417 NFQQRFGpIRIWEFYGSTE------------GNVGLMnyvgHCGAVGRtscilrmltPFELVQFdietaePLRDKQGFCI 484
Cdd:PRK05857 304 RFIEATG-VRTAQVYGLSEtgctalclptddGSIVKI----EAGAVGR---------PYPGVDV------YLAATDGIGP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 485 PVEPGKP----GLLLTKVRKNqpFLGYRGSQAESNRKLVanvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGEN 560
Cdd:PRK05857 364 TAPGAGPsasfGTLWIKSPAN--MLGYWNNPERTAEVLI-------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVN 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 561 VSTGEVECVLSSLDFLEEVNVYGVPVPGCEGKVGMAAVklaPGKTFDG-------QKLYQHVRSWLPAYATPHFIRIQDS 633
Cdd:PRK05857 435 IAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV---ASAELDEsaaralkHTIAARFRRESEPMARPSTIVIVTD 511
|
570
....*....|....
gi 228008365 634 LEITNTYKLVKSRL 647
Cdd:PRK05857 512 IPRTQSGKVMRASL 525
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
288-642 |
2.38e-13 |
|
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: 72.63 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAILSHERVI-QVSNVLSFCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPkfSASRF 366
Cdd:cd05907 89 LATIIYTSGTTGRPKGVMLSHRNILsNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAETL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 367 WAECRQHGVTVILYVGEILRYLCN---VPEQPEDKIHTVRLAMGNGLR----------ANVWKNFQQrFGpIRIWEFYGS 433
Cdd:cd05907 167 LDDLSEVRPTVFLAVPRVWEKVYAaikVKAVPGLKRKLFDLAVGGRLRfaasggaplpAELLHFFRA-LG-IPVYEGYGL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 434 TE------GNVGLMNYVGHCGAVGRtscilrmltPFElVQFDIEtaeplrdkqgfcipvepgkpGLLLtkVRKNQPFLGY 507
Cdd:cd05907 245 TEtsavvtLNPPGDNRIGTVGKPLP---------GVE-VRIADD--------------------GEIL--VRGPNVMLGY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 508 RGSQAESNRKLVAnvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRW-KGENVSTGEVECVLSSLDFLEEVNVYG--- 583
Cdd:cd05907 293 YKNPEATAEALDA------DGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIGdgr 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 584 -----VPVPGCEGKVGMAAVKLAPGKTFDG----QKLYQHVRSW-------LPAYATPHFIRI------QDSLEITNTYK 641
Cdd:cd05907 367 pflvaLIVPDPEALEAWAEEHGIAYTDVAElaanPAVRAEIEAAveaanarLSRYEQIKKFLLlpepftIENGELTPTLK 446
|
.
gi 228008365 642 L 642
Cdd:cd05907 447 L 447
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
194-650 |
2.40e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 73.31 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 194 AKLGCPVAWINPHSRGMPLLHSVRSSGASVLIV-----DPDLQENLEEVLP--------KLLAENI----HCFYLGHSSP 256
Cdd:PRK08315 89 AKIGAILVTINPAYRLSELEYALNQSGCKALIAadgfkDSDYVAMLYELAPelatcepgQLQSARLpelrRVIFLGDEKH 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 257 -----TPGVEALGASLDAAPSDPVPASLRATikwksPAIFI-FTSGTTGLPKPAILSHerviqvSNVL---SFCG--CR- 324
Cdd:PRK08315 169 pgmlnFDELLALGRAVDDAELAARQATLDPD-----DPINIqYTSGTTGFPKGATLTH------RNILnngYFIGeaMKl 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 325 --ADDVVYDVlPLYHTIGLVLGFLGCLQVGATCVL-APKFSASRFWAECRQ------HGV-TviLYVGEIlrylcNVPEQ 394
Cdd:PRK08315 238 teEDRLCIPV-PLYHCFGMVLGNLACVTHGATMVYpGEGFDPLATLAAVEEerctalYGVpT--MFIAEL-----DHPDF 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 395 PEDKIHTVRlamgNGLRA------NVWKNFQQRFGPIRIWEFYGSTEGNVGlmnyvghcgavgrtSCILRMLTPFEL--- 465
Cdd:PRK08315 310 ARFDLSSLR----TGIMAgspcpiEVMKRVIDKMHMSEVTIAYGMTETSPV--------------STQTRTDDPLEKrvt 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 466 ----VQ-------FDIETAEplrdkqgfciPVEPGKPGLLLTK---VRKnqpflGYRGSQAESNRKLVAnvrrvgDLYFN 531
Cdd:PRK08315 372 tvgrALphlevkiVDPETGE----------TVPRGEQGELCTRgysVMK-----GYWNDPEKTAEAIDA------DGWMH 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 532 TGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPgcegKVG---MAAVKLAPGKTFDG 608
Cdd:PRK08315 431 TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDE----KYGeevCAWIILRPGATLTE 506
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 228008365 609 QKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLvRE 650
Cdd:PRK08315 507 EDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKM-RE 547
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
120-647 |
5.46e-13 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 71.59 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 120 ERQALAWPDRVALVCtgsEGSSITNSQLDARSCQAAWVLKAKlkdAVIQNTrdAAAILVlpSKTISALSVFLGLAKLGCP 199
Cdd:cd17655 4 EEQAEKTPDHTAVVF---EDQTLTYRELNERANQLARTLREK---GVGPDT--IVGIMA--ERSLEMIVGILGILKAGGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 200 VAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENL---EEVLpkllAENIHCFYLGHSSptpgvealgasldaapsdpvp 276
Cdd:cd17655 74 YLPIDPDYPEERIQYILEDSGADILLTQSHLQPPIafiGLID----LLDEDTIYHEESE--------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 277 aSLRATIKWKSPAIFIFTSGTTGLPKPAILSHErviQVSNVLSFcgcrADDVVY----DVLPLYHTIGL---VLGFLGCL 349
Cdd:cd17655 129 -NLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR---GVVNLVEW----ANKVIYqgehLRVALFASISFdasVTEIFASL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 350 QVGATCVLAPKFSASRFWAEC---RQHGVTVILYVGEILRYLCNVPEQPEDKIHTVrLAMGNGLRANVWKNFQQRFGP-I 425
Cdd:cd17655 201 LSGNTLYIVRKETVLDGQALTqyiRQNRITIIDLTPAHLKLLDAADDSEGLSLKHL-IVGGEALSTELAKKIIELFGTnP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 426 RIWEFYGSTEGNVGLMNYVGHCGAVGRTSciLRMLTPFELVQFDIetaeplRDKQGFCIPVepGKPGLL------LTKVR 499
Cdd:cd17655 280 TITNAYGPTETTVDASIYQYEPETDQQVS--VPIGKPLGNTRIYI------LDQYGRPQPV--GVAGELyiggegVARGY 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 500 KNQPFLgyrgsqaeSNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEV 579
Cdd:cd17655 350 LNRPEL--------TAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEA 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 228008365 580 NVygVPVPGCEGKVGMAAVkLAPGKTFDGQKLYQHVRSWLPAYATP-HFIRIqDSLEITNTYKLVKSRL 647
Cdd:cd17655 422 VV--IARKDEQGQNYLCAY-IVSEKELPVAQLREFLARELPDYMIPsYFIKL-DEIPLTPNGKVDRKAL 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
120-642 |
9.97e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 72.30 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 120 ERQALAWPDRVALVCtGSEgsSITNSQLDARSCQAAWVLKAKlkdAVIQNTRDAAAIlvlpSKTISALSVFLGLAKLGCP 199
Cdd:PRK12316 518 EEQVERTPEAPALAF-GEE--TLDYAELNRRANRLAHALIER---GVGPDVLVGVAM----ERSIEMVVALLAILKAGGA 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 200 VAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENL--EEVLPKLLAENIHCFYLGHSSPTPGVEALGASLdaapsdpvpa 277
Cdd:PRK12316 588 YVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLplAAGVQVLDLDRPAAWLEGYSEENPGTELNPENL---------- 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 278 slratikwkspAIFIFTSGTTGLPKPAILSHErviQVSNVLSFC----GCRADDVVYDVLPLYHTIGlVLGFLGCLQVGA 353
Cdd:PRK12316 658 -----------AYVIYTSGSTGKPKGAGNRHR---ALSNRLCWMqqayGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 354 TCVLAPK---FSASRFWAECRQHGVTVILYVGEILRYLcnVPEQPEDKIHTVRLAM--GNGLRANVWKNFQQRFGPIRIW 428
Cdd:PRK12316 723 RLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAF--LQDEDVASCTSLRRIVcsGEALPADAQEQVFAKLPQAGLY 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 429 EFYGSTEGNVGLmNYVGHCGAVGRTSCILRMLTpfelvqfdiETAEPLRDKQGFCIPVepGKPG-LLLTKVRKNQPFLGY 507
Cdd:PRK12316 801 NLYGPTEAAIDV-THWTCVEEGGDSVPIGRPIA---------NLACYILDANLEPVPV--GVLGeLYLAGRGLARGYHGR 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 508 RGSQAEsnrKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVpvp 587
Cdd:PRK12316 869 PGLTAE---RFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--- 942
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 228008365 588 gcEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:PRK12316 943 --DGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKL 995
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
293-650 |
1.05e-12 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 71.16 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 293 FTSGTTGLPKPAILSHERViqVSNVLSFCGCRADDVVYDV-----LPLYHTIGLVLGFLGCLQVGATCVLAPKFSASRFW 367
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNL--VANLCSSLFSVGPEMIGQVvtlglIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 368 AECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRL----AMGNGLRANVWKNFQQRFGPIRIWEFYGSTEGNVGLMNY 443
Cdd:PLN02330 269 NALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaimTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTH 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 444 ----VGHcGAVGRTScilrmlTPFELVQFDIETAEPlrdKQGFCIPvePGKPGLLLtkVRKNQPFLGYRGSQAESNRKLV 519
Cdd:PLN02330 349 gdpeKGH-GIAKKNS------VGFILPNLEVKFIDP---DTGRSLP--KNTPGELC--VRSQCVMQGYYNNKEETDRTID 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 520 AnvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVygVPVPGCE-GKVGMAAV 598
Cdd:PLN02330 415 E------DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV--VPLPDEEaGEIPAACV 486
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 228008365 599 KLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKsRLVRE 650
Cdd:PLN02330 487 VINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMR-RLLKE 537
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
287-652 |
4.54e-12 |
|
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: 67.74 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 287 SPAIFIFTSGTTGLPKPAILSHERVI-QVSNVLSFCGCRADDVVYDVLPLYHTIGLVLGFLgCLQVGATCVLAPKFSASR 365
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLaSAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVR-SLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 366 fwAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNglrANVWKNFQQRFGP--IRIWEFYGSTE--GNVGLM 441
Cdd:cd17630 80 --EDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGG---APIPPELLERAADrgIPLYTTYGMTEtaSQVATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 442 NYVGHC-GAVGRtscilrmltPFELVQFDIETAEPLrdkqgfcipvEPGKPGLlltkvrknqpFLGYRGSQAESNRKlva 520
Cdd:cd17630 155 RPDGFGrGGVGV---------LLPGRELRIVEDGEI----------WVGGASL----------AMGYLRGQLVPEFN--- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 521 nvrrvGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKL 600
Cdd:cd17630 203 -----EDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEEL-GQRPVAVIVG 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 228008365 601 APGKtfDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKlVKSRLVREGF 652
Cdd:cd17630 277 RGPA--DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGK-VDRRALRAWL 325
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
119-438 |
7.81e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.22 E-value: 7.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 119 LERQALAWPDRVALVCtgsEGSSITNSQLDARSCQAAWVLKAKlkdAVIQNTRDAAAIlvlpSKTISALSVFLGLAKLGC 198
Cdd:PRK12316 4557 VAERARMTPDAVAVVF---DEEKLTYAELNRRANRLAHALIAR---GVGPEVLVGIAM----ERSAEMMVGLLAVLKAGG 4626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 199 PVAWINPHSRGMPLLHSVRSSGASVLIVdpdlQENLEEVLPklLAENIHCFYL-------GHSSPTPGVEALGASLdaap 271
Cdd:PRK12316 4627 AYVPLDPEYPRERLAYMMEDSGAALLLT----QSHLLQRLP--IPDGLASLALdrdedweGFPAHDPAVRLHPDNL---- 4696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 272 sdpvpaslratikwkspAIFIFTSGTTGLPKPAILSHERVIQ-VSNVLSFCGCRADDVVYDVLPlYHTIGLVLGFLGCLQ 350
Cdd:PRK12316 4697 -----------------AYVIYTSGSTGRPKGVAVSHGSLVNhLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYHPLI 4758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 351 VGATCVLAPK--FSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPED-----KIHTVRLAMGNGLRANVWKNFQqrfg 423
Cdd:PRK12316 4759 NGASVVIRDDslWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEppslrVYCFGGEAVAQASYDLAWRALK---- 4834
|
330
....*....|....*
gi 228008365 424 PIRIWEFYGSTEGNV 438
Cdd:PRK12316 4835 PVYLFNGYGPTETTV 4849
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
565-637 |
8.91e-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: 61.02 E-value: 8.91e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 228008365 565 EVECVLSSLDFLEEVNVYGVPVPGcEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEIT 637
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDEL-KGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKT 72
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
123-647 |
5.56e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 65.40 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 123 ALAWPDRVALVctGSEGSsitnsqLDARSCQ-AAWVLKAKLKDAVIQNTRdAAAILVLPSKTISALSVFLGLakLGCPVA 201
Cdd:PRK13383 45 AARWPGRTAII--DDDGA------LSYRELQrATESLARRLTRDGVAPGR-AVGVMCRNGRGFVTAVFAVGL--LGADVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 202 WINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAENihcfylghsSPTPGVEALGASLDAAPSDpvpaslra 281
Cdd:PRK13383 114 PISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVID---------PATAGAEESGGRPAVAAPG-------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 282 tikwkspAIFIFTSGTTGLPK--PAILSHERVIQVS-NVLSFCGCRADDVVYDVLPLYHTIGLVLGFLgCLQVGATCVLA 358
Cdd:PRK13383 177 -------RIVLLTSGTTGKPKgvPRAPQLRSAVGVWvTILDRTRLRTGSRISVAMPMFHGLGLGMLML-TIALGGTVLTH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 359 PKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQ--PEDKIHTVRLAMGNG--LRANVWKNFQQRFGPIrIWEFYGST 434
Cdd:PRK13383 249 RHFDAEAALAQASLHRADAFTAVPVVLARILELPPRvrARNPLPQLRVVMSSGdrLDPTLGQRFMDTYGDI-LYNGYGST 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 435 EGNVGlmnyvghcgavgrtscilRMLTPFELVQFDIETAEPLrdkqgfcipvePGKPGLLLTkvRKNQPfLGYR------ 508
Cdd:PRK13383 328 EVGIG------------------ALATPADLRDAPETVGKPV-----------AGCPVRILD--RNNRP-VGPRvtgrif 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 509 -GSQAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPvp 587
Cdd:PRK13383 376 vGGELAGTRYTDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVP-- 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 228008365 588 gcEGKVG---MAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:PRK13383 454 --DERFGhrlAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
138-574 |
8.16e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 65.76 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 138 EGSSITNSQLDARscqaAWVLKAKLKDaviqNTRDAAAILVLPSKTISALSVFLGLAKLGCPVAWINPHSRGMPLLHSVR 217
Cdd:PRK06814 655 VNGPLTYRKLLTG----AFVLGRKLKK----NTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACK 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 218 SSGASVLIVDPDLQE--NLEEVLPKLlAENIHCFYLghssptpgvEALGASLDAApsdpvpASLRATIKW---------- 285
Cdd:PRK06814 727 AAQVKTVLTSRAFIEkaRLGPLIEAL-EFGIRIIYL---------EDVRAQIGLA------DKIKGLLAGrfplvyfcnr 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 286 --KSPAIFIFTSGTTGLPKPAILSHERVI----QVSNVLSFcgcRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAP 359
Cdd:PRK06814 791 dpDDPAVILFTSGSEGTPKGVVLSHRNLLanraQVAARIDF---SPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYP 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 360 KFSASRFWAE-CRQHGVTVILYVGEIL----RYlcnvpEQPEDkIHTVRL--AMGNGLRANVWKNFQQRFGpIRIWEFYG 432
Cdd:PRK06814 868 SPLHYRIIPElIYDTNATILFGTDTFLngyaRY-----AHPYD-FRSLRYvfAGAEKVKEETRQTWMEKFG-IRILEGYG 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 433 STEGNVGL-MNYVGHC--GAVGRtscilrmLTPfeLVQFDIEtaeplrdkqgfciPVePGKP--GLLLtkVRKNQPFLGY 507
Cdd:PRK06814 941 VTETAPVIaLNTPMHNkaGTVGR-------LLP--GIEYRLE-------------PV-PGIDegGRLF--VRGPNVMLGY 995
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 228008365 508 RgsQAESNRKLVANVrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLD 574
Cdd:PRK06814 996 L--RAENPGVLEPPA----DGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELW 1056
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
127-642 |
8.99e-11 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 64.70 E-value: 8.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 127 PDRVALVCtgsEGSSITNSQLDARSCQAAWVLKAKlkdAVIQNTRDAAAIlvlpSKTISALSVFLGLAKLG---CPVAWI 203
Cdd:cd17649 1 PDAVALVF---GDQSLSYAELDARANRLAHRLRAL---GVGPEVRVGIAL----ERSLEMVVALLAILKAGgayVPLDPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 204 NPHSRgmpLLHSVRSSGASVLIvdpdlqenleevlpkllaenihcfylghsSPTPgvealgasldaapsdpvpaslrati 283
Cdd:cd17649 71 YPAER---LRYMLEDSGAGLLL-----------------------------THHP------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 284 kwKSPAIFIFTSGTTGLPKPAILSHERVIQVSNVLSFC-GCRADDVVYDVLPLYHTIGlVLGFLGCLQVGATCVLAPK-- 360
Cdd:cd17649 94 --RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERyGLTPGDRELQFASFNFDGA-HEQLLPPLICGACVVLRPDel 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 361 -FSASRFWAECRQHGVTVI----LYVGEILRYLCNVPEQPEDKIHTVRLAmGNGLRANVWknfqQRFGPIRIWEF--YGS 433
Cdd:cd17649 171 wASADELAEMVRELGVTVLdlppAYLQQLAEEADRTGDGRPPSLRLYIFG-GEALSPELL----RRWLKAPVRLFnaYGP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 434 TEGNVGLMNYVGHCGA--VGRTSCILRMLTPFELVQFDietaEPLRdkqgfciPVEPGKPGLLLTK----VRknqpflGY 507
Cdd:cd17649 246 TEATVTPLVWKCEAGAarAGASMPIGRPLGGRSAYILD----ADLN-------PVPVGVTGELYIGgeglAR------GY 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 508 RGSQAESNRKLVAN--VRRVGDLYfNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVP 585
Cdd:cd17649 309 LGRPELTAERFVPDpfGAPGSRLY-RTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALD 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 228008365 586 VPGCEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATP-HFIRIqDSLEITNTYKL 642
Cdd:cd17649 388 GAGGKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPaHLVFL-ARLPLTPNGKL 444
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
112-365 |
1.13e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.57 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 112 PETFVDALERQALAWPDRVAL---VCTGSEGSSITNSQLD--ARSCQAAWVLKAKLKDAviqntrdaaAILVLPSKTiSA 186
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALrflADDPGEGVVLSYRDLDlrARTIAAALQARASFGDR---------AVLLFPSGP-DY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 187 LSVFLG------LAKLGCPVAWINPHSRGMpLLHSVRSSGASVLIVDPDLQENLEEvLPKLLAENihcfylghsspTPGV 260
Cdd:PRK05691 78 VAAFFGclyagvIAVPAYPPESARRHHQER-LLSIIADAEPRLLLTVADLRDSLLQ-MEELAAAN-----------APEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 261 EALGaSLDAAPSDpvpaslratiKWKSPAI------FI-FTSGTTGLPKPAILSHERViqVSN-VLSFCGCR----ADDV 328
Cdd:PRK05691 145 LCVD-TLDPALAE----------AWQEPALqpddiaFLqYTSGSTALPKGVQVSHGNL--VANeQLIRHGFGidlnPDDV 211
|
250 260 270
....*....|....*....|....*....|....*...
gi 228008365 329 VYDVLPLYHTIGLVLGFLGCLQVGATCVL-APKFSASR 365
Cdd:PRK05691 212 IVSWLPLYHDMGLIGGLLQPIFSGVPCVLmSPAYFLER 249
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
289-647 |
2.72e-10 |
|
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: 63.25 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 289 AIFiFTSGTTGLPKPAILSHERVIQVSNVLS--FCGCRADDVVYDVlplyHTIGLVLGFLGCL---QVGATCVLA---PK 360
Cdd:cd05928 178 AIY-FTSGTTGSPKMAEHSHSSLGLGLKVNGryWLDLTASDIMWNT----SDTGWIKSAWSSLfepWIQGACVFVhhlPR 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 361 FSASRFWAECRQHGVTVILYVGEILRYLCNvpeqpED----KIHTVR--LAMGNGLRANVWKNFQQRFGpIRIWEFYGST 434
Cdd:cd05928 253 FDPLVILKTLSSYPITTFCGAPTVYRMLVQ-----QDlssyKFPSLQhcVTGGEPLNPEVLEKWKAQTG-LDIYEGYGQT 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 435 EGNVGLMNYVG---HCGAVGRTScilrmltpfelVQFDIETAeplrDKQGFCIPvePGKPGLLLTKVRKNQPFLGYrgSQ 511
Cdd:cd05928 327 ETGLICANFKGmkiKPGSMGKAS-----------PPYDVQII----DDNGNVLP--PGTEGDIGIRVKPIRPFGLF--SG 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 512 AESNRKLVANVRRvGDLYfNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPgCEG 591
Cdd:cd05928 388 YVDNPEKTAATIR-GDFY-LTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP-IRG 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228008365 592 KVGMAAVKLAPG-KTFDGQKL----YQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd05928 465 EVVKAFVVLAPQfLSHDPEQLtkelQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
120-647 |
5.01e-10 |
|
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: 62.19 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 120 ERQALAWPDRVALVctgSEGSSITNSQLDARSCQAAWVLKAKlkdAVIQNTRdaAAILVLPSKTISAlsVFLGLAKLGCP 199
Cdd:cd17645 5 EEQVERTPDHVAVV---DRGQSLTYKQLNEKANQLARHLRGK---GVKPDDQ--VGIMLDKSLDMIA--AILGVLKAGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 200 VAWINPHSRGMPLLHSVRSSGASVLIVDPDlqeNLeevlpkllaenihcfylghssptpgvealgasldaapsdpvpasl 279
Cdd:cd17645 75 YVPIDPDYPGERIAYMLADSSAKILLTNPD---DL--------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 280 ratikwkspAIFIFTSGTTGLPKPAILSHERVI-------------QVSNVLSFCGCRADDVVYDVLPlYHTIGLVLGFL 346
Cdd:cd17645 107 ---------AYVIYTSGSTGLPKGVMIEHHNLVnlcewhrpyfgvtPADKSLVYASFSFDASAWEIFP-HLTAGAALHVV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 347 GClqvgatcvlAPKFSASRFWAECRQHGVTVilyvgeilRYL-CNVPEQ-PEDKIHTVRLAMGNGlraNVWKNFQQRfgP 424
Cdd:cd17645 177 PS---------ERRLDLDALNDYFNQEGITI--------SFLpTGAAEQfMQLDNQSLRVLLTGG---DKLKKIERK--G 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 425 IRIWEFYGSTEGNVglmnyvghcgavgrtscilrMLTPFELvqfdietaeplrDKQGFCIPVepGKP-----GLLLTKVR 499
Cdd:cd17645 235 YKLVNNYGPTENTV--------------------VATSFEI------------DKPYANIPI--GKPidntrVYILDEAL 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 500 KNQPF--------------LGYRGSQAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGE 565
Cdd:cd17645 281 QLQPIgvagelciageglaRGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGE 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 566 VECVLSSLDFLEEVNVYGVPVPGceGKVGMAAVKLAPgKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKS 645
Cdd:cd17645 361 IEPFLMNHPLIELAAVLAKEDAD--GRKYLVAYVTAP-EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRK 437
|
..
gi 228008365 646 RL 647
Cdd:cd17645 438 AL 439
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
187-660 |
1.81e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.95 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 187 LSVFLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPkllaeniHCfylghssptPGVEAL--- 263
Cdd:PRK05620 78 LEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILK-------EC---------PCVRAVvfi 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 264 GASLDAAPSDPVPASL-----------RATI-KW-----KSPAIFIFTSGTTGLPKPAILSHERV------------IQV 314
Cdd:PRK05620 142 GPSDADSAAAHMPEGIkvysyealldgRSTVyDWpeldeTTAAAICYSTGTTGAPKGVVYSHRSLylqslslrttdsLAV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 315 SNVLSFCGCraddvvydvLPLYHtiglVLGF---LGCLQVGATCVL------APKFSASRFWAECRQ-HGVTViLYVGEI 384
Cdd:PRK05620 222 THGESFLCC---------VPIYH----VLSWgvpLAAFMSGTPLVFpgpdlsAPTLAKIIATAMPRVaHGVPT-LWIQLM 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 385 LRYLCNVPEQpedkiHTVR--LAMGNGLRANVWKNFQQRFGP--IRIWefyGSTE-GNVGLmnyVGH--CGAVGRTSCIL 457
Cdd:PRK05620 288 VHYLKNPPER-----MSLQeiYVGGSAVPPILIKAWEERYGVdvVHVW---GMTEtSPVGT---VARppSGVSGEARWAY 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 458 R-------------------MLTPFELVQFDIETAEPLRDKQGFCIPVEPGkpgllltkvrkNQPFLGYRGSQAESnrkl 518
Cdd:PRK05620 357 RvsqgrfpasleyrivndgqVMESTDRNEGEIQVRGNWVTASYYHSPTEEG-----------GGAASTFRGEDVED---- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 519 vANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAV 598
Cdd:PRK05620 422 -ANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKW-GERPLAVT 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 228008365 599 KLAPGKTFD---GQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL---VREG-FDVGIIADP 660
Cdd:PRK05620 500 VLAPGIEPTretAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLrqhLADGdFEIIKLKGP 568
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
289-583 |
2.30e-09 |
|
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: 60.07 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 289 AIFIFTSGTTGLPKPAILSHERVI-QVSNVLSFCGCRADDVVYDVLPLYHTIGLVLGFLgCLQVGATCVlapkFSASRFW 367
Cdd:cd17640 91 ATIIYTSGTTGNPKGVMLTHANLLhQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYF-IFACGCSQA----YTSIRTL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 368 ----AECRQHGVTVILYVGEILRYlcNVPEQPEDKIHTVR-----LAMGNGLRANV---------WKNFQQRFGpIRIWE 429
Cdd:cd17640 166 kddlKRVKPHYIVSVPRLWESLYS--GIQKQVSKSSPIKQflflfFLSGGIFKFGIsgggalpphVDTFFEAIG-IEVLN 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 430 FYGSTEGNVGLmnyvghcgAVGRTSCILRML-------TPFELVqfDIETAEPLrdkqgfcipvEPGKPGLLltKVRKNQ 502
Cdd:cd17640 243 GYGLTETSPVV--------SARRLKCNVRGSvgrplpgTEIKIV--DPEGNVVL----------PPGEKGIV--WVRGPQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 503 PFLGYRGSQAESNRKLVAnvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWK-GENVSTGEVECVLSSLDFLEEVNV 581
Cdd:cd17640 301 VMKGYYKNPEATSKVLDS------DGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMV 374
|
..
gi 228008365 582 YG 583
Cdd:cd17640 375 VG 376
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
289-642 |
4.10e-09 |
|
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: 59.37 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 289 AIFIFTSGTTGLPKPAILSHERVIQVS-------------NVLSFCGCRADDVVYDVLPLYHTiglvlgflgclqvGATC 355
Cdd:cd17644 109 AYVIYTSGSTGKPKGVMIEHQSLVNLShglikeygitssdRVLQFASIAFDVAAEEIYVTLLS-------------GATL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 356 VLAPK---FSASRFWAECRQHGVTVI--------LYVGEILRYLCNVPEQPEdkihtVRLAMGNGLRANVWKNFQQRFGP 424
Cdd:cd17644 176 VLRPEemrSSLEDFVQYIQQWQLTVLslppaywhLLVLELLLSTIDLPSSLR-----LVIVGGEAVQPELVRQWQKNVGN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 425 -IRIWEFYGSTEGNVglmnyvghcgavgrTSCILRMLTPFELVQFDIETAEPLRDKQGFCI-----PVEPGKPGLL---- 494
Cdd:cd17644 251 fIQLINVYGPTEATI--------------AATVCRLTQLTERNITSVPIGRPIANTQVYILdenlqPVPVGVPGELhigg 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 495 --LTKVRKNQP------FLGYRGSQAESNRklvanvrrvgdLYfNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEV 566
Cdd:cd17644 317 vgLARGYLNRPeltaekFISHPFNSSESER-----------LY-KTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEI 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 567 ECVLSSLDFLEEVNV--------------YGVPVPGCEGKVgmaavklapgktfdgQKLYQHVRSWLPAYATPHFIRIQD 632
Cdd:cd17644 385 EAVLSQHNDVKTAVVivredqpgnkrlvaYIVPHYEESPST---------------VELRQFLKAKLPDYMIPSAFVVLE 449
|
410
....*....|
gi 228008365 633 SLEITNTYKL 642
Cdd:cd17644 450 ELPLTPNGKI 459
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
119-435 |
6.69e-09 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 58.76 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 119 LERQALAWPDRVALVCTGSEGSS-------ITNSQLDARSCQAAWVLKAklkdAVIqnTRDAAAIL-VLPSKTISALsVF 190
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPGGRGADgklaydeLSFAELDARSDAIAHGLNA----AGI--GRGMRAVLmVTPSLEFFAL-TF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 191 lGLAKLGCPVAWINPhsrGM---PLLHSVRSSGASVLIVDPdlqenLEEVLPKLL----AENIHCFYLGHSSPTPGVEAL 263
Cdd:PRK09274 85 -ALFKAGAVPVLVDP---GMgikNLKQCLAEAQPDAFIGIP-----KAHLARRLFgwgkPSVRRLVTVGGRLLWGGTTLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 264 GASLDAAPSDPVPASLRATikwkSPAIFIFTSGTTGLPKPAILSHER-VIQVSNVLSFCGCRADDVVYDVLPLYHTIGLV 342
Cdd:PRK09274 156 TLLRDGAAAPFPMADLAPD----DMAAILFTSGSTGTPKGVVYTHGMfEAQIEALREDYGIEPGEIDLPTFPLFALFGPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 343 LgflgclqvGATCVLaPKFSASR--------FWAECRQHGVTVIL----YVGEILRYLcnvpEQPEDKIHTVRLAMGNGL 410
Cdd:PRK09274 232 L--------GMTSVI-PDMDPTRpatvdpakLFAAIERYGVTNLFgspaLLERLGRYG----EANGIKLPSLRRVISAGA 298
|
330 340
....*....|....*....|....*...
gi 228008365 411 RAN--VWKNFQQRFGP-IRIWEFYGSTE 435
Cdd:PRK09274 299 PVPiaVIERFRAMLPPdAEILTPYGATE 326
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
110-647 |
1.26e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 58.03 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 110 HPPETFVDALERQALAWPDRVALVctgSEGSSITNSQLDARSCQAAwvlkAKLKDAVIQNTRDAAAILvlpSKTISALSV 189
Cdd:PRK08162 15 YVPLTPLSFLERAAEVYPDRPAVI---HGDRRRTWAETYARCRRLA----SALARRGIGRGDTVAVLL---PNIPAMVEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 190 FLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLpkLLAENIHCFYLGHSSPT-PGVEALGAsLD 268
Cdd:PRK08162 85 HFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREAL--ALLPGPKPLVIDVDDPEyPGGRFIGA-LD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 269 ----AAPSDPVPASLRATIKWKspAIFI-FTSGTTGLPKpAILSHER---VIQVSNVLSfCGCRADDVVYDVLPLYH--- 337
Cdd:PRK08162 162 yeafLASGDPDFAWTLPADEWD--AIALnYTSGTTGNPK-GVVYHHRgayLNALSNILA-WGMPKHPVYLWTLPMFHcng 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 338 -----TIGLVLGFLGCLQvgatcvlapKFSASRFWAECRQHGVTviLYVGE--ILRYLCNVPEQPEDKI-HTVR-LAMGN 408
Cdd:PRK08162 238 wcfpwTVAARAGTNVCLR---------KVDPKLIFDLIREHGVT--HYCGApiVLSALINAPAEWRAGIdHPVHaMVAGA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 409 GLRANVWKNFQQRfGpIRIWEFYGSTE--GNVGLMNYVGHCGAVgrtscilrmltPFElvqfdiETAEpLRDKQGFCIPV 486
Cdd:PRK08162 307 APPAAVIAKMEEI-G-FDLTHVYGLTEtyGPATVCAWQPEWDAL-----------PLD------ERAQ-LKARQGVRYPL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 487 EPG---------KP----GLLLTKV--RKNQPFLGYRgsqaeSNRKLVANVRRVGdlYFNTGDVLTLDQEGFFYFQDRLG 551
Cdd:PRK08162 367 QEGvtvldpdtmQPvpadGETIGEImfRGNIVMKGYL-----KNPKATEEAFAGG--WFHTGDLAVLHPDGYIKIKDRSK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 552 DTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIq 631
Cdd:PRK08162 440 DIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKW-GEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF- 517
|
570
....*....|....*.
gi 228008365 632 DSLEITNTYKLVKSRL 647
Cdd:PRK08162 518 GELPKTSTGKIQKFVL 533
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
110-642 |
1.72e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.43 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 110 HPPETFVDAL-ERQALAWPDRVALVCTGSEgssITNSQLDARSCQAAWVLKAKLKDAVIqntrdaaAILVLPSKTISALS 188
Cdd:PRK12316 3053 YPLERGVHRLfEEQVERTPDAVALAFGEQR---LSYAELNRRANRLAHRLIERGVGPDV-------LVGVAVERSLEMVV 3122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 189 VFLGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQenleevLPKllaenihcfylghsspTPGVEALgaSLD 268
Cdd:PRK12316 3123 GLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLR------LPL----------------AQGVQVL--DLD 3178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 269 AAPSDPVPASLRATIKWKSPAIFIFTSGTTGLPKPAILSHERVIQVSNVLSFC-GCRADDVVYDVLPlYHTIGLVLGFLG 347
Cdd:PRK12316 3179 RGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAyGLGVGDRVLQFTT-FSFDVFVEELFW 3257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 348 CLQVGATCVLAPKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANVWKNFQQRFGPIRI 427
Cdd:PRK12316 3258 PLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPL 3337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 428 WEFYGSTEGNVglmnyvghcgavgrTSCILRMLTPFELVQFdieTAEPLRDKQGFCI-----PVEPGKPGLLLtkVRKNQ 502
Cdd:PRK12316 3338 YNLYGPTEATI--------------TVTHWQCVEEGKDAVP---IGRPIANRACYILdgslePVPVGALGELY--LGGEG 3398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 503 PFLGYRGSQAESNRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVY 582
Cdd:PRK12316 3399 LARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL 3478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 583 GVpvpgcEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:PRK12316 3479 AV-----DGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKL 3533
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
288-634 |
5.36e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 55.93 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAILSHER-VIQVSNVLSFCGCRADDVVYDVLPLYHTIGLVLGFlgclqvgaTCVlAPKFSASR- 365
Cdd:cd05910 87 PAAILFTSGSTGTPKGVVYRHGTfAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGL--------TSV-IPDMDPTRp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 366 -------FWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVR--LAMGNGLRANVWKNFQQRFGP-IRIWEFYGSTE 435
Cdd:cd05910 158 aradpqkLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRrvLSAGAPVPIALAARLRKMLSDeAEILTPYGATE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 436 -------GNVGLMNYVGHCGAVGRTSCILRMLTPFELVQFDIeTAEPLRDKQG-FCIPvePGKPGLLLTKvrknqpflGY 507
Cdd:cd05910 238 alpvssiGSRELLATTTAATSGGAGTCVGRPIPGVRVRIIEI-DDEPIAEWDDtLELP--RGEIGEITVT--------GP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 508 RGSQAESNRKLVANVRRVGD----LYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYG 583
Cdd:cd05910 307 TVTPTYVNRPVATALAKIDDnsegFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVG 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 228008365 584 VPVPGCEGKVGmaAVKLAPGKTFDGQKLYQHVRSWLPAYatPHFIRIQDSL 634
Cdd:cd05910 387 VGKPGCQLPVL--CVEPLPGTITPRARLEQELRALAKDY--PHTQRIGRFL 433
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
116-647 |
5.69e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 55.98 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 116 VDALERQALAWPDRVALvctGSEGSSITNSQLDARSCQ-AAWVLK-AKLKDAviqntrDAAAILvLPSKTISALSVFlGL 193
Cdd:PRK12492 27 VEVFERSCKKFADRPAF---SNLGVTLSYAELERHSAAfAAYLQQhTDLVPG------DRIAVQ-MPNVLQYPIAVF-GA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 194 AKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVLPKLLAENIHCFYLGHSSPTPGVEALGASLDAApSD 273
Cdd:PRK12492 96 LRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLLPAAKGWLVNTVVDKV-KK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 274 PVPA-SLRATIKWKSP-------------------AIFIFTSGTTGLPKPAILSHERViqVSNVLSFCGC---------- 323
Cdd:PRK12492 175 MVPAyHLPQAVPFKQAlrqgrglslkpvpvglddiAVLQYTGGTTGLAKGAMLTHGNL--VANMLQVRAClsqlgpdgqp 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 324 ---RADDVVYDVLPLYHTIGLVLGFLgCLQV-GATCVLA--PKfSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPED 397
Cdd:PRK12492 253 lmkEGQEVMIAPLPLYHIYAFTANCM-CMMVsGNHNVLItnPR-DIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 398 KIHTVRL--AMGNGLRANVWKNFQQRFGpIRIWEFYGSTEGN-VGLMNYVGHCGAVGrTSCILRMLTPFELVqfdietae 474
Cdd:PRK12492 331 DFSALKLtnSGGTALVKATAERWEQLTG-CTIVEGYGLTETSpVASTNPYGELARLG-TVGIPVPGTALKVI-------- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 475 plrDKQGFCIPVepGKPGLLLtkVRKNQPFLGYRGSQAESNRKLVAnvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTF 554
Cdd:PRK12492 401 ---DDDGNELPL--GERGELC--IKGPQVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRKKDLI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 555 RWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEGKVGMAAVKLAPGKTFDGQKLYqhVRSWLPAYATPHFIRIQDSL 634
Cdd:PRK12492 468 IVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAY--CKENFTGYKVPKHIVLRDSL 545
|
570
....*....|...
gi 228008365 635 EITNTYKLVKSRL 647
Cdd:PRK12492 546 PMTPVGKILRREL 558
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
287-634 |
5.74e-08 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 55.00 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 287 SPAIFIFTSGTTGLPKPAILSHERVI-QVSNVLSFCGCRADDVVYDVLPLYHtIGLVLGFLGCLQVGATCVLAPKFSASR 365
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLaQALVLAVLQAIDEGTVFLNSGPLFH-IGTLMFTLATFHAGGTNVFVRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 366 FWAECRQHGVTVILYVGEILrylcnvpeqpeDKIHTVRLAMG---NGLRANVWKNFQQRFGPIRIWEF------YGSTE- 435
Cdd:cd17636 80 VLELIEAERCTHAFLLPPTI-----------DQIVELNADGLydlSSLRSSPAAPEWNDMATVDTSPWgrkpggYGQTEv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 436 GNVGLMNYVGHC--GAVGRTS--CILRMLtpfelvqfDIETAEplrdkqgfcipVEPGKPGLLLtkVRKNQPFLGYrgsq 511
Cdd:cd17636 149 MGLATFAALGGGaiGGAGRPSplVQVRIL--------DEDGRE-----------VPDGEVGEIV--ARGPTVMAGY---- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 512 aeSNRKLVaNVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPGCEG 591
Cdd:cd17636 204 --WNRPEV-NARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQ 280
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 228008365 592 KVgMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSL 634
Cdd:cd17636 281 SV-KAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADAL 322
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
293-652 |
1.19e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 54.71 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 293 FTSGTTGLPKPAILSHErviqvSNVL-SFC-------GCRADDVVYDVLPLYHTIGLVLGFLGCLqVGATCVL-APKFSA 363
Cdd:PRK07008 183 YTSGTTGNPKGALYSHR-----STVLhAYGaalpdamGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLpGPDLDG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 364 SRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVR--LAMGNGLRANVWKNFQQRFGpIRIWEFYGSTEgnvglM 441
Cdd:PRK07008 257 KSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRrtVIGGSACPPAMIRTFEDEYG-VEVIHAWGMTE-----M 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 442 NYVGhcgavgrTSCILRmltpFELVQFDIETAEPLRDKQG-------FCIPVEPGKP--------GLLLtkVRKNQPFLG 506
Cdd:PRK07008 331 SPLG-------TLCKLK----WKHSQLPLDEQRKLLEKQGrviygvdMKIVGDDGRElpwdgkafGDLQ--VRGPWVIDR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 507 YRGSQAESnrkLVanvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPV 586
Cdd:PRK07008 398 YFRGDASP---LV-------DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAH 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 228008365 587 PGCEGKVGMAAVKlAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRLvREGF 652
Cdd:PRK07008 468 PKWDERPLLVVVK-RPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL-REQF 531
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
117-647 |
1.24e-07 |
|
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: 54.63 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 117 DALERQALAWPDRVALVCtgsEGSSITNSQLDARSCQAAWVLKAKlkdAVIQNTRdaaaILVLPSKTISALSVFLGLAKL 196
Cdd:cd12115 3 DLVEAQAARTPDAIALVC---GDESLTYAELNRRANRLAARLRAA---GVGPESR----VGVCLERTPDLVVALLAVLKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 197 G---CPVAWINPHSRgmpLLHSVRSSGASVLIVDPDlqenleevlpkllaenihcfylghssptpgvealgasldaapsd 273
Cdd:cd12115 73 GaayVPLDPAYPPER---LRFILEDAQARLVLTDPD-------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 274 pvpaslratikwkSPAIFIFTSGTTGLPKPAILSHerviqvSNVLSFCGCRADDVVYDVLP--LYHT-IGL---VLGFLG 347
Cdd:cd12115 106 -------------DLAYVIYTSGSTGRPKGVAIEH------RNAAAFLQWAAAAFSAEELAgvLASTsICFdlsVFELFG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 348 CLQVGATCVLAPkfSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDkIHTVRLAmGNGLRANVWKNFQQRFGPIRI 427
Cdd:cd12115 167 PLATGGKVVLAD--NVLALPDLPAAAEVTLINTVPSAAAELLRHDALPAS-VRVVNLA-GEPLPRDLVQRLYARLQVERV 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 428 WEFYGSTEGNvglmnyvghcgavgrTSCILRMLTPFELVQFDIETaePLRDKQ-----GFCIPVEPGKPG-LLLTKVRKN 501
Cdd:cd12115 243 VNLYGPSEDT---------------TYSTVAPVPPGASGEVSIGR--PLANTQayvldRALQPVPLGVPGeLYIGGAGVA 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 502 QPFLGYRGSQAEsnrKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVnV 581
Cdd:cd12115 306 RGYLGRPGLTAE---RFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREA-V 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 228008365 582 YGVPVPGCEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd12115 382 VVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
260-346 |
1.29e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 54.62 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 260 VEALGASLDAAPSDPVPASLRAtikwksPAIFIFTSGTTGLPKPAILSHERViqVSNVLSFC-GCRAD---DVVYDVLPL 335
Cdd:PRK07768 132 VLTVADLLAADPIDPVETGEDD------LALMQLTSGSTGSPKAVQITHGNL--YANAEAMFvAAEFDvetDVMVSWLPL 203
|
90
....*....|.
gi 228008365 336 YHTIGLVlGFL 346
Cdd:PRK07768 204 FHDMGMV-GFL 213
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
289-365 |
1.97e-07 |
|
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: 53.99 E-value: 1.97e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008365 289 AIFIFTSGTTGLPKPAILSHERVI-QVSNVLSFCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSASR 365
Cdd:cd05914 92 ALINYTSGTTGNSKGVMLTYRNIVsNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAK 169
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
111-642 |
2.22e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.79 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 111 PPETFVDALERQALAWPDRVALVctgSEGSSITNSQLDARSCQAAWVLKAKlkdAVIQNTRDAAAIlvlpSKTISALSVF 190
Cdd:PRK05691 1129 AQAWLPELLNEQARQTPERIALV---WDGGSLDYAELHAQANRLAHYLRDK---GVGPDVCVAIAA----ERSPQLLVGL 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 191 LGLAKLGCPVAWINPHSRGMPLLHSVRSSGASVLIVDPDLQENLEEVlpkllaenihcfylghssptPGVEALGAS---L 267
Cdd:PRK05691 1199 LAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQA--------------------EGVSAIALDslhL 1258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 268 DAAPSDPVPASLRAtikwKSPAIFIFTSGTTGLPKPAILSH----ERV--IQVSNVLSfcgcrADDVVYDVLPLYHTIGL 341
Cdd:PRK05691 1259 DSWPSQAPGLHLHG----DNLAYVIYTSGSTGQPKGVGNTHaalaERLqwMQATYALD-----DSDVLMQKAPISFDVSV 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 342 VLGFLGcLQVGATCVLA---PKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEdkIHTVRLAM--GNGLRANVWK 416
Cdd:PRK05691 1330 WECFWP-LITGCRLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAA--CTSLRRLFsgGEALPAELRN 1406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 417 NFQQRFGPIRIWEFYGSTEGNVGLMNYvgHCGAV-GRTSCILRMLTPFELVQFDIETAeplrdkqgfciPVEPGKPG-LL 494
Cdd:PRK05691 1407 RVLQRLPQVQLHNRYGPTETAINVTHW--QCQAEdGERSPIGRPLGNVLCRVLDAELN-----------LLPPGVAGeLC 1473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 495 LTKVRKNQPFLGYRGSQAEsnRKLVANVRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLD 574
Cdd:PRK05691 1474 IGGAGLARGYLGRPALTAE--RFVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQP 1551
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 228008365 575 FLEEVNVygVPVPGCEGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATP-HFIRIqDSLEITNTYKL 642
Cdd:PRK05691 1552 GVAQAAV--LVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPaQLIRL-DQMPLGPSGKL 1617
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
289-567 |
3.48e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 53.56 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 289 AIFIFTSGTTGLPKPAILSHE----RVIQVSNVLSFCgcrADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAPKFSAS 364
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKsllaNVEQIKTIADFT---PNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHY 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 365 RFWAE-CRQHGVTVIL----YVGEILRYlcnvpEQPEDkIHTVR--LAMGNGLRANVWKNFQQRFGpIRIWEFYGSTEG- 436
Cdd:PRK08043 445 RIVPElVYDRNCTVLFgtstFLGNYARF-----ANPYD-FARLRyvVAGAEKLQESTKQLWQDKFG-LRILEGYGVTECa 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 437 -----NVGLMNYVghcGAVGRtscILRMLTPFELVQFDIETAEPLRDK-----QGFcIPVEpgKPGLLltkvrkNQPflg 506
Cdd:PRK08043 518 pvvsiNVPMAAKP---GTVGR---ILPGMDARLLSVPGIEQGGRLQLKgpnimNGY-LRVE--KPGVL------EVP--- 579
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228008365 507 yrgsQAESnrklVANVRRVGdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVE 567
Cdd:PRK08043 580 ----TAEN----ARGEMERG--WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE 630
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
210-626 |
4.25e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 52.73 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 210 MPLLHSVRSSGASVLIVDPDLqenleevlPK----LLAENIHCFYLGHSSPTPGVEALGASLDAAPSdpvpaslratikw 285
Cdd:PRK08308 46 ITLVFFLKEKGASVLPIHPDT--------PKeaaiRMAKRAGCHGLLYGESDFTKLEAVNYLAEEPS------------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 286 kspaIFIFTSGTTGLPK---PAILSHERVIQVSNVLsfCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLA---- 358
Cdd:PRK08308 105 ----LLQYSSGTTGEPKlirRSWTEIDREIEAYNEA--LNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIItnkn 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 359 PKFSASRFwAECRQHgvtvILYVGEILRYLCNVPEQPEDKIHTVrlaMGNG----------LRANVWKNFQQrfgpiriw 428
Cdd:PRK08308 179 PKFALNIL-RNTPQH----ILYAVPLMLHILGRLLPGTFQFHAV---MTSGtplpeawfykLRERTTYMMQQ-------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 429 efYGSTEGnvglmnyvghcgavgrtSCIlrmltpfeLVQFDIETAEPLrdkqgfcipvepGKPgllLTKVRKNQpflgyr 508
Cdd:PRK08308 243 --YGCSEA-----------------GCV--------SICPDMKSHLDL------------GNP---LPHVSVSA------ 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 509 GSQAESNRKLVAnvrRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPG 588
Cdd:PRK08308 275 GSDENAPEEIVV---KMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPV 351
|
410 420 430
....*....|....*....|....*....|....*...
gi 228008365 589 CEGKVgmaAVKLAPGKTFDGQKLYQHVRSWLPAYATPH 626
Cdd:PRK08308 352 AGERV---KAKVISHEEIDPVQLREWCIQHLAPYQVPH 386
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
288-369 |
1.41e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 51.31 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAILSHERVIqvSNVLSFCGC----RADDVVYDVLPLYHTIGL---VLGFLGclqvGATCVLAPK 360
Cdd:PRK05851 154 PAVLQGTAGSTGTPRTAILSPGAVL--SNLRGLNARvgldAATDVGCSWLPLYHDMGLaflLTAALA----GAPLWLAPT 227
|
90
....*....|..
gi 228008365 361 --FSASRF-WAE 369
Cdd:PRK05851 228 taFSASPFrWLS 239
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
260-337 |
1.55e-06 |
|
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: 51.45 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 260 VEALGASLDAAPSDPVPASLrATIkwkspaifIFTSGTTGLPKPAILSHERViqVSNVLSFC-------GCRADDVVYDV 332
Cdd:cd05927 97 FEKLGKKNKVPPPPPKPEDL-ATI--------CYTSGTTGNPKGVMLTHGNI--VSNVAGVFkileilnKINPTDVYISY 165
|
....*
gi 228008365 333 LPLYH 337
Cdd:cd05927 166 LPLAH 170
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
219-335 |
1.83e-06 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 51.27 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 219 SGASVLIVDPdlQENLEEVLPkLLAENIHCFYLGHSSPT-------------PGVEALGASLDAAPSDPVPASLRATiKW 285
Cdd:cd17641 82 TGARVVIAED--EEQVDKLLE-IADRIPSVRYVIYCDPRgmrkyddprlisfEDVVALGRALDRRDPGLYEREVAAG-KG 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 228008365 286 KSPAIFIFTSGTTGLPKPAILSHERVI-QVSNVLSFCGCRADDVVYDVLPL 335
Cdd:cd17641 158 EDVAVLCTTSGTTGKPKLAMLSHGNFLgHCAAYLAADPLGPGDEYVSVLPL 208
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
288-606 |
1.95e-06 |
|
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: 50.64 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAILSHeRVIQVSNV--LSFCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVL--APKFSA 363
Cdd:cd05974 87 PMLLYFTSGTTSKPKLVEHTH-RSYPVGHLstMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLfnYARFDA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 364 SRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAMGNGLRANVWKNFQQRFGpIRIWEFYGSTEGNVGLMNY 443
Cdd:cd05974 166 KRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWG-LTIRDGYGQTETTALVGNS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 444 VGHCGAVGRTScilRMLTPFELVQFDIETAEPlrDKQGFCIPVEPGKPGLLLTkvrknqpflGYRGSQAESNRKLvanvr 523
Cdd:cd05974 245 PGQPVKAGSMG---RPLPGYRVALLDPDGAPA--TEGEVALDLGDTRPVGLMK---------GYAGDPDKTAHAM----- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 524 rvGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVygVPVPGcegkvgmaAVKLAPG 603
Cdd:cd05974 306 --RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV--VPSPD--------PVRLSVP 373
|
...
gi 228008365 604 KTF 606
Cdd:cd05974 374 KAF 376
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
287-642 |
2.75e-06 |
|
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: 50.33 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 287 SPAIFIFTSGTTGLPKPAILSHERVIQVSNVLS-FCGCRADDVVYDvlplYHTIGL---VLGFLGCLQVGATCVLAPK-- 360
Cdd:cd17652 94 NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIaAFDVGPGSRVLQ----FASPSFdasVWELLMALLAGATLVLAPAee 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 361 -FSASRFWAECRQHGVTVILYVGEILRYLcnvPEQPEDKIHTVRLAmGNGLRANVwknfQQRFGPIR-IWEFYGSTEGNV 438
Cdd:cd17652 170 lLPGEPLADLLREHRITHVTLPPAALAAL---PPDDLPDLRTLVVA-GEACPAEL----VDRWAPGRrMINAYGPTETTV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 439 GLMnyVGHCGAVGRTSCILRmltPFELVQFDIETAEpLRdkqgfciPVEPGKPGLL------LTKvrknqpflGYRGSQA 512
Cdd:cd17652 242 CAT--MAGPLPGGGVPPIGR---PVPGTRVYVLDAR-LR-------PVPPGVPGELyiagagLAR--------GYLNRPG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 513 ESNRKLVAN-VRRVGDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVnVYGVPVPGCEG 591
Cdd:cd17652 301 LTAERFVADpFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEA-VVVVRDDRPGD 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 228008365 592 KVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKL 642
Cdd:cd17652 380 KRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKL 430
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
280-652 |
3.94e-06 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 50.14 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 280 RATIKWK-----SPAIFIFTSGTTGLPKPAILSHErviqvSNVL--------SFCGCRADDVVYDVLPLYHTIGLVLGFl 346
Cdd:PRK06018 166 DGDFAWKtfdenTAAGMCYTSGTTGDPKGVLYSHR-----SNVLhalmanngDALGTSAADTMLPVVPLFHANSWGIAF- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 347 GCLQVGATCVL-APKFSASRFWAECRQHGVTVILYVGEILRYLCNVPEQPEDKIHTVRLAM--GNGLRANVWKNFQQR-F 422
Cdd:PRK06018 240 SAPSMGTKLVMpGAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVcgGSAMPRSMIKAFEDMgV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 423 GPIRIWefyGSTEgnvglMNYVGhcgavgrTSCILRMltPFELVQFDIETAepLRDKQGF-------CIPVEPGK----- 490
Cdd:PRK06018 320 EVRHAW---GMTE-----MSPLG-------TLAALKP--PFSKLPGDARLD--VLQKQGYppfgvemKITDDAGKelpwd 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 491 ---PGLLltKVRKNQPFLGYRGSQAESNRKlvanvrrvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVE 567
Cdd:PRK06018 381 gktFGRL--KVRGPAVAAAYYRVDGEILDD---------DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 568 CVLSSLDFLEEVNVYGVPVPGCeGKVGMAAVKLAPGKTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:PRK06018 450 NLAVGHPKVAEAAVIGVYHPKW-DERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
....*
gi 228008365 648 vREGF 652
Cdd:PRK06018 529 -REQF 532
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
118-649 |
4.27e-06 |
|
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: 49.87 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 118 ALERQALAWPDRVALVCTGSEGSS---ITNSQLDARSCQAAWVLKA---KLKDAVIqntrdaaaiLVLPskTISALSV-F 190
Cdd:cd05966 58 CLDRHLKERGDKVAIIWEGDEPDQsrtITYRELLREVCRFANVLKSlgvKKGDRVA---------IYMP--MIPELVIaM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 191 LGLAKLGCPvawinphsrgmpllHSVRSSG--ASVL---IVDPD------------------LQENLEEVLpKLLAENIH 247
Cdd:cd05966 127 LACARIGAV--------------HSVVFAGfsAESLadrINDAQcklvitadggyrggkvipLKEIVDEAL-EKCPSVEK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 248 CFYLGHS----SPTPGVEALGASLDAAPSDPVPAslrATIKWKSPAIFIFTSGTTGLPKP-----------AILSHERV- 311
Cdd:cd05966 192 VLVVKRTggevPMTEGRDLWWHDLMAKQSPECEP---EWMDSEDPLFILYTSGSTGKPKGvvhttggyllyAATTFKYVf 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 312 -IQVSNVLsfcGCRADdvvydvlplyhtIGLVLG----FLGCLQVGATCVL---APKF-SASRFWAECRQHGVTvILYVG 382
Cdd:cd05966 269 dYHPDDIY---WCTAD------------IGWITGhsyiVYGPLANGATTVMfegTPTYpDPGRYWDIVEKHKVT-IFYTA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 383 -EILRYLCNVPEQPEDK--------IHTVrlamGNGLRANVWKNFQQRFGPIRI------WEfygsTE-GnvGLMnyVGH 446
Cdd:cd05966 333 pTAIRALMKFGDEWVKKhdlsslrvLGSV----GEPINPEAWMWYYEVIGKERCpivdtwWQ----TEtG--GIM--ITP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 447 CGAVGRT---SCILrmltPFelvqFDIETAepLRDKQGfcIPVEPGKPGLLLTKvrknQPFLG-YRGSQAESNRKLVANV 522
Cdd:cd05966 401 LPGATPLkpgSATR----PF----FGIEPA--ILDEEG--NEVEGEVEGYLVIK----RPWPGmARTIYGDHERYEDTYF 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 523 RRVGDLYFnTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPgCEGKVGMAAVKLAP 602
Cdd:cd05966 465 SKFPGYYF-TGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHD-IKGEAIYAFVTLKD 542
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 228008365 603 GKTFDG---QKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKsRLVR 649
Cdd:cd05966 543 GEEPSDelrKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMR-RILR 591
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
216-647 |
5.54e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 49.63 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 216 VRSSGASVLIVDPDLQENLEEVLPKLLAE--NIH---CFYLGHSSPT-PGVEALGASLDAAPSDPVPASLRATIKWKS-- 287
Cdd:PLN03102 107 LRHAKPKILFVDRSFEPLAREVLHLLSSEdsNLNlpvIFIHEIDFPKrPSSEELDYECLIQRGEPTPSLVARMFRIQDeh 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 -PAIFIFTSGTTGLPKPAILSHeRVIQVSNVLSFCGCRAD--DVVYDVLPLYHTIGLVLGFlGCLQVGATCVLAPKFSAS 364
Cdd:PLN03102 187 dPISLNYTSGTTADPKGVVISH-RGAYLSTLSAIIGWEMGtcPVYLWTLPMFHCNGWTFTW-GTAARGGTSVCMRHVTAP 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 365 RFWAECRQHGVTVILYVGEILRYLC--NVPEQPEDKIHTVRLAMGNGLRANVWKNFQqRFGpIRIWEFYGSTE--GNVGL 440
Cdd:PLN03102 265 EIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSPRSGPVHVLTGGSPPPAALVKKVQ-RLG-FQVMHAYGLTEatGPVLF 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 441 MNYVGHCGAVGRTSCI-------LRMLTpfeLVQFDIETAEPLRDkqgfcIPVEPGKPGLLLTKvrKNQPFLGYRgsqae 513
Cdd:PLN03102 343 CEWQDEWNRLPENQQMelkarqgVSILG---LADVDVKNKETQES-----VPRDGKTMGEIVIK--GSSIMKGYL----- 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 514 SNRKLVANVRRVGdlYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPgCEGKV 593
Cdd:PLN03102 408 KNPKATSEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP-TWGET 484
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 228008365 594 GMAAVKLAPGKTFDGQK----------LYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:PLN03102 485 PCAFVVLEKGETTKEDRvdklvtrerdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
108-354 |
9.84e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 48.89 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 108 NKHPPE----TFVDALERQALAWPDRVALVCTGSEGSSitnsqldarscqaaWVL----KAKLK-DAVIQNTRDAAA--- 175
Cdd:PRK12582 40 SRHPLGpyprSIPHLLAKWAAEAPDRPWLAQREPGHGQ--------------WRKvtygEAKRAvDALAQALLDLGLdpg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 176 --ILVLPSKTISALSVFLGLAKLGCPVAWINP--------HSRGMPLLHSVRSsgASVLIVDPDLQENLEEVLPKLLAEN 245
Cdd:PRK12582 106 rpVMILSGNSIEHALMTLAAMQAGVPAAPVSPayslmshdHAKLKHLFDLVKP--RVVFAQSGAPFARALAALDLLDVTV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 246 IHCFYLGHSSPTPGVEALGASldaAPSDPVPASlRATIKWKSPAIFIFTSGTTGLPKPAILSHErvIQVSNVLSFCGCRA 325
Cdd:PRK12582 184 VHVTGPGEGIASIAFADLAAT---PPTAAVAAA-IAAITPDTVAKYLFTSGSTGMPKAVINTQR--MMCANIAMQEQLRP 257
|
250 260 270
....*....|....*....|....*....|....*
gi 228008365 326 DD------VVYDVLPLYHTIGLVLGFLGCLQVGAT 354
Cdd:PRK12582 258 REpdppppVSLDWMPWNHTMGGNANFNGLLWGGGT 292
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
223-351 |
1.15e-05 |
|
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: 48.43 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 223 VLIVDPDLQENLEevlpKLLAENIHCFYLGHSSptpgvealgASLDAAPSDPVPASLRATikwkSPAIFIFTSGTTGLPK 302
Cdd:cd05906 121 VVLTDAELVAEFA----GLETLSGLPGIRVLSI---------EELLDTAADHDLPQSRPD----DLALLMLTSGSTGFPK 183
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 228008365 303 PAILSHERVI-QVSNVLSFCGCRADDVVYDVLPLYHTIGLVLG-----FLGCLQV 351
Cdd:cd05906 184 AVPLTHRNILaRSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhlravYLGCQQV 238
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
289-647 |
2.07e-05 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 47.39 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 289 AIFIFTSGTTGLPKPAILSHERVIQVSNVLS--FCGCRADDVVYDVLPLY----HTIGLVLGFLGclqvGATCVLAP--- 359
Cdd:cd17648 97 AYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSerYFGRDNGDEAVLFFSNYvfdfFVEQMTLALLN----GQKLVVPPdem 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 360 KFSASRFWAECRQHGVTvilyvgeilrYLCNVPEQPE-------DKIHTVrLAMGNGLRANVWKNFQQRFgPIRIWEFYG 432
Cdd:cd17648 173 RFDPDRFYAYINREKVT----------YLSGTPSVLQqydlarlPHLKRV-DAAGEEFTAPVFEKLRSRF-AGLIINAYG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 433 STEGNVglmnyvghcgavgrTSCILRMLTPfelVQFDIETAEPLRDKQGFCI-----PVEPGKPGLL------LTKVRKN 501
Cdd:cd17648 241 PTETTV--------------TNHKRFFPGD---QRFDKSLGRPVRNTKCYVLndamkRVPVGAVGELylggdgVARGYLN 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 502 QPFL-GYR----GSQAESNRKLVANVRrvgdLYfNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFL 576
Cdd:cd17648 304 RPELtAERflpnPFQTEQERARGRNAR----LY-KTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGV 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 228008365 577 EEVNVYGVPVPGCEGKVGMAAV----KLAPGkTFDGQKLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKSRL 647
Cdd:cd17648 379 RECAVVAKEDASQAQSRIQKYLvgyyLPEPG-HVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
220-309 |
3.05e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 43.71 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 220 GASVLIVDPDL-QENLEEVLPKLLAEniHCFYLGHSSPTPGvealgasLDAAPSDPVPASLRATIKWKSPAIFIFTSGTT 298
Cdd:PRK09029 77 GARVLPLNPQLpQPLLEELLPSLTLD--FALVLEGENTFSA-------LTSLHLQLVEGAHAVAWQPQRLATMTLTSGST 147
|
90
....*....|.
gi 228008365 299 GLPKPAILSHE 309
Cdd:PRK09029 148 GLPKAAVHTAQ 158
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
212-341 |
6.03e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 43.18 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 212 LLHSVRSSGASVLIVDP-------DLQENLEEVlpkllaENIHCFYLGHSSPTPG--------------VEALGASLDAA 270
Cdd:PLN02387 170 LCHSLNETEVTTVICDSkqlkkliDISSQLETV------KRVIYMDDEGVDSDSSlsgssnwtvssfseVEKLGKENPVD 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 228008365 271 PSDPVPASLratikwkspAIFIFTSGTTGLPKPAILSHERVIQ-VSNVLSFC-GCRADDVVYDVLPLYHTIGL 341
Cdd:PLN02387 244 PDLPSPNDI---------AVIMYTSGSTGLPKGVMMTHGNIVAtVAGVMTVVpKLGKNDVYLAYLPLAHILEL 307
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
529-660 |
7.72e-04 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 42.58 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 529 YFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPgCEGKVGMAAVKLAPGKTFDG 608
Cdd:PLN02654 514 YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHE-VKGQGIYAFVTLVEGVPYSE 592
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 228008365 609 Q---KLYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVK-------SRLVREGFDVGIIADP 660
Cdd:PLN02654 593 ElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRrilrkiaSRQLDELGDTSTLADP 654
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
260-337 |
7.79e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 42.78 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 260 VEALGASLDAAPSDPVPASLrATIkwkspaifIFTSGTTGLPKPAILSHERVIQ----VSNVLSFCgcrADDVVYDVLPL 335
Cdd:PLN02736 204 LLAQGRSSPQPFRPPKPEDV-ATI--------CYTSGTTGTPKGVVLTHGNLIAnvagSSLSTKFY---PSDVHISYLPL 271
|
..
gi 228008365 336 YH 337
Cdd:PLN02736 272 AH 273
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
267-357 |
9.64e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 42.24 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 267 LDA-APSDPVPASLRATikwkspAIFIFTSGTTGLPKPAILSHERVI----QV-SNVLSFCGCRA--DDVVYDVLPLYHT 338
Cdd:PRK05850 146 LDSpRGSDARPRDLPST------AYLQYTSGSTRTPAGVMVSHRNVIanfeQLmSDYFGDTGGVPppDTTVVSWLPFYHD 219
|
90
....*....|....*....
gi 228008365 339 IGLVLGFLGCLQVGATCVL 357
Cdd:PRK05850 220 MGLVLGVCAPILGGCPAVL 238
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
246-660 |
1.34e-03 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 41.92 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 246 IHCFYLGHSSPTPGVEALGASLD-------AAPSDPVPASlrATikwkSPAIFIFTSGTTGLPKPAIlsheR------VI 312
Cdd:cd05967 189 HHVLVLNRPQVPADLTKPGRDLDwsellakAEPVDCVPVA--AT----DPLYILYTSGTTGKPKGVV----RdngghaVA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 313 QVSNVLSFCGCRADDVVY---DvlplyhtIGLVLG----FLGCLQVGATCVL-------APkfSASRFWAECRQHGVTVI 378
Cdd:cd05967 259 LNWSMRNIYGIKPGDVWWaasD-------VGWVVGhsyiVYGPLLHGATTVLyegkpvgTP--DPGAFWRVIEKYQVNAL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 379 LYVGEILRYLCNVPEQPED----KIHTVRLAMGNGLRANV-WKNFQQRFGPIRIWEFYGSTEGNVGLM-NYVG------H 446
Cdd:cd05967 330 FTAPTAIRAIRKEDPDGKYikkyDLSSLRTLFLAGERLDPpTLEWAENTLGVPVIDHWWQTETGWPITaNPVGleplpiK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 447 CGAVGRtscilrmltPFELVQFDI--ETAEPLR-DKQGFCIPVEPGKPGLLLTKVRKNQPFLgyRGSQAESnrklvanvr 523
Cdd:cd05967 410 AGSPGK---------PVPGYQVQVldEDGEPVGpNELGNIVIKLPLPPGCLLTLWKNDERFK--KLYLSKF--------- 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 524 rvgDLYFNTGDVLTLDQEGFFYFQDRLGDTFRWKGENVSTGEVECVLSSLDFLEEVNVYGVPVPgCEGKVGMAAVKLAPG 603
Cdd:cd05967 470 ---PGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDE-LKGQVPLGLVVLKEG 545
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 228008365 604 KTFDGQK----LYQHVRSWLPAYATPHFIRIQDSLEITNTYKLVKS--RLVREGFDVGI---IADP 660
Cdd:cd05967 546 VKITAEElekeLVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRtlRKIADGEDYTIpstIEDP 611
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
288-399 |
1.48e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 41.65 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 288 PAIFIFTSGTTGLPKPAILSHERVIQVSNVLSFCGCRADDVVydVLPLYHTIGLV---LGFLGCLQVGATCVL------A 358
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPT--VVFSHSSIGWVsfhGFLYGSLSLGNTFVMfeggiiK 333
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 228008365 359 PKFSASRFWAECRQHGVTVILYVGEILRYLCNVpeQPEDKI 399
Cdd:PTZ00237 334 NKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKT--DPEATI 372
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
289-354 |
1.93e-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: 41.43 E-value: 1.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228008365 289 AIFIFTSGTTGLPKPAILSHERVI-----QVSNVLSFCGcrADDVVYDVLPLYHTIGLVLGFLgCLQVGAT 354
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNLVagiagLGDRVPELLG--PDDRYLAYLPLAHIFELAAENV-CLYRGGT 158
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
208-346 |
2.14e-03 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 41.14 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 208 RGMpllhsVRSSGASVLIVDPDLQENLEEVLPKLlaenihcfylghssptPGVEAL-GASLDAAPSDPVPASlraTIKWK 286
Cdd:PRK09192 121 RGM-----LASAQPAAIITPDELLPWVNEATHGN----------------PLLHVLsHAWFKALPEADVALP---RPTPD 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 228008365 287 SPAIFIFTSGTTGLPKPAILSHERVIQVSNVLSFCG--CRADDVVYDVLPLYHTIGLVlGFL 346
Cdd:PRK09192 177 DIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGlkVRPGDRCVSWLPFYHDMGLV-GFL 237
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
257-340 |
2.28e-03 |
|
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: 41.26 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 257 TPGVEALGASLDAAPSDPVpaslratikwkspAIFIFTSGTTGLPKPAILSHeRVIqVSNVLSFCGCRADD-----VVYD 331
Cdd:cd05921 149 TPPTAAVDAAFAAVGPDTV-------------AKFLFTSGSTGLPKAVINTQ-RML-CANQAMLEQTYPFFgeeppVLVD 213
|
....*....
gi 228008365 332 VLPLYHTIG 340
Cdd:cd05921 214 WLPWNHTFG 222
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
256-349 |
3.83e-03 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 40.63 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008365 256 PTPGVEALGASLDAAPSDPVPASLrATIKWKSPAIFIFTSGTTGLPKPAILSHeRVI-----QVSNVLSFCGcRADDVVY 330
Cdd:PRK08180 180 PGRAATPFAALLATPPTAAVDAAH-AAVGPDTIAKFLFTSGSTGLPKAVINTH-RMLcanqqMLAQTFPFLA-EEPPVLV 256
|
90 100
....*....|....*....|....*
gi 228008365 331 DVLPLYHT------IGLVLGFLGCL 349
Cdd:PRK08180 257 DWLPWNHTfggnhnLGIVLYNGGTL 281
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
291-359 |
5.21e-03 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 39.78 E-value: 5.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228008365 291 FI-FTSGTTGLPKPAILSHERVI-QVSNVLSFCGCRADDVVYDVLPLYHTIGLVLGFLGCLQVGATCVLAP 359
Cdd:cd05908 110 FIqFSSGSTGDPKGVMLTHENLVhNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMP 180
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