|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1-504 |
0e+00 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 916.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 1 MKLLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIP 80
Cdd:PRK04813 2 MDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 81 VDLSIPADRVQRIAENSGAKLLLSATAVTVTDLPVRIVSEDNLKDIFFthKGNTPNPEHAVKGDENFYIIYTSGSTGNPK 160
Cdd:PRK04813 82 VDVSSPAERIEMIIEVAKPSLIIATEELPLEILGIPVITLDELKDIFA--TGNPYDFDHAVKGDDNYYIIFTSGTTGKPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 161 GVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWT 240
Cdd:PRK04813 160 GVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 241 STPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLP 320
Cdd:PRK04813 240 STPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEITDEMLDQYKRLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 321 VGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMIDGERAYKTGDAGYVENGLLFYNGRLDF 400
Cdd:PRK04813 320 IGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQPAYHTGDAGYLEDGLLFYQGRIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 401 QIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFEKEFKLTSAIKKELNERLPNYMIPRKFM 480
Cdd:PRK04813 400 QIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMEYMIPRKFI 479
|
490 500
....*....|....*....|....
gi 446693156 481 YQSSIPMTPNGKVDRKKLLSEVTA 504
Cdd:PRK04813 480 YRDSLPLTPNGKIDRKALIEEVNK 503
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
2-502 |
0e+00 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 724.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 2 KLLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPV 81
Cdd:TIGR01734 1 KLIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 82 DLSIPADRVQRIAENSGAKLLLSATAVTVTDLPVRIVSEDNLKDIFftHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKG 161
Cdd:TIGR01734 81 DTSIPSERIEMIIEAAGPELVIHTAELSIDAVGTQIITLSALEQAE--TSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 162 VQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTS 241
Cdd:TIGR01734 159 VQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 242 TPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPV 321
Cdd:TIGR01734 239 TPSFVDMCLLDPNFNQENYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEILDQYPRLPI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 322 GYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMIDGERAYKTGDAGYVENGLLFYNGRLDFQ 401
Cdd:TIGR01734 319 GFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSHEGQPAYRTGDAGTITDGQLFYQGRLDFQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 402 IKLHGYRMELEEIEHHLRACSYVEGAVIVPI-KKGEKYDYLLAVVVPGEHSFEKEFKLTSAIKKELNERLPNYMIPRKFM 480
Cdd:TIGR01734 399 IKLHGYRIELEDIEFNLRQSSYIESAVVVPKyNKDHKVEYLIAAIVPETEDFEKEFQLTKAIKKELKKSLPAYMIPRKFI 478
|
490 500
....*....|....*....|..
gi 446693156 481 YQSSIPMTPNGKVDRKKLLSEV 502
Cdd:TIGR01734 479 YRDQLPLTANGKIDRKALAEEV 500
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
11-498 |
0e+00 |
|
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: 723.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRV 90
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 91 QRIAENSGAKLLLSAtavtvtdlpvrivsednlkdiffthkgntpnpehavkGDENFYIIYTSGSTGNPKGVQITYNCLV 170
Cdd:cd05945 81 REILDAAKPALLIAD-------------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 171 SFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEMCL 250
Cdd:cd05945 124 SFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 251 MEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVGYCKSDCRL 330
Cdd:cd05945 204 LSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGYAKPGAKL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 331 LIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMIDGERAYKTGDAGYVEN-GLLFYNGRLDFQIKLHGYRM 409
Cdd:cd05945 284 VILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRAYRTGDLVRLEAdGLLFYRGRLDFQVKLNGYRI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 410 ELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSfekEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTP 489
Cdd:cd05945 364 ELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGA---EAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNA 440
|
....*....
gi 446693156 490 NGKVDRKKL 498
Cdd:cd05945 441 NGKIDRKAL 449
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
15-498 |
1.21e-165 |
|
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: 475.86 E-value: 1.21e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 15 PDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIA 94
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 95 ENSGAKLLLsatavtvtdlpvrivsednlkdiffthkgntpnpehaVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTK 174
Cdd:cd05930 81 EDSGAKLVL-------------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 175 WAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEMCLMEAS 254
Cdd:cd05930 124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 255 FSenMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDqYKSLPVGYCKSDCRLLIMK 334
Cdd:cd05930 204 LA--ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEE-DGRVPIGRPIPNTRVYVLD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 335 EDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT---MIDGERAYKTGDAG-YVENGLLFYNGRLDFQIKLHGYRME 410
Cdd:cd05930 281 ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVpnpFGPGERMYRTGDLVrWLPDGNLEFLGRIDDQVKIRGYRIE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 411 LEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFEkefkLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPN 490
Cdd:cd05930 361 LGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGEL----DEEELRAHLAERLPDYMVPSAFVVLDALPLTPN 436
|
....*...
gi 446693156 491 GKVDRKKL 498
Cdd:cd05930 437 GKVDRKAL 444
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
28-428 |
4.63e-130 |
|
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: 383.92 E-value: 4.63e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 28 TYKQLKEDSDALAHWISSEY---PDDRSPIMVygHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKLLL- 103
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGgvgPGDRVAVLL--ERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 104 -SATAVTVTDLPVRIVSEDNLKDIFFTHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNL 182
Cdd:TIGR01733 79 dSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 183 QTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIAR-PKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSenmLP 261
Cdd:TIGR01733 159 DPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDdAALLAALIAEHPVTVLNLTPSLLALLAAALPPA---LA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 262 NMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVGYCKSDCRLLIMKEDGTIAP 341
Cdd:TIGR01733 236 SLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 342 DGEKGEIVIVGPSVSVGYLGSPELTEKAFTMI-----DGERAYKTGD-AGYVENGLLFYNGRLDFQIKLHGYRMELEEIE 415
Cdd:TIGR01733 316 VGVVGELYIGGPGVARGYLNRPELTAERFVPDpfaggDGARLYRTGDlVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395
|
410
....*....|...
gi 446693156 416 HHLRACSYVEGAV 428
Cdd:TIGR01733 396 AALLRHPGVREAV 408
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
5-498 |
5.92e-118 |
|
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: 355.87 E-value: 5.92e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 5 EQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAhWISSEY---PDDRSPIMVygHMQPEMIINFLGCVKAGHAYIPV 81
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLA-RTLREKgvgPDTIVGIMA--ERSLEMIVGILGILKAGGAYLPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 82 DLSIPADRVQRIAENSGAKLLLSATAVtvtDLPVR-IVSEDNLKDIFFTHKGNTpNPEHAVKGDENFYIIYTSGSTGNPK 160
Cdd:cd17655 78 DPDYPEERIQYILEDSGADILLTQSHL---QPPIAfIGLIDLLDEDTIYHEESE-NLEPVSKSDDLAYVIYTSGSTGKPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 161 GVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWT 240
Cdd:cd17655 154 GVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 241 STPSFAEMcLMEASFSENmlPNMKTFLFCGEVLPNEVARKLIERF-PKATIMNTYGPTEATVAVTgIHVTEEVLDQYKSL 319
Cdd:cd17655 234 LTPAHLKL-LDAADDSEG--LSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDAS-IYQYEPETDQQVSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 320 PVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT---MIDGERAYKTGD-AGYVENGLLFYN 395
Cdd:cd17655 310 PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVddpFVPGERMYRTGDlARWLPDGNIEFL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 396 GRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVpgehsFEKEFKlTSAIKKELNERLPNYMI 475
Cdd:cd17655 390 GRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-----SEKELP-VAQLREFLARELPDYMI 463
|
490 500
....*....|....*....|...
gi 446693156 476 PRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd17655 464 PSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
3-504 |
1.64e-116 |
|
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: 372.65 E-value: 1.64e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVygHMQPEMIINFLGCVKAGHAYIP 80
Cdd:COG1020 478 LHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALgvGPGDLVGVCL--ERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 81 VDLSIPADRVQRIAENSGAKLLL--SATAVTVTDLPVRIVSEDNLKdiffTHKGNTPNPEHAVKGDENFYIIYTSGSTGN 158
Cdd:COG1020 556 LDPAYPAERLAYMLEDAGARLVLtqSALAARLPELGVPVLALDALA----LAAEPATNPPVPVTPDDLAYVIYTSGSTGR 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 159 PKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQV 238
Cdd:COG1020 632 PKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTV 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 239 WTSTPSFAEMcLMEASFSEnmLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTgIHVTEEVLDQYKS 318
Cdd:COG1020 712 LNLTPSLLRA-LLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDST-YYEVTPPDADGGS 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 319 LPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAF----TMIDGERAYKTGDAG-YVENGLLF 393
Cdd:COG1020 788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFvadpFGFPGARLYRTGDLArWLPDGNLE 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 394 YNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFEKEFKLTSAikkeLNERLPNY 473
Cdd:COG1020 868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLA----LALLLPPY 943
|
490 500 510
....*....|....*....|....*....|.
gi 446693156 474 MIPRKFMYQSSIPMTPNGKVDRKKLLSEVTA 504
Cdd:COG1020 944 MVPAAVVLLLPLPLTGNGKLDRLALPAPAAA 974
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
8-498 |
3.46e-114 |
|
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: 345.73 E-value: 3.46e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 8 EKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPA 87
Cdd:cd12117 4 EEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 88 DRVQRIAENSGAKLLLS--ATAVTVTDLPVRIVSEDNLKDiffthkGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQIT 165
Cdd:cd12117 84 ERLAFMLADAGAKVLLTdrSLAGRAGGLEVAVVIDEALDA------GPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 166 Y---NCLVSFTKWAVedfnLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQV-WTS 241
Cdd:cd12117 158 HrgvVRLVKNTNYVT----LGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVlWLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 242 TPSFAEMclmeASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQyKSLPV 321
Cdd:cd12117 234 AALFNQL----ADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVA-GSIPI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 322 GYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT---MIDGERAYKTGD-AGYVENGLLFYNGR 397
Cdd:cd12117 309 GRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVadpFGPGERLYRTGDlARWLPDGRLEFLGR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 398 LDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEhsfekefKLTSA-IKKELNERLPNYMIP 476
Cdd:cd12117 389 IDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEG-------ALDAAeLRAFLRERLPAYMVP 461
|
490 500
....*....|....*....|..
gi 446693156 477 RKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd12117 462 AAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
11-498 |
2.78e-102 |
|
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: 315.37 E-value: 2.78e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVygHMQPEMIINFLGCVKAGHAYIPVDLSIPAD 88
Cdd:cd17646 8 AARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARgvGPEDRVAVLL--PRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 89 RVQRIAENSGAKLLLsatavTVTDLPVRIVSEDN---LKDIFFTHKGNTPnPEHAVKGDENFYIIYTSGSTGNPKGVQIT 165
Cdd:cd17646 86 RLAYMLADAGPAVVL-----TTADLAARLPAGGDvalLGDEALAAPPATP-PLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 166 YNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLwaidkdMIARP---KD---LFASLEQSDIQVW 239
Cdd:cd17646 160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARL------VVARPgghRDpayLAALIREHGVTTC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 240 TSTPSFAEMCLMEASFSEnmLPNMKtFLFC-GEVLPNEVARKLIERFPkATIMNTYGPTEATVAVTGIHVTEEVLDqyKS 318
Cdd:cd17646 234 HFVPSMLRVFLAEPAAGS--CASLR-RVFCsGEALPPELAARFLALPG-AELHNLYGPTEAAIDVTHWPVRGPAET--PS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 319 LPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT---MIDGERAYKTGD-AGYVENGLLFY 394
Cdd:cd17646 308 VPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVpdpFGPGSRMYRTGDlARWRPDGALEF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 395 NGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEhsfEKEFKLTSAIKKELNERLPNYM 474
Cdd:cd17646 388 LGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAA---GAAGPDTAALRAHLAERLPEYM 464
|
490 500
....*....|....*....|....
gi 446693156 475 IPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd17646 465 VPAAFVVLDALPLTANGKLDRAAL 488
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
3-504 |
3.90e-102 |
|
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: 313.67 E-value: 3.90e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEY--PDDRspIMVYGHMQPEMIINFLGCVKAGHAYIP 80
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGvgPGDR--VALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 81 VDLSIPADRVQRIAENSGAKLLLSAtavtvtdlpvrivsednlkdiffthkgntpnpehavkgdenfYIIYTSGSTGNPK 160
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------LILYTSGTTGRPK 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 161 GVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLS-VMDIYPSLVTGGTLWAIDKdmiARPKDLFASLEQSDIQVW 239
Cdd:COG0318 117 GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 240 TSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEATVAVTgihVTEEVLDQYKSL 319
Cdd:COG0318 194 FGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVT---VNPEDPGERRPG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 320 PVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFtmIDGerAYKTGDAGYV-ENGLLFYNGRL 398
Cdd:COG0318 270 SVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF--RDG--WLRTGDLGRLdEDGYLYIVGRK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 399 DFQIKLHGYRMELEEIEHHLRACSYV-EGAVI-VPIKK-GEKydyLLAVVVPGE-HSFEKEfkltsAIKKELNERLPNYM 474
Cdd:COG0318 346 KDMIISGGENVYPAEVEEVLAAHPGVaEAAVVgVPDEKwGER---VVAFVVLRPgAELDAE-----ELRAFLRERLARYK 417
|
490 500 510
....*....|....*....|....*....|
gi 446693156 475 IPRKFMYQSSIPMTPNGKVDRKKLLSEVTA 504
Cdd:COG0318 418 VPRRVEFVDELPRTASGKIDRRALRERYAA 447
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
7-498 |
3.44e-99 |
|
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: 307.35 E-value: 3.44e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIP 86
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 87 ADRVQRIAENSGAKLLLSATAVTvTDLPVRIVSeDNLKDIFFTHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQITY 166
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALA-GELAVELVA-VTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 167 NCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFA 246
Cdd:cd17651 159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 247 EMCLMEASFSENMLPNMKTFLFCGEVLPNEVA-RKLIERFPKATIMNTYGPTEATVaVTGIHVTEEVLDQYKSLPVGYCK 325
Cdd:cd17651 239 RALAEHGRPLGVRLAALRYLLTGGEQLVLTEDlREFCAGLPGLRLHNHYGPTETHV-VTALSLPGDPAAWPAPPPIGRPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 326 SDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT---MIDGERAYKTGD-AGYVENGLLFYNGRLDFQ 401
Cdd:cd17651 318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVpdpFVPGARMYRTGDlARWLPDGELEFLGRADDQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 402 IKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGehsfEKEFKLTSAIKKELNERLPNYMIPRKFMY 481
Cdd:cd17651 398 VKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGD----PEAPVDAAELRAALATHLPEYMVPSAFVL 473
|
490
....*....|....*..
gi 446693156 482 QSSIPMTPNGKVDRKKL 498
Cdd:cd17651 474 LDALPLTPNGKLDRRAL 490
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
15-498 |
1.19e-93 |
|
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: 292.66 E-value: 1.19e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 15 PDQTAFVWRDAKITYKQLKEDSDALA-HWISSEYPDDRsPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRI 93
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAaRLRARGVGPGD-RVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 94 AENSGAKLLLsATAVTVTDLPVRI-VSEDNLKDIffthKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSF 172
Cdd:cd12116 80 LEDAEPALVL-TDDALPDRLPAGLpVLLLALAAA----AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 173 TKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEMcLME 252
Cdd:cd12116 155 LHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRM-LLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 253 ASFSEnmLPNMkTFLFCGEVLPNEVARKLIERfpKATIMNTYGPTEATVAVTGIHVTEEVldqyKSLPVGYCKSDCRLLI 332
Cdd:cd12116 234 AGWQG--RAGL-TALCGGEALPPDLAARLLSR--VGSLWNLYGPTETTIWSTAARVTAAA----GPIPIGRPLANTQVYV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 333 MKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT----MIDGERAYKTGD-AGYVENGLLFYNGRLDFQIKLHGY 407
Cdd:cd12116 305 LDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVpdpfAGPGSRLYRTGDlVRRRADGRLEYLGRADGQVKIRGH 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 408 RMELEEIEHHLRACSYVEGAVIVpIKKGEKYDYLLAVVVPGE-HSFEkefklTSAIKKELNERLPNYMIPRKFMYQSSIP 486
Cdd:cd12116 385 RIELGEIEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAgAAPD-----AAALRAHLRATLPAYMVPSAFVRLDALP 458
|
490
....*....|..
gi 446693156 487 MTPNGKVDRKKL 498
Cdd:cd12116 459 LTANGKLDRKAL 470
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
3-502 |
2.06e-93 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 292.14 E-value: 2.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTA-FVWrDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPV 81
Cdd:cd05918 1 VHDLIEERARSQPDAPAvCAW-DGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 82 DLSIPADRVQRIAENSGAKLLLSATavtvtdlpvrivsednlkdiffthkgntpnPEHAVkgdenfYIIYTSGSTGNPKG 161
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVLTSS------------------------------PSDAA------YVIFTSGSTGKPKG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 162 VQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDmiARPKDLFASLEQSDIQvWTS 241
Cdd:cd05918 124 VVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEE--DRLNDLAGFINRLRVT-WAF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 242 -TPSFAemclmeASFSENMLPNMKTFLFCGEVLPNEVARKLIERfpkATIMNTYGPTEATVAVTGIHVTEEVldqyKSLP 320
Cdd:cd05918 201 lTPSVA------RLLDPEDVPSLRTLVLGGEALTQSDVDTWADR---VRLINAYGPAECTIAATVSPVVPST----DPRN 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 321 VGYCkSDCRLLIMKEDGT--IAPDGEKGEIVIVGPSVSVGYLGSPELTEKAF----------TMIDGERAYKTGD-AGYV 387
Cdd:cd05918 268 IGRP-LGATCWVVDPDNHdrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFiedpawlkqeGSGRGRRLYRTGDlVRYN 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 388 ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIV---PIKKGEKYDYLLAVVVPGEHS------------- 451
Cdd:cd05918 347 PDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVevvKPKDGSSSPQLVAFVVLDGSSsgsgdgdslflep 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446693156 452 FEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSEV 502
Cdd:cd05918 427 SDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
7-404 |
3.37e-91 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 284.59 E-value: 3.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVW-RDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDL 83
Cdd:pfam00501 1 LERQAARTPDKTALEVgEGRRLTYRELDERANRLAAGLRALgvGKGDR--VAILLPNSPEWVVAFLACLKAGAVYVPLNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 84 SIPADRVQRIAENSGAKLLLSATAVTVTDL---------PVRIVSEDNLKDIFFT-------HKGNTPNPEHAVKGDENF 147
Cdd:pfam00501 79 RLPAEELAYILEDSGAKVLITDDALKLEELlealgklevVKLVLVLDRDPVLKEEplpeeakPADVPPPPPPPPDPDDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 148 YIIYTSGSTGNPKGVQITYNCLVSFTKWA----VEDFNLQTGQVFLNQAPFSFDLSV-MDIYPSLVTGGTLWAIDKDMIA 222
Cdd:pfam00501 159 YIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 223 RPKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKAtIMNTYGPTEATVA 302
Cdd:pfam00501 239 DPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 303 VTgiHVTEEVLDQYKSLPVGYCKSDCRLLIMKED-GTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFtmiDGERAYKT 381
Cdd:pfam00501 318 VT--TPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAF---DEDGWYRT 392
|
410 420
....*....|....*....|....
gi 446693156 382 GDAGYV-ENGLLFYNGRLDFQIKL 404
Cdd:pfam00501 393 GDLGRRdEDGYLEIVGRKKDQIKL 416
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
15-498 |
1.08e-89 |
|
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: 281.50 E-value: 1.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 15 PDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVygHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQR 92
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEgvGPGDRVALAL--PRSAELIVALLAILKAGGAYVPIDPAYPVERIAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 93 IAENSGAKLLLSatavtvtdlpvrivsednlkdiffthkgntpNPEHAVkgdenfYIIYTSGSTGNPKGVQITYNCLVSF 172
Cdd:cd17643 79 ILADSGPSLLLT-------------------------------DPDDLA------YVIYTSGSTGRPKGVVVSHANVLAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 173 TKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSfAEMCLME 252
Cdd:cd17643 122 FAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPS-AFYQLVE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 253 ASFSENM-LPNMKTFLFCGEVLPNEVARKLIERF--PKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVGYCKSDCR 329
Cdd:cd17643 201 AADRDGRdPLALRYVIFGGEALEAAMLRPWAGRFglDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 330 LLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT----MIDGERAYKTGD-AGYVENGLLFYNGRLDFQIKL 404
Cdd:cd17643 281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVanpfGGPGSRMYRTGDlARRLPDGELEYLGRADEQVKI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 405 HGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEhsfEKEFkLTSAIKKELNERLPNYMIPRKFMYQSS 484
Cdd:cd17643 361 RGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADD---GAAA-DIAELRALLKELLPDYMVPARYVPLDA 436
|
490
....*....|....
gi 446693156 485 IPMTPNGKVDRKKL 498
Cdd:cd17643 437 LPLTVNGKLDRAAL 450
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
5-498 |
4.48e-88 |
|
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: 277.78 E-value: 4.48e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 5 EQIEKwaaeTPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLS 84
Cdd:cd17644 8 EQVER----TPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 85 IPADRVQRIAENSGAKLLLSatavtvtdlpvrivsednlkdiffthkgntpNPEHAVkgdenfYIIYTSGSTGNPKGVQI 164
Cdd:cd17644 84 YPQERLTYILEDAQISVLLT-------------------------------QPENLA------YVIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 165 TYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPS 244
Cdd:cd17644 127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 245 FAEMCLMEASFSENMLPN-MKTFLFCGE-VLPNEVA--RKLIERFPkaTIMNTYGPTEATVAVTGIHVTEEVLDQYKSLP 320
Cdd:cd17644 207 YWHLLVLELLLSTIDLPSsLRLVIVGGEaVQPELVRqwQKNVGNFI--QLINVYGPTEATIAATVCRLTQLTERNITSVP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 321 VGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELT-EK----AFTMIDGERAYKTGD-AGYVENGLLFY 394
Cdd:cd17644 285 IGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTaEKfishPFNSSESERLYKTGDlARYLPDGNIEY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 395 NGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPgeHSfeKEFKLTSAIKKELNERLPNYM 474
Cdd:cd17644 365 LGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVP--HY--EESPSTVELRQFLKAKLPDYM 440
|
490 500
....*....|....*....|....
gi 446693156 475 IPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd17644 441 IPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
7-498 |
9.84e-88 |
|
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: 276.11 E-value: 9.84e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVYGhmQPEMIINFLGCVKAGHAYIPVDLS 84
Cdd:cd17653 3 FERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLgvVPGDVVPLLSDR--SLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 85 IPADRVQRIAENSGAKLLLSATAvtvtdlpvrivsednlkdiffthkgntpnpehavkGDENFYIIYTSGSTGNPKGVQI 164
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTTDS-----------------------------------PDDLAYIIFTSGSTGIPKGVMV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 165 TYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLwaidkdMIARPKDLFASLEQSdIQVWTSTPS 244
Cdd:cd17653 126 PHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTL------VLADPSDPFAHVART-VDALMSTPS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 245 FAEMClmeasfSENMLPNMKTFLFCGEVLPNEVARKLIERfpkATIMNTYGPTEATVAVTgihvTEEVLDQyKSLPVGYC 324
Cdd:cd17653 199 ILSTL------SPQDFPNLKTIFLGGEAVPPSLLDRWSPG---RRLYNAYGPTECTISST----MTELLPG-QPVTIGKP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 325 --KSDCRLLimKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMI---DGERAYKTGDAGY-VENGLLFYNGRL 398
Cdd:cd17653 265 ipNSTCYIL--DADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDpfwPGSRMYRTGDYGRwTEDGGLEFLGRE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 399 DFQIKLHGYRMELEEIEHH-LRACSYVEGAVIVPIKkgekyDYLLAVVVPgehsfekEFKLTSAIKKELNERLPNYMIPR 477
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEVvLQSQPEVTQAAAIVVN-----GRLVAFVTP-------ETVDVDGLRSELAKHLPSYAVPD 410
|
490 500
....*....|....*....|.
gi 446693156 478 KFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd17653 411 RIIALDSFPLTANGKVDRKAL 431
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-498 |
2.31e-87 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 293.99 E-value: 2.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVygHMQPEMIINFLGCVKAGHAYIPVDLS 84
Cdd:PRK12467 518 IEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAgvGPDVLVGIAV--ERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 85 IPADRVQRIAENSGAKLLLSATAV-TVTDLP--VRIVSEDNLKDIFFTHKGNtpNPEHAVKGDENFYIIYTSGSTGNPKG 161
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLlAQLPVPagLRSLCLDEPADLLCGYSGH--NPEVALDPDNLAYVIYTSGSTGQPKG 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 162 VQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTS 241
Cdd:PRK12467 674 VAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKI 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 242 TPSFAEMcLMEASFSENMLPnMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSlPV 321
Cdd:PRK12467 754 VPSHLQA-LLQASRVALPRP-QRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFGNV-PI 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 322 GYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTM----IDGERAYKTGD-AGYVENGLLFYNG 396
Cdd:PRK12467 831 GQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPdpfgADGGRLYRTGDlARYRADGVIEYLG 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 397 RLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIkKGEKYDYLLAVVVP------GEHSfekefKLTSAIKKELNERL 470
Cdd:PRK12467 911 RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ-PGDAGLQLVAYLVPaavadgAEHQ-----ATRDELKAQLRQVL 984
|
490 500
....*....|....*....|....*...
gi 446693156 471 PNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK12467 985 PDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-498 |
1.79e-85 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 288.60 E-value: 1.79e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWI--SSEYPDDRSPIMVYGHMqpEMIINFLGCVKAGHAYIPVDLS 84
Cdd:PRK12467 1580 IEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLiaLGVGPEVLVGIAVERSL--EMVVGLLAILKAGGAYVPLDPE 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 85 IPADRVQRIAENSGAKLLLSATAVtVTDLP----VRIVSEDNLKDIFFTHkgNTPNPEHAVKGDENFYIIYTSGSTGNPK 160
Cdd:PRK12467 1658 YPRERLAYMIEDSGIELLLTQSHL-QARLPlpdgLRSLVLDQEDDWLEGY--SDSNPAVNLAPQNLAYVIYTSGSTGRPK 1734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 161 GVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLwAIDKDMIAR-PKDLFASLEQSDIQVW 239
Cdd:PRK12467 1735 GAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARL-VIAPPGAHRdPEQLIQLIERQQVTTL 1813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 240 TSTPSFAEMcLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSL 319
Cdd:PRK12467 1814 HFVPSMLQQ-LLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDSV 1892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 320 PVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTM----IDGERAYKTGD-AGYVENGLLFY 394
Cdd:PRK12467 1893 PIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVAdpfgTVGSRLYRTGDlARYRADGVIEY 1972
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 395 NGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPiKKGEKYDYLLAVVVPGEHSF----EKEFKLTSAIKKELNERL 470
Cdd:PRK12467 1973 LGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYVVPTDPGLvdddEAQVALRAILKNHLKASL 2051
|
490 500
....*....|....*....|....*...
gi 446693156 471 PNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK12467 2052 PEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
3-498 |
4.16e-85 |
|
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: 269.57 E-value: 4.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVD 82
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 83 LSIPADRVQRIAENSGAKLLLsataVTVTDLPvrivsednlkdiffthkgntpnpehavkgdenfYIIYTSGSTGNPKGV 162
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVL----TDPDDLA---------------------------------YVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 163 QITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMiarpkDLFASLEQSDIQVWTST 242
Cdd:cd12115 124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVL-----ALPDLPAAAEVTLINTV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 243 PSfaemcLMEASFSENMLP-NMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQyksLPV 321
Cdd:cd12115 199 PS-----AAAELLRHDALPaSVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGE---VSI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 322 GYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMI---DGERAYKTGD-AGYVENGLLFYNGR 397
Cdd:cd12115 271 GRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDpfgPGARLYRTGDlVRWRPDGLLEFLGR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 398 LDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVV--PGEHSfekefkLTSAIKKELNERLPNYMI 475
Cdd:cd12115 351 ADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVaePGAAG------LVEDLRRHLGTRLPAYMV 424
|
490 500
....*....|....*....|...
gi 446693156 476 PRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd12115 425 PSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
15-498 |
1.18e-84 |
|
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: 268.47 E-value: 1.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 15 PDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVygHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQR 92
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALgvGPEVRVGIAL--ERSLEMVVALLAILKAGGAYVPLDPEYPAERLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 93 IAENSGAKLLLSATavtvtdlpvrivsednlkdiffthkgntpnPEHAVkgdenfYIIYTSGSTGNPKGVQITYNCLVSF 172
Cdd:cd17649 79 MLEDSGAGLLLTHH------------------------------PRQLA------YVIYTSGSTGTPKGVAVSHGPLAAH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 173 TKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEMCLME 252
Cdd:cd17649 123 CQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 253 A-SFSENMLPNMKTFLFCGEVLPNEVARKLieRFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVGYCKSDCRLL 331
Cdd:cd17649 203 AdRTGDGRPPSLRLYIFGGEALSPELLRRW--LKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 332 IMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT----MIDGERAYKTGD-AGYVENGLLFYNGRLDFQIKLHG 406
Cdd:cd17649 281 ILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVpdpfGAPGSRLYRTGDlARWRDDGVIEYLGRVDHQVKIRG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 407 YRMELEEIEHHLRACSYV-EGAVIVPIKKGEKydYLLAVVVPGEHSFEKEfkLTSAIKKELNERLPNYMIPRKFMYQSSI 485
Cdd:cd17649 361 FRIELGEIEAALLEHPGVrEAAVVALDGAGGK--QLVAYVVLRAAAAQPE--LRAQLRTALRASLPDYMVPAHLVFLARL 436
|
490
....*....|...
gi 446693156 486 PMTPNGKVDRKKL 498
Cdd:cd17649 437 PLTPNGKLDRKAL 449
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
14-498 |
2.35e-83 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 266.26 E-value: 2.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 14 TPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRI 93
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 94 AENSGAKLLLsaTAVTVTDLPVRIVSEDNLKDIFFTHkGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFT 173
Cdd:cd17656 81 MLDSGVRVVL--TQRHLKSKLSFNKSTILLEDPSISQ-EDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 174 KWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEMCLMEA 253
Cdd:cd17656 158 HFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 254 SFSENMLPNMKTFLFCGE--VLPNEVARKLIERfpKATIMNTYGPTEATVaVTGIHVTEEvlDQYKSL-PVGYCKSDCRL 330
Cdd:cd17656 238 EFINRFPTCVKHIITAGEqlVITNEFKEMLHEH--NVHLHNHYGPSETHV-VTTYTINPE--AEIPELpPIGKPISNTWI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 331 LIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT---MIDGERAYKTGD-AGYVENGLLFYNGRLDFQIKLHG 406
Cdd:cd17656 313 YILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFpdpFDPNERMYRTGDlARYLPDGNIEFLGRADHQVKIRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 407 YRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPgehsfekEFKLT-SAIKKELNERLPNYMIPRKFMYQSSI 485
Cdd:cd17656 393 YRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM-------EQELNiSQLREYLAKQLPEYMIPSFFVPLDQL 465
|
490
....*....|...
gi 446693156 486 PMTPNGKVDRKKL 498
Cdd:cd17656 466 PLTPNGKVDRKAL 478
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
15-498 |
3.31e-83 |
|
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: 265.67 E-value: 3.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 15 PDQTAFVWRDAKITYKQLKEDSDALAHWI--SSEYPDDRSPIMvyGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQR 92
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALkaAGVRPGDLVAVT--LPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 93 IAENSGAKLLLSATAVTVTDLPVRIVSEDNLKDIffthKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQIT----YNC 168
Cdd:cd12114 79 ILADAGARLVLTDGPDAQLDVAVFDVLILDLDAL----AAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMIShraaLNT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 169 LVSFTkwavEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEM 248
Cdd:cd12114 155 ILDIN----RRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 249 CLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTgIHVTEEVLDQYKSLPVGYCKSDC 328
Cdd:cd12114 231 LLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSI-YHPIDEVPPDWRSIPYGRPLANQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 329 RLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAF-TMIDGERAYKTGDAG-YVENGLLFYNGRLDFQIKLHG 406
Cdd:cd12114 310 RYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvTHPDGERLYRTGDLGrYRPDGTLEFLGRRDGQVKVRG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 407 YRMELEEIEHHLRACSYVEGAVIVPIkkGEKYD-YLLAVVVPGEhsfEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSI 485
Cdd:cd12114 390 YRIELGEIEAALQAHPGVARAVVVVL--GDPGGkRLAAFVVPDN---DGTPIAPDALRAFLAQTLPAYMIPSRVIALEAL 464
|
490
....*....|...
gi 446693156 486 PMTPNGKVDRKKL 498
Cdd:cd12114 465 PLTANGKVDRAAL 477
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
8-498 |
1.25e-82 |
|
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: 262.88 E-value: 1.25e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 8 EKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMvyghMQP--EMIINFLGCVKAGHAYIPVDL 83
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKgvKPDDQVGIM----LDKslDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 84 SIPADRVQRIAENSGAKLLLSatavtvtdlpvrivsednlkdiffthkgntpNPEHAVkgdenfYIIYTSGSTGNPKGVQ 163
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLT-------------------------------NPDDLA------YVIYTSGSTGLPKGVM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 164 ITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDM---IARPKDLFaslEQSDIqvwt 240
Cdd:cd17645 124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERrldLDALNDYF---NQEGI---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 241 sTPSFAEMCLMEaSFSENMLPNMKTFLFCGEVLpnevarKLIERFPkATIMNTYGPTEATVAVTGIHVTEEvldqYKSLP 320
Cdd:cd17645 197 -TISFLPTGAAE-QFMQLDNQSLRVLLTGGDKL------KKIERKG-YKLVNNYGPTENTVVATSFEIDKP----YANIP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 321 VGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT---MIDGERAYKTGD-AGYVENGLLFYNG 396
Cdd:cd17645 264 IGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIvhpFVPGERMYRTGDlAKFLPDGNIEFLG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 397 RLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPgehsfEKEFKLtSAIKKELNERLPNYMIP 476
Cdd:cd17645 344 RLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA-----PEEIPH-EELREWLKNDLPDYMIP 417
|
490 500
....*....|....*....|..
gi 446693156 477 RKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd17645 418 TYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-498 |
2.71e-81 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 276.45 E-value: 2.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 5 EQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEY--PDDRSPIMVygHMQPEMIINFLGCVKAGHAYIPVD 82
Cdd:PRK12316 4555 QLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGvgPEVLVGIAM--ERSAEMMVGLLAVLKAGGAYVPLD 4632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 83 LSIPADRVQRIAENSGAKLLLsatavTVTDLPVRIVSEDNLKDIFFTHKGN-----TPNPEHAVKGDENFYIIYTSGSTG 157
Cdd:PRK12316 4633 PEYPRERLAYMMEDSGAALLL-----TQSHLLQRLPIPDGLASLALDRDEDwegfpAHDPAVRLHPDNLAYVIYTSGSTG 4707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 158 NPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLwAIDKDMIARPKDLFASLEQSDIQ 237
Cdd:PRK12316 4708 RPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASV-VIRDDSLWDPERLYAEIHEHRVT 4786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 238 VWTSTPSFAEMCLMEASFSENmLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYK 317
Cdd:PRK12316 4787 VLVFPPVYLQQLAEHAERDGE-PPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAA 4865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 318 SLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTM----IDGERAYKTGD-AGYVENGLL 392
Cdd:PRK12316 4866 YMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPdpfgAPGGRLYRTGDlARYRADGVI 4945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 393 FYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPiKKGEKYDYLLAVVVPGE----HSFEKEFKLTSAIKKELNE 468
Cdd:PRK12316 4946 DYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA-QEGAVGKQLVGYVVPQDpalaDADEAQAELRDELKAALRE 5024
|
490 500 510
....*....|....*....|....*....|
gi 446693156 469 RLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK12316 5025 RLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
15-498 |
1.33e-80 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 258.17 E-value: 1.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 15 PDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIA 94
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 95 ENSGAKLLLSatavtvtdlpvrivsednlkdiffthkgntpNPEHAVkgdenfYIIYTSGSTGNPKGVQITY-NCLVSFT 173
Cdd:cd17650 81 EDSGAKLLLT-------------------------------QPEDLA------YVIYTSGTTGKPKGVMVEHrNVAHAAH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 174 KWAVEdFNLQTGQVFLNQ-APFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAeMCLME 252
Cdd:cd17650 124 AWRRE-YELDSFPVRLLQmASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALI-RPVMA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 253 ASFSENM-LPNMKTFLFCGEVLPNEVARKLIERFPKAT-IMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVGYCKSDCRL 330
Cdd:cd17650 202 YVYRNGLdLSAMRLLIVGSDGCKAQDFKTLAARFGQGMrIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 331 LIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT---MIDGERAYKTGD-AGYVENGLLFYNGRLDFQIKLHG 406
Cdd:cd17650 282 YVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVenpFAPGERMYRTGDlARWRADGNVELLGRVDHQVKIRG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 407 YRMELEEIEHHLRACSYVEGAVIV--PIKKGEKydYLLAVVVPGEhsfekefKL-TSAIKKELNERLPNYMIPRKFMYQS 483
Cdd:cd17650 362 FRIELGEIESQLARHPAIDEAVVAvrEDKGGEA--RLCAYVVAAA-------TLnTAELRAFLAKELPSYMIPSYYVQLD 432
|
490
....*....|....*
gi 446693156 484 SIPMTPNGKVDRKKL 498
Cdd:cd17650 433 ALPLTPNGKVDRRAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-498 |
3.43e-80 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 273.37 E-value: 3.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIP 86
Cdd:PRK12316 517 FEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYP 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 87 ADRVQRIAENSGAKLLLSATAVTVTdLPV----RIVSEDNLKDIFFTHKGNtpNPEHAVKGDENFYIIYTSGSTGNPKGV 162
Cdd:PRK12316 597 AERLAYMLEDSGVQLLLSQSHLGRK-LPLaagvQVLDLDRPAAWLEGYSEE--NPGTELNPENLAYVIYTSGSTGKPKGA 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 163 QITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTST 242
Cdd:PRK12316 674 GNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFV 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 243 PSFAEMCLMEASFSEnmLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDqykSLPVG 322
Cdd:PRK12316 754 PSMLQAFLQDEDVAS--CTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGD---SVPIG 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 323 YCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT---MIDGERAYKTGD-AGYVENGLLFYNGRL 398
Cdd:PRK12316 829 RPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVpspFVAGERMYRTGDlARYRADGVIEYAGRI 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 399 DFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEkydyLLAVVVPGEHSFEkefkLTSAIKKELNERLPNYMIPRK 478
Cdd:PRK12316 909 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQ----LVGYVVLESEGGD----WREALKAHLAASLPEYMVPAQ 980
|
490 500
....*....|....*....|
gi 446693156 479 FMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK12316 981 WLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-498 |
4.33e-78 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 267.21 E-value: 4.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 5 EQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVygHMQPEMIINFLGCVKAGHAYIPVD 82
Cdd:PRK12316 2007 QRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARgvGPEVRVAIAA--ERSFELVVALLAVLKAGGAYVPLD 2084
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 83 LSIPADRVQRIAENSGAKLLLSATAVtVTDLPVrivsEDNLKDIFFTHKGNTP-----NPEHAVKGDENFYIIYTSGSTG 157
Cdd:PRK12316 2085 PNYPAERLAYMLEDSGAALLLTQRHL-LERLPL----PAGVARLPLDRDAEWAdypdtAPAVQLAGENLAYVIYTSGSTG 2159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 158 NPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDkDMIARPKDLFASLEQSDIQ 237
Cdd:PRK12316 2160 LPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRD-DELWDPEQLYDEMERHGVT 2238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 238 VWTSTPSFAEMcLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYK 317
Cdd:PRK12316 2239 ILDFPPVYLQQ-LAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAA 2317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 318 SLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFtMID-----GERAYKTGD-AGYVENGL 391
Cdd:PRK12316 2318 YVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERF-VPDpfsasGERLYRTGDlARYRADGV 2396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 392 LFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIkKGEKYDYLLAVVVPGEHSFEkefkLTSAIKKELNERLP 471
Cdd:PRK12316 2397 VEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAED----LLAELRAWLAARLP 2471
|
490 500
....*....|....*....|....*..
gi 446693156 472 NYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK12316 2472 AYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
15-498 |
2.21e-77 |
|
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: 249.09 E-value: 2.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 15 PDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVYGhmQPEMIINFLGCVKAGHAYIPVDLSIPADRVQR 92
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARgvGPERLVALALPR--SAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 93 IAENSGAKLLLSatavtvtdlpvrivsednlkdiffthkgntpNPEHAVkgdenfYIIYTSGSTGNPKGVQITYNCLVSF 172
Cdd:cd17652 79 MLADARPALLLT-------------------------------TPDNLA------YVIYTSGSTGRPKGVVVTHRGLANL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 173 TKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAemclme 252
Cdd:cd17652 122 AAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAAL------ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 253 ASFSENMLPNMKTFLFCGEVLPNEVARKLIerfPKATIMNTYGPTEATVAVTgihvTEEVLDQYKSLPVGYCKSDCRLLI 332
Cdd:cd17652 196 AALPPDDLPDLRTLVVAGEACPAELVDRWA---PGRRMINAYGPTETTVCAT----MAGPLPGGGVPPIGRPVPGTRVYV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 333 MKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTM----IDGERAYKTGD-AGYVENGLLFYNGRLDFQIKLHGY 407
Cdd:cd17652 269 LDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVAdpfgAPGSRMYRTGDlARWRADGQLEFLGRADDQVKIRGF 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 408 RMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGehsfEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPM 487
Cdd:cd17652 349 RIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPA----PGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPL 424
|
490
....*....|.
gi 446693156 488 TPNGKVDRKKL 498
Cdd:cd17652 425 TPNGKLDRRAL 435
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
5-498 |
7.27e-76 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 260.48 E-value: 7.27e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 5 EQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLS 84
Cdd:PRK12467 3099 QLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPE 3178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 85 IPADRVQRIAENSGAKLLLSaTAVTVTDLPVRIVSEDNLKDIFFTHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQI 164
Cdd:PRK12467 3179 YPRERLAYMIEDSGVKLLLT-QAHLLEQLPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGV 3257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 165 TYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMiARPKDLFASLEQSDIQVWTSTPS 244
Cdd:PRK12467 3258 RHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDL-WDPEELWQAIHAHRISIACFPPA 3336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 245 FAEMCLMEASFSEnmLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVGYC 324
Cdd:PRK12467 3337 YLQQFAEDAGGAD--CASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRP 3414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 325 KSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT----MIDGERAYKTGD-AGYVENGLLFYNGRLD 399
Cdd:PRK12467 3415 VAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVadpfSGSGGRLYRTGDlARYRADGVIEYLGRID 3494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 400 FQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIkKGEKYDYLLAVVVPGEHSFEkefkLTSAIKKELNERLPNYMIPRKF 479
Cdd:PRK12467 3495 HQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGD----WRETLRDHLAASLPDYMVPAQL 3569
|
490
....*....|....*....
gi 446693156 480 MYQSSIPMTPNGKVDRKKL 498
Cdd:PRK12467 3570 LVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-498 |
1.44e-75 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 259.72 E-value: 1.44e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEY--PDDRSPIMVygHMQPEMIINFLGCVKAGHAYIP 80
Cdd:PRK05691 1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGvgPDVCVAIAA--ERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 81 VDLSIPADRVQRIAENSGAKLLLSATAVtVTDLP----VRIVSEDNLkdifftHKGNTPN--PEHAVKGDENFYIIYTSG 154
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLTQSHL-LERLPqaegVSAIALDSL------HLDSWPSqaPGLHLHGDNLAYVIYTSG 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 155 STGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLwaidkdMIARPKD------LF 228
Cdd:PRK05691 1284 STGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRL------VLAGPGEhrdpqrIA 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 229 ASLEQSDIQVWTSTPSfaemcLMEASFSENMLPNMKTF--LFCG-EVLPNEVARKLIERFPKATIMNTYGPTEATVAVTG 305
Cdd:PRK05691 1358 ELVQQYGVTTLHFVPP-----LLQLFIDEPLAAACTSLrrLFSGgEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTH 1432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 306 IHVTEEvlDQYKSlPVGYCKSD--CRLLimKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMI----DGERAY 379
Cdd:PRK05691 1433 WQCQAE--DGERS-PIGRPLGNvlCRVL--DAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDplgeDGARLY 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 380 KTGD-AGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVpIKKGEKYDYLLAVVVpGEHSFEKEfkl 458
Cdd:PRK05691 1508 RTGDrARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYT-GEAGQEAE--- 1582
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446693156 459 TSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK05691 1583 AERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-498 |
5.48e-74 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 255.27 E-value: 5.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIP 86
Cdd:PRK12316 3063 FEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYP 3142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 87 ADRVQRIAENSGAKLLLSATAVTVTDLP-VRIVSEDNLKDIFFTHkgntpNPEHAVKGDENFYIIYTSGSTGNPKGVQIT 165
Cdd:PRK12316 3143 EERLAYMLEDSGAQLLLSQSHLRLPLAQgVQVLDLDRGDENYAEA-----NPAIRTMPENLAYVIYTSGSTGKPKGVGIR 3217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 166 YNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSF 245
Cdd:PRK12316 3218 HSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSM 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 246 AEMCLMEASFSEnmLPNMKTFLFCGEVLPNEVARKLIERFPkatIMNTYGPTEATVAVTGIHVTEEVLDQyksLPVGYCK 325
Cdd:PRK12316 3298 LQAFLEEEDAHR--CTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTHWQCVEEGKDA---VPIGRPI 3369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 326 SDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT---MIDGERAYKTGD-AGYVENGLLFYNGRLDFQ 401
Cdd:PRK12316 3370 ANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVpdpFVPGERLYRTGDlARYRADGVIEYIGRVDHQ 3449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 402 IKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKgekyDYLLAVVVPGehsfEKEFKLTSAIKKELNERLPNYMIPRKFMY 481
Cdd:PRK12316 3450 VKIRGFRIELGEIEARLLEHPWVREAVVLAVDG----RQLVAYVVPE----DEAGDLREALKAHLKASLPEYMVPAHLLF 3521
|
490
....*....|....*..
gi 446693156 482 QSSIPMTPNGKVDRKKL 498
Cdd:PRK12316 3522 LERMPLTPNGKLDRKAL 3538
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
3-498 |
2.09e-68 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 238.41 E-value: 2.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVyghmqP---EMIINFLGCVKAGHA 77
Cdd:PRK10252 460 LSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERgvKPGDSVAVAL-----PrsvFLTLALHAIVEAGAA 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 78 YIPVDLSIPADRVQRIAENSGAKLLLSATAV--TVTDLPvrivsednlKDIFFTHKGNTPNPEHAVKG----DENFYIIY 151
Cdd:PRK10252 535 WLPLDTGYPDDRLKMMLEDARPSLLITTADQlpRFADVP---------DLTSLCYNAPLAPQGAAPLQlsqpHHTAYIIF 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 152 TSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLwaidkdMIARP---KDLF 228
Cdd:PRK10252 606 TSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKL------VMAEPeahRDPL 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 229 AsLEQ--SDIQVWTS--TPSfaemclMEASF-----SENMLPNMKTF--LFC-GEVLPNEVARKLiERFPKATIMNTYGP 296
Cdd:PRK10252 680 A-MQQffAEYGVTTThfVPS------MLAAFvasltPEGARQSCASLrqVFCsGEALPADLCREW-QQLTGAPLHNLYGP 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 297 TEATVAVTGIHVTEEVLDQYK--SLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT--- 371
Cdd:PRK10252 752 TEAAVDVSWYPAFGEELAAVRgsSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadp 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 372 MIDGERAYKTGD-AGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPI------KKGEKYDYLLAV 444
Cdd:PRK10252 832 FAPGERMYRTGDvARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGY 911
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446693156 445 VVPGehsfEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK10252 912 LVSQ----SGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
15-498 |
6.51e-67 |
|
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: 222.28 E-value: 6.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 15 PDQTAFVWRDAKITYKQLKEDSDALAHWISSE---YPDDRSPIMVygHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQ 91
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVaeiRPDDLVGLVL--DKSELMIIAILAVWKAGAAYVPIDPSYPDERIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 92 RIAENSGAKLLLSatavTVTDLPvrivsednlkdiffthkgntpnpehavkgdenfYIIYTSGSTGNPKGVQITYNCLVS 171
Cdd:cd17648 79 FILEDTGARVVIT----NSTDLA---------------------------------YAIYTSGTTGKPKGVLVEHGSVVN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 172 FTKWAVEDFNLQT--GQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEMc 249
Cdd:cd17648 122 LRTSLSERYFGRDngDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQ- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 250 lmeasFSENMLPNMKTFLFCGEVLPNEVARKLIERFPkATIMNTYGPTEATVAVtgiHVTEEVLDQYKSLPVGYCKSDCR 329
Cdd:cd17648 201 -----YDLARLPHLKRVDAAGEEFTAPVFEKLRSRFA-GLIINAYGPTETTVTN---HKRFFPGDQRFDKSLGRPVRNTK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 330 LLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT----MIDGERA-------YKTGD-AGYVENGLLFYNGR 397
Cdd:cd17648 272 CYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLpnpfQTEQERArgrnarlYKTGDlVRWLPSGELEYLGR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 398 LDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPiKKGEKY------DYLLAVVVPGEHSFEKefkltSAIKKELNERLP 471
Cdd:cd17648 352 NDFQVKIRGQRIEPGEVEAALASYPGVRECAVVA-KEDASQaqsriqKYLVGYYLPEPGHVPE-----SDLLSFLRAKLP 425
|
490 500
....*....|....*....|....*..
gi 446693156 472 NYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd17648 426 RYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
148-494 |
1.06e-64 |
|
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: 1.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 148 YIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDmiaRPKDL 227
Cdd:cd04433 4 LILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 228 FASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEATVAVTGIH 307
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAP-GIKLVNGYGLTETGGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 308 VTEevlDQYKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFtmIDGerAYKTGDAGYV 387
Cdd:cd04433 160 PDD---DARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--EDG--WYRTGDLGRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 388 -ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEhsfekEFKLTSA-IKKE 465
Cdd:cd04433 233 dEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEeLRAH 307
|
330 340
....*....|....*....|....*....
gi 446693156 466 LNERLPNYMIPRKFMYQSSIPMTPNGKVD 494
Cdd:cd04433 308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-498 |
4.79e-63 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 223.12 E-value: 4.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 4 LEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDL 83
Cdd:PRK05691 3723 VRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDP 3802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 84 SIPADRVQRIAENSGAKLLLSATA-----------VTVTDLPVRIVSEDNLKDIFFTHkgntpNPEHAVKGDENFYIIYT 152
Cdd:PRK05691 3803 GLPAQRLQRIIELSRTPVLVCSAAcreqaralldeLGCANRPRLLVWEEVQAGEVASH-----NPGIYSGPDNLAYVIYT 3877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 153 SGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLE 232
Cdd:PRK05691 3878 SGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQ 3957
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 233 QSDIQVWTSTPSFAEMCLMEasfSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEV 312
Cdd:PRK05691 3958 AQGITVLESVPSLIQGMLAE---DRQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLAS 4034
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 313 lDQYKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT----MIDGERAYKTGD-AGYV 387
Cdd:PRK05691 4035 -TRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVphpfGAPGERLYRTGDlARRR 4113
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 388 ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV-EGAVIVpiKKGEKYDYLLAVVVPGEhSFEKEFKLTSAIKKEL 466
Cdd:PRK05691 4114 SDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVrEAAVAV--QEGVNGKHLVGYLVPHQ-TVLAQGALLERIKQRL 4190
|
490 500 510
....*....|....*....|....*....|..
gi 446693156 467 NERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK05691 4191 RAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
7-501 |
2.94e-57 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 198.47 E-value: 2.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIP 86
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 87 ADRVQRIAENSGAKLLLSA---------TAVTVTDLPVRIVSEDNLKDIFFTHKGN-----------TPNPEHAVKGDEN 146
Cdd:TIGR03098 86 AEQVAHILADCNVRLLVTSserldllhpALPGCHDLRTLIIVGDPAHASEGHPGEEpaswpkllalgDADPPHPVIDSDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 147 FYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMiarPKD 226
Cdd:TIGR03098 166 AAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLL---PRD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 227 LFASLEQSDIQVWTSTPS-FAEmcLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTg 305
Cdd:TIGR03098 243 VLKALEKHGITGLAAVPPlWAQ--LAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEAFRSTY- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 306 ihVTEEVLDQyKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMIDG--------ER 377
Cdd:TIGR03098 320 --LPPEEVDR-RPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPfpgelhlpEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 378 AYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEH-SFEKE 455
Cdd:TIGR03098 397 AVWSGDTVRRdEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGeELDRA 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446693156 456 fkltsAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSE 501
Cdd:TIGR03098 477 -----ALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAKE 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
11-495 |
2.24e-51 |
|
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: 180.50 E-value: 2.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPAD 88
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALgvAKGDR--VAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 89 RVQRIAENSGAKLLLsatavtvtdlpvrivsednlkdiffthkgntpnpehavkgDENFYIIYTSGSTGNPKGVQITYNC 168
Cdd:cd17631 83 EVAYILADSGAKVLF----------------------------------------DDLALLMYTSGTTGRPKGAMLTHRN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 169 LVSFTKWAVEDFNLQTGQVFLNQAP-FSFDLSVMDIYPSLVTGGTLwaidkdMIAR---PKDLFASLEQSDIQVWTSTPS 244
Cdd:cd17631 123 LLWNAVNALAALDLGPDDVLLVVAPlFHIGGLGVFTLPTLLRGGTV------VILRkfdPETVLDLIERHRVTSFFLVPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 245 FAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKatIMNTYGPTEATVAVTGIhVTEEVLDqyKSLPVGYC 324
Cdd:cd17631 197 MIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVK--FVQGYGMTETSPGVTFL-SPEDHRR--KLGSAGRP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 325 KSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmiDGerAYKTGDAGYV-ENGLLFYNGRLDFQIK 403
Cdd:cd17631 272 VFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR--DG--WFHTGDLGRLdEDGYLYIVDRKKDMII 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 404 LHG---YRMELEEIEHHLRACsyVEGAVI-VPIKK-GEKydyLLAVVVPGEHSFEKEfkltSAIKKELNERLPNYMIPRK 478
Cdd:cd17631 348 SGGenvYPAEVEDVLYEHPAV--AEVAVIgVPDEKwGEA---VVAVVVPRPGAELDE----DELIAHCRERLARYKIPKS 418
|
490
....*....|....*..
gi 446693156 479 FMYQSSIPMTPNGKVDR 495
Cdd:cd17631 419 VEFVDALPRNATGKILK 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
11-498 |
7.18e-51 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 187.30 E-value: 7.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRV 90
Cdd:PRK05691 2198 AARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERL 2277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 91 QRIAENSGAKLLLSATAV--TVTDLPV---RIVSEDNLKDIFFTHKGNTPN---PEHAVkgdenfYIIYTSGSTGNPKGV 162
Cdd:PRK05691 2278 HYMIEDSGIGLLLSDRALfeALGELPAgvaRWCLEDDAAALAAYSDAPLPFlslPQHQA------YLIYTSGSTGKPKGV 2351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 163 QITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTL-------WAIDkdmiarpkDLFASLEQSD 235
Cdd:PRK05691 2352 VVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVvlraqgqWGAE--------EICQLIREQQ 2423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 236 IQVWTSTPSFAEMCLMEASFSENMLPnMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQ 315
Cdd:PRK05691 2424 VSILGFTPSYGSQLAQWLAGQGEQLP-VRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQLEEG 2502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 316 YKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT----MIDGERAYKTGD-AGYVENG 390
Cdd:PRK05691 2503 AASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVadpfAADGGRLYRTGDlVRLRADG 2582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 391 LLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIK-KGEKY--DYLLAVVVpgEHSFEKEFKLTSAIKKELN 467
Cdd:PRK05691 2583 LVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDtPSGKQlaGYLVSAVA--GQDDEAQAALREALKAHLK 2660
|
490 500 510
....*....|....*....|....*....|.
gi 446693156 468 ERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK05691 2661 QQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
7-498 |
4.80e-48 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 174.53 E-value: 4.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRDA-----KITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYI 79
Cdd:COG0365 15 LDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALgvKKGDR--VAIYLPNIPEAVIAMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 80 PV--DLSiPADRVQRIaENSGAKLLLSATAVtvtdlpVRIVSEDNLKDIFFTHKGNTPNPEH-----------AVKGDEN 146
Cdd:COG0365 93 PVfpGFG-AEALADRI-EDAEAKVLITADGG------LRGGKVIDLKEKVDEALEELPSLEHvivvgrtgadvPMEGDLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 147 F----------------------YIIYTSGSTGNPKGVQIT---YncLVSFTKWAVEDFNLQTGQVFLNQAPFSFdlsVM 201
Cdd:COG0365 165 WdellaaasaefepeptdaddplFILYTSGTTGKPKGVVHThggY--LVHAATTAKYVLDLKPGDVFWCTADIGW---AT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 202 D----IYPSLVTGGTLWAID-KDMIARPKDLFASLEQSDIQVWTSTPSFAEMCL-MEASFSENM-LPNMKTFLFCGEVLP 274
Cdd:COG0365 240 GhsyiVYGPLLNGATVVLYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMkAGDEPLKKYdLSSLRLLGSAGEPLN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 275 NEVARKLIERFpKATIMNTYGPTEATVAVTGIHVTEEVldqyK----SLPV-GYcksDCRLLimKEDGTIAPDGEKGEIV 349
Cdd:COG0365 320 PEVWEWWYEAV-GVPIVDGWGQTETGGIFISNLPGLPV----KpgsmGKPVpGY---DVAVV--DEDGNPVPPGEEGELV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 350 IVGPSVS--VGYLGSPELTEKA-FTMIDGerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRM---ELEE--IEHHLRA 420
Cdd:COG0365 390 IKGPWPGmfRGYWNDPERYRETyFGRFPG--WYRTGDGARRdEDGYFWILGRSDDVINVSGHRIgtaEIESalVSHPAVA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 421 csyvEGAVI-VPI-KKGEKydyLLAVVVPgehsfEKEFKLTSAIKKELN----ERLPNYMIPRKFMYQSSIPMTPNGKVD 494
Cdd:COG0365 468 ----EAAVVgVPDeIRGQV---VKAFVVL-----KPGVEPSDELAKELQahvrEELGPYAYPREIEFVDELPKTRSGKIM 535
|
....
gi 446693156 495 RKKL 498
Cdd:COG0365 536 RRLL 539
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
3-498 |
1.15e-46 |
|
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: 168.90 E-value: 1.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWI--SSEYPDDRSPIMVYGhmQPEMIINFLGCVKAGHAYIP 80
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLqnLGVQPGDRVALMLPN--CPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 81 VDLSIPADRVQRIAENSGAKLLLsaTAVTVTDLpvrivsednlkdiffTHKGNTPNPEHAVKGDENFYIIYTSGSTGNPK 160
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALI--VAVSFTDL---------------LAAGAPLGERVALTPEDVAVLQYTSGTTGVPK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 161 GVQITYNCLVS--FTKWAVEDFNLQTGQVFLNQAPF--SFDLSVMDIYPsLVTGGTLWAIDKdmiARPKDLFASLEQSDI 236
Cdd:cd05936 142 GAMLTHRNLVAnaLQIKAWLEDLLEGDDVVLAALPLfhVFGLTVALLLP-LALGATIVLIPR---FRPIGVLKEIRKHRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 237 QVWTSTPS-FAEMCLMEAsFSENMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEATVAVTGIHVTEEvldq 315
Cdd:cd05936 218 TIFPGVPTmYIALLNAPE-FKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVAVNPLDGP---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 316 YKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmiDGerAYKTGDAGYV-ENGLLFY 394
Cdd:cd05936 292 RKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV--DG--WLRTGDIGYMdEDGYFFI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 395 NGRLDFQIKLHGYRM---ELEEIEHHLRAcsyVEGAVIVPIKKGEKYDYLLAVVVPGE-HSFEKEfkltsAIKKELNERL 470
Cdd:cd05936 368 VDRKKDMIIVGGFNVyprEVEEVLYEHPA---VAEAAVVGVPDPYSGEAVKAFVVLKEgASLTEE-----EIIAFCREQL 439
|
490 500
....*....|....*....|....*...
gi 446693156 471 PNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05936 440 AGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
78-499 |
1.07e-45 |
|
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: 166.08 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 78 YIPVDLSIPADRVQRIAENSGAKLLLSAT--------AVTVTDLPVRIVSEDNLKDiffthkGNTPNPEHAVKGDENFYI 149
Cdd:cd05922 49 FVPLNPTLKESVLRYLVADAGGRIVLADAgaadrlrdALPASPDPGTVLDADGIRA------ARASAPAHEVSHEDLALL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 150 IYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFD--LSVMDIypSLVTGGTLwAIDKDMIArPKDL 227
Cdd:cd05922 123 LYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDygLSVLNT--HLLRGATL-VLTNDGVL-DDAF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 228 FASLEQSDIQVWTSTPSFAEMcLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTgIH 307
Cdd:cd05922 199 WEDLREHGATGLAGVPSTYAM-LTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMT-YL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 308 VTEEVLDQYKSlpVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMIDgerAYKTGDAGYV 387
Cdd:cd05922 277 PPERILEKPGS--IGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGG---VLHTGDLARR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 388 -ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIV--PIKKGEKydylLAVVVPGEHSFEkefklTSAIKK 464
Cdd:cd05922 352 dEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVglPDPLGEK----LALFVTAPDKID-----PKDVLR 422
|
410 420 430
....*....|....*....|....*....|....*
gi 446693156 465 ELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLL 499
Cdd:cd05922 423 SLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
24-498 |
1.24e-43 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 159.95 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 24 DAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKlll 103
Cdd:cd17654 14 DTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVS--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 104 satavtvtdlpvRIVSEDNLKDIFfthKGNTPNPEH-AVKGDENF-YIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFN 181
Cdd:cd17654 91 ------------YLLQNKELDNAP---LSFTPEHRHfNIRTDECLaYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 182 LQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSD-IQVWTSTPSFAEMCLMEASFSENM- 259
Cdd:cd17654 156 ITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRHrITVLQATPTLFRRFGSQSIKSTVLs 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 260 -LPNMKTFLFCGEVLP-NEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEvldqykSLPVGYCKSDCRLLIMKEDG 337
Cdd:cd17654 236 aTSSLRVLALGGEPFPsLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEE------DSPVQLGSPLLGTVIEVRDQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 338 TiapdGEKGEIVIVGPSVSVGYLGSPELTEKAFTMidgeraYKTGDAGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHH 417
Cdd:cd17654 310 N----GSEGTGQVFLGGLNRVCILDDEVTVPKGTM------RATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 418 LRACSYVEgAVIVPIKKGEKydyLLAVVVPGEHSfekefkltSAIKKELN-ERLPNYMIPRKFMYQSSIPMTPNGKVDRK 496
Cdd:cd17654 380 IESCLGVE-SCAVTLSDQQR---LIAFIVGESSS--------SRIHKELQlTLLSSHAIPDTFVQIDKLPLTSHGKVDKS 447
|
..
gi 446693156 497 KL 498
Cdd:cd17654 448 EL 449
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
7-498 |
7.81e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 151.11 E-value: 7.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDLS 84
Cdd:PRK06187 12 LRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALgvKKGDR--VAVFDWNSHEYLEAYFAVPKIGAVLHPINIR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 85 IPADRVQRIAENSGAKLLL------------------SATAVTVTDLPVRIVSEDNLKdiFFTHKGNTPNPEHAVKGDEN 146
Cdd:PRK06187 90 LKPEEIAYILNDAEDRVVLvdsefvpllaailpqlptVRTVIVEGDGPAAPLAPEVGE--YEELLAAASDTFDFPDIDEN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 147 --FYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAP-F-SFDLSVMdiYPSLVTGGTLwaidkdMIA 222
Cdd:PRK06187 168 daAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPmFhVHAWGLP--YLALMAGAKQ------VIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 223 R---PKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEA 299
Cdd:PRK06187 240 RrfdPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTET 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 300 TVAVTGIHVTEEVLDQY-------KSLPvGYcksdcRLLIMKEDGTIAP--DGEKGEIVIVGPSVSVGYLGSPELTEKaf 370
Cdd:PRK06187 319 SPVVSVLPPEDQLPGQWtkrrsagRPLP-GV-----EARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAE-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 371 TMIDGerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHG---YRMELEEIEHHLRACsyVEGAVI-VPIKK-GEKydyLLAV 444
Cdd:PRK06187 391 TIDGG--WLHTGDVGYIdEDGYLYITDRIKDVIISGGeniYPRELEDALYGHPAV--AEVAVIgVPDEKwGER---PVAV 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446693156 445 VV--PGEHSFEKEfkltsaIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK06187 464 VVlkPGATLDAKE------LRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
26-493 |
1.27e-39 |
|
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: 149.67 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 26 KITYKQLKEDSDALAHWISSEY--PDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKLLL 103
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGlkKGDV--VGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 104 SATA------------------VTVTDLPVRIVSEDNLKDIFFTHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQIT 165
Cdd:cd05911 88 TDPDglekvkeaakelgpkdkiIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 166 -YNCLVSFTK-WAVEDFNLQTGQVFLNQAPF--SFDLSVMDIypSLVTGGTLWAIDK-DMIarpkDLFASLEQSDIQVWT 240
Cdd:cd05911 168 hRNLIANLSQvQTFLYGNDGSNDVILGFLPLyhIYGLFTTLA--SLLNGATVIIMPKfDSE----LFLDLIEKYKITFLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 241 STPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTgihVTEEVLDQYKSlp 320
Cdd:cd05911 242 LVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILT---VNPDGDDKPGS-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 321 VGYCKSDCRLLIMKEDG-TIAPDGEKGEIVIVGPSVSVGYLGSPELTEKaftMIDGERAYKTGDAGYV-ENGLLFYNGRL 398
Cdd:cd05911 317 VGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKE---TFDEDGWLHTGDIGYFdEDGYLYIVDRK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 399 DFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVV--PGEHSFEKEfkltsaIKKELNERLPNYmip 476
Cdd:cd05911 394 KELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVrkPGEKLTEKE------VKDYVAKKVASY--- 464
|
490 500
....*....|....*....|....*
gi 446693156 477 rkfmYQ--------SSIPMTPNGKV 493
Cdd:cd05911 465 ----KQlrggvvfvDEIPKSASGKI 485
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
15-498 |
6.75e-38 |
|
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: 145.15 E-value: 6.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 15 PDQTAFV--WRDAKITYKQLKEDSDALAHWISSE--YPDDR-SPIMVYGhmqPEMIINFLGCVKAGHAYIPVDLSIPADR 89
Cdd:cd05926 1 PDAPALVvpGSTPALTYADLAELVDDLARQLAALgiKKGDRvAIALPNG---LEFVVAFLAAARAGAVVAPLNPAYKKAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 90 VQRIAENSGAKLLL-----------SATAVTVT------DLPVRIVSEDNLKDIFFTHKGNTPNPEHAVKGDENFYIIYT 152
Cdd:cd05926 78 FEFYLADLGSKLVLtpkgelgpasrAASKLGLAilelalDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDLALILHT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 153 SGSTGNPKGVQITYNCLVSFTKwavedfNLQTGqvfLNQAPFSFDLSVMDIY----------PSLVTGGTLWaidkdMIA 222
Cdd:cd05926 158 SGTTGRPKGVPLTHRNLAASAT------NITNT---YKLTPDDRTLVVMPLFhvhglvasllSTLAAGGSVV-----LPP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 223 R--PKDLFASLEQSDIQVWTSTPSFAEMCLM-EASFSENMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEA 299
Cdd:cd05926 224 RfsASTFWPDVRDYNATWYTAVPTIHQILLNrPEPNPESPPPKLRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 300 TVAVTGIHVTEEVlDQYKS--LPVGycksdCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmidGER 377
Cdd:cd05926 303 AHQMTSNPLPPGP-RKPGSvgKPVG-----VEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAF---KDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 378 AYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKgEKYDYLL-AVVVPGehsfEKE 455
Cdd:cd05926 374 WFRTGDLGYLdADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPD-EKYGEEVaAAVVLR----EGA 448
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446693156 456 FKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05926 449 SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
21-498 |
9.61e-38 |
|
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: 143.89 E-value: 9.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 21 VWRDakITYKQLKEDSDALAHWISSE--YPDDRSPIMvyGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSG 98
Cdd:cd05907 2 VWQP--ITWAEFAEEVRALAKGLIALgvEPGDRVAIL--SRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 99 AKLLLsatavtvtdlpvrivsednlkdiffthkgnTPNPEH-AVkgdenfyIIYTSGSTGNPKGVQITYNCLVSFTKWAV 177
Cdd:cd05907 78 AKALF------------------------------VEDPDDlAT-------IIYTSGTTGRPKGVMLSHRNILSNALALA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 178 EDFNLQTGQVFLNQAPFSFDL-SVMDIYPSLVTGGTLWaidkdMIARPKDLFASLEQSDIQVWTSTPSFAEMclMEASFS 256
Cdd:cd05907 121 ERLPATEGDRHLSFLPLAHVFeRRAGLYVPLLAGARIY-----FASSAETLLDDLSEVRPTVFLAVPRVWEK--VYAAIK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 257 ENMLPNMKTFLFCGEVLPN---------EVARKLIERFPKA--TIMNTYGPTEATVAVTGIHvteevLDQYKSLPVG--Y 323
Cdd:cd05907 194 VKAVPGLKRKLFDLAVGGRlrfaasggaPLPAELLHFFRALgiPVYEGYGLTETSAVVTLNP-----PGDNRIGTVGkpL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 324 CKSDCRllimkedgtIAPDgekGEIVIVGPSVSVGYLGSPELTEKAFtmiDGERAYKTGDAGYV-ENGLLFYNGRL-DFQ 401
Cdd:cd05907 269 PGVEVR---------IADD---GEILVRGPNVMLGYYKNPEATAEAL---DADGWLHTGDLGEIdEDGFLHITGRKkDLI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 402 IKLHGYRMELEEIEHHLRACSYVEGAVIVpikkGEKYDYLLAVVVPGEHSFEKEFKLTSAIK------------------ 463
Cdd:cd05907 334 ITSGGKNISPEPIENALKASPLISQAVVI----GDGRPFLVALIVPDPEALEAWAEEHGIAYtdvaelaanpavraeiea 409
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446693156 464 --KELNERLPNYMIPRKF------MYQSSIPMTPNGKVDRKKL 498
Cdd:cd05907 410 avEAANARLSRYEQIKKFlllpepFTIENGELTPTLKLKRPVI 452
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
9-495 |
6.82e-37 |
|
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: 143.15 E-value: 6.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 9 KWAAETPDQTAFVW------RDAKITYKQLKEDSDALAHWISSE-YPDDRsPIMVYGHmQPEMIINFLGCVKAGhaYIPV 81
Cdd:cd05931 1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVgKPGDR-VLLLAPP-GLDFVAAFLGCLYAG--AIAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 82 DLSIP-----ADRVQRIAENSGAKLLLSATAV----------TVTDLPVRIVSEDNLKDiffthKGNTPNPEHAVKGDEN 146
Cdd:cd05931 77 PLPPPtpgrhAERLAAILADAGPRVVLTTAAAlaavrafaasRPAAGTPRLLVVDLLPD-----TSAADWPPPSPDPDDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 147 FYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLS-VMDIYPSLVTGGTLWAID-KDMIARP 224
Cdd:cd05931 152 AYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGlIGGLLTPLYSGGPSVLMSpAAFLRRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 225 kdlFASLEQ-SDIQ-VWTSTPSFA-EMCLMEASfSENM----LPNMKtFLFCG-E-VLPNEVARkLIERF-----PKATI 290
Cdd:cd05931 232 ---LRWLRLiSRYRaTISAAPNFAyDLCVRRVR-DEDLegldLSSWR-VALNGaEpVRPATLRR-FAEAFapfgfRPEAF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 291 MNTYGPTEATVAVTG---------IHVTEEVLDQYKSLP------------VGYCKSDCRLLIMKEDG-TIAPDGEKGEI 348
Cdd:cd05931 306 RPSYGLAEATLFVSGgppgtgpvvLRVDRDALAGRAVAVaaddpaarelvsCGRPLPDQEVRIVDPETgRELPDGEVGEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 349 VIVGPSVSVGYLGSPELTEKAFTMIDGERA---YKTGDAGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACS--Y 423
Cdd:cd05931 386 WVRGPSVASGYWGRPEATAETFGALAATDEggwLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHpaL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 424 VEGAVI---VPIKKGEKydyLLAVVVPGEHSFEKEFKltsAIKKELNERLPN---------YMIPRkfmyqSSIPMTPNG 491
Cdd:cd05931 466 RPGCVAafsVPDDGEER---LVVVAEVERGADPADLA---AIAAAIRAAVARehgvapadvVLVRP-----GSIPRTSSG 534
|
....
gi 446693156 492 KVDR 495
Cdd:cd05931 535 KIQR 538
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
28-498 |
1.15e-35 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 139.19 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 28 TYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRvQRI----AENSGAKLLL 103
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR-QNIylgvAKPRGLIVIR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 104 SATAVtvtdlpvrivsednlkdiffthkgntpnpehaVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQ 183
Cdd:cd17647 101 AAGVV--------------------------------VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 184 TGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEMCLMEASfseNMLPNM 263
Cdd:cd17647 149 ENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQAT---TPFPKL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 264 KTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVT-----EEVLDQYKS-LPVGYCKSDCRLLIM-KED 336
Cdd:cd17647 226 HHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVPsrssdPTFLKNLKDvMPAGRGMLNVQLLVVnRND 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 337 GT-IAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT---MIDGE----------------------RAYKTGDAG-YVEN 389
Cdd:cd17647 306 RTqICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwFVEPDhwnyldkdnnepwrqfwlgprdRLYRTGDLGrYLPN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 390 GLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFEKEF------------- 456
Cdd:cd17647 386 GDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDESfaqedvpkevstd 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446693156 457 ----------KLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd17647 466 pivkgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
26-498 |
3.13e-35 |
|
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: 136.27 E-value: 3.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 26 KITYKQLKEDSDALAHWI--SSEYPDDRSPIMVygHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKLLl 103
Cdd:cd05934 3 RWTYAELLRESARIAAALaaLGIRPGDRVALML--DNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 104 satavtVTDLpvrivsednlkdiffthkgntpnpehavkgdenFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQ 183
Cdd:cd05934 80 ------VVDP---------------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 184 TGQVFLNQAP-FSFDLSVMDIYPSLVTGGTLWAIDKdmiarpkdlF-ASLEQSDIQVWTST-----PSFAEMcLMEASFS 256
Cdd:cd05934 121 EDDVYLTVLPlFHINAQAVSVLAALSVGATLVLLPR---------FsASRFWSDVRRYGATvtnylGAMLSY-LLAQPPS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 257 ENMLPNMKTFLFCGEVLPNEVARkLIERFpKATIMNTYGPTEATVAVTGIHvteevlDQY-KSLPVGYCKSDCRLLIMKE 335
Cdd:cd05934 191 PDDRAHRLRAAYGAPNPPELHEE-FEERF-GVRLLEGYGMTETIVGVIGPR------DEPrRPGSIGRPAPGYEVRIVDD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 336 DGTIAPDGEKGEIVI---VGPSVSVGYLGSPELTEKAftMIDGerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMEL 411
Cdd:cd05934 263 DGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEA--MRNG--WFHTGDLGYRdADGFFYFVDRKKDMIRRRGENISS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 412 EEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVV--PGEHSFEKEFKLTSAikkelnERLPNYMIPRKFMYQSSIPMTP 489
Cdd:cd05934 339 AEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVlrPGETLDPEELFAFCE------GQLAYFKVPRYIRFVDDLPKTP 412
|
....*....
gi 446693156 490 NGKVDRKKL 498
Cdd:cd05934 413 TEKVAKAQL 421
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
17-498 |
5.28e-35 |
|
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: 136.05 E-value: 5.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 17 QTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGhaYIPV---DLSIPADrVQ 91
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLgvSSGDR--VLLLMLDSPELVQLFLGCLARG--AIAVvinPLLHPDD-YA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 92 RIAENSGAKLLlsatavtvtdlpvrIVSEDNLKdiffthkgntpnpehavkgdenfYIIYTSGSTGNPKGVQITYNCLVS 171
Cdd:cd05919 76 YIARDCEARLV--------------VTSADDIA-----------------------YLLYSSGTTGPPKGVMHAHRDPLL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 172 FTK-WAVEDFNLQTGQVFLNQAP--FSFDLSVMDIYPsLVTGGTlwAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEM 248
Cdd:cd05919 119 FADaMAREALGLTPGDRVFSSAKmfFGYGLGNSLWFP-LAVGAS--AVLNPGWPTAERVLATLARFRPTVLYGVPTFYAN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 249 CLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEatvaVTGIHVTEEVlDQYK----SLPV-GY 323
Cdd:cd05919 196 LLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATE----VGHIFLSNRP-GAWRlgstGRPVpGY 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 324 cksDCRLLimKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmidgERAYKTGDAGYV-ENGLLFYNGRLDFQI 402
Cdd:cd05919 270 ---EIRLV--DEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN----GGWYRTGDKFCRdADGWYTHAGRADDML 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 403 KLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPgEHSFEKEFKLTSAIKKELNERLPNYMIPRKFMYQ 482
Cdd:cd05919 341 KVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVL-KSPAAPQESLARDIHRHLLERLSAHKVPRRIAFV 419
|
490
....*....|....*.
gi 446693156 483 SSIPMTPNGKVDRKKL 498
Cdd:cd05919 420 DELPRTATGKLQRFKL 435
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
15-499 |
2.69e-34 |
|
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: 135.19 E-value: 2.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 15 PDQTAFVWRDAKITYKQLKEDSDALAHWISSEY--PDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQR 92
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGvkREER--VLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 93 IAENSGAKLLL----------SATAVTVTDLPVRIVS--------EDNLKDIFFTHKGN-TPNPEHAvkgDENFYIIYTS 153
Cdd:cd05959 96 YLEDSRARVVVvsgelapvlaAALTKSEHTLVVLIVSggagpeagALLLAELVAAEAEQlKPAATHA---DDPAFWLYSS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 154 GSTGNPKG-VQITYNCLVSFTKWAVEDFNLQTGQVFLNQAP--FSFDLSVMDIYPSLVTGGTLWaidkdMIARPKD--LF 228
Cdd:cd05959 173 GSTGRPKGvVHLHADIYWTAELYARNVLGIREDDVCFSAAKlfFAYGLGNSLTFPLSVGATTVL-----MPERPTPaaVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 229 ASLEQSDIQVWTSTPS-FAEMCLMEASFSENmLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEAtvavtgIH 307
Cdd:cd05959 248 KRIRRYRPTVFFGVPTlYAAMLAAPNLPSRD-LSSLRLCVSAGEALPAEVGERWKARF-GLDILDGIGSTEM------LH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 308 V-----TEEVLDQYKSLPV-GYcksdcRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFtmiDGErAYKT 381
Cdd:cd05959 320 IflsnrPGRVRYGTTGKPVpGY-----EVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF---QGE-WTRT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 382 GDAgYV--ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEhSFEKEFKLT 459
Cdd:cd05959 391 GDK-YVrdDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRP-GYEDSEALE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446693156 460 SAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLL 499
Cdd:cd05959 469 EELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
27-498 |
4.51e-34 |
|
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: 133.37 E-value: 4.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 27 ITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKlllsaT 106
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK-----V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 107 AVTVTDLpvrivseDNLKDIFfthkgntpnpehavkgdenfyiiYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQ 186
Cdd:cd05935 77 AVVGSEL-------DDLALIP-----------------------YTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 187 VFLNQAPF----SFDLSVMdiyPSLVTGGTL-----WaiDKDMIArpkDLFaslEQSDIQVWTSTPSFAEMCLMEASFSE 257
Cdd:cd05935 127 VILACLPLfhvtGFVGSLN---TAVYVGGTYvlmarW--DRETAL---ELI---EKYKVTFWTNIPTMLVDLLATPEFKT 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 258 NMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEAtvavtgihvteevLDQYKSLPVGYCKSDCR-------- 329
Cdd:cd05935 196 RDLSSLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTET-------------MSQTHTNPPLRPKLQCLgip*fgvd 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 330 -LLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGY 407
Cdd:cd05935 262 aRVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKGRRFFRTGDLGYMdEEGYFFFVDRVKRMINVSGF 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 408 RMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVpgehsFEKEFKLTSA---IKKELNERLPNYMIPRKFMYQSS 484
Cdd:cd05935 342 KVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIV-----LRPEYRGKVTeedIIEWAREQMAAYKYPREVEFVDE 416
|
490
....*....|....
gi 446693156 485 IPMTPNGKVDRKKL 498
Cdd:cd05935 417 LPRSASGKILWRLL 430
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1-495 |
3.06e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 131.83 E-value: 3.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 1 MKLLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISS-EYPDDRSPIMVYGHMqpEMIINFLGCVKAGHAYI 79
Cdd:PRK07638 1 MGITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEkESKNKTIAILLENRI--EFLQLFAGAAMAGWTCV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 80 PVDL-SIPADRVQRIAENSGAKLLLSATAVT-VTDLPVRIVSEDNLK---DIFFTHKGNTPNPEHAvkgdeNFYIIYTSG 154
Cdd:PRK07638 79 PLDIkWKQDELKERLAISNADMIVTERYKLNdLPDEEGRVIEIDEWKrmiEKYLPTYAPIENVQNA-----PFYMGFTSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 155 STGNPKG-VQITYNCLVSFTKwAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKdmiARPKDLFASLEQ 233
Cdd:PRK07638 154 STGKPKAfLRAQQSWLHSFDC-NVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRK---FIPNQVLDKLET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 234 SDIQVWTSTPSFAEMCLMEASFSENMLpnmkTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVaVTGIHVTEEVL 313
Cdd:PRK07638 230 ENISVMYTVPTMLESLYKENRVIENKM----KIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 314 dqyKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGS----PELTEKAFTMIDgerayktgDAGYV-E 388
Cdd:PRK07638 305 ---RPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGgvlaRELNADGWMTVR--------DVGYEdE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 389 NGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKK---GEKydyLLAVVVPGEHSFEkefkltsaIKKE 465
Cdd:PRK07638 374 EGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDsywGEK---PVAIIKGSATKQQ--------LKSF 442
|
490 500 510
....*....|....*....|....*....|
gi 446693156 466 LNERLPNYMIPRKFMYQSSIPMTPNGKVDR 495
Cdd:PRK07638 443 CLQRLSSFKIPKEWHFVDEIPYTNSGKIAR 472
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
27-498 |
3.71e-32 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 131.34 E-value: 3.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 27 ITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRvQRI----AENSGakLL 102
Cdd:TIGR03443 271 FTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPAR-QTIylsvAKPRA--LI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 103 LSATAVTVTDLpVRIVSEDNLK--------------------------DIFFTHKGNTPNPEHAVKG-DENFYIIYTSGS 155
Cdd:TIGR03443 348 VIEKAGTLDQL-VRDYIDKELElrteipalalqddgslvggsleggetDVLAPYQALKDTPTGVVVGpDSNPTLSFTSGS 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 156 TGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSD 235
Cdd:TIGR03443 427 EGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYG 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 236 IQVWTSTPSFAEMCLMEASfseNMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVT-----E 310
Cdd:TIGR03443 507 ATVTHLTPAMGQLLSAQAT---TPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETQRAVSYFEIPsrssdS 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 311 EVLDQYKSL-PVGYCKSDCRLLIM-KEDGT-IAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFT---MIDGE-------- 376
Cdd:TIGR03443 584 TFLKNLKDVmPAGKGMKNVQLLVVnRNDRTqTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVnnwFVDPShwidldke 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 377 --------------RAYKTGDAG-YVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAV------------- 428
Cdd:TIGR03443 664 nnkperefwlgprdRLYRTGDLGrYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVtlvrrdkdeeptl 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 429 ---IVPIKKGEKYDYLLAVVvPGEHSFE-------KEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:TIGR03443 744 vsyIVPQDKSDELEEFKSEV-DDEESSDpvvkgliKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
3-501 |
1.02e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 127.69 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVD 82
Cdd:PRK06145 4 LSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 83 LSIPADRVQRIAENSGAKLLL---SATAVTVTDLPVRIVSEDNLKDIFFTHKGNTPNPEHAVKGDENFY-IIYTSGSTGN 158
Cdd:PRK06145 84 YRLAADEVAYILGDAGAKLLLvdeEFDAIVALETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTDLVrLMYTSGTTDR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 159 PKGVQITYNCLvsftKWAVED----FNLQTGQVFLNQAPF----SFDLSVMDIypsLVTGGTLwAIDKDMiaRPKDLFAS 230
Cdd:PRK06145 164 PKGVMHSYGNL----HWKSIDhviaLGLTASERLLVVGPLyhvgAFDLPGIAV---LWVGGTL-RIHREF--DPEAVLAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 231 LEQSDIQVWTSTPSFAEMCLmeaSFSENMLPNMKTFLFC---GEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIH 307
Cdd:PRK06145 234 IERHRLTCAWMAPVMLSRVL---TVPDRDRFDLDSLAWCiggGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLME 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 308 VTEEvLDQYKSlpVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFtmIDGerAYKTGDAGYV 387
Cdd:PRK06145 311 AGRE-IEKIGS--TGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF--YGD--WFRSGDVGYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 388 -ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV-EGAVI-VPIKK-GEKydyLLAVVV--PGEhSFEKEfkltsA 461
Cdd:PRK06145 384 dEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVaEAAVIgVHDDRwGER---ITAVVVlnPGA-TLTLE-----A 454
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446693156 462 IKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSE 501
Cdd:PRK06145 455 LDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
3-493 |
1.09e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 128.15 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEY---PDDRspIMVYghMQ--PEMIINFLGCVKAGHA 77
Cdd:PRK08314 12 LFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECgvrKGDR--VLLY--MQnsPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 78 YIPVDLSIPADRVQRIAENSGAKL------LLSATAVTVTDLPVRIVSEDNLKDIFFTHKG------------------- 132
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVaivgseLAPKVAPAVGNLRLRHVIVAQYSDYLPAEPEiavpawlraepplqalapg 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 133 -----------NTPNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCL----VSFTKWavedFNLQTGQVFLNQAPFsFD 197
Cdd:PRK08314 168 gvvawkealaaGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVmanaVGSVLW----SNSTPESVVLAVLPL-FH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 198 LSVM--DIYPSLVTGGTL-----WaiDKDMIARpkdlfaSLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCG 270
Cdd:PRK08314 243 VTGMvhSMNAPIYAGATVvlmprW--DREAAAR------LIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 271 EVLPNEVARKLIERFpKATIMNTYGPTEaTVAVTgiHVTEevLDQYKS--LPVGYCKSDCRLlIMKEDGTIAPDGEKGEI 348
Cdd:PRK08314 315 AAMPEAVAERLKELT-GLDYVEGYGLTE-TMAQT--HSNP--PDRPKLqcLGIPTFGVDARV-IDPETLEELPPGEVGEI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 349 VIVGPSVSVGYLGSPELTEKAFTMIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGA 427
Cdd:PRK08314 388 VVHGPQVFKGYWNRPEATAEAFIEIDGKRFFRTGDLGRMdEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEA 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446693156 428 VIVPIK---KGEKydyLLAVVVPGEHSFEKefklTSA--IKKELNERLPNYMIPRKFMYQSSIPMTPNGKV 493
Cdd:PRK08314 468 CVIATPdprRGET---VKAVVVLRPEARGK----TTEeeIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
28-498 |
4.55e-30 |
|
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: 122.23 E-value: 4.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 28 TYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKLLlsa 105
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLgvGKGDR--VFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 106 taVTVTDLPVRIVSEDNlkdiffthkgntpnpehavkgdenFYIIYTSGSTGNPKGVQITYNCLVSFtkwavedfnLQTG 185
Cdd:cd05969 77 --ITTEELYERTDPEDP------------------------TLLHYTSGTTGTPKGVLHVHDAMIFY---------YFTG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 186 QvflnqapFSFDLSVMDIY-----PSLVTGGT--LWA---------IDKDMIArPKDLFASLEQSDIQVWTSTPSFAEMC 249
Cdd:cd05969 122 K-------YVLDLHPDDIYwctadPGWVTGTVygIWApwlngvtnvVYEGRFD-AESWYGIIERVKVTVWYTAPTAIRML 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 250 L-----MEASFSENMLpnmKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEatvavTGihvtEEVLDQYKSLPV--- 321
Cdd:cd05969 194 MkegdeLARKYDLSSL---RFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTE-----TG----SIMIANYPCMPIkpg 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 322 --GYCKSDCRLLIMKEDGTIAPDGEKGEIVIVG--PSVSVGYLGSPELTEKAFtmIDGerAYKTGDAGYV-ENGLLFYNG 396
Cdd:cd05969 261 smGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF--IDG--WYLTGDLAYRdEDGYFWFVG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 397 RLDFQIKLHGYRMELEEIEHHLRACSYV-EGAVIvpikkgEKYDYLLAVVVPGEHSFEKEFKLTSAIKKEL----NERLP 471
Cdd:cd05969 337 RADDIIKTSGHRVGPFEVESALMEHPAVaEAGVI------GKPDPLRGEIIKAFISLKEGFEPSDELKEEIinfvRQKLG 410
|
490 500
....*....|....*....|....*..
gi 446693156 472 NYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05969 411 AHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
28-498 |
4.82e-30 |
|
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: 121.68 E-value: 4.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 28 TYKQLKEDSDALAHWISSE--YPDDRSPIMVygHMQPEMIINFLGCVKAGHAYIPV-DLSIPADRVQRIaENSGAKLlls 104
Cdd:cd05972 2 SFRELKRESAKAANVLAKLglRKGDRVAVLL--PRVPELWAVILAVIKLGAVYVPLtTLLGPKDIEYRL-EAAGAKA--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 105 atavtvtdlpvrIVSEDNlkDIFFthkgntpnpehavkgdenfyIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQT 184
Cdd:cd05972 76 ------------IVTDAE--DPAL--------------------IYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 185 GQVFLNQAPFSFDLSVM-DIYPSLVTGGTLWAIDKDMIArPKDLFASLEQSDIQVWTSTPSFAEMcLMEASFSENMLPNM 263
Cdd:cd05972 122 DDIHWNIADPGWAKGAWsSFFGPWLLGATVFVYEGPRFD-AERILELLERYGVTSFCGPPTAYRM-LIKQDLSSYKFSHL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 264 KTFLFCGEVLPNEVARkLIERFPKATIMNTYGPTEaTVAVTGIHVTEEVLDQYKSLPV-GYcksdcRLLIMKEDGTIAPD 342
Cdd:cd05972 200 RLVVSAGEPLNPEVIE-WWRAATGLPIRDGYGQTE-TGLTVGNFPDMPVKPGSMGRPTpGY-----DVAIIDDDGRELPP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 343 GEKGEIVI--VGPSVSVGYLGSPELTEKAFtmidGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLR 419
Cdd:cd05972 273 GEEGDIAIklPPPGLFLGYVGDPEKTEASI----RGDYYLTGDRAYRdEDGYFWFVGRADDIIKSSGYRIGPFEVESALL 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446693156 420 ACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHsFEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05972 349 EHPAVAEAAVVGSPDPVRGEVVKAFVVLTSG-YEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
3-500 |
3.72e-29 |
|
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: 120.46 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQ-TAFVWRDAK---ITYKQLKEDSDALAHWI--SSEYPDDRspIMVYGHMQPEMIINFLGCVKAGh 76
Cdd:cd05906 12 LLELLLRAAERGPTKgITYIDADGSeefQSYQDLLEDARRLAAGLrqLGLRPGDS--VILQFDDNEDFIPAFWACVLAG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 77 aYIPVDLSIPADrvQRIAENSGAKL-----------LLS--------ATAVTVTDLPV-RIVSEDNLKDiffthkgnTPN 136
Cdd:cd05906 89 -FVPAPLTVPPT--YDEPNARLRKLrhiwqllgspvVLTdaelvaefAGLETLSGLPGiRVLSIEELLD--------TAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 137 PEHAV--KGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPF-----SFDLSVMDIYpslvT 209
Cdd:cd05906 158 DHDLPqsRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLdhvggLVELHLRAVY----L 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 210 GG-TLWAIDKDMIARPKDLFASLEQSDIQVwTSTPSFAEMCLMEASFSEN----MLPNMKTFLFCGEVLPNEVARKLIER 284
Cdd:cd05906 234 GCqQVHVPTEEILADPLRWLDLIDRYRVTI-TWAPNFAFALLNDLLEEIEdgtwDLSSLRYLVNAGEAVVAKTIRRLLRL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 285 F-----PKATIMNTYGPTEATVAVTGIHV--TEEVLDQYKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSV 357
Cdd:cd05906 313 LepyglPPDAIRPAFGMTETCSGVIYSRSfpTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 358 GYLGSPELTEKAFTMiDGerAYKTGDAGYVENGLLFYNGRLDFQIKLHGYRMELEEIEhhlracSYVEGAVIV------- 430
Cdd:cd05906 393 GYYNNPEANAEAFTE-DG--WFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIE------AAVEEVPGVepsftaa 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446693156 431 -PIKKGEKYDYLLAVV-VPGEHSFEKEFKLTSAIKKELNERL---PNYMIPrkfMYQSSIPMTPNGKVDRKKLLS 500
Cdd:cd05906 464 fAVRDPGAETEELAIFfVPEYDLQDALSETLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKLKA 535
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
11-498 |
4.00e-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: 120.03 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVwrDA----KITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIP 86
Cdd:cd05904 15 ASAHPSRPALI--DAatgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLST 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 87 ADRVQRIAENSGAKLLLSATA----VTVTDLPVRIVSED------NLKDIFFTHKGNTPNPEhaVKGDENFYIIYTSGST 156
Cdd:cd05904 93 PAEIAKQVKDSGAKLAFTTAElaekLASLALPVVLLDSAefdslsFSDLLFEADEAEPPVVV--IKQDDVAALLYSSGTT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 157 GNPKGVQITYNCLVSFTKWAVEDFNLQTG--QVFLNQAPF--SFDLSVMdIYPSLVTGGTLWAIDK-DMiarpKDLFASL 231
Cdd:cd05904 171 GRSKGVMLTHRNLIAMVAQFVAGEGSNSDseDVFLCVLPMfhIYGLSSF-ALGLLRLGATVVVMPRfDL----EELLAAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 232 EQSDIqvwTSTPSFAEMCL------MEASFSenmLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTG 305
Cdd:cd05904 246 ERYKV---THLPVVPPIVLalvkspIVDKYD---LSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 306 IHVTEEvlDQYKSLPVGycksdcRLLIMKE-------DGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEkafTMIDGERA 378
Cdd:cd05904 320 CFAPEK--DRAKYGSVG------RLVPNVEakivdpeTGESLPPNQTGELWIRGPSIMKGYLNNPEATA---ATIDKEGW 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 379 YKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVV--PGEHSFEKE 455
Cdd:cd05904 389 LHTGDLCYIdEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVrkPGSSLTEDE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446693156 456 fkltsaIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05904 469 ------IMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
11-498 |
5.39e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 120.04 E-value: 5.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPAD 88
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLglKKGDR--VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 89 RVQRIAENSGAKLLLSATAV-----------TVTDLPVRIV-----SEDNLKDIF-FTHKGNTPNPEHAVKGDENFYIIY 151
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPALaptaeaalallPVDTLILSLVlggreAPGGWLDFAdWAEAGSVAEPDVELADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 152 TSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFsFDLSVMDIY--PSLVTGGTLWAIDKdmiARPKDLFA 229
Cdd:PRK08316 179 TSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPL-YHCAQLDVFlgPYLYVGATNVILDA---PDPELILR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 230 SLEQSDI-------QVWTSTpsfaemcLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTE---- 298
Cdd:PRK08316 255 TIEAERItsffappTVWISL-------LRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEiapl 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 299 ATVAvtgihVTEEVLDQYKS--LPVGYCKSDcrllIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmiDGe 376
Cdd:PRK08316 328 ATVL-----GPEEHLRRPGSagRPVLNVETR----VVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFR--GG- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 377 rAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRM---ELEEIEHHLRACSyvEGAVI-VPikkGEKY-DYLLAVVVP-GE 449
Cdd:PRK08316 396 -WFHSGDLGVMdEEGYITVVDRKKDMIKTGGENVasrEVEEALYTHPAVA--EVAVIgLP---DPKWiEAVTAVVVPkAG 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 446693156 450 HSFEKEfkltsAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK08316 470 ATVTED-----ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-498 |
1.21e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 118.85 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 1 MKLLEQIEKWAAETPDQTAFVWRDAKITYKQLKED----SDALAHW-ISseyPDDRspIMVYGHMQPEMIINFLGCVKAG 75
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARvrraAAALAALgIG---KGDR--VAIWAPNSPHWVIAALGALKAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 76 HAYIPVDLSIPADRVQRIAENSGAKLLLSATA------VTVTDLPV---RIVSEDNLKDIF---------FTHKGNTPNP 137
Cdd:PRK07656 80 AVVVPLNTRYTADEAAYILARGDAKALFVLGLflgvdySATTRLPAlehVVICETEEDDPHtekmktftdFLAAGDPAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 138 EHAVKGDENFYIIYTSGSTGNPKGVQITY-NCLVSFTKWAvEDFNLQTGQVFLNQAPF--SFDLSVMDIYPsLVTGGTlw 214
Cdd:PRK07656 160 APEVDPDDVADILFTSGTTGRPKGAMLTHrQLLSNAADWA-EYLGLTEGDRYLAANPFfhVFGYKAGVNAP-LMRGAT-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 215 aidkdMIARPK----DLFASLEQSDIQVWTSTPSFAEMCLMEASFSENmlpNMKTFLFC---GEVLPNEVARKLIERFPK 287
Cdd:PRK07656 236 -----ILPLPVfdpdEVFRLIETERITVLPGPPTMYNSLLQHPDRSAE---DLSSLRLAvtgAASMPVALLERFESELGV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 288 ATIMNTYGPTEATVAVT--GIHvteevlDQYKSLP--VGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSP 363
Cdd:PRK07656 308 DIVLTGYGLSEASGVTTfnRLD------DDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 364 ELTEKAftmIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHL-RACSYVEGAVI-VPIKK-GE--K 437
Cdd:PRK07656 382 EATAAA---IDADGWLHTGDLGRLdEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLyEHPAVAEAAVIgVPDERlGEvgK 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446693156 438 ydyllAVVVPGEHSFEKEFKLTSAIKkelnERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK07656 459 -----AYVVLKPGAELTEEELIAYCR----EHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
11-502 |
2.51e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 118.31 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFV-WRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVYGhmQPEMIINFLGCVKAGHAYIPVDLSIPA 87
Cdd:PRK06087 33 ARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLAKgiEPGDRVAFQLPG--WCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 88 DRVQRIAENSGAKLLLSATAVTVTD-----LPVR--------IVSEDNLK----DIFFTH--KGNTP-NPEHAVKGDENF 147
Cdd:PRK06087 111 AELVWVLNKCQAKMFFAPTLFKQTRpvdliLPLQnqlpqlqqIVGVDKLApatsSLSLSQiiADYEPlTTAITTHGDELA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 148 YIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFS----FDLSVmdIYPSLVtGGTLWAIDkdmIAR 223
Cdd:PRK06087 191 AVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGhatgFLHGV--TAPFLI-GARSVLLD---IFT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 224 PKDLFASLEQSDIqVWT--STPSFAEM-CLMEASFSEnmLPNMKTFLFCGEVLPNEVARKLIERFPKatIMNTYGPTEAT 300
Cdd:PRK06087 265 PDACLALLEQQRC-TCMlgATPFIYDLlNLLEKQPAD--LSALRFFLCGGTTIPKKVARECQQRGIK--LLSVYGSTESS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 301 VavtgiHVteeVLDQYKSLPV-----GYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAftmIDG 375
Cdd:PRK06087 340 P-----HA---VVNLDDPLSRfmhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA---LDE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 376 ERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV--EGAVIVPIKK-GEKYdYLLAVVVPGEHS 451
Cdd:PRK06087 409 EGWYYSGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIhdACVVAMPDERlGERS-CAYVVLKAPHHS 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446693156 452 FEKEfKLTSAIKKelnERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSEV 502
Cdd:PRK06087 488 LTLE-EVVAFFSR---KRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDI 534
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
16-500 |
8.00e-27 |
|
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: 112.77 E-value: 8.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 16 DQTAFVWRDAKITYKQLKEDSDALAHWISSEYPD---DRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQR 92
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDlrgDR--VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 93 IAENSGAKLLLSATAvtvtdlpvrivsednlkdiffthkgntpnpehavkgdenfyIIYTSGSTGNPKGVQITY------ 166
Cdd:cd05941 79 VITDSEPSLVLDPAL-----------------------------------------ILYTSGTTGRPKGVVLTHanlaan 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 167 -NCLVSFTKWAVEDFNLQtgqvflnqapfsfdlsVMDIYP--SLVTG--GTLWAiDKDMIARPKD----LFASLEQSDIQ 237
Cdd:cd05941 118 vRALVDAWRWTEDDVLLH----------------VLPLHHvhGLVNAllCPLFA-GASVEFLPKFdpkeVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 238 VWTSTPSF--------AEMCLMEASFSENMLPNMKTFLfCGEV-LPNEVARKLIERFPKaTIMNTYGPTEATVAVT-GIH 307
Cdd:cd05941 181 VFMGVPTIytrllqyyEAHFTDPQFARAAAAERLRLMV-SGSAaLPVPTLEEWEAITGH-TLLERYGMTEIGMALSnPLD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 308 vtEEVLDQY--KSLP-VgycksDCRLlIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmidGERAYKTGDA 384
Cdd:cd05941 259 --GERRPGTvgMPLPgV-----QARI-VDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFT---DDGWFKTGDL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 385 G-YVENGLLFYNGRL-DFQIKLHGYRMELEEIEHHLRACSYV-EGAVI-VPIKK-GEKydyLLAVVVPGEhsfEKEFKLT 459
Cdd:cd05941 328 GvVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVsECAVIgVPDPDwGER---VVAVVVLRA---GAAALSL 401
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446693156 460 SAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLS 500
Cdd:cd05941 402 EELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
11-498 |
1.64e-25 |
|
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: 109.52 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFV--WRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPAD 88
Cdd:cd05923 11 ASRAPDACAIAdpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 89 RVQRIAENSGAKLLLSATAVTVT----DLPVRIVSEDNLKDIFFTHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQI 164
Cdd:cd05923 91 ELAELIERGEMTAAVIAVDAQVMdaifQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 165 TYNCLVSFTKWAVEDFNLQTG--QVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMiaRPKDLFASLEQSDIQVWTST 242
Cdd:cd05923 171 PQRAAESRVLFMSTQAGLRHGrhNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADALKLIEQERVTSLFAT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 243 PSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLiERFPKATIMNTYGPTEATVAVTGIHVTEEvldqyKSLPVG 322
Cdd:cd05923 249 PTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERV-NQHLPGEKVNIYGTTEAMNSLYMRDARTG-----TEMRPG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 323 YcKSDCRLL-IMKEDGTIAPDGEKGEIVI--VGPSVSVGYLGSPELTEKAFTmidgERAYKTGDAGYVE-NGLLFYNGRL 398
Cdd:cd05923 323 F-FSEVRIVrIGGSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKLQ----DGWYRTGDVGYVDpSGDVRILGRV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 399 DFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFE----KEFKLTSAikkelnerLPNYM 474
Cdd:cd05923 398 DDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSadelDQFCRASE--------LADFK 469
|
490 500
....*....|....*....|....
gi 446693156 475 IPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05923 470 RPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
10-498 |
1.70e-25 |
|
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: 109.34 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 10 WAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGhaYIPVdLSIPA 87
Cdd:cd05920 24 SAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLgiRPGDR--VVVQLPNVAEFVVLFFALLRLG--AVPV-LALPS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 88 drvQRIAENSGAKLLLSATAVTVTDlpvrivsednlkdiffTHKGNTPNP---EHAVKGDENFYIIYTSGSTGNPKGVQI 164
Cdd:cd05920 99 ---HRRSELSAFCAHAEAVAYIVPD----------------RHAGFDHRAlarELAESIPEVALFLLSGGTTGTPKLIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 165 TYNCLVSFTKWAVEDFNLQTGQVFL--NQAPFSFDLSVMDIYPSLVTGGTLwAIDKDmiARPKDLFASLEQSDIQVWTST 242
Cdd:cd05920 160 THNDYAYNVRASAEVCGLDQDTVYLavLPAAHNFPLACPGVLGTLLAGGRV-VLAPD--PSPDAAFPLIEREGVTVTALV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 243 PSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVg 322
Cdd:cd05920 237 PALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRPM- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 323 ycKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMiDGerAYKTGD-AGYVENGLLFYNGRLDFQ 401
Cdd:cd05920 315 --SPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTP-DG--FYRTGDlVRRTPDGYLVVEGRIKDQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 402 IKLHGYRMELEEIEHHLRACSYVEGAVIVPIKK---GEKydyLLAVVVPGEHSFEkefklTSAIKKELNER-LPNYMIPR 477
Cdd:cd05920 390 INRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDellGER---SCAFVVLRDPPPS-----AAQLRRFLRERgLAAYKLPD 461
|
490 500
....*....|....*....|.
gi 446693156 478 KFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05920 462 RIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
2-496 |
1.71e-25 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 109.59 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 2 KLLEQIEKWAAETPDQTAFVWRDAKI--TYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHA 77
Cdd:PRK05852 17 RIADLVEVAATRLPEAPALVVTADRIaiSYRDLARLVDDLAGQLTRSglLPGDR--VALRMGSNAEFVVALLAASRADLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 78 YIPVDLSIP-ADRVQRIAENSGAKLLLSATAVTVTDLP--------VRIVSEDNLKD-IFFTHKGNTPNPEHAVK----- 142
Cdd:PRK05852 95 VVPLDPALPiAEQRVRSQAAGARVVLIDADGPHDRAEPttrwwpltVNVGGDSGPSGgTLSVHLDAATEPTPATStpegl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 143 GDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVM-DIYPSLVTGGTLWaidkdMI 221
Cdd:PRK05852 175 RPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIaALLATLASGGAVL-----LP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 222 ARPK----DLFASLEQSDIQVWTSTPSFAEMCLMEAS--FSENMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYG 295
Cdd:PRK05852 250 ARGRfsahTFWDDIKAVGATWYTAVPTIHQILLERAAtePSGRKPAALRFIRSCSAPLTAETAQALQTEF-AAPVVCAFG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 296 PTEAT--VAVTGIHVTEEVLDQYKSL-PVGYcKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTm 372
Cdd:PRK05852 329 MTEAThqVTTTQIEGIGQTENPVVSTgLVGR-STGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT- 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 373 iDGerAYKTGDAGYVE-NGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHS 451
Cdd:PRK05852 407 -DG--WLRTGDLGSLSaAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESA 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446693156 452 FEKEFKLTSAIKkelnERLPNYMIPRKFMYQSSIPMTPNGKVDRK 496
Cdd:PRK05852 484 PPTAEELVQFCR----ERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
149-495 |
2.67e-25 |
|
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: 106.58 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 IIYTSGSTGNPKGVQITYNCLVSFTK-WAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGtLWAIDKDMIaRPKDL 227
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDiLQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGG-LCVTGGENT-TYKSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 228 FASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEvLPNEVARKLIERFPKATIMNTYGPTEaTVAVTGIH 307
Cdd:cd17635 84 FKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGS-RAIAADVRFIEATGLTNTAQVYGLSE-TGTALCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 308 VTEEVLDQYKslpVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmidgERAYKTGDAGYV 387
Cdd:cd17635 162 TDDDSIEINA---VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI----DGWVNTGDLGER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 388 -ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYD-YLLAVVVPGEhsfeKEFKLTSAIKKE 465
Cdd:cd17635 235 rEDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGElVGLAVVASAE----LDENAIRALKHT 310
|
330 340 350
....*....|....*....|....*....|
gi 446693156 466 LNERLPNYMIPRKFMYQSSIPMTPNGKVDR 495
Cdd:cd17635 311 IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
7-495 |
3.11e-25 |
|
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: 109.12 E-value: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRD-----AKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPV 81
Cdd:cd05970 23 VDAMAKEYPDKLALVWCDdageeRIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 82 DLSI-PADRVQRIaENSGAKLLLSATAVTVTD-----------LPVRIVSEDNLKDIFFT-HKG--------NTPNPEHA 140
Cdd:cd05970 103 THQLtAKDIVYRI-ESADIKMIVAIAEDNIPEeiekaapecpsKPKLVWVGDPVPEGWIDfRKLiknaspdfERPTANSY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 141 VKGDENFYIIYTSGSTGNPKGVQitynclvsftkwavEDF-----NLQTGQVFLNQAPFSFDLSVMD----------IYP 205
Cdd:cd05970 182 PCGEDILLVYFSSGTTGMPKMVE--------------HDFtyplgHIVTAKYWQNVREGGLHLTVADtgwgkavwgkIYG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 206 SLVTGGTLWAIDKDMIArPKDLFASLEQSDIQVWTSTPSFAEMcLMEASFSENMLPNMKTFLFCGEVLPNEVarklIERF 285
Cdd:cd05970 248 QWIAGAAVFVYDYDKFD-PKALLEKLSKYGVTTFCAPPTIYRF-LIREDLSRYDLSSLRYCTTAGEALNPEV----FNTF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 286 PKAT---IMNTYGPTEATVAVTGIHVTEEvldqyKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVI-------VGpsV 355
Cdd:cd05970 322 KEKTgikLMEGFGQTETTLTIATFPWMEP-----KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskgkpVG--L 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 356 SVGYLGSPELTEKAFTmiDGerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRA-CSYVEGAVI-VPi 432
Cdd:cd05970 395 FGGYYKDAEKTAEVWH--DG--YYHTGDAAWMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQhPAVLECAVTgVP- 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446693156 433 kkgekyDYLLAVVVPGEHSFEKEFKLTSAIKKELNERLPN----YMIPRKFMYQSSIPMTPNGKVDR 495
Cdd:cd05970 470 ------DPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKvtapYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
139-498 |
9.71e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 108.47 E-value: 9.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 139 HAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPF--SFDLSVMDIYPSLV-------- 208
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTVTLWLPLLEgikvvyhp 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 209 --TGGTlwAIDKdMIARPKD--LFAsleqsdiqvwtsTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIER 284
Cdd:PRK08633 857 dpTDAL--GIAK-LVAKHRAtiLLG------------TPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEK 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 285 FPKaTIMNTYGPTEAT--VAVtgihvteevldqykSLPVGYCKSDCRLLIMK------------------EDGTIAPDGE 344
Cdd:PRK08633 922 FGI-RILEGYGATETSpvASV--------------NLPDVLAADFKRQTGSKegsvgmplpgvavrivdpETFEELPPGE 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 345 KGEIVIVGPSVSVGYLGSPELTEKAFTMIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSY 423
Cdd:PRK08633 987 DGLILIGGPQVMKGYLGDPEKTAEVIKDIDGIGWYVTGDKGHLdEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALG 1066
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 424 VEGAVI----VP-IKKGEKydyLLAVVVPGEHSFEKefkltsaIKKELNE-RLPNYMIPRKFMYQSSIPMTPNGKVDRKK 497
Cdd:PRK08633 1067 GEEVVFavtaVPdEKKGEK---LVVLHTCGAEDVEE-------LKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKG 1136
|
.
gi 446693156 498 L 498
Cdd:PRK08633 1137 L 1137
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
28-498 |
1.21e-24 |
|
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: 106.31 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 28 TYKQLKEDSDALAHWISSE--YPDDRSPIMVYGHMqpEMIINFLGCVKAGHAYIPVdlsIPADRVQRIAensgakLLLSA 105
Cdd:cd05903 3 TYSELDTRADRLAAGLAALgvGPGDVVAFQLPNWW--EFAVLYLACLRIGAVTNPI---LPFFREHELA------FILRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 106 TAVTVTDLPVRIVSEDnlkdiffthkgntpnpeHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTG 185
Cdd:cd05903 72 AKAKVFVVPERFRQFD-----------------PAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 186 QVFLNQAPFSFDLSVMDIYPSLVTGGTlwAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKT 265
Cdd:cd05903 135 DVFLVASPMAHQTGFVYGFTLPLLLGA--PVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 266 FLFCGEVLPNEVARKLIERFpKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSlpvGYCKSDCRLLIMKEDGTIAPDGEK 345
Cdd:cd05903 213 FVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSITPAPEDRRLYTD---GRPLPGVEIKVVDDTGATLAPGVE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 346 GEIVIVGPSVSVGYLGSPELTEKAFTmidgERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV 424
Cdd:cd05903 289 GELLSRGPSVFLGYLDRPDLTADAAP----EGWFRTGDLARLdEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 425 EGAVIVPI---KKGEKydyLLAVVV---PGEHSFEkefKLTSAIKKelnERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05903 365 IEAAVVALpdeRLGER---ACAVVVtksGALLTFD---ELVAYLDR---QGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
26-498 |
2.24e-24 |
|
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: 105.59 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 26 KITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQ-RIAeNSGAKLLls 104
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEyRLS-NSGASAL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 105 atavtVTDLPvrivsednlkdiffthkgntpnpehavkgDENFYIIYTSGSTGNPKG------VQITYNCLVSFTkwave 178
Cdd:cd05971 83 -----VTDGS-----------------------------DDPALIIYTSGTTGPPKGalhahrVLLGHLPGVQFP----- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 179 dFNL--QTGQVFLNQAPFSFDLSVMDIY-PSLVTGGTLWAIDKDMIArPKDLFASLEQSDIQVWTSTPSFAEMCLMEASF 255
Cdd:cd05971 124 -FNLfpRDGDLYWTPADWAWIGGLLDVLlPSLYFGVPVLAHRMTKFD-PKAALDLMSRYGVTTAFLPPTALKMMRQQGEQ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 256 SENMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPV-GYcksdcRLLIMK 334
Cdd:cd05971 202 LKHAQVKLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIpGH-----RVAIVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 335 EDGTIAPDGEKGEIVIVGP-SVS-VGYLGSPELTEKAFTmidgERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMEL 411
Cdd:cd05971 276 DNGTPLPPGEVGEIAVELPdPVAfLGYWNNPSATEKKMA----GDWLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 412 EEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVV--PGEHSFEkefkltsAIKKELNE----RLPNYMIPRKFMYQSSI 485
Cdd:cd05971 352 AEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnPGETPSD-------ALAREIQElvktRLAAHEYPREIEFVNEL 424
|
490
....*....|...
gi 446693156 486 PMTPNGKVDRKKL 498
Cdd:cd05971 425 PRTATGKIRRREL 437
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
3-499 |
2.39e-24 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 106.72 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAK----ITYKQLKEDSDALAHW-----ISseyPDDRspIMVYGHMQPEMIINFLGCVK 73
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGiwqsLTWAEFAERVRALAAGllalgVK---PGDR--VAILSDNRPEWVIADLAILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 74 AGHAYIPVDLSIPADRVQRIAENSGAKLLLSATAVTV-------TDLP--VRIVSED-----------NLKDIFFTHKGN 133
Cdd:COG1022 88 AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLdkllevrDELPslRHIVVLDprglrddprllSLDELLALGREV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 134 TPNPE-----HAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLnqapfSF-DLS-----VMD 202
Cdd:COG1022 168 ADPAElearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL-----SFlPLAhvferTVS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 203 IYpSLVTGGTLwAIDKDmiarPKDLfasleQSDIQ-----VWTSTPSFAEMclMEASFSENM--LPNMKTFLF------- 268
Cdd:COG1022 243 YY-ALAAGATV-AFAES----PDTL-----AEDLRevkptFMLAVPRVWEK--VYAGIQAKAeeAGGLKRKLFrwalavg 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 269 --------------CGEVLPNEVARKLIerFPK----------------A---------------TIMNTYGPTEATVAV 303
Cdd:COG1022 310 rryararlagkspsLLLRLKHALADKLV--FSKlrealggrlrfavsggAalgpelarffralgiPVLEGYGLTETSPVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 304 TGihvteEVLDQYKSLPVGycksdcRLLimkeDGT---IAPDGEkgeIVIVGPSVSVGYLGSPELTEKAFTmIDGerAYK 380
Cdd:COG1022 388 TV-----NRPGDNRIGTVG------PPL----PGVevkIAEDGE---ILVRGPNVMKGYYKNPEATAEAFD-ADG--WLH 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 381 TGDAGYV-ENGLLFYNGRLDFQIKL-HGYRMELEEIEHHLRACSYVEGAVIVpikkGEKYDYLLAVVVPGEHSFEKEFK- 457
Cdd:COG1022 447 TGDIGELdEDGFLRITGRKKDLIVTsGGKNVAPQPIENALKASPLIEQAVVV----GDGRPFLAALIVPDFEALGEWAEe 522
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 458 ----------------LTSAIKKEL---NERLPNYMIPRKFmyqSSIP---------MTPNGKVDRKKLL 499
Cdd:COG1022 523 nglpytsyaelaqdpeVRALIQEEVdraNAGLSRAEQIKRF---RLLPkeftiengeLTPTLKLKRKVIL 589
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
3-494 |
3.57e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 105.74 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIekwAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIP 80
Cdd:PRK07798 8 LFEAV---ADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQglGPGDH--VGIYARNRIEYVEAMLGAFKARAVPVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 81 VDLSIPADRVQRIAENSGAKLL-----LSATAVTV----TDLPVRIVSEDNLKDIFFTH--------KGNTPNPEHAVKG 143
Cdd:PRK07798 83 VNYRYVEDELRYLLDDSDAVALvyereFAPRVAEVlprlPKLRTLVVVEDGSGNDLLPGavdyedalAAGSPERDFGERS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 144 DENFYIIYTSGSTGNPKGV----QITYncLVSF------------TKWAVEDFNLQ-TGQVFLNQAPFSFDLSVMDIYPS 206
Cdd:PRK07798 163 PDDLYLLYTGGTTGMPKGVmwrqEDIF--RVLLggrdfatgepieDEEELAKRAAAgPGMRRFPAPPLMHGAGQWAAFAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 207 LVTGGT-------------LW-AIDK----------DMIARPkdLFASLEQ------SDIQVWTSTPsfaemclmeASFS 256
Cdd:PRK07798 241 LFSGQTvvllpdvrfdadeVWrTIERekvnvitivgDAMARP--LLDALEArgpydlSSLFAIASGG---------ALFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 257 EnmlpnmktflfcgevlpnEVARKLIERFPKATIMNTYGPTEAtvAVTGIHVTEEvldqyKSLPVGYCK----SDCRLLi 332
Cdd:PRK07798 310 P------------------SVKEALLELLPNVVLTDSIGSSET--GFGGSGTVAK-----GAVHTGGPRftigPRTVVL- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 333 mKEDGTIAP--DGEKGEIVIVGPsVSVGYLGSPELTEKAFTMIDGERAYKTGDAGYVENG----LLfynGRLDFQIKLHG 406
Cdd:PRK07798 364 -DEDGNPVEpgSGEIGWIARRGH-IPLGYYKDPEKTAETFPTIDGVRYAIPGDRARVEADgtitLL---GRGSVCINTGG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 407 YRMELEEIEHHLRACSYVEGAVIVPI---KKGEKydyLLAVVVPGE-HSFEKEfkltsAIKKELNERLPNYMIPRKFMYQ 482
Cdd:PRK07798 439 EKVFPEEVEEALKAHPDVADALVVGVpdeRWGQE---VVAVVQLREgARPDLA-----ELRAHCRSSLAGYKVPRAIWFV 510
|
570
....*....|..
gi 446693156 483 SSIPMTPNGKVD 494
Cdd:PRK07798 511 DEVQRSPAGKAD 522
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
7-498 |
8.30e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 104.17 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEY---PDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDL 83
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELnvkKGER--IAILSQNSLEYIVLLFAIAKVECIAVPLNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 84 SIPADRVQRIAENSGAKLLL----------SATAVTVTDLPVRIVSEDNLKDifftHKGNTPNPEhavKGDENFYIIYTS 153
Cdd:PRK06839 86 RLTENELIFQLKDSGTTVLFvektfqnmalSMQKVSYVQRVISITSLKEIED----RKIDNFVEK---NESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 154 GSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFsFDLSVMDIY--PSLVTGGTLWAIDKdmiARPKDLFASL 231
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLFafPTLFAGGVIIVPRK---FEPTKALSMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 232 EQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIER-FPkatIMNTYGPTEATVAVtgIHVTE 310
Cdd:PRK06839 235 EKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRgFL---FGQGFGMTETSPTV--FMLSE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 311 EVLDQyKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKafTMIDGerAYKTGD-AGYVEN 389
Cdd:PRK06839 310 EDARR-KVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE--TIQDG--WLCTGDlARVDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 390 GLLFYNGRLDFQIKLHG---YRMELEEIEHHLRACsyVEGAVI-VPIKKGEKYDYLLAVVVPGEHSFEKEfkltsaIKKE 465
Cdd:PRK06839 385 GFVYIVGRKKEMIISGGeniYPLEVEQVINKLSDV--YEVAVVgRQHVKWGEIPIAFIVKKSSSVLIEKD------VIEH 456
|
490 500 510
....*....|....*....|....*....|...
gi 446693156 466 LNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK06839 457 CRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
147-495 |
1.07e-23 |
|
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: 101.71 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 147 FYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLwAIDKDMIarPKD 226
Cdd:cd17633 3 FYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTF-IGQRKFN--PKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 227 LFASLEQSDIQVWTSTPSFAEMcLMEASFSENmlpNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATvavtgi 306
Cdd:cd17633 80 WIRKINQYNATVIYLVPTMLQA-LARTLEPES---KIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELS------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 307 HVTEEVLDQ-YKSLPVGYCKSDCRLLIMKEDGtiapdGEKGEIVIVGPSVSVGYLGSPELTEKAFtmidgeraYKTGDAG 385
Cdd:cd17633 150 FITYNFNQEsRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW--------MSVGDIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 386 YV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKgEKYDYLLAVVVPGEhsfekefKLT-SAIK 463
Cdd:cd17633 217 YVdEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPD-ARFGEIAVALYSGD-------KLTyKQLK 288
|
330 340 350
....*....|....*....|....*....|..
gi 446693156 464 KELNERLPNYMIPRKFMYQSSIPMTPNGKVDR 495
Cdd:cd17633 289 RFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
5-504 |
3.16e-23 |
|
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: 102.92 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 5 EQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGhaYIPVd 82
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALglRPGDR--VVVQLPNVAEFVIVFFALFRAG--AIPV- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 83 LSIPADRVQRI---AENSGAKLLLSATAVTVTD--------------LPVRIVSEDNLKDIFFTHKGNTP--NPEHAVKG 143
Cdd:COG1021 104 FALPAHRRAEIshfAEQSEAVAYIIPDRHRGFDyralarelqaevpsLRHVLVVGDAGEFTSLDALLAAPadLSEPRPDP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 144 DENFYIIYTSGSTGNPKGVQIT-----YNCLVSftkwaVEDFNLQTGQVFLNQAP--FSFDLSvmdiypSLVTGGTLWAI 216
Cdd:COG1021 184 DDVAFFQLSGGTTGLPKLIPRThddylYSVRAS-----AEICGLDADTVYLAALPaaHNFPLS------SPGVLGVLYAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 217 DKDMIAR---PKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPkATIMNT 293
Cdd:COG1021 253 GTVVLAPdpsPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALG-CTLQQV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 294 YGPTEATVAVTGIHVTEEVLDQYKSLPVGyckSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMi 373
Cdd:COG1021 332 FGMAEGLVNYTRLDDPEEVILTTQGRPIS---PDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTP- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 374 DGerAYKTGD-AGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKkgekyDYLL-----AVVVP 447
Cdd:COG1021 408 DG--FYRTGDlVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMP-----DEYLgerscAFVVP 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446693156 448 GehsfEKEFKLtSAIKKELNER-LPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSEVTA 504
Cdd:COG1021 481 R----GEPLTL-AELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
11-501 |
3.41e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 102.81 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPAD 88
Cdd:PRK07470 17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARgvRKGDR--ILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 89 RVQRIAENSGAKLLLS-------ATAVTVTDLPVRIV-------SEDNLKDIFFTHKGnTPNPEHAVKGDENFYIIYTSG 154
Cdd:PRK07470 95 EVAYLAEASGARAMIChadfpehAAAVRAASPDLTHVvaiggarAGLDYEALVARHLG-ARVANAAVDHDDPCWFFFTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 155 STGNPKGVQITYNclvsftkwavedfnlQTGQVFLNQapfsfdlsVMDIYP-------SLVT-----GGTLWAIDKdmIA 222
Cdd:PRK07470 174 TTGRPKAAVLTHG---------------QMAFVITNH--------LADLMPgtteqdaSLVVaplshGAGIHQLCQ--VA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 223 R-PKDLFASLEQSDI-QVWT-----------STPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKaT 289
Cdd:PRK07470 229 RgAATVLLPSERFDPaEVWAlverhrvtnlfTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGK-V 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 290 IMNTYGPTEATVAVT----GIHVTEEVlDQYKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPEL 365
Cdd:PRK07470 308 LVQYFGLGEVTGNITvlppALHDAEDG-PDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 366 TEKAFTmiDGerAYKTGDAGYV-ENGLLFYNGRL-DFQIKlhG----YRMELEEIEhhLRACSYVEGAVI-VPIKK-GEk 437
Cdd:PRK07470 387 NAKAFR--DG--WFRTGDLGHLdARGFLYITGRAsDMYIS--GgsnvYPREIEEKL--LTHPAVSEVAVLgVPDPVwGE- 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446693156 438 ydYLLAVVVPGEHSFEKEfkltSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVdRKKLLSE 501
Cdd:PRK07470 458 --VGVAVCVARDGAPVDE----AELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI-TKKMVRE 514
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
139-498 |
7.26e-23 |
|
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: 101.25 E-value: 7.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 139 HAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPF--SFDLSVMDIYPSLVTGGTLWAI 216
Cdd:cd05909 142 APVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhSFGLTGCLWLPLLSGIKVVFHP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 217 DKdmiARPKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSEnmLPNMKtFLFCG-EVLPNEVARKLIERFPKAtIMNTYG 295
Cdd:cd05909 222 NP---LDYKKIPELIYDKKATILLGTPTFLRGYARAAHPED--FSSLR-LVVAGaEKLKDTLRQEFQEKFGIR-ILEGYG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 296 PTEATvAVTGIHVTEEvldQYKSLPVGYC--KSDCRLlIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFtmi 373
Cdd:cd05909 295 TTECS-PVISVNTPQS---PNKEGTVGRPlpGMEVKI-VSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF--- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 374 dGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPI----KKGEKydyllAVVVPG 448
Cdd:cd05909 367 -GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSvpdgRKGEK-----IVLLTT 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446693156 449 EHSFEKEfKLTSAIKkelNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05909 441 TTDTDPS-SLNDILK---NAGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
24-495 |
9.92e-23 |
|
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: 100.98 E-value: 9.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 24 DAKITYKQLKEDSDALAHW--ISSEYPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKL 101
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLlkINGVGTGDR--VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 102 LLsatavtvtdlpvriVSEDnlkdiffthkgntpnpehavkgDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFN 181
Cdd:cd05914 83 IF--------------VSDE----------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 182 LQTGQVFLNQAPFS--FDLSVMDIYPSLVtGGTLWAIDKdmIARPKDLFASLEQSDIQVWTSTPsfaemCLMEASFSENM 259
Cdd:cd05914 127 LGKGDKILSILPLHhiYPLTFTLLLPLLN-GAHVVFLDK--IPSAKIIALAFAQVTPTLGVPVP-----LVIEKIFKMDI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 260 LP--NMKTFLFCGEVLPNE------VARKLIERFPKA------------------------TIMNTYGPTEATVAVTGIH 307
Cdd:cd05914 199 IPklTLKKFKFKLAKKINNrkirklAFKKVHEAFGGNikefviggakinpdveeflrtigfPYTIGYGMTETAPIISYSP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 308 VTEEVLDQykslpVGYCKSDCRLLIMKEDgtiaPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmIDGerAYKTGDAG-Y 386
Cdd:cd05914 279 PNRIRLGS-----AGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFD-KDG--WFHTGDLGkI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 387 VENGLLFYNGRLDFQIKL-HGYRMELEEIEHHLRACSYV-EGAVIVPIKKGEkydyLLAVVVPgEHSFEKEFKLTSAIKK 464
Cdd:cd05914 347 DAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVlESLVVVQEKKLV----ALAYIDP-DFLDVKALKQRNIIDA 421
|
490 500 510
....*....|....*....|....*....|....*....
gi 446693156 465 -------ELNERLPNYMIPRKF-MYQSSIPMTPNGKVDR 495
Cdd:cd05914 422 ikwevrdKVNQKVPNYKKISKVkIVKEEFEKTPKGKIKR 460
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
4-503 |
1.95e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 100.04 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 4 LEQIEKW----AAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMII-----NFLGCVKA 74
Cdd:PRK03640 1 METMPNWlkqrAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILvihalQQLGAVAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 75 ghaYIPVDLSiPADRVQRIaENSGAKLLLSA---TAVTVTDLPVRI--VSEDNLKDIFFThkgnTPNPEhavkgDENFYI 149
Cdd:PRK03640 81 ---LLNTRLS-REELLWQL-DDAEVKCLITDddfEAKLIPGISVKFaeLMNGPKEEAEIQ----EEFDL-----DEVATI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 150 IYTSGSTGNPKGVQITYNclvsfTKWA-----VEDFNLQTGQVFLNQAPFsFDLSVMDI-YPSLVTGGTLWAIDK-Dmia 222
Cdd:PRK03640 147 MYTSGTTGKPKGVIQTYG-----NHWWsavgsALNLGLTEDDCWLAAVPI-FHISGLSIlMRSVIYGMRVVLVEKfD--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 223 rPKDLFASLEQSDIQVWTSTPSFAEMCLMEASfSENMLPNMKTFLFCGEVLPNEVARKLIER-FPkatIMNTYGPTEATV 301
Cdd:PRK03640 218 -AEKINKLLQTGGVTIISVVSTMLQRLLERLG-EGTYPSSFRCMLLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETAS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 302 AVtgihVT---EEVLDQYKSlpVGYCKSDCRLLIMKeDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFtmIDGerA 378
Cdd:PRK03640 293 QI----VTlspEDALTKLGS--AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF--QDG--W 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 379 YKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFEKEfk 457
Cdd:PRK03640 362 FKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEE-- 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446693156 458 ltsaIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSEVT 503
Cdd:PRK03640 440 ----LRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
151-501 |
2.26e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 100.49 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 151 YTSGSTGNPKGVQITYNCLVSFTKWAVE-DFNLQTGQ-VFLNQAPFsFDL----SVMDIypSLVTGGTLWAIDK-DMiar 223
Cdd:PRK06710 213 YTGGTTGFPKGVMLTHKNLVSNTLMGVQwLYNCKEGEeVVLGVLPF-FHVygmtAVMNL--SIMQGYKMVLIPKfDM--- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 224 pKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLiERFPKATIMNTYGPTEATVAV 303
Cdd:PRK06710 287 -KMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKF-ETVTGGKLVEGYGLTESSPVT 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 304 TGIHVTEEVLDqyKSLPVGYCKSDCRLLIMkEDGTIAPDGEKGEIVIVGPSVSVGYLGSPEltEKAFTMIDGerAYKTGD 383
Cdd:PRK06710 365 HSNFLWEKRVP--GSIGVPWPDTEAMIMSL-ETGEALPPGEIGEIVVKGPQIMKGYWNKPE--ETAAVLQDG--WLHTGD 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 384 AGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFEKEFKLTSAI 462
Cdd:PRK06710 438 VGYMdEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFA 517
|
330 340 350
....*....|....*....|....*....|....*....
gi 446693156 463 KKelneRLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSE 501
Cdd:PRK06710 518 RK----YLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
11-504 |
1.34e-21 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 97.91 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVygHMQPEMIINFLGCVKAGHAYIPVDLSIPAD 88
Cdd:PRK06155 31 AERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAgvKRGDRVALMC--GNRIEFLDVFLGCAWLGAIAVPINTALRGP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 89 RVQRIAENSGAKLL---------LSATAVTVTDLP-VRIVSEDNLKDIFFTHK------GNTPNPEHAVKGDENFYIIYT 152
Cdd:PRK06155 109 QLEHILRNSGARLLvveaallaaLEAADPGDLPLPaVWLLDAPASVSVPAGWStaplppLDAPAPAAAVQPGDTAAILYT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 153 SGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFsFDLSVMD-IYPSLVTGGTLWAIDKDMIARpkdLFASL 231
Cdd:PRK06155 189 SGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPL-FHTNALNaFFQALLAGATYVLEPRFSASG---FWPAV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 232 EQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGevLPNEVARKLIERFpKATIMNTYGPTEATVAVTGIHvtee 311
Cdd:PRK06155 265 RRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPG--VPAALHAAFRERF-GVDLLDGYGSTETNFVIAVTH---- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 312 vlDQYKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVG--P-SVSVGYLGSPELTEKAFTMIdgerAYKTGDAGYVE 388
Cdd:PRK06155 338 --GSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdePfAFATGYFGMPEKTVEAWRNL----WFHTGDRVVRD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 389 -NGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGE-HSFEKEfkltsAIKKEL 466
Cdd:PRK06155 412 aDGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDgTALEPV-----ALVRHC 486
|
490 500 510
....*....|....*....|....*....|....*....
gi 446693156 467 NERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSE-VTA 504
Cdd:PRK06155 487 EPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQgVTA 525
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
16-498 |
1.71e-21 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 97.45 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 16 DQTAFVWRDA-----KITYKQLKEDSDALAH-WISSEY-PDDRSPIMVYGhmQPEMIINFLGCVKAGHAYIPVDLSIPAD 88
Cdd:PRK08008 22 HKTALIFESSggvvrRYSYLELNEEINRTANlFYSLGIrKGDKVALHLDN--CPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 89 RVQRIAENSGAKLLLSATAVTVTDLPVRIVSEDNLKDIFFTHKGntpnpEHAVKGDENFY-------------------- 148
Cdd:PRK08008 100 ESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVA-----LPADDGVSSFTqlkaqqpatlcyapplstdd 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 ---IIYTSGSTGNPKGVQIT-YNCLVS--FTKWAVedfNLQTGQVFLNQAP-FSFDLSVMDIYPSLVTGGTLWAIDKdmi 221
Cdd:PRK08008 175 taeILFTSGTTSRPKGVVIThYNLRFAgyYSAWQC---ALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEK--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 222 arpkdlfasleQSDIQVWtstpsfAEMCLMEASFSENMlPNMKTFLFCGEVLPNEVARKL-----------------IER 284
Cdd:PRK08008 249 -----------YSARAFW------GQVCKYRATITECI-PMMIRTLMVQPPSANDRQHCLrevmfylnlsdqekdafEER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 285 FpKATIMNTYGPTEATVAVTGIHVTEEvlDQYKSL-PVGYCKsdcRLLIMKEDGTIAPDGEKGEIVIVG-PSVSV--GYL 360
Cdd:PRK08008 311 F-GVRLLTSYGMTETIVGIIGDRPGDK--RRWPSIgRPGFCY---EAEIRDDHNRPLPAGEIGEICIKGvPGKTIfkEYY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 361 GSPELTEKAFTMiDGerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYD 439
Cdd:PRK08008 385 LDPKATAKVLEA-DG--WLHTGDTGYVdEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDE 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446693156 440 YLLAVVV--PGEHSFEKEFKLTSAikkelnERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK08008 462 AIKAFVVlnEGETLSEEEFFAFCE------QNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
3-402 |
4.84e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 96.65 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDA------KITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGH 76
Cdd:PRK12582 51 IPHLLAKWAAEAPDRPWLAQREPghgqwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 77 AYIPVD-----LSIPADRVQRIAE---------NSGAKLLLSATAVTVTDlpVRIVSEDNLKD----IFFTHKGNTPnPE 138
Cdd:PRK12582 131 PAAPVSpayslMSHDHAKLKHLFDlvkprvvfaQSGAPFARALAALDLLD--VTVVHVTGPGEgiasIAFADLAATP-PT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 139 HAVKG-------DENFYIIYTSGSTGNPKGVQITYN--CLVSFTKWAVEDFNLQTG-QVFLNQAPFSFDLSVMDIY-PSL 207
Cdd:PRK12582 208 AAVAAaiaaitpDTVAKYLFTSGSTGMPKAVINTQRmmCANIAMQEQLRPREPDPPpPVSLDWMPWNHTMGGNANFnGLL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 208 VTGGTLWaIDKdmiARP-KDLFA----SLEQSDIQVWTSTP-SFAEMC-LMEA--SFSENMLPNMKTFLFCGEVLPNEVA 278
Cdd:PRK12582 288 WGGGTLY-IDD---GKPlPGMFEetirNLREISPTVYGNVPaGYAMLAeAMEKddALRRSFFKNLRLMAYGGATLSDDLY 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 279 RKLIERFPKAT-----IMNTYGPTEATVAVTGIH-VTEEVldQYKSLPV-GycksdcrlLIMKedgtIAPDGEKGEIVIV 351
Cdd:PRK12582 364 ERMQALAVRTTghripFYTGYGATETAPTTTGTHwDTERV--GLIGLPLpG--------VELK----LAPVGDKYEVRVK 429
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446693156 352 GPSVSVGYLGSPELTEKAFtmiDGERAYKTGDAG-YV-----ENGLLFyNGRL--DFQI 402
Cdd:PRK12582 430 GPNVTPGYHKDPELTAAAF---DEEGFYRLGDAArFVdpddpEKGLIF-DGRVaeDFKL 484
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
140-498 |
6.51e-21 |
|
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: 94.72 E-value: 6.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 140 AVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFsFDLSVMDI-YPSLVTGGTLWAIDK 218
Cdd:cd05912 73 DVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPL-FHISGLSIlMRSVIYGMTVYLVDK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 219 -DmiarPKDLFASLEQSDIQVWTSTPSFAEMCLmeASFSENMLPNMKTFLFCGEVLPNEVARKLIER-FPkatIMNTYGP 296
Cdd:cd05912 152 fD----AEQVLHLINSGKVTIISVVPTMLQRLL--EILGEGYPNNLRCILLGGGPAPKPLLEQCKEKgIP---VYQSYGM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 297 TEATVAVtgihVT---EEVLDQYKSlpVGYCKSDCRLLIMKEDGtiaPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmi 373
Cdd:cd05912 223 TETCSQI----VTlspEDALNKIGS--AGKPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESFE-- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 374 DGerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVpGEHSF 452
Cdd:cd05912 292 NG--WFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV-SERPI 368
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446693156 453 EKEfkltsAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05912 369 SEE-----ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
139-498 |
1.54e-20 |
|
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: 94.08 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 139 HAVKGDENFYII-YTSGSTGNPKG-VQITYNCLVSFTKWAVEDFNLQTGQVFLNQAP--FSFDLSVMDIYPSLVtGGTLW 214
Cdd:cd05958 91 HALTASDDICILaFTSGTTGAPKAtMHFHRDPLASADRYAVNVLRLREDDRFVGSPPlaFTFGLGGVLLFPFGV-GASGV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 215 AIDKdmiARPKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTY 294
Cdd:cd05958 170 LLEE---ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEAT-GIPIIDGI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 295 GPTEAtvavtgIHV-----TEEVLDQYKSLPV-GYcksdcRLLIMKEDGTIAPDGEKGEIVIVGPSvsvGYLGSPEltEK 368
Cdd:cd05958 246 GSTEM------FHIfisarPGDARPGATGKPVpGY-----EAKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLAD--KR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 369 AFTMIDGERAYkTGDAGYVE-NGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV-EGAVI-VPIKKGEKYDYLLAVV 445
Cdd:cd05958 310 QRTYVQGGWNI-TGDTYSRDpDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVaECAVVgHPDESRGVVVKAFVVL 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446693156 446 VPGEHSFEKefkLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05958 389 RPGVIPGPV---LARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
149-457 |
3.72e-20 |
|
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: 93.19 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 IIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAP-----------FSFDLSVMDIYPSLVTggtlwaID 217
Cdd:cd17640 93 IIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPiwhsyersaeyFIFACGCSQAYTSIRT------LK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 218 KDMIARPKDLFASLEqsdiQVWTSTPSFAEMCLMEASFSENMLpnMKTFLFCGEV---------LPNEVarkliERFPKA 288
Cdd:cd17640 167 DDLKRVKPHYIVSVP----RLWESLYSGIQKQVSKSSPIKQFL--FLFFLSGGIFkfgisgggaLPPHV-----DTFFEA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 289 T---IMNTYGPTEATVAVTGIHVTEEVLDQykslpVGYCKSDCRLLIMKEDG-TIAPDGEKGEIVIVGPSVSVGYLGSPE 364
Cdd:cd17640 236 IgieVLNGYGLTETSPVVSARRLKCNVRGS-----VGRPLPGTEIKIVDPEGnVVLPPGEKGIVWVRGPQVMKGYYKNPE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 365 LTEKAftmIDGERAYKTGDAGY-VENGLLFYNGRLDFQIKL-HGYRMELEEIEHHLRACSYVEGAVIVpikkGEKYDYLL 442
Cdd:cd17640 311 ATSKV---LDSDGWFNTGDLGWlTCGGELVLTGRAKDTIVLsNGENVEPQPIEEALMRSPFIEQIMVV----GQDQKRLG 383
|
330
....*....|....*
gi 446693156 443 AVVVPGEHSFEKEFK 457
Cdd:cd17640 384 ALIVPNFEELEKWAK 398
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1-496 |
8.40e-20 |
|
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: 92.55 E-value: 8.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 1 MKLLEQ-IEKWAAETPDQTAFVWRDAK-----ITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKA 74
Cdd:cd05968 60 MNIVEQlLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 75 GHAYIPVDLSIPADRVQRIAENSGAKLLLSATAVTVTDLPV-----------------RIVSEDNLKDIFFTHKGN---- 133
Cdd:cd05968 140 GGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREVnlkeeadkacaqcptveKVVVVRHLGNDFTPAKGRdlsy 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 134 -----TPNPEHAVKGDEN-FYIIYTSGSTGNPKGVqITYNClvSFTKWAVED----FNLQTGQVFLnqapFSFDLSVMD- 202
Cdd:cd05968 220 deekeTAGDGAERTESEDpLMIIYTSGTTGKPKGT-VHVHA--GFPLKAAQDmyfqFDLKPGDLLT----WFTDLGWMMg 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 203 ---IYPSLVTGGTLW----AIDKDmiaRPKDLFASLEQSDIQVWTSTPSF--AEMCLMEASFSENMLPNMKTFLFCGEVL 273
Cdd:cd05968 293 pwlIFGGLILGATMVlydgAPDHP---KADRLWRMVEDHEITHLGLSPTLirALKPRGDAPVNAHDLSSLRVLGSTGEPW 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 274 PNE-----VARKLIERFPkatIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVGYCKSDcrllIMKEDGTIAPDgEKGEI 348
Cdd:cd05968 370 NPEpwnwlFETVGKGRNP---IINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKAD----VLDESGKPARP-EVGEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 349 VIVGPSVSV--GYLGSPE-LTEKAFTMIDGerAYKTGD-AGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV 424
Cdd:cd05968 442 VLLAPWPGMtrGFWRDEDrYLETYWSRFDN--VWVHGDfAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAV 519
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446693156 425 -EGAVI-VPIK-KGEKYdYLLAVVVPGehsfekeFKLTSAIKKELNERLPNYM----IPRKFMYQSSIPMTPNGKVDRK 496
Cdd:cd05968 520 lESAAIgVPHPvKGEAI-VCFVVLKPG-------VTPTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRR 590
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
149-498 |
3.92e-19 |
|
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: 88.49 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 IIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPF--SFDLsVMDIYPSLVTGGTLWAIDKDMiaRPKD 226
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLfhCFGS-VLGVLACLTHGATMVFPSPSF--DPLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 227 LFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATvAVTGI 306
Cdd:cd05917 84 VLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETS-PVSTQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 307 HVTEEVLDQyKSLPVGYCKSDCRLLIM-KEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAftmIDGERAYKTGDAG 385
Cdd:cd05917 163 TRTDDSIEK-RVNTVGRIMPHTEAKIVdPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA---IDGDGWLHTGDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 386 YV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKgEKYDYLLAVVV---PGEHSFEKEfkltsa 461
Cdd:cd05917 239 VMdEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPD-ERYGEEVCAWIrlkEGAELTEED------ 311
|
330 340 350
....*....|....*....|....*....|....*..
gi 446693156 462 IKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05917 312 IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
68-498 |
4.12e-19 |
|
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: 90.24 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 68 FLGCVKAGhaYIPVDLSIPADRVQRIAENSGAKLLLSatavtvtdlPVRIVSEDNLKDiffthkgntpNPEHAVkgdenf 147
Cdd:cd05908 57 FWACLLGG--MIAVPVSIGSNEEHKLKLNKVWNTLKN---------PYLITEEEVLCE----------LADELA------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 148 YIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGT--LWAIDKDMIARPK 225
Cdd:cd05908 110 FIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMnqYLMPTRLFIRRPI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 226 DLFASLEQSDIQVwTSTPSFAEMCLMEASFSENM----LPNMKTFLFCGEVLPNEVARKLIERFP-----KATIMNTYGP 296
Cdd:cd05908 190 LWLKKASEHKATI-VSSPNFGYKYFLKTLKPEKAndwdLSSIRMILNGAEPIDYELCHEFLDHMSkyglkRNAILPVYGL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 297 TEATVAVT------------------GIHVTEEVLDQ-----YKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGP 353
Cdd:cd05908 269 AEASVGASlpkaqspfktitlgrrhvTHGEPEPEVDKkdsecLTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 354 SVSVGYLGSPELTEKAFTMiDGerAYKTGDAGYVENGLLFYNGRLDFQIKLHGYRMELEEIEhhlRACSYVEG-----AV 428
Cdd:cd05908 349 NVTPGYYNNPEATAKVFTD-DG--WLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIE---RIAEELEGvelgrVV 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 429 IVPIKKGEKYDYLLAVVVPGEHSFEKEFKLTSAIKKELNERlPNYMIpRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05908 423 ACGVNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKR-GGWQI-NEVLPIRRIPKTTSGKVKRYEL 490
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
7-402 |
4.78e-19 |
|
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: 90.18 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRDA-----KITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPV 81
Cdd:cd05921 1 LAHWARQAPDRTWLAEREGnggwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 82 ---------DLSIPADRVQRIAE-----NSGAKLLLSATAVTVTDLPVrIVSEDNLKDIFFTH---------KGNTPNPE 138
Cdd:cd05921 81 spayslmsqDLAKLKHLFELLKPglvfaQDAAPFARALAAIFPLGTPL-VVSRNAVAGRGAISfaelaatppTAAVDAAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 139 HAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQ--VFLNQAPFSFDLSV-MDIYPSLVTGGTLWa 215
Cdd:cd05921 160 AAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGnHNFNLVLYNGGTLY- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 216 ID--KDMIARPKDLFASLEQSDIQVWTSTPSFAEMCL--ME--ASFSENMLPNMKTFLFCGEVLPN-------EVARKLI 282
Cdd:cd05921 239 IDdgKPMPGGFEETLRNLREISPTVYFNVPAGWEMLVaaLEkdEALRRRFFKRLKLMFYAGAGLSQdvwdrlqALAVATV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 283 -ERFPkatIMNTYGPTEATVAVTGIH-VTEEVldQYKSLPVGYCKsdcrlliMKedgtIAPDGEKGEIVIVGPSVSVGYL 360
Cdd:cd05921 319 gERIP---MMAGLGATETAPTATFTHwPTERS--GLIGLPAPGTE-------LK----LVPSGGKYEVRVKGPNVTPGYW 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446693156 361 GSPELTEKAFtmiDGERAYKTGDAGYV------ENGLLFyNGRL--DFQI 402
Cdd:cd05921 383 RQPELTAQAF---DEEGFYCLGDAAKLadpddpAKGLVF-DGRVaeDFKL 428
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
5-493 |
4.81e-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: 90.33 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 5 EQIEKWAAETPDQTAFVWRDAK------ITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAY 78
Cdd:cd17634 57 NALDRHLRENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVH 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 79 IPVDLSI-PADRVQRIAEnSGAKLLLSAT-----------------AVTVTDLPVRIV----------SEDNLKDIFFTH 130
Cdd:cd17634 137 SVIFGGFaPEAVAGRIID-SSSRLLITADggvragrsvplkknvddALNPNVTSVEHVivlkrtgsdiDWQEGRDLWWRD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 131 KGNTPNPEH---AVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVED-FNLQTGQVFLNQApfsfDLSVMD---- 202
Cdd:cd17634 216 LIAKASPEHqpeAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYvFDYGPGDIYWCTA----DVGWVTghsy 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 203 -IYPSLVTGGTLWAID-KDMIARPKDLFASLEQSDIQVWTSTPSfAEMCLMEA---SFSENMLPNMKTFLFCGEVLPNEV 277
Cdd:cd17634 292 lLYGPLACGATTLLYEgVPNWPTPARMWQVVDKHGVNILYTAPT-AIRALMAAgddAIEGTDRSSLRILGSVGEPINPEA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 278 ARKLIERFPKA--TIMNTYGPTEATVA-VTGIHVTEEVLDQYKSLPV-GYcksdcRLLIMKEDGTIAPDGEKGEIVIVG- 352
Cdd:cd17634 371 YEWYWKKIGKEkcPVVDTWWQTETGGFmITPLPGAIELKAGSATRPVfGV-----QPAVVDNEGHPQPGGTEGNLVITDp 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 353 -PSVSVGYLGSPELTEKA-FTMIDGerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVI 429
Cdd:cd17634 446 wPGQTRTLFGDHERFEQTyFSTFKG--MYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAV 523
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446693156 430 V----PIKKGEKYDYLlaVVVPGEhsfEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKV 493
Cdd:cd17634 524 VgiphAIKGQAPYAYV--VLNHGV---EPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
15-498 |
5.18e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 90.05 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 15 PDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVD-LSIPADRVQrI 93
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHpLGSLDDHAY-V 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 94 AENSGAKLLLSATAVTVTDLPVRIVSEDNLKDIF----------FTHKGNTPNPEHAVKGD---ENFYIIYTSGSTGNPK 160
Cdd:PRK06188 105 LEDAGISTLIVDPAPFVERALALLARVPSLKHVLtlgpvpdgvdLLAAAAKFGPAPLVAAAlppDIAGLAYTGGTTGKPK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 161 GVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMdIYPSLVTGGTLWAIDK-------DMIAR---------P 224
Cdd:PRK06188 185 GVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF-FLPTLLRGGTVIVLAKfdpaevlRAIEEqritatflvP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 225 KDLFASLEQSDIQvwTSTPSFAEMCLMEASfseNMLPnmkTFLfcgevlpnevaRKLIERF-PkaTIMNTYGPTEATVAV 303
Cdd:PRK06188 264 TMIYALLDHPDLR--TRDLSSLETVYYGAS---PMSP---VRL-----------AEAIERFgP--IFAQYYGQTEAPMVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 304 TGIHVTEEVLDQYKSL-PVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmiDGerAYKTG 382
Cdd:PRK06188 323 TYLRKRDHDPDDPKRLtSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFR--DG--WLHTG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 383 DAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV-EGAVI-VPIKK-GEKydyLLAVVV--PGEHSFEKEf 456
Cdd:PRK06188 399 DVAREdEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVaQVAVIgVPDEKwGEA---VTAVVVlrPGAAVDAAE- 474
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446693156 457 kLTSAIKkelnERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK06188 475 -LQAHVK----ERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
149-498 |
5.66e-19 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 89.88 E-value: 5.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 IIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLN-QAPF-SFDLSVMDIYPSLVTGGTLWAIDKdmiARPKD 226
Cdd:PRK06334 188 ILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSfLPPFhAYGFNSCTLFPLLSGVPVVFAYNP---LYPKK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 227 LFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTgi 306
Cdd:PRK06334 265 IVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTECSPVIT-- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 307 hVTEEVLDQYKSLpVGYCKSDCRLLIMKEDGTI-APDGEKGEIVIVGPSVSVGYLGSPEltEKAFTMIDGERAYKTGDAG 385
Cdd:PRK06334 343 -INTVNSPKHESC-VGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGEDF--GQGFVELGGETWYVTGDLG 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 386 YVE-NGLLFYNGRLDFQIKLHGYRMELEEIEHHLracsyVEGaviVPIKKGEKYDYLLAVVVPGEHSFEKEFKLTSAIKK 464
Cdd:PRK06334 419 YVDrHGELFLKGRLSRFVKIGAEMVSLEALESIL-----MEG---FGQNAADHAGPLVVCGLPGEKVRLCLFTTFPTSIS 490
|
330 340 350
....*....|....*....|....*....|....*....
gi 446693156 465 ELNERLPNYMIPR--KFMYQ---SSIPMTPNGKVDRKKL 498
Cdd:PRK06334 491 EVNDILKNSKTSSilKISYHhqvESIPMLGTGKPDYCSL 529
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-415 |
8.67e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 90.61 E-value: 8.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVW------RDAKITYKQLKEDSDALAHWISSEY-PDDRSPIMVygHMQPEMIINFLGCVKAG 75
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARAsFGDRAVLLF--PSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 76 ----HAYIPVD---------LSIPADRVQRIAENSGA--KLLLSATAVTVTDLPvRIVSEDNLkDIFFTHKGNTPnpehA 140
Cdd:PRK05691 89 viavPAYPPESarrhhqerlLSIIADAEPRLLLTVADlrDSLLQMEELAAANAP-ELLCVDTL-DPALAEAWQEP----A 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 141 VKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTG--QVFLNQAPFSFDLSVMdiypslvtGGTLWAI-- 216
Cdd:PRK05691 163 LQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLI--------GGLLQPIfs 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 217 --------DKDMIARPKDLFASLEQSDIQVwTSTPSFA-EMC---LMEASFSENMLPNMKTFLFCGEVLPNEVARKLIER 284
Cdd:PRK05691 235 gvpcvlmsPAYFLERPLRWLEAISEYGGTI-SGGPDFAyRLCserVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 285 FPKA-----TIMNTYGPTEATVAVTG---------IHVTEEVLDQYKSLP--------VGYCKSDCRLLIMK-EDGTIAP 341
Cdd:PRK05691 314 FAACgfdpdSFFASYGLAEATLFVSGgrrgqgipaLELDAEALARNRAEPgtgsvlmsCGRSQPGHAVLIVDpQSLEVLG 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446693156 342 DGEKGEIVIVGPSVSVGYLGSPELTEKAFTMIDGERAYKTGDAGYVENGLLFYNGRLDFQIKLHGYRMELEEIE 415
Cdd:PRK05691 394 DNRVGEIWASGPSIAHGYWRNPEASAKTFVEHDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIE 467
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
11-498 |
3.01e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 87.49 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPAD 88
Cdd:PRK06164 20 ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQgvRRGDR--VAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 89 RVQRIAENSGAKLLLSATAVTVTDLPVRIVSED-----NLKDIFFTHKGN--TPNP---------------EHAVKG--- 143
Cdd:PRK06164 98 EVAHILGRGRARWLVVWPGFKGIDFAAILAAVPpdalpPLRAIAVVDDAAdaTPAPapgarvqlfalpdpaPPAAAGera 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 144 -DENFYIIY--TSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFS--FDLSVmdIYPSLVTGGTLwaIDK 218
Cdd:PRK06164 178 aDPDAGALLftTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCgvFGFST--LLGALAGGAPL--VCE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 219 DMIARPKDLFASLEQSDIQVWTSTPSFAEMcLMEASFSENmLPNMKTFLFcGEVLP---NEVARKLIERFPKATImntYG 295
Cdd:PRK06164 254 PVFDAARTARALRRHRVTHTFGNDEMLRRI-LDTAGERAD-FPSARLFGF-ASFAPalgELAALARARGVPLTGL---YG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 296 PTEATVAVTGIHVTEEVLDQYKS--LPVgycKSDCRLLIMK-EDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTM 372
Cdd:PRK06164 328 SSEVQALVALQPATDPVSVRIEGggRPA---SPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 373 iDGerAYKTGDAGY-VENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIK-KGEKYDYLLAVVVPGEH 450
Cdd:PRK06164 405 -DG--YFRTGDLGYtRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATrDGKTVPVAFVIPTDGAS 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446693156 451 SFEKEfkltsaIKKELNERLPNYMIPRKFMYQSSIPMT--PNG-KVDRKKL 498
Cdd:PRK06164 482 PDEAG------LMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRL 526
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
11-495 |
3.27e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 87.52 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWR--DAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDlsiP 86
Cdd:PRK12583 28 VARFPDREALVVRhqALRYTWRQLADAVDRLARGLLALgvQPGDR--VGIWAPNCAEWLLTQFATARIGAILVNIN---P 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 87 ADRVQRIA---ENSGAKLLLSATAVTVTDL---------------PVRIVSED--NLKDIFFTHKGNTPN---------- 136
Cdd:PRK12583 103 AYRASELEyalGQSGVRWVICADAFKTSDYhamlqellpglaegqPGALACERlpELRGVVSLAPAPPPGflawhelqar 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 137 -----------PEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPF--SFDLsVMDI 203
Cdd:PRK12583 183 getvsrealaeRQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhCFGM-VLAN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 204 YPSLVTGGTLwaidkdmiARPKDLF---ASLEQSDIQVWTSTPSFAEMCLME---ASFSENMLPNMKTFLFCGEVLPNEV 277
Cdd:PRK12583 262 LGCMTVGACL--------VYPNEAFdplATLQAVEEERCTALYGVPTMFIAEldhPQRGNFDLSSLRTGIMAGAPCPIEV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 278 ARKLIERFPKATIMNTYGPTEATvAVTGIHVTEEVLDQY-----KSLPVGYCKsdcrllIMKEDGTIAPDGEKGEIVIVG 352
Cdd:PRK12583 334 MRRVMDEMHMAEVQIAYGMTETS-PVSLQTTAADDLERRvetvgRTQPHLEVK------VVDPDGATVPRGEIGELCTRG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 353 PSVSVGYLGSPELTEKAftmIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHL-RACSYVEGAVI- 429
Cdd:PRK12583 407 YSVMKGYWNNPEATAES---IDEDGWMHTGDLATMdEQGYVRIVGRSKDMIIRGGENIYPREIEEFLfTHPAVADVQVFg 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446693156 430 VPIKK-GEKydyLLAVVV--PGEHSFEKEfkltsaIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDR 495
Cdd:PRK12583 484 VPDEKyGEE---IVAWVRlhPGHAASEEE------LREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
149-498 |
3.77e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 87.42 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 IIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMdiY----PsLVTGGTlwAIDKDmIARP 224
Cdd:PRK13295 202 LIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFM--YglmmP-VMLGAT--AVLQD-IWDP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 225 kDLFASLEQSDIQVWT--STPSFAEMCLMEASfSENMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEaTVA 302
Cdd:PRK13295 276 -ARAAELIRTEGVTFTmaSTPFLTDLTRAVKE-SGRPVSSLRTFLCAGAPIPGALVERARAAL-GAKIVSAWGMTE-NGA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 303 VTGIHV--TEEVLDQYKSLPVgyckSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEkaftmIDGERAYK 380
Cdd:PRK13295 352 VTLTKLddPDERASTTDGCPL----PGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG-----TDADGWFD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 381 TGDAGYVE-NGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPI---KKGEKydyLLAVVVPGE-HSFEKE 455
Cdd:PRK13295 423 TGDLARIDaDGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYpdeRLGER---ACAFVVPRPgQSLDFE 499
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446693156 456 fkltsAIKKELNE-RLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK13295 500 -----EMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
3-499 |
4.69e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 87.02 E-value: 4.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIP 80
Cdd:PRK06178 35 LTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRgvGAGDR--VAVFLPNCPQFHIVFFGILKLGAVHVP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 81 VDlsiPADRVQRIA---ENSGAKLLLSATAVTVTDLPVRivSEDNLKDIFFTHKGNT----------------------- 134
Cdd:PRK06178 113 VS---PLFREHELSyelNDAGAEVLLALDQLAPVVEQVR--AETSLRHVIVTSLADVlpaeptlplpdslraprlaaaga 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 135 ------------PNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLV----SFTKWAVEdfnLQTGQVFLNQAPfSF-- 196
Cdd:PRK06178 188 idllpalractaPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVytaaAAYAVAVV---GGEDSVFLSFLP-EFwi 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 197 ---DLSVmdIYPsLVTGGTL-----W-------AIDK---DMIARPKDLFASLEQsdiqvwtsTPSFAEMCL------ME 252
Cdd:PRK06178 264 ageNFGL--LFP-LFSGATLvllarWdavafmaAVERyrvTRTVMLVDNAVELMD--------HPRFAEYDLsslrqvRV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 253 ASFSENMLPNMktflfcgevlpnevaRKLIERFPKATIMNT-YGPTEATVAVT---GIHVTEEVLdqyKSLP--VGYCKS 326
Cdd:PRK06178 333 VSFVKKLNPDY---------------RQRWRALTGSVLAEAaWGMTETHTCDTftaGFQDDDFDL---LSQPvfVGLPVP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 327 DCRLLIMKED-GTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmiDGerAYKTGDAG-YVENGLLFYNGRLDFQIKL 404
Cdd:PRK06178 395 GTEFKICDFEtGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR--DG--WLHTGDIGkIDEQGFLHYLGRRKEMLKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 405 HGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFEKEFKLTSAIKkelnERLPNYMIPrKFMYQSS 484
Cdd:PRK06178 471 NGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCR----ENMAVYKVP-EIRIVDA 545
|
570
....*....|....*
gi 446693156 485 IPMTPNGKVDRKKLL 499
Cdd:PRK06178 546 LPMTATGKVRKQDLQ 560
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
149-496 |
6.29e-18 |
|
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: 84.69 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 IIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKD-----MIAR 223
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNqalaeDLAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 224 PKDLFASLEQSdiQVWTstpsfaemcLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERfpKATIMNTYGPTEatvav 303
Cdd:cd17630 85 PGVTHVSLVPT--QLQR---------LLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTE----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 304 TGIHVTEEVLDQYKSLPVGycksdcRLLimkeDG---TIAPDgekGEIVIVGPSVSVGYLGSPELTEkaftmIDGERAYK 380
Cdd:cd17630 147 TASQVATKRPDGFGRGGVG------VLL----PGrelRIVED---GEIWVGGASLAMGYLRGQLVPE-----FNEDGWFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 381 TGDAGYVE-NGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKK---GEKydyLLAVVVPGEHsfekef 456
Cdd:cd17630 209 TKDLGELHaDGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDeelGQR---PVAVIVGRGP------ 279
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446693156 457 KLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRK 496
Cdd:cd17630 280 ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
2-404 |
7.10e-18 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 86.47 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 2 KLLEQIEKWAAETPDQTAFVWRDA-----KITYKQLKEDSDALAHW-ISSEYPDDRsPIMVYG-----HMQpeMIinfLG 70
Cdd:PRK08180 40 RLTDRLVHWAQEAPDRVFLAERGAdggwrRLTYAEALERVRAIAQAlLDRGLSAER-PLMILSgnsieHAL--LA---LA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 71 CVKAGHAYIPVD-----LSIPADRVQRIAE---------NSGAKLLLSATAVTVTDLPVrIVSEDNLKD---IFFTHKGN 133
Cdd:PRK08180 114 AMYAGVPYAPVSpayslVSQDFGKLRHVLElltpglvfaDDGAAFARALAAVVPADVEV-VAVRGAVPGraaTPFAALLA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 134 TPNPEH------AVKGDENFYIIYTSGSTGNPKGVQITYN--CLVSFTKWAVEDFNLQTGQVFLNQAPFS------FDLS 199
Cdd:PRK08180 193 TPPTAAvdaahaAVGPDTIAKFLFTSGSTGLPKAVINTHRmlCANQQMLAQTFPFLAEEPPVLVDWLPWNhtfggnHNLG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 200 VMdiypsLVTGGTLWaIDKdmiARPkdLFASLEQS-----DIQ--VWTSTPSFAEMCL--ME--ASFSENMLPNMKTFLF 268
Cdd:PRK08180 273 IV-----LYNGGTLY-IDD---GKP--TPGGFDETlrnlrEISptVYFNVPKGWEMLVpaLErdAALRRRFFSRLKLLFY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 269 CGEVLPNEVARKLiERFPKAT------IMNTYGPTEATVAVTGIHVTEEvLDQYKSLPVGYCKsdcrlliMKedgtIAPD 342
Cdd:PRK08180 342 AGAALSQDVWDRL-DRVAEATcgerirMMTGLGMTETAPSATFTTGPLS-RAGNIGLPAPGCE-------VK----LVPV 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 343 GEKGEIVIVGPSVSVGYLGSPELTEKAFtmiDGERAYKTGDAG------YVENGLLFyNGRL--DFqiKL 404
Cdd:PRK08180 409 GGKLEVRVKGPNVTPGYWRAPELTAEAF---DEEGYYRSGDAVrfvdpaDPERGLMF-DGRIaeDF--KL 472
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
5-498 |
5.15e-17 |
|
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: 83.67 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 5 EQIEKwAAETPDQTAFVW-----RDAKITYKQLKEDSDALAHWIS---SEYPDDRspIMVYGHMQPEMIINFLGCVKAGH 76
Cdd:cd05928 16 ADKEK-AGKRPPNPALWWvngkgDEVKWSFRELGSLSRKAANVLSgacGLQRGDR--VAVILPRVPEWWLVNVACIRTGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 77 AYIPVDLSIPADRVQRIAENSGAKLLLS---------ATAVTVTDLPVRIVSEDNLKDIFFTHKG--NTPNPEHA---VK 142
Cdd:cd05928 93 VFIPGTIQLTAKDILYRLQASKAKCIVTsdelapevdSVASECPSLKTKLLVSEKSRDGWLNFKEllNEASTEHHcveTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 143 GDENFYIIYTSGSTGNPKGVQITYNCL-----VSFTKWavedFNLQTGQVFLNQAPFSFDLSVM-DIYPSLVTGGTLWAi 216
Cdd:cd05928 173 SQEPMAIYFTSGTTGSPKMAEHSHSSLglglkVNGRYW----LDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACVFV- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 217 dkDMIAR--PKDLFASLEQSDIQVWTSTPSFAEMcLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERfPKATIMNTY 294
Cdd:cd05928 248 --HHLPRfdPLVILKTLSSYPITTFCGAPTVYRM-LVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQ-TGLDIYEGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 295 GPTEaTVAVTGIHVTEEVldqyKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVI-VGPSVSVG----YLGSPELTEKA 369
Cdd:cd05928 324 GQTE-TGLICANFKGMKI----KPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrVKPIRPFGlfsgYVDNPEKTAAT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 370 ftmIDGErAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHL-RACSYVEGAVIV---PIKkGEKYDYLLaV 444
Cdd:cd05928 399 ---IRGD-FYLTGDRGIMdEDGYFWFMGRADDVINSSGYRIGPFEVESALiEHPAVVESAVVSspdPIR-GEVVKAFV-V 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446693156 445 VVPGEHSFEKEfKLTsaikKELNERLPN----YMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd05928 473 LAPQFLSHDPE-QLT----KELQQHVKSvtapYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
148-499 |
5.35e-17 |
|
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: 83.20 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 148 YIIYTSGSTGNPKGVQITYNClVSFTKWAVEDFNLQTG----QVFLN------QAPFSFDLSVmdiypsLVTGGTLWAID 217
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLPG-GPPDNDTLMAAALGFGpgadSVYLSpaplyhAAPFRWSMTA------LFMGGTLVLME 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 218 KdmiARPKDLFASLEQSDIQVWTSTPS-FAEMC-LMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKaTIMNTYG 295
Cdd:cd05929 202 K---FDPEEFLRLIERYRVTFAQFVPTmFVRLLkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGP-IIWEYYG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 296 PTEAtVAVTGIHvTEEVLDQYKSL--PVGycksdCRLLIMKEDGTIAPDGEKGEIVIVGPSvSVGYLGSPELTEKAFTmi 373
Cdd:cd05929 278 GTEG-QGLTIIN-GEEWLTHPGSVgrAVL-----GKVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARN-- 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 374 dgERAYKT-GDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHS 451
Cdd:cd05929 348 --EGGWSTlGDVGYLdEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGA 425
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446693156 452 FEKEfKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLL 499
Cdd:cd05929 426 DAGT-ALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
149-493 |
6.46e-17 |
|
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: 81.78 E-value: 6.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 IIYTSGSTGNPKGVQITY-NCLVSFTKWAvEDFNLQTGQVFLNQAPF--SFDLSVmDIYPSLVTGGTLWAIdkdMIARPK 225
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHrQTLRAAAAWA-DCADLTEDDRYLIINPFfhTFGYKA-GIVACLLTGATVVPV---AVFDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 226 DLFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTg 305
Cdd:cd17638 80 AILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVATM- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 306 ihvteevldqykslpvgyCK-SDCRLLIMKEDGTIAPD-----GEKGEIVIVGPSVSVGYLGSPELTEKAftmIDGERAY 379
Cdd:cd17638 159 ------------------CRpGDDAETVATTCGRACPGfevriADDGEVLVRGYNVMQGYLDDPEATAEA---IDADGWL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 380 KTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHL-RACSYVEGAVI-VPIKKGEKYDYLLAVVVPGEHSFEKEF 456
Cdd:cd17638 218 HTGDVGELdERGYLRITDRLKDMYIVGGFNVYPAEVEGALaEHPGVAQVAVIgVPDERMGEVGKAFVVARPGVTLTEEDV 297
|
330 340 350
....*....|....*....|....*....|....*..
gi 446693156 457 KLTSaikkelNERLPNYMIPRKFMYQSSIPMTPNGKV 493
Cdd:cd17638 298 IAWC------RERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
149-498 |
7.78e-17 |
|
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: 83.06 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 IIYTSGSTGNPKGVQITYNCLV--SFTKWAVEDFNLQTGQVFLNQAPFsFDLSVMDI-YPSLVTGGTLWAIDKDMiaRPK 225
Cdd:cd12119 168 ICYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVLPGPYL--DPA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 226 DLFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPnevaRKLIERFPKATI--MNTYGPTE----A 299
Cdd:cd12119 245 SLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVP----RSLIEAFEERGVrvIHAWGMTEtsplG 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 300 TVAVTGIHVTEEVLDQ---YKSLPvGYCKSDCRLLIMKEDGTIAP-DGE-KGEIVIVGPSVSVGYLGSPELTEKAFTmiD 374
Cdd:cd12119 321 TVARPPSEHSNLSEDEqlaLRAKQ-GRPVPGVELRIVDDDGRELPwDGKaVGELQVRGPWVTKSYYKNDEESEALTE--D 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 375 GerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHG---YRMELEEIehhLRACSYV-EGAVI-VPIKK-GEKydyLLAVVV- 446
Cdd:cd12119 398 G--WLRTGDVATIdEDGYLTITDRSKDVIKSGGewiSSVELENA---IMAHPAVaEAAVIgVPHPKwGER---PLAVVVl 469
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446693156 447 -PGEHSFEKEfkltsaIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:cd12119 470 kEGATVTAEE------LLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
6-493 |
1.56e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 82.13 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 6 QIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPD--DRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDL 83
Cdd:PRK07786 22 QLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGfgDR--VLILMLNRTEFVESVLAANMLGAIAVPVNF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 84 SIPADRVQRIAENSGAKLLLS-------ATAV--TVTDLPVRIVSEDNLKDIFFTHKG--NTPNPEHA---VKGDENFYI 149
Cdd:PRK07786 100 RLTPPEIAFLVSDCGAHVVVTeaalapvATAVrdIVPLLSTVVVAGGSSDDSVLGYEDllAEAGPAHApvdIPNDSPALI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 150 IYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTG-QVFLNQAPFSFDLSVMDIYPSLVTGGT-----LWAIDkdmiar 223
Cdd:PRK07786 180 MYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINsDVGFVGVPLFHIAGIGSMLPGLLLGAPtviypLGAFD------ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 224 PKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLpNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATvAV 303
Cdd:PRK07786 254 PGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMS-PV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 304 TGIHVTEEVLDQYKSlpVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFtmiDGErAYKTGD 383
Cdd:PRK07786 332 TCMLLGEDAIRKLGS--VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF---AGG-WFHSGD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 384 AGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRA-CSYVEGAVI---------VPIkkgekydyllAVVVPGEHSF 452
Cdd:PRK07786 406 LVRQdEEGYVWVVDRKKDMIISGGENIYCAEVENVLAShPDIVEVAVIgradekwgeVPV----------AVAAVRNDDA 475
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446693156 453 EKEFkltSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKV 493
Cdd:PRK07786 476 ALTL---EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
27-495 |
2.13e-16 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 81.41 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 27 ITYKQLKEDSDALAHWISSE--YPDDRspimVYGHM--QPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKLL 102
Cdd:cd05973 1 LTFGELRALSARFANALQELgvGPGDV----VAGLLprTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 103 lsatavtVTDLpvrivseDNLKDIffthkgntpnpehavkGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNL 182
Cdd:cd05973 77 -------VTDA-------ANRHKL----------------DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 183 QTGQVFLNQAP--FSFDLsvmdiYpSLVTGGTLWAIDKDMIA---RPKDLFASLEQSDIQVWTSTPSFAEMcLMEASFSE 257
Cdd:cd05973 127 RPEDSFWNAADpgWAYGL-----Y-YAITGPLALGHPTILLEggfSVESTWRVIERLGVTNLAGSPTAYRL-LMAAGAEV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 258 NMLP--NMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEATVAVTGIHVTEEVLdqyKSLPVGYCKSDCRLLIMKE 335
Cdd:cd05973 200 PARPkgRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLANHHALEHPV---HAGSAGRAMPGWRVAVLDD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 336 DGTIAPDGEKGEIVI-VGPSVSVGYLGSPELTEKAftmIDGeRAYKTGDAGYVE-NGLLFYNGRLDFQIKLHGYRMELEE 413
Cdd:cd05973 276 DGDELGPGEPGRLAIdIANSPLMWFRGYQLPDTPA---IDG-GYYLTGDTVEFDpDGSFSFIGRADDVITMSGYRIGPFD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 414 IEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEhSFEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKV 493
Cdd:cd05973 352 VESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRG-GHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI 430
|
..
gi 446693156 494 DR 495
Cdd:cd05973 431 QR 432
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
145-494 |
2.27e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 80.50 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 145 ENFYIIYTSGSTGNPKGVQitynclvsftkWAVEDFnlqtGQVFLNQAPFSF-----------------DLSVMDIYP-- 205
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVM-----------WRQEDI----FRMLMGGADFGTgeftpsedahkaaaaaaGTVMFPAPPlm 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 206 ----------SLVTGGTLWAIDKDMiaRPKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSENM--LPNMKTFLFCGEVL 273
Cdd:cd05924 69 hgtgswtafgGLLGGQTVVLPDDRF--DPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPydLSSLFAISSGGALL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 274 PNEVARKLIERFPKATIMNTYGPTEAtvAVTGIHVTEEVLDQYKSlpvgYCKSDCRLLIMKEDGTIAPDGEKGEIVIvGP 353
Cdd:cd05924 147 SPEVKQGLLELVPNITLVDAFGSSET--GFTGSGHSAGSGPETGP----FTRANPDTVVLDDDGRVVPPGSGGVGWI-AR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 354 S--VSVGYLGSPELTEKAFTMIDGERAYKTGD-AGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIV 430
Cdd:cd05924 220 RghIPLGYYGDEAKTAETFPEVDGVRYAVPGDrATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVV 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446693156 431 PIKKgEKYDYLLAVVVPGEHSFEKEfklTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVD 494
Cdd:cd05924 300 GRPD-ERWGQEVVAVVQLREGAGVD---LEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
11-500 |
3.34e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 81.20 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSeypDDRSPIMVYGHMQPEMIiNFLGCVKA----GHAYIPVDLSIP 86
Cdd:PRK13383 45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTR---DGVAPGRAVGVMCRNGR-GFVTAVFAvgllGADVVPISTEFR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 87 ADRVQRIAENSGAKLLLS----ATAVTVTDLPVRIVSEDNLkdiffTHKGNTPNPEHAVKGDenfYIIYTSGSTGNPKGV 162
Cdd:PRK13383 121 SDALAAALRAHHISTVVAdnefAERIAGADDAVAVIDPATA-----GAEESGGRPAVAAPGR---IVLLTSGTTGKPKGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 163 ----QITYNCLVSFTkwAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLwaidkdMIARPKDLFASLEQSDIQv 238
Cdd:PRK13383 193 prapQLRSAVGVWVT--ILDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTV------LTHRHFDAEAALAQASLH- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 239 wtSTPSFAEMCLMEASFSE--------NMLPNMKTFLFCGEVLPNEVARKLIERFPKaTIMNTYGPTEatVAVTGIHVTE 310
Cdd:PRK13383 264 --RADAFTAVPVVLARILElpprvrarNPLPQLRVVMSSGDRLDPTLGQRFMDTYGD-ILYNGYGSTE--VGIGALATPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 311 EVLDQYKSlpVGYCKSDCRLLIMKEDGTiaPDGEK--GEIVIVGPSVSVGYLGSpelTEKAftMIDGERAykTGDAGYVE 388
Cdd:PRK13383 339 DLRDAPET--VGKPVAGCPVRILDRNNR--PVGPRvtGRIFVGGELAGTRYTDG---GGKA--VVDGMTS--TGDMGYLD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 389 N-GLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV-EGAVI-VPikkGEKYDYLLAVVVPGEHSFEKEfklTSAIKKE 465
Cdd:PRK13383 408 NaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVaDNAVIgVP---DERFGHRLAAFVVLHPGSGVD---AAQLRDY 481
|
490 500 510
....*....|....*....|....*....|....*
gi 446693156 466 LNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLS 500
Cdd:PRK13383 482 LKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
11-397 |
3.43e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 81.10 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDAK----------ITYKQLKEDSDALAHWISsEY---PDDRS-----------------------PI 54
Cdd:PRK09274 16 AQERPDQLAVAVPGGRgadgklaydeLSFAELDARSDAIAHGLN-AAgigRGMRAvlmvtpsleffaltfalfkagavPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 55 MVyghmQPEM-IINFLGCVKAGH--AYIPVDLSIPADRVQRIAENSGAKLL-----LSATAVTVTDLPVrivsednlkdi 126
Cdd:PRK09274 95 LV----DPGMgIKNLKQCLAEAQpdAFIGIPKAHLARRLFGWGKPSVRRLVtvggrLLWGGTTLATLLR----------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 127 fftHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAP-FS-FDlsvmdiy 204
Cdd:PRK09274 160 ---DGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPlFAlFG------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 205 PSLvtGGTlwAIDKDMIAR------PKDLFASLEQsdiqvWTSTPSFAEMCLME--ASFSENM---LPNMKTFLFCGEVL 273
Cdd:PRK09274 230 PAL--GMT--SVIPDMDPTrpatvdPAKLFAAIER-----YGVTNLFGSPALLErlGRYGEANgikLPSLRRVISAGAPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 274 PnevaRKLIERF-----PKATIMNTYGPTEAT-VAVTG----IHVTEEVLDQYKSLPVGYCKSDCRLLIMK--------- 334
Cdd:PRK09274 301 P----IAVIERFramlpPDAEILTPYGATEALpISSIEsreiLFATRAATDNGAGICVGRPVDGVEVRIIAisdapipew 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446693156 335 EDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAfTMIDGERA--YKTGDAGYV-ENGLLFYNGR 397
Cdd:PRK09274 377 DDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLA-KIPDGQGDvwHRMGDLGYLdAQGRLWFCGR 441
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
11-498 |
4.21e-16 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 80.96 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDAKITYKQLKEDSDALA---HWISSEYPDdRSPIMVYGHMqpemiinflGCVKA--GHAYIPVDL-- 83
Cdd:PRK13382 53 AQRCPDRPGLIDELGTLTWRELDERSDALAaalQALPIGEPR-VVGIMCRNHR---------GFVEAllAANRIGADIll 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 84 ---SIPADRVQRIAENSGAKLLLSATAVTVT------DLP--VRIVS------EDNLKDIFFTHKGNTPNPehavKGDEN 146
Cdd:PRK13382 123 lntSFAGPALAEVVTREGVDTVIYDEEFSATvdralaDCPqaTRIVAwtdedhDLTVEVLIAAHAGQRPEP----TGRKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 147 FYIIYTSGSTGNPKGVQ-------ITYNCLVSFTKWAVEdfnlqtgQVFLNQAPFSFDLSVMDIYPSLVTGGTlwaidkd 219
Cdd:PRK13382 199 RVILLTSGTTGTPKGARrsgpggiGTLKAILDRTPWRAE-------EPTVIVAPMFHAWGFSQLVLAASLACT------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 220 MIARPK-DLFASLEQSDIQVWTSTPSFAEMC--LMEASfSENMLP----NMKTFLFCGEVLPNEVARKLIERFPKAtIMN 292
Cdd:PRK13382 265 IVTRRRfDPEATLDLIDRHRATGLAVVPVMFdrIMDLP-AEVRNRysgrSLRFAAASGSRMRPDVVIAFMDQFGDV-IYN 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 293 TYGPTEATVAVTGihvTEEVLdqyKSLP--VGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSpelTEKAF 370
Cdd:PRK13382 343 NYNATEAGMIATA---TPADL---RAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 371 tmIDGERAykTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV-EGAVI-VPikkGEKYDYLLAV-VV 446
Cdd:PRK13382 414 --HDGFMA--SGDVGYLdENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVaEAAVIgVD---DEQYGQRLAAfVV 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446693156 447 PGEHSFEKEfkltSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK13382 487 LKPGASATP----ETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
11-504 |
5.60e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 80.24 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFV-------WrdakiTYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDL 83
Cdd:PRK09088 5 ARLQPQRLAAVdlalgrrW-----TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 84 SIPADRVQRIAENSGAKLLLSATAVTVTdlpvRIVSEDnLKDIFFTHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQ 163
Cdd:PRK09088 80 RLSASELDALLQDAEPRLLLGDDAVAAG----RTDVED-LAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 164 ITYNCLvsftKWAVEDFNLqTGQV-----FLNQAP-FSFDLSVMDIYPSLVTGGTLWAIDKdmiARPKDLFASLEQSDIQ 237
Cdd:PRK09088 155 LSERNL----QQTAHNFGV-LGRVdahssFLCDAPmFHIIGLITSVRPVLAVGGSILVSNG---FEPKRTLGRLGDPALG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 238 V--WTSTPSFAEMCLMEASFSENMLPNMkTFLFCGEVlPN---EVARKLIERFPkatIMNTYGPTEATVaVTGIHVTEEV 312
Cdd:PRK09088 227 IthYFCVPQMAQAFRAQPGFDAAALRHL-TALFTGGA-PHaaeDILGWLDDGIP---MVDGFGMSEAGT-VFGMSVDCDV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 313 LDQyKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmidGERAYKTGDA------GY 386
Cdd:PRK09088 301 IRA-KAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFT---GDGWFRTGDIarrdadGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 387 VenglLFYNGRLDFQIK--LHGYRMELEEI--EH-HLRACsyvegAVI-VPIKKGEKYDYLLAVVVPGEHSfekefkLTS 460
Cdd:PRK09088 377 F----WVVDRKKDMFISggENVYPAEIEAVlaDHpGIREC-----AVVgMADAQWGEVGYLAIVPADGAPL------DLE 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446693156 461 AIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVdRKKLLSEVTA 504
Cdd:PRK09088 442 RIRSHLSTRLAKYKVPKHLRLVDALPRTASGKL-QKARLRDALA 484
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
21-491 |
5.98e-16 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 80.58 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 21 VWRDAKITYKQLKEDSDALAHWISSE---YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENS 97
Cdd:cd17632 62 LPRFETITYAELWERVGAVAAAHDPEqpvRPGDF--VAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAET 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 98 GAKLLlsatAVTVTDLPV------------RIV-----------------SEDNLKDIFFTHKGNT------------PN 136
Cdd:cd17632 140 EPRLL----AVSAEHLDLaveavleggtppRLVvfdhrpevdahraalesARERLAAVGIPVTTLTliavrgrdlppaPL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 137 PEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAV--EDFNLQTGqVFLNQAPFSFDLSVMDIYPSLVTGGTLW 214
Cdd:cd17632 216 FRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSsiQDIRPPAS-ITLNFMPMSHIAGRISLYGTLARGGTAY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 215 -AIDKDM--------IARPK---------DLFASLEQSDIQVWTSTPSFAEMCLME--ASFSENMLPNMKTFLFCGEVLP 274
Cdd:cd17632 295 fAAASDMstlfddlaLVRPTelflvprvcDMLFQRYQAELDRRSVAGADAETLAERvkAELRERVLGGRLLAAVCGSAPL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 275 NEVARKLIERFPKATIMNTYGPTEA-TVAVTGIHVTEEVLDqYKSLPV---GYCKSDcrllimkedgtiAPDgEKGEIVI 350
Cdd:cd17632 375 SAEMKAFMESLLDLDLHDGYGSTEAgAVILDGVIVRPPVLD-YKLVDVpelGYFRTD------------RPH-PRGELLV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 351 VGPSVSVGYLGSPELTEKAFtmiDGERAYKTGDA-GYVENGLLFYNGRLDFQIKLHgyRMELEEIEhHLRAcSYVEGAVI 429
Cdd:cd17632 441 KTDTLFPGYYKRPEVTAEVF---DEDGFYRTGDVmAELGPDRLVYVDRRNNVLKLS--QGEFVTVA-RLEA-VFAASPLV 513
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446693156 430 VPI---KKGEKyDYLLAVVVPGEHSFEKE--FKLTSAIKKELNE-----RLPNYMIPRKFMYQSSiPMTP-NG 491
Cdd:cd17632 514 RQIfvyGNSER-AYLLAVVVPTQDALAGEdtARLRAALAESLQRiareaGLQSYEIPRDFLIETE-PFTIaNG 584
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
10-502 |
7.58e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 79.65 E-value: 7.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 10 WAAETPDQTAFVWR--DAKITYKQLKEDSDALAHWISseypdDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPA 87
Cdd:PRK07787 7 AAVAAAADIADAVRigGRVLSRSDLAGAATAVAERVA-----GARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 88 DRVQRIAENSGAKLLLSATAVTVTDLPVRIVSEDNLKDifftHKGNTPNPEHAVkgdenfYIIYTSGSTGNPKGVQI--- 164
Cdd:PRK07787 82 AERRHILADSGAQAWLGPAPDDPAGLPHVPVRLHARSW----HRYPEPDPDAPA------LIVYTSGTTGPPKGVVLsrr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 165 ----TYNCLVSFTKWAVED--------FN-----------LQTGQVFLNQAPFSFDlsvmDIYPSLVTGGTLWAIDKDM- 220
Cdd:PRK07787 152 aiaaDLDALAEAWQWTADDvlvhglplFHvhglvlgvlgpLRIGNRFVHTGRPTPE----AYAQALSEGGTLYFGVPTVw 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 221 --IARPKDLFASLEQSDIQVWTSTPsfaemclmeasfsenmLPnmktfLFCGEVLPNEVARKLIERfpkatimntYGPTE 298
Cdd:PRK07787 228 srIAADPEAARALRGARLLVSGSAA----------------LP-----VPVFDRLAALTGHRPVER---------YGMTE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 299 aTVAVTGIHVTEEVLDQYKSLPVGycksDCRLLIMKEDGTIAP-DGEK-GEIVIVGPSVSVGYLGSPELTEKAFTMiDGe 376
Cdd:PRK07787 278 -TLITLSTRADGERRPGWVGLPLA----GVETRLVDEDGGPVPhDGETvGELQVRGPTLFDGYLNRPDATAAAFTA-DG- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 377 rAYKTGDAGYVE-NGLLFYNGR--LDFqIKLHGYRMELEEIEHHLRACSYV-EGAVIvpikkGEKYDYL----LAVVVPG 448
Cdd:PRK07787 351 -WFRTGDVAVVDpDGMHRIVGResTDL-IKSGGYRIGAGEIETALLGHPGVrEAAVV-----GVPDDDLgqriVAYVVGA 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446693156 449 EHSFEKEfkLTSAIKKEL--NERlpnymiPRKFMYQSSIPMTPNGKVDRKKLLSEV 502
Cdd:PRK07787 424 DDVAADE--LIDFVAQQLsvHKR------PREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
142-498 |
1.01e-15 |
|
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: 79.43 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 142 KGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQV----FLNQAPFSFDLSVMDIYPslvtggtlwAID 217
Cdd:cd05910 83 KADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVdlatFPLFALFGPALGLTSVIP---------DMD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 218 KDMIAR--PKDLFASLEQsdiqvWTSTPSFAEMCLME--ASFSENM---LPNMKTFLFCGEVLPNEVA---RKLIErfPK 287
Cdd:cd05910 154 PTRPARadPQKLVGAIRQ-----YGVSIVFGSPALLErvARYCAQHgitLPSLRRVLSAGAPVPIALAarlRKMLS--DE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 288 ATIMNTYGPTEA-TVAVTGIH----VTEEVLDQYKSLPVGYCKSDCRLLIMK-EDGTIA--------PDGEKGEIVIVGP 353
Cdd:cd05910 227 AEILTPYGATEAlPVSSIGSRellaTTTAATSGGAGTCVGRPIPGVRVRIIEiDDEPIAewddtlelPRGEIGEITVTGP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 354 SVSVGYLGSPELTekAFTMIDGERA---YKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVI 429
Cdd:cd05910 307 TVTPTYVNRPVAT--ALAKIDDNSEgfwHRMGDLGYLdDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAL 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446693156 430 VPI-KKGEKYDYLlaVVVPGEHSFEKEFKLTSAIkKELNERLPNYMIPRKFMYQSSIPMTP--NGKVDRKKL 498
Cdd:cd05910 385 VGVgKPGCQLPVL--CVEPLPGTITPRARLEQEL-RALAKDYPHTQRIGRFLIHPSFPVDIrhNAKIFREKL 453
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
3-504 |
2.22e-15 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 78.56 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEY---PDDRSPIMVYGHMQ-PemiINFLGCVKAGHA- 77
Cdd:PRK08974 25 LVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLglkKGDRVALMMPNLLQyP---IALFGILRAGMIv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 78 ------YIPVDL---------------SIPADRVQRIAENSGAKL--------LLSATAVTVTDLPV----RIVSEDNLK 124
Cdd:PRK08974 102 vnvnplYTPRELehqlndsgakaivivSNFAHTLEKVVFKTPVKHviltrmgdQLSTAKGTLVNFVVkyikRLVPKYHLP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 125 D-IFFT---HKGNTPN---PEhaVKGDENFYIIYTSGSTGNPKGVQITYNCLVSF---TKWAVEDFnLQTGQVFLNQApf 194
Cdd:PRK08974 182 DaISFRsalHKGRRMQyvkPE--LVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqAKAAYGPL-LHPGKELVVTA-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 195 sfdLSVMDIYPslVTGGTLWAIDKD----MIARPKDLFA---SLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKtfL 267
Cdd:PRK08974 257 ---LPLYHIFA--LTVNCLLFIELGgqnlLITNPRDIPGfvkELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLK--L 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 268 FCGEVLPneVARKLIERFPKAT---IMNTYGPTEATVAVTGIHVTeevLDQYKS---LPVGycKSDCRllIMKEDGTIAP 341
Cdd:PRK08974 330 SVGGGMA--VQQAVAERWVKLTgqyLLEGYGLTECSPLVSVNPYD---LDYYSGsigLPVP--STEIK--LVDDDGNEVP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 342 DGEKGEIVIVGPSVSVGYLGSPELTEKAFTmiDGERAykTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRA 420
Cdd:PRK08974 401 PGEPGELWVKGPQVMLGYWQRPEATDEVIK--DGWLA--TGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVML 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 421 CSYV-EGAVI-VPIK-KGEKydyLLAVVVPGEHSFEKEfkltsAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKK 497
Cdd:PRK08974 477 HPKVlEVAAVgVPSEvSGEA---VKIFVVKKDPSLTEE-----ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRE 548
|
....*..
gi 446693156 498 LLSEVTA 504
Cdd:PRK08974 549 LRDEARA 555
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
147-495 |
2.95e-15 |
|
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: 76.92 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 147 FYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFsfdLSVMDIYPSLVT---GGTLWAIDK-Dmia 222
Cdd:cd17637 3 FVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPL---FHIAGLNLALATfhaGGANVVMEKfD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 223 rPKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLfcGEVLPNEVARklIERFPKATIMNTYGPTEATVA 302
Cdd:cd17637 77 -PAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVL--GLDAPETIQR--FEETTGATFWSLYGQTETSGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 303 VTGIHVTEEVLDQYKSLPVgycksdCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmiDGerAYKTG 382
Cdd:cd17637 152 VTLSPYRERPGSAGRPGPL------VRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFR--NG--WHHTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 383 DAGYV-ENGLLFYNGR-----LdfqIKLHGYRMELEEIEHHLRACSYVEGAVI--VPIKK-GEKydyLLAVVV--PGEHS 451
Cdd:cd17637 222 DLGRFdEDGYLWYAGRkpekeL---IKPGGENVYPAEVEKVILEHPAIAEVCVigVPDPKwGEG---IKAVCVlkPGATL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446693156 452 FEKEfkLTSAIKkelnERLPNYMIPRKFMYQSSIPMTPNGKVDR 495
Cdd:cd17637 296 TADE--LIEFVG----SRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
62-504 |
3.34e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 78.10 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 62 PEMIINFLGCVKAGHAYIPVD-LSIPADrVQRIAENSGAKLLL--SATAVTVTDLP----VRIVSEDNLKD--IFF---T 129
Cdd:PLN02246 86 PEFVLAFLGASRRGAVTTTANpFYTPAE-IAKQAKASGAKLIItqSCYVDKLKGLAeddgVTVVTIDDPPEgcLHFselT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 130 HKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVE----DFNLQTGQVFLNQAP----FSFDlSVM 201
Cdd:PLN02246 165 QADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDgenpNLYFHSDDVILCVLPmfhiYSLN-SVL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 202 diYPSLVTGGTLwaidkdMIARPKDLFASLEQsdIQVWTST-PSFAEMCLMEASFSENM----LPNMKTFLFCGEVLPNE 276
Cdd:PLN02246 244 --LCGLRVGAAI------LIMPKFEIGALLEL--IQRHKVTiAPFVPPIVLAIAKSPVVekydLSSIRMVLSGAAPLGKE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 277 VARKLIERFPKATIMNTYGPTEA-TVAVTGIHVTEEVLDqYKSlpvGYCKSDCRLLIMK----EDGTIAPDGEKGEIVIV 351
Cdd:PLN02246 314 LEDAFRAKLPNAVLGQGYGMTEAgPVLAMCLAFAKEPFP-VKS---GSCGTVVRNAELKivdpETGASLPRNQPGEICIR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 352 GPSVSVGYLGSPELTEKAftmIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIV 430
Cdd:PLN02246 390 GPQIMKGYLNDPEATANT---IDKDGWLHTGDIGYIdDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVV 466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446693156 431 PIKKGEKYDYLLAVVV--PGEHSFEKEfkltsaIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSEVTA 504
Cdd:PLN02246 467 PMKDEVAGEVPVAFVVrsNGSEITEDE------IKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKLAA 536
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
125-504 |
3.47e-15 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 77.92 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 125 DIFFTHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLV--SFTKWAVEDFNlqTGQVFLNQAPF------Sf 196
Cdd:PLN02860 153 EMLKQRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIvqSLAKIAIVGYG--EDDVYLHTAPLchigglS- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 197 dlSVMDIypsLVTGGTLWAIDKdmiARPKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSEN--MLPNMKTFLFCGEVLP 274
Cdd:PLN02860 230 --SALAM---LMVGACHVLLPK---FDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTwkVFPSVRKILNGGGSLS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 275 NEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYK--------------SLPVGYC--KSDCRLLIMkedgt 338
Cdd:PLN02860 302 SRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLESPKqtlqtvnqtksssvHQPQGVCvgKPAPHVELK----- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 339 IAPDGEK--GEIVIVGPSVSVGYLGSPELTEKAFTmidGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIE 415
Cdd:PLN02860 377 IGLDESSrvGRILTRGPHVMLGYWGQNSETASVLS---NDGWLDTGDIGWIdKAGNLWLIGRSNDRIKTGGENVYPEEVE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 416 HHLRACSYVEGAVIVPIKKGEKYDYLLAVV--------VPGEH-SFEKEFKLTSAIKK----ELNerLPNYMIPRKFM-Y 481
Cdd:PLN02860 454 AVLSQHPGVASVVVVGVPDSRLTEMVVACVrlrdgwiwSDNEKeNAKKNLTLSSETLRhhcrEKN--LSRFKIPKLFVqW 531
|
410 420
....*....|....*....|...
gi 446693156 482 QSSIPMTPNGKVDRKKLLSEVTA 504
Cdd:PLN02860 532 RKPFPLTTTGKIRRDEVRREVLS 554
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
3-398 |
4.45e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 77.85 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVW------RDA---KITYKQLKEDSDALAHWISS-EYPDDRSPIMVYGHMqpEMIINFLGCV 72
Cdd:PRK07769 23 LVRHVERWAKVRGDKLAYRFldfsteRDGvarDLTWSQFGARNRAVGARLQQvTKPGDRVAILAPQNL--DYLIAFFGAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 73 KAGHAYIPV-DLSIP--ADRVQRIAENSGAKLLLSATAVT------VTDLPV----RIVSEDNLKDifftHKGNT---PN 136
Cdd:PRK07769 101 YAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAegvrkfFRARPAkerpRVIAVDAVPD----EVGATwvpPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 137 PEHavkgDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLS-VMDIYPSLVTGGTLWA 215
Cdd:PRK07769 177 ANE----DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGlITVLLPALLGHYITFM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 216 IDKDMIARP----KDLfASLEQSDIQVWTSTPSFA-EMCLMEASFSENMLP----NMKTFLFCGEVLPNEVARKLIERF- 285
Cdd:PRK07769 253 SPAAFVRRPgrwiREL-ARKPGGTGGTFSAAPNFAfEHAAARGLPKDGEPPldlsNVKGLLNGSEPVSPASMRKFNEAFa 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 286 ----PKATIMNTYGPTEAT--VAVTG-------IHVTEEVLDQYKSLPV-------------GYCKSDCRLLIMK-EDGT 338
Cdd:PRK07769 332 pyglPPTAIKPSYGMAEATlfVSTTPmdeeptvIYVDRDELNAGRFVEVpadapnavaqvsaGKVGVSEWAVIVDpETAS 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446693156 339 IAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMI--------------DGERAYKTGDAGYVENGLLFYNGRL 398
Cdd:PRK07769 412 ELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNIlksrlseshaegapDDALWVRTGDYGVYFDGELYITGRV 485
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
3-498 |
4.61e-15 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 77.74 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRD--AKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIP 80
Cdd:PRK05857 16 VLDRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 81 VDLSIPADRVQRIAE---------NSGAKLLLSATAVTVTDLPVrIVSEDNLKDIFFTHKGNT--PNPEHAVKGDENFYI 149
Cdd:PRK05857 96 ADGNLPIAAIERFCQitdpaaalvAPGSKMASSAVPEALHSIPV-IAVDIAAVTRESEHSLDAasLAGNADQGSEDPLAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 150 IYTSGSTGNPKGVqitynCLVSFTKWAVEDFNLQTGqvfLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDM----IARPK 225
Cdd:PRK05857 175 IFTSGTTGEPKAV-----LLANRTFFAVPDILQKEG---LNWVTWVVGETTYSPLPATHIGGLWWILTCLMhgglCVTGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 226 DLFASLEQ--SDIQVWTS--TPSFAEMCLMEASFSENMLPNMKTFLFCG-EVLPNEVarklieRFPKATIMNT---YGPT 297
Cdd:PRK05857 247 ENTTSLLEilTTNAVATTclVPTLLSKLVSELKSANATVPSLRLVGYGGsRAIAADV------RFIEATGVRTaqvYGLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 298 EATVAVTGIHVTEEVLDQYKSLPVGYCKSDCRLLIMKEDG------TIAPDGEKGEIVIVGPSVSVGYLGSPELTEKafT 371
Cdd:PRK05857 321 ETGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPERTAE--V 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 372 MIDGerAYKTGD-AGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEkYDYL--LAVVVPG 448
Cdd:PRK05857 399 LIDG--WVNTGDlLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEE-FGALvgLAVVASA 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 446693156 449 EHSFEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK05857 476 ELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
3-498 |
5.11e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 77.55 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE---YPDDR----------SPIMVYGHMQPEMII--- 66
Cdd:PRK12492 26 VVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtdlVPGDRiavqmpnvlqYPIAVFGALRAGLIVvnt 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 67 NFLGCV-------KAGHAYIPVDLSIPADRVQRIAENSGAKLLLSAT------------AVTVTDLPVRIVSEDNL---- 123
Cdd:PRK12492 106 NPLYTAremrhqfKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKmgdllpaakgwlVNTVVDKVKKMVPAYHLpqav 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 124 --KDIFFTHKGNTPNPeHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQ--TGQVFLNQ------AP 193
Cdd:PRK12492 186 pfKQALRQGRGLSLKP-VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpDGQPLMKEgqevmiAP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 194 ------FSFDLSVMDIypsLVTGGtlwaiDKDMIARPKDLFASLEQsdIQVWtstpSFAEMCLMEASFSENM-LPNMKTF 266
Cdd:PRK12492 265 lplyhiYAFTANCMCM---MVSGN-----HNVLITNPRDIPGFIKE--LGKW----RFSALLGLNTLFVALMdHPGFKDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 267 LFCGEVLPNEVARKLI----ERFPKAT---IMNTYGPTEAT-VAVTGIHVTEEVLDQykslpVGYCKSDCRLLIMKEDGT 338
Cdd:PRK12492 331 DFSALKLTNSGGTALVkataERWEQLTgctIVEGYGLTETSpVASTNPYGELARLGT-----VGIPVPGTALKVIDDDGN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 339 IAPDGEKGEIVIVGPSVSVGYLGSPELTEKAftmIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHH 417
Cdd:PRK12492 406 ELPLGERGELCIKGPQVMKGYWQQPEATAEA---LDAEGWFKTGDIAVIdPDGFVRIVDRKKDLIIVSGFNVYPNEIEDV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 418 LRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFEKEfkltsAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKK 497
Cdd:PRK12492 483 VMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVE-----ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRE 557
|
.
gi 446693156 498 L 498
Cdd:PRK12492 558 L 558
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
11-498 |
9.57e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 76.50 E-value: 9.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVYGHMqpEMIINFLGCVKAGHAYIPVDLSIPAD 88
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALgvRAGDGVAVLARNHR--GFVLALYAAGKVGARIILLNTGFSGP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 89 RVQRIAENSGAKL---------LLSATAVTVTDLPVRIVSEDNLK---------DIFFTHKGNTPNPEHAVKGdenFYII 150
Cdd:PRK07788 137 QLAEVAAREGVKAlvyddeftdLLSALPPDLGRLRAWGGNPDDDEpsgstdetlDDLIAGSSTAPLPKPPKPG---GIVI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 151 YTSGSTGNPKGVQITYncLVSFTKWA--VEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLwaidkdmIAR----P 224
Cdd:PRK07788 214 LTSGTTGTPKGAPRPE--PSPLAPLAglLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTV-------VLRrrfdP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 225 KDLFASLEQSDIQVWTSTPSFAEMCLMEAsfsENMLPNMKT----FLFC-GEVLPNEVARKLIERFPKaTIMNTYGPTEA 299
Cdd:PRK07788 285 EATLEDIAKHKATALVVVPVMLSRILDLG---PEVLAKYDTsslkIIFVsGSALSPELATRALEAFGP-VLYNLYGSTEV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 300 TVAVTGihvTEEVLDQYKSL----PVGycksdCRLLIMKEDGTIAPDGEKGEIvIVGPSVSV-GYLG--SPEltekaftM 372
Cdd:PRK07788 361 AFATIA---TPEDLAEAPGTvgrpPKG-----VTVKILDENGNEVPRGVVGRI-FVGNGFPFeGYTDgrDKQ-------I 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 373 IDGERAykTGDAGYV-ENGLLFYNGRLDFQIKLHG---YRMELEE-IEHHlraCSYVEGAVI-VPIKkgEKYDYLLAVVV 446
Cdd:PRK07788 425 IDGLLS--SGDVGYFdEDGLLFVDGRDDDMIVSGGenvFPAEVEDlLAGH---PDVVEAAVIgVDDE--EFGQRLRAFVV 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446693156 447 PGEHSfekefKLTS-AIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK07788 498 KAPGA-----ALDEdAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
11-498 |
1.41e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 75.82 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRDA--KITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPAD 88
Cdd:PRK13390 7 AQIAPDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 89 RVQRIAENSGAKLLLSATAV------TVTDLPVRIV---SEDNLKDIFFTHKGNTP----NPEHAVkgdenfyIIYTSGS 155
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALdglaakVGADLPLRLSfggEIDGFGSFEAALAGAGPrlteQPCGAV-------MLYSSGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 156 TGNPKGVQitynclVSFTKWAVEdfnlQTGQVFLNQAPFSFDLSVMDIYPSLVT----------------GGTLwaidkd 219
Cdd:PRK13390 160 TGFPKGIQ------PDLPGRDVD----APGDPIVAIARAFYDISESDIYYSSAPiyhaaplrwcsmvhalGGTV------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 220 MIARPKDLFASL---EQSDIQVWTSTPS-FAEMCLMEASF-SENMLPNMKTFLFCGEVLPNEVARKLIErFPKATIMNTY 294
Cdd:PRK13390 224 VLAKRFDAQATLghvERYRITVTQMVPTmFVRLLKLDADVrTRYDVSSLRAVIHAAAPCPVDVKHAMID-WLGPIVYEYY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 295 GPTEA---TVAVTGihvteevldQYKSLPVGYCKSDC-RLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKA- 369
Cdd:PRK13390 303 SSTEAhgmTFIDSP---------DWLAHPGSVGRSVLgDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAq 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 370 ------FTMIdgerayktGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLL 442
Cdd:PRK13390 374 hpahpfWTTV--------GDLGSVdEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVK 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446693156 443 AVV--VPGEHSFEKefkLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK13390 446 AVIqlVEGIRGSDE---LARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
137-498 |
1.76e-14 |
|
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: 75.64 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 137 PEHAVKGDENFYIIYTSGSTGNPKGVQITY-NCLVSFTKWAVEDFNLQT--GQVFLNQAPFSFDLSVMDIYPSLVTGGTL 213
Cdd:cd17642 177 PPSFDRDEQVALIMNSSGSTGLPKGVQLTHkNIVARFSHARDPIFGNQIipDTAILTVIPFHHGFGMFTTLGYLICGFRV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 214 WAIDKdmiARPKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNT 293
Cdd:cd17642 257 VLMYK---FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 294 YGPTEATVAVTgihVTEEVLDQY----KSLPVGYCKsdcrlLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEka 369
Cdd:cd17642 334 YGLTETTSAIL---ITPEGDDKPgavgKVVPFFYAK-----VVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATK-- 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 370 fTMIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVV-- 446
Cdd:cd17642 404 -ALIDKDGWLHSGDIAYYdEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVle 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446693156 447 PGEHSFEKEFKLTSAIKKELNERLPNYMIprkfmYQSSIPMTPNGKVDRKKL 498
Cdd:cd17642 483 AGKTMTEKEVMDYVASQVSTAKRLRGGVK-----FVDEVPKGLTGKIDRRKI 529
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
77-498 |
6.05e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 73.96 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 77 AY-IPVDLSIPADRVQRIAENSGAKLLL--------------SATAVTVTDLPVRIVSEDNLKDIFFTHKGNT------- 134
Cdd:PRK12406 61 AYaVPVNWHFKPEEIAYILEDSGARVLIahadllhglasalpAGVTVLSVPTPPEIAAAYRISPALLTPPAGAidwegwl 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 135 ----PNPEHAVKGDENfyIIYTSGSTGNPKGVQ---ITYNCLVSFTKWAVEDFNLQTGQVFL------NQAPFSFDLSvm 201
Cdd:PRK12406 141 aqqePYDGPPVPQPQS--MIYTSGTTGHPKGVRraaPTPEQAAAAEQMRALIYGLKPGIRALltgplyHSAPNAYGLR-- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 202 diypSLVTGGTLWaidkdMIAR--PKDLFASLEQSDIQVWTSTPS-FAE-MCLMEASFSENMLPNMKTFLFCGEVLPNEV 277
Cdd:PRK12406 217 ----AGRLGGVLV-----LQPRfdPEELLQLIERHRITHMHMVPTmFIRlLKLPEEVRAKYDVSSLRHVIHAAAPCPADV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 278 ARKLIERF-PkaTIMNTYGPTEaTVAVTGiHVTEEVLDqyKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVS 356
Cdd:PRK12406 288 KRAMIEWWgP--VIYEYYGSTE-SGAVTF-ATSEDALS--HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNP 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 357 -VGYLGSPEltekAFTMIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKK 434
Cdd:PRK12406 362 dFTYHNKPE----KRAEIDRGGFITSGDVGYLdADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPD 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446693156 435 GEKYDYLLAVVVPgehsfEKEFKL-TSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK12406 438 AEFGEALMAVVEP-----QPGATLdEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
132-497 |
6.45e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 74.27 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 132 GNTPNPEHAVKGDENFyIIYTSGSTGNPKGVQITYNCLVSftkwavedfNLQTGQ-----------VFLNQAPF--SFDL 198
Cdd:PRK05605 208 GSDVSHPRPTPDDVAL-ILYTSGTTGKPKGAQLTHRNLFA---------NAAQGKawvpglgdgpeRVLAALPMfhAYGL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 199 SvMDIYPSLVTGGTLW---AIDKDMIARpkdlfasleqsdiQVWTSTPSFAEMC------LMEASFSENM-LPNMKtFLF 268
Cdd:PRK05605 278 T-LCLTLAVSIGGELVllpAPDIDLILD-------------AMKKHPPTWLPGVpplyekIAEAAEERGVdLSGVR-NAF 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 269 CGEV-LPNEvarkLIERFPKAT---IMNTYGPTEATVAVTGIHVTEEVLDQYKSLPvgYCKSDCRLLIMKEDGTIAPDGE 344
Cdd:PRK05605 343 SGAMaLPVS----TVELWEKLTgglLVEGYGLTETSPIIVGNPMSDDRRPGYVGVP--FPDTEVRIVDPEDPDETMPDGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 345 KGEIVIVGPSVSVGYLGSPELTEKAFTmiDGerAYKTGDAGYVE-NGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSY 423
Cdd:PRK05605 417 EGELLVRGPQVFKGYWNRPEETAKSFL--DG--WFRTGDVVVMEeDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPG 492
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446693156 424 VEGAVIVPIKKGEKYDYLLAVVVPGEHS-FEKEfkltsAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKK 497
Cdd:PRK05605 493 VEDAAVVGLPREDGSEEVVAAVVLEPGAaLDPE-----GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRRE 562
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
14-498 |
8.70e-14 |
|
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: 73.89 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 14 TPDQTAFVWRDA------KITYKQLKEDSDALA-----HWISSeypDDRspIMVYGHMQPEMIINFLGCVKAG--HAYI- 79
Cdd:cd05967 64 RGDQIALIYDSPvtgterTYTYAELLDEVSRLAgvlrkLGVVK---GDR--VIIYMPMIPEAAIAMLACARIGaiHSVVf 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 80 ----PVDLSipadrvQRIaENSGAKLLLSATA---------------------------VTVTDLP-VRIVSEDNLKDIF 127
Cdd:cd05967 139 ggfaAKELA------SRI-DDAKPKLIVTASCgiepgkvvpykplldkalelsghkphhVLVLNRPqVPADLTKPGRDLD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 128 FTH--KGNTPNPEHAVKGDENFYIIYTSGSTGNPKGV---------------QITYNCLVSFTKWAVEDFNLQTGQVFLN 190
Cdd:cd05967 212 WSEllAKAEPVDCVPVAATDPLYILYTSGTTGKPKGVvrdngghavalnwsmRNIYGIKPGDVWWAASDVGWVVGHSYIV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 191 QAPFSFDL-SVMdiYPSLVTG----GTLW-AIDKDMIARpkdLFAS------LEQSDIQVwtstpSFAEMCLMEAsfsen 258
Cdd:cd05967 292 YGPLLHGAtTVL--YEGKPVGtpdpGAFWrVIEKYQVNA---LFTAptairaIRKEDPDG-----KYIKKYDLSS----- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 259 mlpnMKTFLFCGEVLPNEVARKLIERFPKAtIMNTYGPTEATVAVTGIHVTEEVLD-----QYKSLPvGYcksdcRLLIM 333
Cdd:cd05967 357 ----LRTLFLAGERLDPPTLEWAENTLGVP-VIDHWWQTETGWPITANPVGLEPLPikagsPGKPVP-GY-----QVQVL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 334 KEDGTIAPDGEKGEIVIVGP---SVSVGYLGSPELTEKA-FTMIDGerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYR 408
Cdd:cd05967 426 DEDGEPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKLyLSKFPG--YYDTGDAGYKdEDGYLFIMGRTDDVINVAGHR 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 409 MELEEIEHHLraCSY---VEGAVI-VPIK-KGEkydYLLAVVVPGEHSFEKEFKLTSAIKKELNERLPNYMIPRKFMYQS 483
Cdd:cd05967 504 LSTGEMEESV--LSHpavAECAVVgVRDElKGQ---VPLGLVVLKEGVKITAEELEKELVALVREQIGPVAAFRLVIFVK 578
|
570
....*....|....*
gi 446693156 484 SIPMTPNGKVDRKKL 498
Cdd:cd05967 579 RLPKTRSGKILRRTL 593
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
135-504 |
2.86e-13 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 72.37 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 135 PNPEHAVKGDENFYIIYTSGSTGNPKGVqITYNCLVsFT----------KWAVEDFNLQTGQVFlnqapFSFDLSVMDIY 204
Cdd:PRK06060 136 PGGYEPMGGDALAYATYTSGTTGPPKAA-IHRHADP-LTfvdamcrkalRLTPEDTGLCSARMY-----FAYGLGNSVWF 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 205 PsLVTGGTLWAIDKDMIAR-PKDLFASLEQSdiqVWTSTPSFaeMCLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIE 283
Cdd:PRK06060 209 P-LATGGSAVINSAPVTPEaAAILSARFGPS---VLYGVPNF--FARVIDSCSPDSFRSLRCVVSAGEALELGLAERLME 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 284 RFPKATIMNTYGPTEatvavTGIHVTEEVLDQYKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSP 363
Cdd:PRK06060 283 FFGGIPILDGIGSTE-----VGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 364 EltekafTMIDGERAYKTGDAGYVE-NGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLL 442
Cdd:PRK06060 358 D------SPVANEGWLDTRDRVCIDsDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQ 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446693156 443 AVVVPGEHSFEKEfKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSEVTA 504
Cdd:PRK06060 432 AFLVATSGATIDG-SVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPT 492
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
16-501 |
3.44e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 71.72 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 16 DQTAFVWRDAKITYKQLKEDSDALAHWISSEY---PDDR----------SPIMVYGHMQPEMIInflgcVKAGHAYIP-- 80
Cdd:PRK05677 39 DKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTdlkPGDRiavqlpnvlqYPVAVFGAMRAGLIV-----VNTNPLYTAre 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 81 -------------VDLSIPADRVQRIAENSGAK----------------LLLSATA------VTVTDLPVRIvsedNLKD 125
Cdd:PRK05677 114 mehqfndsgakalVCLANMAHLAEKVLPKTGVKhvivtevadmlpplkrLLINAVVkhvkkmVPAYHLPQAV----KFND 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 126 IFFTHKGNTPNPEhAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSF---TKWAVEDfNLQTG-QVFLNQAP----FSFD 197
Cdd:PRK05677 190 ALAKGAGQPVTEA-NPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGS-NLNEGcEILIAPLPlyhiYAFT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 198 LSVMDIypsLVTGGtlwaiDKDMIARPKDLFASLEqsDIQVWTST------PSFAEMCLMEAsFSENMLPNMKTFLFCGE 271
Cdd:PRK05677 268 FHCMAM---MLIGN-----HNILISNPRDLPAMVK--ELGKWKFSgfvglnTLFVALCNNEA-FRKLDFSALKLTLSGGM 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 272 VLPNEVArkliERFPKAT---IMNTYGPTEATVAVTgIHVTEEVLDQYKSLPV--GYCKsdcrllIMKEDGTIAPDGEKG 346
Cdd:PRK05677 337 ALQLATA----ERWKEVTgcaICEGYGMTETSPVVS-VNPSQAIQVGTIGIPVpsTLCK------VIDDDGNELPLGEVG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 347 EIVIVGPSVSVGYLGSPELTEKaftMIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV- 424
Cdd:PRK05677 406 ELCVKGPQVMKGYWQRPEATDE---ILDSDGWLKTGDIALIqEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVl 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446693156 425 EGAVI-VPIKKGEKYDYLLAVVVPGEhSFEKEfkltsAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSE 501
Cdd:PRK05677 483 QCAAIgVPDEKSGEAIKVFVVVKPGE-TLTKE-----QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDE 554
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
137-498 |
3.58e-13 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 71.83 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 137 PEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVS----FTKWAVEDFNLQTGQVFLNQApfsfdLSVMDIYPSLVTGGT 212
Cdd:PRK08751 201 PTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVAnmqqAHQWLAGTGKLEEGCEVVITA-----LPLYHIFALTANGLV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 213 LWAID--KDMIARPKDL---FASLEQSDIQVWTSTPSFAEMCLMEASFSENMLPNMKTFLFCGEVlpneVARKLIERFPK 287
Cdd:PRK08751 276 FMKIGgcNHLISNPRDMpgfVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMA----VQRSVAERWKQ 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 288 AT---IMNTYGPTEATVAVTgihVTEEVLDQYKSlPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPE 364
Cdd:PRK08751 352 VTgltLVEAYGLTETSPAAC---INPLTLKEYNG-SIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 365 LTEKAftmIDGERAYKTGD-AGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVE--GAVIVPikkGEKYDYL 441
Cdd:PRK08751 428 ETAKV---MDADGWLHTGDiARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLevAAVGVP---DEKSGEI 501
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446693156 442 LAVVVpgehsFEKEFKLTSA-IKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK08751 502 VKVVI-----VKKDPALTAEdVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
11-398 |
4.73e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 71.51 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVWRD---------AKITYKQLKEDSDALAHWISSE-YPDDRSPIMVyghmqP---EMIINFLGCVKAGha 77
Cdd:PRK05850 11 ASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHgSTGDRAVILA-----PqglEYIVAFLGALQAG-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 78 YIPVDLSIPA-----DRVQRIAENSGAKLLL--SATAVTVTDL-------PVRIVSEDNLKDIffthkgNTPNPEHAVKG 143
Cdd:PRK05850 84 LIAVPLSVPQggahdERVSAVLRDTSPSVVLttSAVVDDVTEYvapqpgqSAPPVIEVDLLDL------DSPRGSDARPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 144 D--ENFYIIYTSGSTGNPKGVQITY-NCLVSFTKwAVEDFNLQTGQV------FLNQAPFSFDLSVM-DIYPSLVTGgtl 213
Cdd:PRK05850 158 DlpSTAYLQYTSGSTRTPAGVMVSHrNVIANFEQ-LMSDYFGDTGGVpppdttVVSWLPFYHDMGLVlGVCAPILGG--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 214 waidkdmiaRPKDL---FASLEQ---------SDIQVWTSTPSFA-EMCLMEASfSENM----LPNMKTFLFCGE-VLPN 275
Cdd:PRK05850 234 ---------CPAVLtspVAFLQRparwmqllaSNPHAFSAAPNFAfELAVRKTS-DDDMagldLGGVLGIISGSErVHPA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 276 EVaRKLIERF-----PKATIMNTYGPTEATVAV-TGI--HVTEEVLDQYKSLPVGY---CKSD--CRLL----------- 331
Cdd:PRK05850 304 TL-KRFADRFapfnlRETAIRPSYGLAEATVYVaTREpgQPPESVRFDYEKLSAGHakrCETGggTPLVsygsprsptvr 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446693156 332 IMKEDGTI-APDGEKGEIVIVGPSVSVGYLGSPELTEKAF-TMIDGERA-------YKTGDAGYVENGLLFYNGRL 398
Cdd:PRK05850 383 IVDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERTFgATLVDPSPgtpegpwLRTGDLGFISEGELFIVGRI 458
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
3-498 |
5.11e-13 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 71.20 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVYGHMQ-PemiINFLGCVKAGHAYI 79
Cdd:PRK07059 25 LADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRglAKGARVAIMMPNVLQyP---VAIAAVLRAGYVVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 80 PVD-LSIPADRVQRIaENSGAK--LLLSATAVTV------TDLP---------------------VRIV----------S 119
Cdd:PRK07059 102 NVNpLYTPRELEHQL-KDSGAEaiVVLENFATTVqqvlakTAVKhvvvasmgdllgfkghivnfvVRRVkkmvpawslpG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 120 EDNLKDIFFTHKGNTPNPEHAVKGDENFyIIYTSGSTGNPKGVQITYNCLVS------------FTKWA-VEDFNlqtgq 186
Cdd:PRK07059 181 HVRFNDALAEGARQTFKPVKLGPDDVAF-LQYTGGTTGVSKGATLLHRNIVAnvlqmeawlqpaFEKKPrPDQLN----- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 187 vFLNQAPFS--FDLSVMDIYpSLVTGGTlwaidKDMIARPKD---LFASLEQSDIQVWTSTPSFAEMCLMEASFSENMLP 261
Cdd:PRK07059 255 -FVCALPLYhiFALTVCGLL-GMRTGGR-----NILIPNPRDipgFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 262 NMKTFLFCGEVLPNEVArkliERFPKAT---IMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVgyckSDCRLLIMKEDGT 338
Cdd:PRK07059 328 KLIVANGGGMAVQRPVA----ERWLEMTgcpITEGYGLSETSPVATCNPVDATEFSGTIGLPL----PSTEVSIRDDDGN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 339 IAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMiDGerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHH 417
Cdd:PRK07059 400 DLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTA-DG--FFRTGDVGVMdERGYTKIVDRKKDMILVSGFNVYPNEIEEV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 418 LRACSYV-EGAvivpikkgekydyllAVVVPGEHSFE--------KEFKLTSA-IKKELNERLPNYMIPRKFMYQSSIPM 487
Cdd:PRK07059 477 VASHPGVlEVA---------------AVGVPDEHSGEavklfvvkKDPALTEEdVKAFCKERLTNYKRPKFVEFRTELPK 541
|
570
....*....|.
gi 446693156 488 TPNGKVDRKKL 498
Cdd:PRK07059 542 TNVGKILRREL 552
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
148-495 |
6.82e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 70.93 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 148 YIIYTSGSTGNPKGVqITYN-----CLVSFTKWAVEDfnlQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDmIA 222
Cdd:PTZ00237 258 YILYTSGTTGNSKAV-VRSNgphlvGLKYYWRSIIEK---DIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGG-II 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 223 RPK----DLFASLEQSDIQVWTSTPSFAEMCLMEASFSENM-----LPNMKTFLFCGEVLPNEVArKLIERFPKATIMNT 293
Cdd:PTZ00237 333 KNKhiedDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIrskydLSNLKEIWCGGEVIEESIP-EYIENKLKIKSSRG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 294 YGPTEatVAVTGIHVTEEVLDQYKS--LPVGYCKSdcrlLIMKEDGTIAPDGEKGEIVI---VGPSVSVGYLGSPELTEK 368
Cdd:PTZ00237 412 YGQTE--IGITYLYCYGHINIPYNAtgVPSIFIKP----SILSEDGKELNVNEIGEVAFklpMPPSFATTFYKNDEKFKQ 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 369 AFTMIDGerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIE----HH---LRACSyvegaviVPIKKGEKYDY 440
Cdd:PTZ00237 486 LFSKFPG--YYNSGDLGFKdENGYYTIVSRSDDQIKISGNKVQLNTIEtsilKHplvLECCS-------IGIYDPDCYNV 556
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446693156 441 LLAVVV---PGEHSFEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDR 495
Cdd:PTZ00237 557 PIGLLVlkqDQSNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
3-501 |
8.65e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 70.39 E-value: 8.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAaetpDQTAFV--WRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIP 80
Cdd:PLN02330 34 VLQDAELYA----DKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 81 VDLSIPADRVQRIAENSGAKLLLSATA----VTVTDLPVRIVSED------NLKDIFFT--HKGNTPNPEHAVKGDEnFY 148
Cdd:PLN02330 110 ANPTALESEIKKQAEAAGAKLIVTNDTnygkVKGLGLPVIVLGEEkiegavNWKELLEAadRAGDTSDNEEILQTDL-CA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 IIYTSGSTGNPKGVQITYNCLVSftKWAVEDFNLQT---GQVF-LNQAPFSFDLSVMDI-YPSLVTGGTLWAIDK----- 218
Cdd:PLN02330 189 LPFSSGTTGISKGVMLTHRNLVA--NLCSSLFSVGPemiGQVVtLGLIPFFHIYGITGIcCATLRNKGKVVVMSRfelrt 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 219 ---DMIARPKDlFASLEQSDIQVWTSTPSFAEMCLMEASfsenmlpnMKTFLFCGEVLPNEVARKLIERFPKATIMNTYG 295
Cdd:PLN02330 267 flnALITQEVS-FAPIVPPIILNLVKNPIVEEFDLSKLK--------LQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 296 PTEATvAVTGIHVT-EEVLDQYKSLPVGYCKSDCRL-LIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAftmI 373
Cdd:PLN02330 338 LTEHS-CITLTHGDpEKGHGIAKKNSVGFILPNLEVkFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRT---I 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 374 DGERAYKTGDAGYVEN-GLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSF 452
Cdd:PLN02330 414 DEDGWLHTGDIGYIDDdGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAK 493
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 446693156 453 EKEfkltSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRkKLLSE 501
Cdd:PLN02330 494 ESE----EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMR-RLLKE 537
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
27-498 |
9.45e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 70.32 E-value: 9.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 27 ITYKQLKEDSDALAHWISSE--YPDDRSPIMVYGHmqPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKLLLS 104
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALglREGDVVAILLENN--PEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 105 ----------ATAVTVTDLPVRIV---------SEDNLKDIFFThkgnTPNPEHAVKGDenfyIIYTSGSTGNPKGV--- 162
Cdd:PRK08276 90 saaladtaaeLAAELPAGVPLLLVvagpvpgfrSYEEALAAQPD----TPIADETAGAD----MLYSSGTTGRPKGIkrp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 163 ----QITYNCLVsFTKWAVEDFNLQTGQVFLNQAPF------SFDLSVMDIypslvtGGTLWAIDK-DmiarPKDLFASL 231
Cdd:PRK08276 162 lpglDPDEAPGM-MLALLGFGMYGGPDSVYLSPAPLyhtaplRFGMSALAL------GGTVVVMEKfD----AEEALALI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 232 EQSDIQVWTSTPS-FAEMC-LMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERF-PkaTIMNTYGPTEA---TVAVTg 305
Cdd:PRK08276 231 ERYRVTHSQLVPTmFVRMLkLPEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWgP--IIHEYYASSEGggvTVITS- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 306 ihvtEEVLDQYKSlpVGycKS-DCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAftmiDGERAYKT-GD 383
Cdd:PRK08276 308 ----EDWLAHPGS--VG--KAvLGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAA----RNPHGWVTvGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 384 AGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV-EGAVI-VPIKK-GEKydyLLAVVVPGEhSFEKEFKLT 459
Cdd:PRK08276 376 VGYLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVaDVAVFgVPDEEmGER---VKAVVQPAD-GADAGDALA 451
|
490 500 510
....*....|....*....|....*....|....*....
gi 446693156 460 SAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK08276 452 AELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
149-406 |
9.67e-13 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 70.46 E-value: 9.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 IIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQV----FLNQAPFSF-DLSVMDIYPSLVTGGTLWAIDKDMI-- 221
Cdd:cd05933 155 LIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesVVSYLPLSHiAAQILDIWLPIKVGGQVYFAQPDALkg 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 222 --------ARPKDLFA------SLEQSDIQVWTSTPSFAEMCL---MEASFSEN---MLPNMKTFLFCGevlpneVARKL 281
Cdd:cd05933 235 tlvktlreVRPTAFMGvprvweKIQEKMKAVGAKSGTLKRKIAswaKGVGLETNlklMGGESPSPLFYR------LAKKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 282 I-ERFPKA-----------------------------TIMNTYGPTEATvavtGIHvTEEVLDQYKSLPVGYCKSDCRLL 331
Cdd:cd05933 309 VfKKVRKAlgldrcqkfftgaapisretlefflslniPIMELYGMSETS----GPH-TISNPQAYRLLSCGKALPGCKTK 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446693156 332 IMKEDGtiapDGEkGEIVIVGPSVSVGYLGSPELTEKAftmIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHG 406
Cdd:cd05933 384 IHNPDA----DGI-GEICFWGRHVFMGYLNMEDKTEEA---IDEDGWLHSGDLGKLdEDGFLYITGRIKELIITAG 451
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
19-454 |
1.04e-12 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 70.32 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 19 AFVWrdakITYKQLKEDSDALAHWISSEY--PDDRSPIMVYGHMQPEMIINFLGCVkaGHAYIPVDL--SIPADRVQRIA 94
Cdd:cd05927 2 PYEW----ISYKEVAERADNIGSALRSLGgkPAPASFVGIYSINRPEWIISELACY--AYSLVTVPLydTLGPEAIEYIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 95 ENSGAKLLlsatavtVTDLPVRIVSEDNLKDIFFTHKGNTPNPehavKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTK 174
Cdd:cd05927 76 NHAEISIV-------FCDAGVKVYSLEEFEKLGKKNKVPPPPP----KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 175 wAVEDFNLQTGQVFLNQAPFSFdLSVMDIYPSLVTGGTLWA--------------IDKDMIARPkDLFASLE-------- 232
Cdd:cd05927 145 -GVFKILEILNKINPTDVYISY-LPLAHIFERVVEALFLYHgakigfysgdirllLDDIKALKP-TVFPGVPrvlnriyd 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 233 --QSDIQvwtSTPSFAEMCLmeasfseNMLPNMKTF-LFCGEVLPNEVARKLI--------------------------E 283
Cdd:cd05927 222 kiFNKVQ---AKGPLKRKLF-------NFALNYKLAeLRSGVVRASPFWDKLVfnkikqalggnvrlmltgsaplspevL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 284 RFPKAT----IMNTYGPTEATVAVTGIHVTEEVLDQYKSlPVGYCksDCRLLIMKEDGTIAPDGE-KGEIVIVGPSVSVG 358
Cdd:cd05927 292 EFLRVAlgcpVLEGYGQTECTAGATLTLPGDTSVGHVGG-PLPCA--EVKLVDVPEMNYDAKDPNpRGEVCIRGPNVFSG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 359 YLGSPELTEKAFTmIDGerAYKTGDAgyvenGLLFYNGRLdfQI--------KL-HGYRMELEEIEHHLRACSYVeGAVI 429
Cdd:cd05927 369 YYKDPEKTAEALD-EDG--WLHTGDI-----GEWLPNGTL--KIidrkknifKLsQGEYVAPEKIENIYARSPFV-AQIF 437
|
490 500
....*....|....*....|....*.
gi 446693156 430 VpikKGEKY-DYLLAVVVPGEHSFEK 454
Cdd:cd05927 438 V---YGDSLkSFLVAIVVPDPDVLKE 460
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
12-498 |
1.55e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 69.92 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 12 AETP--DQTAFVWRDA----KITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAG-------H 76
Cdd:PRK04319 53 ADGGrkDKVALRYLDAsrkeKYTYKELKELSNKFANVLKELgvEKGDR--VFIFMPRIPELYFALLGALKNGaivgplfE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 77 AYIPVDLsipADRVqriaENSGAKLLlsataVTVTDLPVRIVSED--NLKDIFFT--HKGNTPN----PEHAVKGDENFY 148
Cdd:PRK04319 131 AFMEEAV---RDRL----EDSEAKVL-----ITTPALLERKPADDlpSLKHVLLVgeDVEEGPGtldfNALMEQASDEFD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 II-----------YTSGSTGNPKGVQITYNCLVsfTKWavedfnlQTGQVFLnqapfsfDLSVMDIY-----PSLVTgGT 212
Cdd:PRK04319 199 IEwtdredgailhYTSGSTGKPKGVLHVHNAML--QHY-------QTGKYVL-------DLHEDDVYwctadPGWVT-GT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 213 LWAIdkdmIA---------------RPKDLFASLEQSDIQVWTSTPSFAEMcLMEAS---FSENMLPNMKTFLFCGEVLP 274
Cdd:PRK04319 262 SYGI----FApwlngatnvidggrfSPERWYRILEDYKVTVWYTAPTAIRM-LMGAGddlVKKYDLSSLRHILSVGEPLN 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 275 NEVARKLIERFPKaTIMNTYGPTEatvavTGIHvteeVLDQYKSLPV--GyckSDCRLL------IMKEDGTIAPDGEKG 346
Cdd:PRK04319 337 PEVVRWGMKVFGL-PIHDNWWMTE-----TGGI----MIANYPAMDIkpG---SMGKPLpgieaaIVDDQGNELPPNRMG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 347 EIVI-VG-PSVSVGYLGSPELTEKAFtmIDGerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRM---ELEE--IEHHL 418
Cdd:PRK04319 404 NLAIkKGwPSMMRGIWNNPEKYESYF--AGD--WYVSGDSAYMdEDGYFWFQGRVDDVIKTSGERVgpfEVESklMEHPA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 419 RAcsyvEGAVIvpikkGeKYDYLLAVVVPGEHSFEKEFKLTSAIKKEL----NERLPNYMIPRKFMYQSSIPMTPNGKVD 494
Cdd:PRK04319 480 VA----EAGVI-----G-KPDPVRGEIIKAFVALRPGYEPSEELKEEIrgfvKKGLGAHAAPREIEFKDKLPKTRSGKIM 549
|
....
gi 446693156 495 RKKL 498
Cdd:PRK04319 550 RRVL 553
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
135-498 |
1.97e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 69.49 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 135 PNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVS----FTKWAVEDF-NLQTGQVFLNQAP----FSFDLSVMdiyp 205
Cdd:PLN02574 189 FVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAmvelFVRFEASQYeYPGSDNVYLAALPmfhiYGLSLFVV---- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 206 SLVTGGTLWAIDKDMIArpKDLFASLEQSDIQVWTSTPSFAeMCLMEASFSENMLPNMKTFLFCGEVLPneVARKLIERF 285
Cdd:PLN02574 265 GLLSLGSTIVVMRRFDA--SDMVKVIDRFKVTHFPVVPPIL-MALTKKAKGVCGEVLKSLKQVSCGAAP--LSGKFIQDF 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 286 ----PKATIMNTYGPTEATvAVTGIHVTEEVLDQYKSlpVGYCKSDCRLLIMK-EDGTIAPDGEKGEIVIVGPSVSVGYL 360
Cdd:PLN02574 340 vqtlPHVDFIQGYGMTEST-AVGTRGFNTEKLSKYSS--VGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 361 GSPELTEkafTMIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYD 439
Cdd:PLN02574 417 NNPKATQ---STIDKDGWLRTGDIAYFdEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGE 493
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446693156 440 YLLAVVVPGEHSFEKEFKLTSAIKKELNErlpnYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PLN02574 494 IPVAFVVRRQGSTLSQEAVINYVAKQVAP----YKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
142-498 |
2.30e-12 |
|
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: 69.17 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 142 KGDENFYIIYTSGSTGNPKGVQITYNCLVS----FTKWAVEDFNLQtgQVFLNQAPFS--FDLSVMDIypSLVTGGTLWa 215
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAgiagLGDRVPELLGPD--DRYLAYLPLAhiFELAAENV--CLYRGGTIG- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 216 idkdmIARPKDLFASL---EQSDI------------QVWTS----------TPSFAEMCLMEASFS--ENMLPNMKTFLF 268
Cdd:cd17639 161 -----YGSPRTLTDKSkrgCKGDLtefkptlmvgvpAIWDTirkgvlaklnPMGGLKRTLFWTAYQskLKALKEGPGTPL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 269 CGEVLPNEVaRKLI------------------ERFPK---ATIMNTYGPTEaTVAVTGIHVTEEVLDQYKSLPVGYCksD 327
Cdd:cd17639 236 LDELVFKKV-RAALggrlrymlsggaplsadtQEFLNivlCPVIQGYGLTE-TCAGGTVQDPGDLETGRVGPPLPCC--E 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 328 CRLLIMKEDGTIAPDGE-KGEIVIVGPSVSVGYLGSPELTEKAFtmiDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKL- 404
Cdd:cd17639 312 IKLVDWEEGGYSTDKPPpRGEILIRGPNVFKGYYKNPEKTKEAF---DGDGWFHTGDIGEFhPDGTLKIIDRKKDLVKLq 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 405 HGYRMELEEIEHHLRACSYVEG--AVIVPIKkgekyDYLLAVVVPGEHSFEK----------EF-------KLTSAIKKE 465
Cdd:cd17639 389 NGEYIALEKLESIYRSNPLVNNicVYADPDK-----SYPVAIVVPNEKHLTKlaekhgvinsEWeelcedkKLQKAVLKS 463
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446693156 466 LNE-----RLPNYMIPRKFMYqSSIPMTP-NG------KVDRKKL 498
Cdd:cd17639 464 LAEtaraaGLEKFEIPQGVVL-LDEEWTPeNGlvtaaqKLKRKEI 507
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
152-503 |
2.48e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 68.87 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 152 TSGSTGNPKGVQITYNCLVSFTKWAVE--DFNLQTGqVFLNQAPFSFDLSVMD--IYPsLVTGGTLWAIdkdmiaRPKDL 227
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVaaEFDVETD-VMVSWLPLFHDMGMVGflTVP-MYFGAELVKV------TPMDF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 228 FAsleqsDIQVW-----------TSTPSFAEMCL--------MEASFSenmLPNMKTFLFCGEVLPNEVARKLIE---RF 285
Cdd:PRK07768 232 LR-----DPLLWaeliskyrgtmTAAPNFAYALLarrlrrqaKPGAFD---LSSLRFALNGAEPIDPADVEDLLDagaRF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 286 --PKATIMNTYGPTEATVAV------TGIHVTE---EVLD-QYKSLPV-----------GYCKSDCRLLIMKEDGTIAPD 342
Cdd:PRK07768 304 glRPEAILPAYGMAEATLAVsfspcgAGLVVDEvdaDLLAaLRRAVPAtkgntrrlatlGPPLPGLEVRVVDEDGQVLPP 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 343 GEKGEIVIVGPSVSVGYlgspeLTEKAF-TMIDGERAYKTGDAGY-VENGLLFYNGRLDFQIKLHGYRMELEEIEhhlRA 420
Cdd:PRK07768 384 RGVGVIELRGESVTPGY-----LTMDGFiPAQDADGWLDTGDLGYlTEEGEVVVCGRVKDVIIMAGRNIYPTDIE---RA 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 421 CSYVEG-----AVIVPIKKGEKYDYLLAVVVPGEHSFEKEFK-----LTSAIKKELNERlpnymiPRK--FMYQSSIPMT 488
Cdd:PRK07768 456 AARVEGvrpgnAVAVRLDAGHSREGFAVAVESNAFEDPAEVRrirhqVAHEVVAEVGVR------PRNvvVLGPGSIPKT 529
|
410
....*....|....*
gi 446693156 489 PNGKVDRKKLLSEVT 503
Cdd:PRK07768 530 PSGKLRRANAAELVT 544
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
8-501 |
1.62e-11 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 66.44 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 8 EKWAAETPDQTAFVWRDakitykqLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIP----- 80
Cdd:PRK07514 17 DAPFIETPDGLRYTYGD-------LDAASARLANLLVALgvKPGDR--VAVQVEKSPEALALYLATLRAGAVFLPlntay 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 81 ----VDLSI----PA---------DRVQRIAENSGAKLLLSATAVTVTDLPVRivsEDNLKDIFFTHkgntpnpehAVKG 143
Cdd:PRK07514 88 tlaeLDYFIgdaePAlvvcdpanfAWLSKIAAAAGAPHVETLDADGTGSLLEA---AAAAPDDFETV---------PRGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 144 DENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPfsfdlsvmdIYPS----LVTGGTLWAIDKd 219
Cdd:PRK07514 156 DDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALP---------IFHThglfVATNVALLAGAS- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 220 MIARPK----DLFASLEQSdiQVWTSTPSFAEMCLMEASFSENMLPNMKTFLfCGEV-LPNEVARKLIERFPKA------ 288
Cdd:PRK07514 226 MIFLPKfdpdAVLALMPRA--TVMMGVPTFYTRLLQEPRLTREAAAHMRLFI-SGSApLLAETHREFQERTGHAileryg 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 289 ---TIMNTYGPTE-----ATV--AVTGihVTEEVLDQykslpvgycksdcrllimkEDGTIAPDGEKGEIVIVGPSVSVG 358
Cdd:PRK07514 303 mteTNMNTSNPYDgerraGTVgfPLPG--VSLRVTDP-------------------ETGAELPPGEIGMIEVKGPNVFKG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 359 YLGSPELTEKAFTMiDGerAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV-EGAVI-VPIKK- 434
Cdd:PRK07514 362 YWRMPEKTAEEFRA-DG--FFITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVvESAVIgVPHPDf 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446693156 435 GEKydyLLAVVVPgehsfEKEFKLT-SAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVdRKKLLSE 501
Cdd:PRK07514 439 GEG---VTAVVVP-----KPGAALDeAAILAALKGRLARFKQPKRVFFVDELPRNTMGKV-QKNLLRE 497
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
29-397 |
3.15e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 65.80 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 29 YKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGhaYIPVDLSIPA---------DRVQRIAENS 97
Cdd:PRK09192 52 YQTLRARAEAGARRLLALglKPGDR--VALIAETDGDFVEAFFACQYAG--LVPVPLPLPMgfggresyiAQLRGMLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 98 GAKLLLS--------ATAVTVTDLPVRIVSED-NLKDiffthKGNTPNPEhaVKGDENFYIIYTSGSTGNPKGVQITYNC 168
Cdd:PRK09192 128 QPAAIITpdellpwvNEATHGNPLLHVLSHAWfKALP-----EADVALPR--PTPDDIAYLQYSSGSTRFPRGVIITHRA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 169 LVSFTKWAVED-FNLQTGQVFLNQAPFSFD-------LSVMDIYPS---LVTGG-----TLWAidkDMIARPKdlfASLE 232
Cdd:PRK09192 201 LMANLRAISHDgLKVRPGDRCVSWLPFYHDmglvgflLTPVATQLSvdyLPTRDfarrpLQWL---DLISRNR---GTIS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 233 QSdiqvwtstPSFA-EMCLMEASFSENMLPNMKTFLFCG---EVLPNEVARKLIERFPKA-----TIMNTYGPTEATVAV 303
Cdd:PRK09192 275 YS--------PPFGyELCARRVNSKDLAELDLSCWRVAGigaDMIRPDVLHQFAEAFAPAgfddkAFMPSYGLAEATLAV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 304 T------GIH---VTEEVL-DQYKSLPVGY----------CKS---DCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYL 360
Cdd:PRK09192 347 SfsplgsGIVveeVDRDRLeYQGKAVAPGAetrrvrtfvnCGKalpGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYF 426
|
410 420 430
....*....|....*....|....*....|....*..
gi 446693156 361 GSPElTEKAFtMIDGerAYKTGDAGYVENGLLFYNGR 397
Cdd:PRK09192 427 RDEE-SQDVL-AADG--WLDTGDLGYLLDGYLYITGR 459
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
11-498 |
8.59e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 63.94 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 11 AAETPDQTAFVW--RDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVYGHmqPEMIINFLGCVKAGHAYIPVDLSIP 86
Cdd:PRK13391 7 AQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLglKRGDHVAIFMENN--LRYLEVCWAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 87 ADRVQRIAENSGAKLLL--SATAVTVTDLPVRI--VSEDNLKDIFFTHKGNTPNPEhAVKG-------DENF--YIIYTS 153
Cdd:PRK13391 85 PAEAAYIVDDSGARALItsAAKLDVARALLKQCpgVRHRLVLDGDGELEGFVGYAE-AVAGlpatpiaDESLgtDMLYSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 154 GSTGNPKGVQITYNCLVSFTKWAVEDF-----NLQTGQVFLNQAPF--SFDLSVMDIYPSLvtGGTLWAIDK-DmiarPK 225
Cdd:PRK13391 164 GTTGRPKGIKRPLPEQPPDTPLPLTAFlqrlwGFRSDMVYLSPAPLyhSAPQRAVMLVIRL--GGTVIVMEHfD----AE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 226 DLFASLEQSDIQVWTSTPS-FAEMC-LMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERF-PkaTIMNTYGPTEAtVA 302
Cdd:PRK13391 238 QYLALIEEYGVTHTQLVPTmFSRMLkLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWgP--IIHEYYAATEG-LG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 303 VTGIHvTEEVLDQYKSlpVGycksdcRLL-----IMKEDGTIAPDGEKGEIVIVGPSvSVGYLGSPELTEKAfTMIDGER 377
Cdd:PRK13391 315 FTACD-SEEWLAHPGT--VG------RAMfgdlhILDDDGAELPPGEPGTIWFEGGR-PFEYLNDPAKTAEA-RHPDGTW 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 378 AyKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV-EGAVI-VPIKK-GEKydyLLAVVVPGEHSfe 453
Cdd:PRK13391 384 S-TVGDIGYVdEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVaDAAVFgVPNEDlGEE---VKAVVQPVDGV-- 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 446693156 454 kefKLTSAIKKEL----NERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK13391 458 ---DPGPALAAELiafcRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
332-498 |
1.53e-10 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 63.47 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 332 IMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFtmiDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRME 410
Cdd:PRK10946 367 VADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAF---DANGFYCSGDLVSIdPDGYITVVGREKDQINRGGEKIA 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 411 LEEIEHHLRACSYVEGAVIVPIKK---GEKYdylLAVVVPGEhsfekEFKlTSAIKKELNER-LPNYMIPRKFMYQSSIP 486
Cdd:PRK10946 444 AEEIENLLLRHPAVIHAALVSMEDelmGEKS---CAFLVVKE-----PLK-AVQLRRFLREQgIAEFKLPDRVECVDSLP 514
|
170
....*....|..
gi 446693156 487 MTPNGKVDRKKL 498
Cdd:PRK10946 515 LTAVGKVDKKQL 526
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
27-498 |
1.65e-10 |
|
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: 62.97 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 27 ITYKQLKEDSDALAHWISSE--YPDDRSPIMVYGhmQPEMIINFLGCVKAGHAYIPvdlsipadrvqriaensgAKLLLS 104
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIgvGRGDRILLMLGN--VVELWEAMLAAMKLGAVVIP------------------ATTLLT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 105 AtavtvtdlpvrivseDNLKDIFFTHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCL----VSFTKWavedF 180
Cdd:cd05974 61 P---------------DDLRDRVDRGGAVYAAVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYpvghLSTMYW----I 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 181 NLQTGQVFLN-QAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIaRPKDLFASLEQSDIQVWTSTPSFAEMcLMEASFSENM 259
Cdd:cd05974 122 GLKPGDVHWNiSSPGWAKHAWSCFFAPWNAGATVFLFNYARF-DAKRVLAALVRYGVTTLCAPPTVWRM-LIQQDLASFD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 260 LPnMKTFLFCGEVLPNEVarklIERFPKA---TIMNTYGPTEATVAVT---GIHVTEEVLDqyKSLPvGYcksdcRLLIM 333
Cdd:cd05974 200 VK-LREVVGAGEPLNPEV----IEQVRRAwglTIRDGYGQTETTALVGnspGQPVKAGSMG--RPLP-GY-----RVALL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 334 KEDGTIAPDGEK----GEIVIVGpsVSVGYLGSPELTEKAftMIDGEraYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYR 408
Cdd:cd05974 267 DPDGAPATEGEValdlGDTRPVG--LMKGYAGDPDKTAHA--MRGGY--YRTGDIAMRdEDGYLTYVGRADDVFKSSDYR 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 409 M---ELEE--IEHHLracsyVEGAVIVPIKKGEKYDYLLAVVVPGEhSFEKEFKLTSAIKKELNERLPNYMIPRKFMYqS 483
Cdd:cd05974 341 IspfELESvlIEHPA-----VAEAAVVPSPDPVRLSVPKAFIVLRA-GYEPSPETALEIFRFSRERLAPYKRIRRLEF-A 413
|
490
....*....|....*
gi 446693156 484 SIPMTPNGKVDRKKL 498
Cdd:cd05974 414 ELPKTISGKIRRVEL 428
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
144-404 |
1.83e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 63.58 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 144 DENFY--IIYTSGSTGNPKGVQIT----YNCLVSFTKWAV-EDFNLQTGQVFLnqaPFSFDLSVMDIYPSLVTGGTLWAI 216
Cdd:PTZ00342 302 DPDFItsIVYTSGTSGKPKGVMLSnknlYNTVVPLCKHSIfKKYNPKTHLSYL---PISHIYERVIAYLSFMLGGTINIW 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 217 DKDMIARPKDLFASLEQ-------------SDIQVWTSTPSFAEMCLME-----------ASFS---ENML--------- 260
Cdd:PTZ00342 379 SKDINYFSKDIYNSKGNilagvpkvfnriyTNIMTEINNLPPLKRFLVKkilslrksnnnGGFSkflEGIThisskikdk 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 261 --PNMKTFLFCGEVLPNEVARKLierfpkATIMNT-----YGPTEATVAVTGIHVTeevldqykslpvgycksDCRLLIM 333
Cdd:PTZ00342 459 vnPNLEVILNGGGKLSPKIAEEL------SVLLNVnyyqgYGLTETTGPIFVQHAD-----------------DNNTESI 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 334 keDGTIAPDGE----------------KGEIVIVGPSVSVGYLGSPELTEKAFTMiDGerAYKTGDAGYV-ENGLLFYNG 396
Cdd:PTZ00342 516 --GGPISPNTKykvrtwetykatdtlpKGELLIKSDSIFSGYFLEKEQTKNAFTE-DG--YFKTGDIVQInKNGSLTFLD 590
|
....*...
gi 446693156 397 RLDFQIKL 404
Cdd:PTZ00342 591 RSKGLVKL 598
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
7-498 |
3.30e-10 |
|
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: 62.32 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAGHAYIPVDLS 84
Cdd:cd12118 10 LERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALgiSRGDT--VAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 85 IPADRVQRIAENSGAKLLLSATAVTVTDLpvriVSEDNlkdiffthkgntPNPEHAVKGDENFYII--YTSGSTGNPKGV 162
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLFVDREFEYEDL----LAEGD------------PDFEWIPPADEWDPIAlnYTSGTTGRPKGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 163 QITY-----NCLVsftkwAVEDFNLQTGQVFLNQAP------FSFDLSVMDIypslvtGGTLWAIDKdmiARPKDLFASL 231
Cdd:cd12118 152 VYHHrgaylNALA-----NILEWEMKQHPVYLWTLPmfhcngWCFPWTVAAV------GGTNVCLRK---VDAKAIYDLI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 232 EQSDIQVWTSTPSFAEMCLMEASFSENMLPNmKTFLFCGEVLPNEVARKLIER--FpkaTIMNTYGPTEatvaVTGIHVT 309
Cdd:cd12118 218 EKHKVTHFCGAPTVLNMLANAPPSDARPLPH-RVHVMTAGAPPPAAVLAKMEElgF---DVTHVYGLTE----TYGPATV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 310 EEVLDQYKSLP------------VGYCKSDCRLLIMKEDGTIAP-DGEK-GEIVIVGPSVSVGYLGSPELTEKAFTmiDG 375
Cdd:cd12118 290 CAWKPEWDELPteerarlkarqgVRYVGLEEVDVLDPETMKPVPrDGKTiGEIVFRGNIVMKGYLKNPEATAEAFR--GG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 376 erAYKTGDAGYVENgllfyNGRLDFQ-----IKLHG----YRMELEEIEHHLRACsyVEGAVI-VPIKK-GEKydyLLAV 444
Cdd:cd12118 368 --WFHSGDLAVIHP-----DGYIEIKdrskdIIISGgeniSSVEVEGVLYKHPAV--LEAAVVaRPDEKwGEV---PCAF 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446693156 445 VVPGEHSFEKEFKLTSAIKkelnERLPNYMIPRKFMYqSSIPMTPNGKVDRKKL 498
Cdd:cd12118 436 VELKEGAKVTEEEIIAFCR----EHLAGFMVPKTVVF-GELPKTSTGKIQKFVL 484
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
28-470 |
3.58e-10 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 62.10 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 28 TYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKLL----L 103
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALfvgkL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 104 SATAVTVTDLPVRIVS-----------EDNLKDIFFTHKgntPNPEHAVKGDENFY-IIYTSGSTGNPKGVQITYNclvS 171
Cdd:cd05932 88 DDWKAMAPGVPEGLISislpppsaancQYQWDDLIAQHP---PLEERPTRFPEQLAtLIYTSGTTGQPKGVMLTFG---S 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 172 FTkWA----VEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWA----ID---KDM-IARPKdLFASLEqsdiQVW 239
Cdd:cd05932 162 FA-WAaqagIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAfaesLDtfvEDVqRARPT-LFFSVP----RLW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 240 TstpsfaemclmeaSFSENM---LPNMKTFLfcgeVLPNEVARKLIERfpkaTIMNTYGPTEATVAVTG-IHVTEEVLDQ 315
Cdd:cd05932 236 T-------------KFQQGVqdkIPQQKLNL----LLKIPVVNSLVKR----KVLKGLGLDQCRLAGCGsAPVPPALLEW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 316 YKSLPVGYCKS-----DCRLLIM-----KEDGTIAPD--------GEKGEIVIVGPSVSVGYLGSPELTEKAFTMiDGer 377
Cdd:cd05932 295 YRSLGLNILEAygmteNFAYSHLnypgrDKIGTVGNAgpgvevriSEDGEILVRSPALMMGYYKDPEATAEAFTA-DG-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 378 AYKTGDAGYV-ENGLLFYNGRLDFQIKL-HGYRMELEEIEHHLRACSYVEGAVIVpikkGEKYDYLLAVVVPGEhsfEKE 455
Cdd:cd05932 372 FLRTGDKGELdADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI----GSGLPAPLALVVLSE---EAR 444
|
490
....*....|....*
gi 446693156 456 FKLTSAIKKELNERL 470
Cdd:cd05932 445 LRADAFARAELEASL 459
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
151-498 |
7.28e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 61.19 E-value: 7.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 151 YTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKdmIARPkDLFAS 230
Cdd:PLN03102 193 YTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRH--VTAP-EIYKN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 231 LEQSDIQVWTSTPSFAEMcLMEASFSENMLPNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTEATVAVtgihVTE 310
Cdd:PLN03102 270 IEMHNVTHMCCVPTVFNI-LLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL-GFQVMHAYGLTEATGPV----LFC 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 311 EVLDQYKSLP---------------VGYCKSDCRlliMKEDGTIAP-DGEK-GEIVIVGPSVSVGYLGSPELTEKAFTmi 373
Cdd:PLN03102 344 EWQDEWNRLPenqqmelkarqgvsiLGLADVDVK---NKETQESVPrDGKTmGEIVIKGSSIMKGYLKNPKATSEAFK-- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 374 dgERAYKTGDAGYVE-NGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSF 452
Cdd:PLN03102 419 --HGWLNTGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGET 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446693156 453 EKEFKLTSAIKKELN------ERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PLN03102 497 TKEDRVDKLVTRERDlieycrENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
24-501 |
2.10e-09 |
|
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: 59.67 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 24 DAKITYKQLKEDSDALAHWISSeypddrspimvyghmqpemiinfLGcVKAGhayipvdlsipaDRVQRIAENSGAKLLL 103
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKS-----------------------LG-LKPG------------DVVALFMENRPEYVLL 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 104 SATAVTVTDLPVRIvsEDNLKDIFFTHKGNTPNPEHAVKgDENFYIiYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQ 183
Cdd:cd05940 45 WLGLVKIGAVAALI--NYNLRGESLAHCLNVSSAKHLVV-DAALYI-YTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 184 TGQVFLNQAPFSFDLSVM-DIYPSLVTGGTlwaidkdmIARPKDLFASLEQSDIQVWTST--PSFAEMC--LMEASFSEN 258
Cdd:cd05940 121 PSDVLYTCLPLYHSTALIvGWSACLASGAT--------LVIRKKFSASNFWDDIRKYQATifQYIGELCryLLNQPPKPT 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 259 MLPNmKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTG-------IHVTEEVLDQYKSLPVGYCKSDCRLL 331
Cdd:cd05940 193 ERKH-KVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINffgkpgaIGRNPSLLRKVAPLALVKYDLESGEP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 332 IMKEDGTI--APDGEKGEIV--IVGPSVSVGYLGSPELTEKAFTMI--DGERAYKTGDAGYV-ENGLLFYNGRLDFQIKL 404
Cdd:cd05940 272 IRDAEGRCikVPRGEPGLLIsrINPLEPFDGYTDPAATEKKILRDVfkKGDAWFNTGDLMRLdGEGFWYFVDRLGDTFRW 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 405 HGYRMELEEIEHHLRACSYVEGAVI--VPIKKGEKYDYLLAVVVPGEHSFEkefklTSAIKKELNERLPNYMIPRKFMYQ 482
Cdd:cd05940 352 KGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIVLQPNEEFD-----LSALAAHLEKNLPGYARPLFLRLQ 426
|
490
....*....|....*....
gi 446693156 483 SSIPMTPNGKVDRKKLLSE 501
Cdd:cd05940 427 PEMEITGTFKQQKVDLRNE 445
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
140-445 |
2.73e-09 |
|
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: 59.36 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 140 AVKGDENFYIIYTSGSTGNPKGVQITYNCLvsftkwavedfnLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKD 219
Cdd:cd17641 154 AGKGEDVAVLCTTSGTTGKPKLAMLSHGNF------------LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 220 MIARPKDLF---ASLEQSDIQ------------VWTSTPSFAEMCLMEAsfsenmlPNMKTFLF---------------- 268
Cdd:cd17641 222 LVCGFIVNFpeePETMMEDLReigptfvllpprVWEGIAADVRARMMDA-------TPFKRFMFelgmklglraldrgkr 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 269 -----CGEVLPNEVARKLIERFPKATImntyGPTEATVAVT-GIHVTEEVLDQYKSLPVG----YCKSD-CRLLIMKEDG 337
Cdd:cd17641 295 grpvsLWLRLASWLADALLFRPLRDRL----GFSRLRSAATgGAALGPDTFRFFHAIGVPlkqlYGQTElAGAYTVHRDG 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 338 TIAPD-------------GEKGEIVIVGPSVSVGYLGSPELTEKAFtmiDGERAYKTGDAGYV-ENGLLFYNGRL-DFQI 402
Cdd:cd17641 371 DVDPDtvgvpfpgtevriDEVGEILVRSPGVFVGYYKNPEATAEDF---DEDGWLHTGDAGYFkENGHLVVIDRAkDVGT 447
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446693156 403 KLHGYRMELEEIEHHLRACSYVEGAVIVpikkGEKYDYLLAVV 445
Cdd:cd17641 448 TSDGTRFSPQFIENKLKFSPYIAEAVVL----GAGRPYLTAFI 486
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
238-470 |
3.96e-09 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 58.62 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 238 VWTSTPSFA-----EMCLMEASFSEnmlPNMKTFLFCGEVLPNEVaRKLIERFPKATIMNTYGPTEATVAV-------TG 305
Cdd:COG1541 178 VLVGTPSYLlylaeVAEEEGIDPRD---LSLKKGIFGGEPWSEEM-RKEIEERWGIKAYDIYGLTEVGPGVayeceaqDG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 306 IHVTE-----EVLDqykslPvgycksdcrllimkEDGTIAPDGEKGEIVIVGpsvsvgylgspeLTEKAFTMIdgeRaYK 380
Cdd:COG1541 254 LHIWEdhflvEIID-----P--------------ETGEPVPEGEEGELVVTT------------LTKEAMPLI---R-YR 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 381 TGDAGYVENG----------LLFYNGRLDFQIKLHG---YRmelEEIEHHLRACSYVEG-AVIVPIKKGEKyDYLLaVVV 446
Cdd:COG1541 299 TGDLTRLLPEpcpcgrthprIGRILGRADDMLIIRGvnvFP---SQIEEVLLRIPEVGPeYQIVVDREGGL-DELT-VRV 373
|
250 260
....*....|....*....|....
gi 446693156 447 PGEHSFEKEfKLTSAIKKELNERL 470
Cdd:COG1541 374 ELAPGASLE-ALAEAIAAALKAVL 396
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
93-501 |
9.93e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 57.73 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 93 IAENSGAKLLlsaTAVTVTDLPVRIVSEDNLKDIFFTHKGNTPNPEhaVKGDENFYIIYTSGSTGNPKGVQITYNCLVSF 172
Cdd:PRK13388 104 VTDAEHRPLL---DGLDLPGVRVLDVDTPAYAELVAAAGALTPHRE--VDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 173 TKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIY-PSLVTGGTlwaidkdmIARPKDLFASLEQSDIQVW------------ 239
Cdd:PRK13388 179 GRALTERFGLTRDDVCYVSMPLFHSNAVMAGWaPAVASGAA--------VALPAKFSASGFLDDVRRYgatyfnyvgkpl 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 240 ---TSTPSFAEMclmeasfSENMLpnmkTFLFCGEVLPNEVARkLIERFpKATIMNTYGPTEATVAVTGIHVTEEvldqy 316
Cdd:PRK13388 251 ayiLATPERPDD-------ADNPL----RVAFGNEASPRDIAE-FSRRF-GCQVEDGYGSSEGAVIVVREPGTPP----- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 317 KSLPVGY---------CKSDCRLLIMKEDGTIA-PDGEKGEIVIV-GPSVSVGYLGSPELTekAFTMIDGEraYKTGDAG 385
Cdd:PRK13388 313 GSIGRGApgvaiynpeTLTECAVARFDAHGALLnADEAIGELVNTaGAGFFEGYYNNPEAT--AERMRHGM--YWSGDLA 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 386 YV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLL-AVVVPGEHSFE-KEFKLTSAI 462
Cdd:PRK13388 389 YRdADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMaALVLRDGATFDpDAFAAFLAA 468
|
410 420 430
....*....|....*....|....*....|....*....
gi 446693156 463 KKELNERlpnyMIPRKFMYQSSIPMTPNGKVDRKKLLSE 501
Cdd:PRK13388 469 QPDLGTK----AWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
7-188 |
1.31e-08 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 57.26 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVW------RDAKITYKQLKEDSDALAhWISSEY---PDDRspIMVYGHMQPEMIINFLGCVKAG-- 75
Cdd:TIGR02188 63 VDRHLEARPDKVAIIWegdepgEVRKITYRELHREVCRFA-NVLKSLgvkKGDR--VAIYMPMIPEAAIAMLACARIGai 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 76 HAYIPVDLS--IPADRVQriaeNSGAKLLLSA----------------------TAVTV--------TDLPVRIVSEDnl 123
Cdd:TIGR02188 140 HSVVFGGFSaeALADRIN----DAGAKLVITAdeglrggkviplkaivdealekCPVSVehvlvvrrTGNPVVPWVEG-- 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446693156 124 KDIFFTHKGNTPNPEHAVK--GDENF-YIIYTSGSTGNPKGVQIT---YNCLVSFTKWAVedFNLQTGQVF 188
Cdd:TIGR02188 214 RDVWWHDLMAKASAYCEPEpmDSEDPlFILYTSGSTGKPKGVLHTtggYLLYAAMTMKYV--FDIKDGDIF 282
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
3-453 |
3.69e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 55.90 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 3 LLEQIEKWAAETPDQTAFVWRD---------AKITYKQLKEDSDAL-AHWISSEYPDDRSPIMVyghmqP---EMIINFL 69
Cdd:PRK12476 36 LISLIERNIANVGDTVAYRYLDhshsaagcaVELTWTQLGVRLRAVgARLQQVAGPGDRVAILA-----PqgiDYVAGFF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 70 GCVKAGHAYIPV---DLSIPADRVQRIAENSGAKLLLSATAVT------VTDLPV----RIVSEDNLKDifftHKGNTPN 136
Cdd:PRK12476 111 AAIKAGTIAVPLfapELPGHAERLDTALRDAEPTVVLTTTAAAeavegfLRNLPRlrrpRVIAIDAIPD----SAGESFV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 137 PEHaVKGDENFYIIYTSGSTGNPKGVQITY-----NCLVSFTKWAVEDFNLQtGQVFLnqaPFSFDLSV-MDIYPSLVTG 210
Cdd:PRK12476 187 PVE-LDTDDVSHLQYTSGSTRPPVGVEITHravgtNLVQMILSIDLLDRNTH-GVSWL---PLYHDMGLsMIGFPAVYGG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 211 GTLWAIDKDMIARP----KDLfaSLEQSDIQVWTSTPSFAemclMEASFSENMLPNMKTFLFCGEVLPN---EVARKLIE 283
Cdd:PRK12476 262 HSTLMSPTAFVRRPqrwiKAL--SEGSRTGRVVTAAPNFA----YEWAAQRGLPAEGDDIDLSNVVLIIgsePVSIDAVT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 284 RF---------PKATIMNTYGPTEATVAVTGI---------HVTEEVLDQYKSLPVGY----------CKSDCRLL---I 332
Cdd:PRK12476 336 TFnkafapyglPRTAFKPSYGIAEATLFVATIapdaepsvvYLDREQLGAGRAVRVAAdapnavahvsCGQVARSQwavI 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 333 MKED-GTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAF------TMIDGERA---------YKTGDAGYVENGLLFYNG 396
Cdd:PRK12476 416 VDPDtGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsRLAEGSHAdgaaddgtwLRTGDLGVYLDGELYITG 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 446693156 397 RLDFQIKLHGYRMELEEIEHHLRACSYVegavivpIKKGekydYLLAVVVPGEHSFE 453
Cdd:PRK12476 496 RIADLIVIDGRNHYPQDIEATVAEASPM-------VRRG----YVTAFTVPAEDNER 541
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
7-188 |
4.21e-08 |
|
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: 55.65 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVW------RDAKITYKQLKEDSDALAHWISSEY--PDDRspIMVYGHMQPEMIINFLGCVKAG--H 76
Cdd:cd05966 59 LDRHLKERGDKVAIIWegdepdQSRTITYRELLREVCRFANVLKSLGvkKGDR--VAIYMPMIPELVIAMLACARIGavH 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 77 AYI-----PVDLsipADRVqriaENSGAKLLLSATAVTVTDLPVrivsedNLKDIFFTHKGNTPNPEHAV-----KGDEN 146
Cdd:cd05966 137 SVVfagfsAESL---ADRI----NDAQCKLVITADGGYRGGKVI------PLKEIVDEALEKCPSVEKVLvvkrtGGEVP 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446693156 147 F------------------------------YIIYTSGSTGNPKGVQIT---YNCLVSFT-KWAvedFNLQTGQVF 188
Cdd:cd05966 204 MtegrdlwwhdlmakqspecepewmdsedplFILYTSGSTGKPKGVVHTtggYLLYAATTfKYV---FDYHPDDIY 276
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
149-498 |
5.31e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 55.56 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 IIYTSGSTGNPKGVQITYNCLV--SFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDmiARPKD 226
Cdd:PRK05620 186 ICYSTGTTGAPKGVVYSHRSLYlqSLSLRTTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPD--LSAPT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 227 LFASLEQSDIQVWTSTPSFAeMCLM---EASFSENMlpNMKTFLFCGEVLPNEVARKLIERFpKATIMNTYGPTE----A 299
Cdd:PRK05620 264 LAKIIATAMPRVAHGVPTLW-IQLMvhyLKNPPERM--SLQEIYVGGSAVPPILIKAWEERY-GVDVVHVWGMTEtspvG 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 300 TVAVTGIHVTEEVLDQYK----SLPVGYcksDCRLLimkEDGTI--APDGEKGEIVIVGPSVSVGYLGSPELTEK-AFTM 372
Cdd:PRK05620 340 TVARPPSGVSGEARWAYRvsqgRFPASL---EYRIV---NDGQVmeSTDRNEGEIQVRGNWVTASYYHSPTEEGGgAAST 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 373 IDGERA------------YKTGDAGYV-ENGLLFYNGRLDFQIKLHG---YRMELEEieHHLRACSYVEGAVI-VPIKK- 434
Cdd:PRK05620 414 FRGEDVedandrftadgwLRTGDVGSVtRDGFLTIHDRARDVIRSGGewiYSAQLEN--YIMAAPEVVECAVIgYPDDKw 491
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446693156 435 GEKydyLLAVVV--PGehsFEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK05620 492 GER---PLAVTVlaPG---IEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
16-501 |
6.21e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 55.07 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 16 DQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSP-IMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIA 94
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 95 ENSGAKLLL--SATAVTVTDLP--VRIVSEDNLK--DIFFTHKGNTPNPEhAVKGDENFYIIYTSGSTGNPKGVQITYNC 168
Cdd:PRK07867 98 AHADCQLVLteSAHAELLDGLDpgVRVINVDSPAwaDELAAHRDAEPPFR-VADPDDLFMLIFTSGTSGDPKAVRCTHRK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 169 LVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIY-PSLVTGGTlwaidkdmIARPKDLFASLEQSDIQVWTSTpsFAE 247
Cdd:PRK07867 177 VASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWaVALAAGAS--------IALRRKFSASGFLPDVRRYGAT--YAN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 248 MCLMEASF----------SENMLPNMktflFCGEVLPNEVARkLIERFpKATIMNTYGPTEATVAVTGIHVTEE------ 311
Cdd:PRK07867 247 YVGKPLSYvlatperpddADNPLRIV----YGNEGAPGDIAR-FARRF-GCVVVDGFGSTEGGVAITRTPDTPPgalgpl 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 312 -----VLDqykslPVGycKSDCRLLIMKEDGTIAPDGEKGEIV-IVGPSVSVGYLGSPELTekAFTMIDGerAYKTGDAG 385
Cdd:PRK07867 321 ppgvaIVD-----PDT--GTECPPAEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEAD--AERMRGG--VYWSGDLA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 386 YV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGE-HSFEKEfkltsAIK 463
Cdd:PRK07867 390 YRdADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPgAKFDPD-----AFA 464
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446693156 464 KELNER--LPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSE 501
Cdd:PRK07867 465 EFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
149-494 |
8.13e-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: 54.23 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 149 IIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFsFDLSV-MDIYPSLVTGGTlwaidKDMIAR--PK 225
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPL-FHIGTlMFTLATFHAGGT-----NVFVRRvdAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 226 DLFASLEQSDIQ-VWTSTPSFAEMclmeASFSENMLPNMKTfLFCGEVLPNEVARKLIERFPKATIMNTYGPTEatvaVT 304
Cdd:cd17636 79 EVLELIEAERCThAFLLPPTIDQI----VELNADGLYDLSS-LRSSPAAPEWNDMATVDTSPWGRKPGGYGQTE----VM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 305 GIHVTEEVLDQYKSLpVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTmiDGerAYKTGDA 384
Cdd:cd17636 150 GLATFAALGGGAIGG-AGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR--GG--WHHTNDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 385 GYVE-NGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYV-EGAVI-VPikkGEKYDY-LLAVVV--PGEHSFEKEfkl 458
Cdd:cd17636 225 GRREpDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVaDAAVIgVP---DPRWAQsVKAIVVlkPGASVTEAE--- 298
|
330 340 350
....*....|....*....|....*....|....*.
gi 446693156 459 tsaIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVD 494
Cdd:cd17636 299 ---LIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
342-498 |
8.17e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 54.62 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 342 DGEKGEIVIVGPSVSVGYLgsPELtekaftmIDGERAYKTGDAGYVEN-GLLFYNGRLDFQIKLHGYRMELEEIEHHLRA 420
Cdd:PRK07445 298 ANQTGNITIQAQSLALGYY--PQI-------LDSQGIFETDDLGYLDAqGYLHILGRNSQKIITGGENVYPAEVEAAILA 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446693156 421 CSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFEKEfKLTSAIKKELNerlpNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK07445 369 TGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE-ELKTAIKDQLS----PFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
319-454 |
9.55e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 54.74 E-value: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 319 LPVGYCKsdcrLLIMKEDGTIAPDGE--KGEIVIVGPSVSVGYLGSPELTEKAFTmID--GERAYKTGDAG-YVENGLLF 393
Cdd:PLN02387 478 LPCCYVK----LVSWEEGGYLISDKPmpRGEIVIGGPSVTLGYFKNQEKTDEVYK-VDerGMRWFYTGDIGqFHPDGCLE 552
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446693156 394 YNGRLDFQIKL-HGYRMELEEIEHHLRACSYVEGAVIV--PIkkgekYDYLLAVVVPGEHSFEK 454
Cdd:PLN02387 553 IIDRKKDIVKLqHGEYVSLGKVEAALSVSPYVDNIMVHadPF-----HSYCVALVVPSQQALEK 611
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
28-501 |
1.23e-07 |
|
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: 53.98 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 28 TYKQLKEDSDALAHWISSEY---PDDRspIMVYGHMQPEMIINFLGCVKAGhayipvdlSIPAdrvqriaensgaklLLS 104
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDLgvqAGDF--VAIDLTNSPEFVFLWLGLWSIG--------AAPA--------------FIN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 105 AtavtvtdlpvrivsedNLKDIFFTHKGNTPNPEHAVKGDENFYI-IYTSGSTGNPKGVQITY-NCLVS---FTKWAVED 179
Cdd:cd05937 63 Y----------------NLSGDPLIHCLKLSGSRFVIVDPDDPAIlIYTSGTTGLPKAAAISWrRTLVTsnlLSHDLNLK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 180 FNLQTgqvflnqapfsfdLSVMDIYPS----------LVTGGTLwAIDKDMIARP--KDLFASleQSDIQVWTstpsfAE 247
Cdd:cd05937 127 NGDRT-------------YTCMPLYHGtaaflgacncLMSGGTL-ALSRKFSASQfwKDVRDS--GATIIQYV-----GE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 248 MC--LMEASFSenmlP---NMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVT------------GIH--- 307
Cdd:cd05937 186 LCryLLSTPPS----PydrDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTnhnvgdfgagaiGHHgli 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 308 -------------VTEEVLDQYKSLPVGYCKSdcrllimkedgtiAPDGEKGEIVIVGPSVSV----GYLGSPELTEKAF 370
Cdd:cd05937 262 rrwkfenqvvlvkMDPETDDPIRDPKTGFCVR-------------APVGEPGEMLGRVPFKNReafqGYLHNEDATESKL 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 371 ---TMIDGERAYKTGDA-GYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKgEKYD---YLLA 443
Cdd:cd05937 329 vrdVFRKGDIYFRTGDLlRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKV-PGHDgraGCAA 407
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446693156 444 VVVPGEHSFEKEFKLtSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSE 501
Cdd:cd05937 408 ITLEESSAVPTEFTK-SLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
266-397 |
1.36e-07 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 54.19 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 266 FLFCGEV-LPNEVARklieRFPKAT---IMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVGYCksDCRLLIMKEDGTI-- 339
Cdd:PRK07529 337 YALCGAApLPVEVFR----RFEAATgvrIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQ--RVRVVILDDAGRYlr 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 340 -APDGEKGEIVIVGPSVSVGYLgSPELTEKAFTmidGERAYKTGDAGYV-ENGLLFYNGR 397
Cdd:PRK07529 411 dCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL---EDGWLNTGDLGRIdADGYFWLTGR 466
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
375-504 |
3.96e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 52.35 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 375 GERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIvpIKK-----GEKydylLAVVVPG 448
Cdd:PRK08308 289 GDKEIFTKDLGYKsERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVV--YRGkdpvaGER----VKAKVIS 362
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446693156 449 EHSFEkefklTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL-LSEVTA 504
Cdd:PRK08308 363 HEEID-----PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLeLGEVTA 414
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
6-165 |
9.98e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 51.41 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 6 QIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSE--YPDDRSPIMVYGHmqPEMIINFLGCVKAG-------- 75
Cdd:PRK08279 42 VFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARgvGKGDVVALLMENR--PEYLAAWLGLAKLGavvallnt 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 76 --------HAyipVDLSIP------ADRVQRIAE----NSGAKLLLSATAVTVTDLPVRivseDNLKDIFFTHkgNTPNP 137
Cdd:PRK08279 120 qqrgavlaHS---LNLVDAkhlivgEELVEAFEEaradLARPPRLWVAGGDTLDDPEGY----EDLAAAAAGA--PTTNP 190
|
170 180 190
....*....|....*....|....*....|.
gi 446693156 138 EHA---VKGDENFYiIYTSGSTGNPKGVQIT 165
Cdd:PRK08279 191 ASRsgvTAKDTAFY-IYTSGTTGLPKAAVMS 220
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
344-498 |
1.19e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 50.43 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 344 EKGEIVIVGPSVSVGYLGSPEltEKAFTmidGERAYKTGDAGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSY 423
Cdd:PRK07824 206 EDGRIALGGPTLAKGYRNPVD--PDPFA---EPGWFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPA 280
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446693156 424 VEGAVIVPIKKGEKYDYLLAVVVPGEHSFEkefkLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK07824 281 VADCAVFGLPDDRLGQRVVAAVVGDGGPAP----TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-498 |
1.45e-06 |
|
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: 50.17 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 266 FLFCGEV-LPNEVaRKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVGYcksdCRLLIMKEDGT------ 338
Cdd:cd05944 125 FAMSGAApLPVEL-RARFEDATGLPVVEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPY----ARVRIKVLDGVgrllrd 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 339 IAPDgEKGEIVIVGPSVSVGYLGspelTEKAFTMIDGERAYKTGDAGYV-ENGLLFYNGRLDFQIKLHGYRMELEEIEHH 417
Cdd:cd05944 200 CAPD-EVGEICVAGPGVFGGYLY----TEGNKNAFVADGWLNTGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 418 LRACSYVE--GAVIVP-IKKGE---KYDYLL--AVVVPGEhsfekefkLTSAIKKELNERLPnymIPRKFMYQSSIPMTP 489
Cdd:cd05944 275 LLRHPAVAfaGAVGQPdAHAGElpvAYVQLKpgAVVEEEE--------LLAWARDHVPERAA---VPKHIEVLEELPVTA 343
|
....*....
gi 446693156 490 NGKVDRKKL 498
Cdd:cd05944 344 VGKVFKPAL 352
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
7-498 |
2.64e-06 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 49.95 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 7 IEKWAAETPDQTAFVW------RDAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAG--H 76
Cdd:PRK10524 59 VDRHLAKRPEQLALIAvstetdEERTYTFRQLHDEVNRMAAMLRSLgvQRGDR--VLIYMPMIAEAAFAMLACARIGaiH 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 77 A-----YIPVDLSipadrvQRIaENSGAKLLLSATA---------------------------VTVTD---LPVRIVSEd 121
Cdd:PRK10524 137 SvvfggFASHSLA------ARI-DDAKPVLIVSADAgsrggkvvpykplldeaialaqhkprhVLLVDrglAPMARVAG- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 122 nlKDIFFT-----HKGNTPNPEHaVKGDENFYIIYTSGSTGNPKGVQ---------------ITYNCLVSFTKWAVEDFN 181
Cdd:PRK10524 209 --RDVDYAtlraqHLGARVPVEW-LESNEPSYILYTSGTTGKPKGVQrdtggyavalatsmdTIFGGKAGETFFCASDIG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 182 LQTGQVFLNQAPFSFDL-SVMdiYPSLVT---GGTLWAIdkdmiarpkdlfasLEQSDIQVWTSTPS-------FAEMCL 250
Cdd:PRK10524 286 WVVGHSYIVYAPLLAGMaTIM--YEGLPTrpdAGIWWRI--------------VEKYKVNRMFSAPTairvlkkQDPALL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 251 MEASFSenmlpNMKTFLFCGEVLPNEVARKLIERFPKATIMNtYGPTE----ATVAVTGIHVTEEVLDQyKSLPV-GYck 325
Cdd:PRK10524 350 RKHDLS-----SLRALFLAGEPLDEPTASWISEALGVPVIDN-YWQTEtgwpILAIARGVEDRPTRLGS-PGVPMyGY-- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 326 sDCRlLIMKEDGTIAPDGEKGEIVIVGP----SVSVGYLGSPELTEKAFTMIdGERAYKTGDAGYV-ENGLLFYNGRLDF 400
Cdd:PRK10524 421 -NVK-LLNEVTGEPCGPNEKGVLVIEGPlppgCMQTVWGDDDRFVKTYWSLF-GRQVYSTFDWGIRdADGYYFILGRTDD 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 401 QIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSF----EKEFKLTSAIKKELNERLPNYMIP 476
Cdd:PRK10524 498 VINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSladrEARLALEKEIMALVDSQLGAVARP 577
|
570 580
....*....|....*....|..
gi 446693156 477 RKFMYQSSIPMTPNGKVDRKKL 498
Cdd:PRK10524 578 ARVWFVSALPKTRSGKLLRRAI 599
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
413-492 |
4.56e-06 |
|
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: 44.46 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 413 EIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVP--GEHSFEKEfkltsaIKKELNERLPNYMIPRKFMYQSSIPMTPN 490
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLkpGVELLEEE------LVAHVREELGPYAVPKEVVFVDELPKTRS 74
|
..
gi 446693156 491 GK 492
Cdd:pfam13193 75 GK 76
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
317-500 |
6.01e-06 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 48.81 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 317 KSLPVGYCKSDCRLLIM-----KEDGTIAPdGEKGEIVIVG--PSVSVGYLGSPELT--EKA-FTMIDGERAYktGDagY 386
Cdd:cd05943 417 PLLPVYRGEIQCRGLGMaveafDEEGKPVW-GEKGELVCTKpfPSMPVGFWNDPDGSryRAAyFAKYPGVWAH--GD--W 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 387 VE----NGLLFYnGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIK-KGEKYDYLLAVVVPGEHSFEKEfkLTSA 461
Cdd:cd05943 492 IEitprGGVVIL-GRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEwKDGDERVILFVKLREGVELDDE--LRKR 568
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446693156 462 IKKELNERLPNYMIPRKFMYQSSIPMTPNGK---VDRKKLLS 500
Cdd:cd05943 569 IRSTIRSALSPRHVPAKIIAVPDIPRTLSGKkveVAVKKIIA 610
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
335-498 |
1.43e-05 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 47.50 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 335 EDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAftmIDGERAYKTGDAGYV-ENGllFYN--GRL-DFQIKlhG---- 406
Cdd:PRK08315 388 ETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA---IDADGWMHTGDLAVMdEEG--YVNivGRIkDMIIR--Ggeni 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 407 YRMELEEIEHHLRACSYVegAVI-VPIKK-GEKydyLLAVVV--PGEHSFEKEfkltsaIKKELNERLPNYMIPRKFMYQ 482
Cdd:PRK08315 461 YPREIEEFLYTHPKIQDV--QVVgVPDEKyGEE---VCAWIIlrPGATLTEED------VRDFCRGKIAHYKIPRYIRFV 529
|
170
....*....|....*.
gi 446693156 483 SSIPMTPNGKVDRKKL 498
Cdd:PRK08315 530 DEFPMTVTGKIQKFKM 545
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
152-429 |
4.25e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.91 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 152 TSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQ-VFLNQAPFSFDLSVMDIYPSLVTGGTLW-AIDKDMIARPKDLFA 229
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATdVGCSWLPLYHDMGLAFLLTAALAGAPLWlAPTTAFSASPFRWLS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 230 SLEQSDIQVwTSTPSFAEMCLMEAS--FSENMLPNMKTFLFCGEvlpnEVARKLIERFPKAT---------IMNTYGPTE 298
Cdd:PRK05851 240 WLSDSRATL-TAAPNFAYNLIGKYArrVSDVDLGALRVALNGGE----PVDCDGFERFATAMapfgfdagaAAPSYGLAE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 299 ATVAVT------GIHVTEEVLDQYKSLP----VGYCKSDCRLLIMKEDGTIAPDG-EKGEIVIVGPSVSVGYLGSPElte 367
Cdd:PRK05851 315 STCAVTvpvpgiGLRVDEVTTDDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGrEIGEIEIRGASMMSGYLGQAP--- 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446693156 368 kaftmIDGERAYKTGDAGYVENGLLFYNGRLDFQIKLHGYRMELEEIEhhlRACSYV----EGAVI 429
Cdd:PRK05851 392 -----IDPDDWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIE---RVAAQVrgvrEGAVV 449
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
16-188 |
1.03e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 44.75 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 16 DQTAFVWR------DAKITYKQLKEDSDALAHWISSE--YPDDRspIMVYGHMQPEMIINFLGCVKAG--HAYI-----P 80
Cdd:PRK00174 82 DKVAIIWEgddpgdSRKITYRELHREVCRFANALKSLgvKKGDR--VAIYMPMIPEAAVAMLACARIGavHSVVfggfsA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 81 VDLsipADRVQriaeNSGAKLLLSA-----------------TAVTVTD-----LPVRIVSED----NLKDIFFTHKGNT 134
Cdd:PRK00174 160 EAL---ADRII----DAGAKLVITAdegvrggkpiplkanvdEALANCPsvekvIVVRRTGGDvdwvEGRDLWWHELVAG 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 135 PNPEH---AVKGDENFYIIYTSGSTGNPKGVQIT---YNCLVSFTKWAVedFNLQTGQVF 188
Cdd:PRK00174 233 ASDECepePMDAEDPLFILYTSGSTGKPKGVLHTtggYLVYAAMTMKYV--FDYKDGDVY 290
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
90-383 |
4.32e-04 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 42.61 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 90 VQRIAENSGA-KLLLSATAVTvtdlPVRIVSEDNLKDIFFTHK----GNTPNPEHAVKGDENFYIIYTSGSTGNPKgvqi 164
Cdd:cd05913 23 VRHAYENVPFyRRKFAAAGID----PDDIKSLDDLRKLPFTTKedlrDNYPFGLFAVPREKVVRIHASSGTTGKPT---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 165 tyncLVSFTKWAVEDF-NLQtgQVFLNQAPFSFDLSVMDIYP-SLVTGG-----TLWAIDKDMIA----RPKDLFASLEQ 233
Cdd:cd05913 95 ----VVGYTKNDLDVWaELV--ARCLDAAGVTPGDRVQNAYGyGLFTGGlgfhyGAERLGALVIPagggNTERQLQLIKD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 234 SDIQVWTSTPSFAeMCLMEASFSENMLP---NMKTFLFCGEVLPNEvARKLIERFPKATIMNTYGPTEAT---VAVT--- 304
Cdd:cd05913 169 FGPTVLCCTPSYA-LYLAEEAEEEGIDPrelSLKVGIFGAEPWTEE-MRKRIERRLGIKAYDIYGLTEIIgpgVAFEcee 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 305 --GIHVTE-----EVLDqykslPvgycksdcrllimkEDGTIAPDGEKGEIVIVgpsvsvgylgspELTEKAFTMIdgeR 377
Cdd:cd05913 247 kdGLHIWEdhfipEIID-----P--------------ETGEPVPPGEVGELVFT------------TLTKEAMPLI---R 292
|
....*.
gi 446693156 378 aYKTGD 383
Cdd:cd05913 293 -YRTRD 297
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
9-162 |
1.39e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 41.01 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446693156 9 KWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPAD 88
Cdd:PRK09029 11 HWAQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQP 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446693156 89 RVQRIAENSGAKLLLSATA-VTVTDLPVRIVSEDNlkdiffthkgntPNPEHAVKGDENFYIIYTSGSTGNPKGV 162
Cdd:PRK09029 91 LLEELLPSLTLDFALVLEGeNTFSALTSLHLQLVE------------GAHAVAWQPQRLATMTLTSGSTGLPKAA 153
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
144-171 |
5.93e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 39.19 E-value: 5.93e-03
10 20
....*....|....*....|....*...
gi 446693156 144 DENFYIIYTSGSTGNPKGVQITYNCLVS 171
Cdd:PTZ00216 264 DDLALIMYTSGTTGDPKGVMHTHGSLTA 291
|
|
| |
