|
Name |
Accession |
Description |
Interval |
E-value |
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
2-503 |
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: 924.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 2 KLLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRIsGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIP 81
Cdd:TIGR01734 1 KLIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRI-LPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 82 VDLSIPSERIAKIIESSGAELLIHAAGLSIDAVGQQIQTVSAEELLENEGGSVSQDQWVKEHETFYIIYTSGSTGNPKGV 161
Cdd:TIGR01734 80 VDTSIPSERIEMIIEAAGPELVIHTAELSIDAVGTQIITLSALEQAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 162 QISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTST 241
Cdd:TIGR01734 160 QISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 242 PSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVISRSESLPVG 321
Cdd:TIGR01734 240 PSFVDMCLLDPNFNQENYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEILDQYPRLPIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 322 FAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSHEGQWAYRTGDAGFIQDGQIFCQGRLDFQI 401
Cdd:TIGR01734 320 FAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSHEGQPAYRTGDAGTITDGQLFYQGRLDFQI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 402 KLHGYRMELEEIEFHVRQSQYVRSAVVIP-YQPNGTVEYLIAAIVPEEHEFEKEFQLTSAIKKELAASLPAYMIPRKFIY 480
Cdd:TIGR01734 400 KLHGYRIELEDIEFNLRQSSYIESAVVVPkYNKDHKVEYLIAAIVPETEDFEKEFQLTKAIKKELKKSLPAYMIPRKFIY 479
|
490 500
....*....|....*....|...
3E7X_A 481 QDHIQMTANGKIDRKRIGEEVLV 503
Cdd:TIGR01734 480 RDQLPLTANGKIDRKALAEEVNG 502
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1-501 |
0e+00 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 899.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 1 MKLLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISgEKKSPILVYGHMEPHMIVSFLGSVKAGHPYI 80
Cdd:PRK04813 2 MDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKL-PDKSPIIVFGHMSPEMLATFLGAVKAGHAYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 81 PVDLSIPSERIAKIIESSGAELLIHAAGLSIDAVGqqIQTVSAEELLEN--EGGSVSQDQWVKEHETFYIIYTSGSTGNP 158
Cdd:PRK04813 81 PVDVSSPAERIEMIIEVAKPSLIIATEELPLEILG--IPVITLDELKDIfaTGNPYDFDHAVKGDDNYYIIFTSGTTGKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 159 KGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVW 238
Cdd:PRK04813 159 KGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 239 TSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVISRSESL 318
Cdd:PRK04813 239 VSTPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEITDEMLDQYKRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 319 PVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSHEGQWAYRTGDAGFIQDGQIFCQGRLD 398
Cdd:PRK04813 319 PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQPAYHTGDAGYLEDGLLFYQGRID 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 399 FQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEFEKEFQLTSAIKKELAASLPAYMIPRKF 478
Cdd:PRK04813 399 FQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMEYMIPRKF 478
|
490 500
....*....|....*....|...
3E7X_A 479 IYQDHIQMTANGKIDRKRIGEEV 501
Cdd:PRK04813 479 IYRDSLPLTPNGKIDRKALIEEV 501
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
11-497 |
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: 705.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRiSGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSER 90
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 91 IAKIIESSGAELLIHAaglsidavgqqiqtvsaeelleneggsvsqdqwvkEHETFYIIYTSGSTGNPKGVQISAANLQS 170
Cdd:cd05945 80 IREILDAAKPALLIAD-----------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 171 FTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMCLM 250
Cdd:cd05945 125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 251 DPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVISRSESLPVGFAKPDMNIF 330
Cdd:cd05945 205 SPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGYAKPGAKLV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 331 IMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSHEGQWAYRTGDAGFIQ-DGQIFCQGRLDFQIKLHGYRME 409
Cdd:cd05945 285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRAYRTGDLVRLEaDGLLFYRGRLDFQVKLNGYRIE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 410 LEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEfekEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTAN 489
Cdd:cd05945 365 LEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGA---EAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNAN 441
|
....*...
3E7X_A 490 GKIDRKRI 497
Cdd:cd05945 442 GKIDRKAL 449
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
19-496 |
1.06e-148 |
|
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: 433.11 E-value: 1.06e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 19 AFRSQGQSLTYQELWEQSDRAAAAIQKRISGeKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESS 98
Cdd:cd05930 5 AVVDGDQSLTYAELDARANRLARYLRERGVG-PGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 99 GAELLIHAAGlsidavgqqiqtvsaeelleneggsvsqdqwvkehETFYIIYTSGSTGNPKGVQISAANLQSFTDWICAD 178
Cdd:cd05930 84 GAKLVLTDPD-----------------------------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 179 FPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQdl 258
Cdd:cd05930 129 YPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA-- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 259 LPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVIsRSESLPVGFAKPDMNIFIMDEEGQP 338
Cdd:cd05930 207 LPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDE-EDGRVPIGRPIPNTRVYVLDENLRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 339 LPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSH---EGQWAYRTGDAG-FIQDGQIFCQGRLDFQIKLHGYRMELEEIE 414
Cdd:cd05930 286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNpfgPGERMYRTGDLVrWLPDGNLEFLGRIDDQVKIRGYRIELGEIE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 415 FHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHefekEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDR 494
Cdd:cd05930 366 AALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEG----GELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDR 441
|
..
3E7X_A 495 KR 496
Cdd:cd05930 442 KA 443
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
28-428 |
9.00e-121 |
|
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: 360.43 E-value: 9.00e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 28 TYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLIHAA 107
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 108 GLSIDAVGQQIQTV---SAEELLENEGGSVSQDQWVKEHETF-YIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSG 183
Cdd:TIGR01733 81 ALASRLAGLVLPVIlldPLELAALDDAPAPPPPDAPSGPDDLaYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 184 GKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSG-LNVWTSTPSFVQMCLMDPGFSqdlLPHA 262
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAALPPA---LASL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 263 DTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVISRSESLPVGFAKPDMNIFIMDEEGQPLPEG 342
Cdd:TIGR01733 238 RLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 343 EKGEIVIAGPSVSRGYLGEPELTEKAFFSH-----EGQWAYRTGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFH 416
Cdd:TIGR01733 318 VVGELYIGGPGVARGYLNRPELTAERFVPDpfaggDGARLYRTGDlVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
410
....*....|..
3E7X_A 417 VRQSQYVRSAVV 428
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2-496 |
1.20e-114 |
|
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: 368.03 E-value: 1.20e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 2 KLLHA-IQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRisGEKK-SPILVYghME--PHMIVSFLGSVKAGH 77
Cdd:COG1020 476 ATLHElFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRAL--GVGPgDLVGVC--LErsLEMVVALLAVLKAGA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 78 PYIPVDLSIPSERIAKIIESSGAELLIHAAGLSIDAVGQQIQTVSAEELLENEGGSVSQDQWVKEHETFYIIYTSGSTGN 157
Cdd:COG1020 552 AYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGR 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 158 PKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNV 237
Cdd:COG1020 632 PKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTV 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 238 WTSTPSFVQMcLMDPGFSQdlLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITnDVISRSES 317
Cdd:COG1020 712 LNLTPSLLRA-LLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVT-PPDADGGS 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 318 LPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWAYRTGDAG-FIQDGQIF 392
Cdd:COG1020 788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFvadpFGFPGARLYRTGDLArWLPDGNLE 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 393 CQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEFEKEFQLTSAikkeLAASLPAY 472
Cdd:COG1020 868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLA----LALLLPPY 943
|
490 500
....*....|....*....|....
3E7X_A 473 MIPRKFIYQDHIQMTANGKIDRKR 496
Cdd:COG1020 944 MVPAAVVLLLPLPLTGNGKLDRLA 967
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
7-403 |
2.47e-108 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 328.89 E-value: 2.47e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 7 IQTHAETYPQTDAFRSQ-GQSLTYQELWEQSDRAAAAIQKRisG-EKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDL 84
Cdd:pfam00501 1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRAL--GvGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 85 SIPSERIAKIIESSGAELLIHAAGL---SIDAVGQQIQTVSAEELLENEGGSVS---------------QDQWVKEHETF 146
Cdd:pfam00501 79 RLPAEELAYILEDSGAKVLITDDALkleELLEALGKLEVVKLVLVLDRDPVLKEeplpeeakpadvpppPPPPPDPDDLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 147 YIIYTSGSTGNPKGVQISAANLQSFTDWIC----ADFPVSGGKIFLNQAPFSFDLSV-MDLYPCLQSGGTLHCVTKDAVN 221
Cdd:pfam00501 159 YIIYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 222 KPKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAkIFNTYGPTEATVA 301
Cdd:pfam00501 239 DPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 302 VTSVEITNDVISRSESlpVGFAKPDMNIFIMDEE-GQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFshEGQWaYRT 380
Cdd:pfam00501 318 VTTPLPLDEDLRSLGS--VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD--EDGW-YRT 392
|
410 420
....*....|....*....|....
3E7X_A 381 GDAGFIQ-DGQIFCQGRLDFQIKL 403
Cdd:pfam00501 393 GDLGRRDeDGYLEIVGRKKDQIKL 416
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
7-499 |
8.36e-108 |
|
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: 330.06 E-value: 8.36e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 7 IQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAA-AAIQKRISGEKKSPILVYGHMEphMIVSFLGSVKAGHPYIPVDLS 85
Cdd:cd17655 3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLArTLREKGVGPDTIVGIMAERSLE--MIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 86 IPSERIAKIIESSGAELLIHAAGLSIDAVGQQIQTVSAEELLENEGGSvSQDQWVKEHETFYIIYTSGSTGNPKGVQISA 165
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESE-NLEPVSKSDDLAYVIYTSGSTGKPKGVMIEH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 166 ANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFV 245
Cdd:cd17655 160 RGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 246 QMclmdpgfsqdlLPHADTFMFC--------GEVLPVSVAKALLERF-PKAKIFNTYGPTEATVAVTSVEITNDViSRSE 316
Cdd:cd17655 240 KL-----------LDAADDSEGLslkhlivgGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYEPET-DQQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 317 SLPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSHE---GQWAYRTGD-AGFIQDGQIF 392
Cdd:cd17655 308 SVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPfvpGERMYRTGDlARWLPDGNIE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 393 CQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVpeeheFEKEFQlTSAIKKELAASLPAY 472
Cdd:cd17655 388 FLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-----SEKELP-VAQLREFLARELPDY 461
|
490 500
....*....|....*....|....*..
3E7X_A 473 MIPRKFIYQDHIQMTANGKIDRKRIGE 499
Cdd:cd17655 462 MIPSYFIKLDEIPLTPNGKVDRKALPE 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
11-496 |
5.99e-106 |
|
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: 324.92 E-value: 5.99e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGeKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSER 90
Cdd:cd12117 7 AARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVG-PGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 91 IAKIIESSGAELLIHAAGLSIDAVGQQIQTVSAEEL----LENEGGSVSQDQwvkeheTFYIIYTSGSTGNPKGVQISAA 166
Cdd:cd12117 86 LAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALdagpAGNPAVPVSPDD------LAYVMYTSGSTGRPKGVAVTHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 167 NLQSF---TDWIcadfPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNV-WTSTP 242
Cdd:cd12117 160 GVVRLvknTNYV----TLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVlWLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 243 SFVQMCLMDPgfsqDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVISRSeSLPVGF 322
Cdd:cd12117 236 LFNQLADEDP----ECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAG-SIPIGR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 323 AKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSHE---GQWAYRTGD-AGFIQDGQIFCQGRLD 398
Cdd:cd12117 311 PIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPfgpGERLYRTGDlARWLPDGRLEFLGRID 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 399 FQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEhefekefQLTSA-IKKELAASLPAYMIPRK 477
Cdd:cd12117 391 DQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEG-------ALDAAeLRAFLRERLPAYMVPAA 463
|
490
....*....|....*....
3E7X_A 478 FIYQDHIQMTANGKIDRKR 496
Cdd:cd12117 464 FVVLDELPLTANGKVDRRA 482
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
3-502 |
2.45e-103 |
|
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: 317.14 E-value: 2.45e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRisGEKK-SPILVYGHMEPHMIVSFLGSVKAGHPYIP 81
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRAL--GVGPgDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 82 VDLSIPSERIAKIIESSGAELLIHAaglsidavgqqiqtvsaeelleneggsvsqdqwvkehetfYIIYTSGSTGNPKGV 161
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA----------------------------------------LILYTSGTTGRPKGV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 162 QISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLS-VMDLYPCLQSGGTLHCVTK-DavnkPKVLFEELKKSGLNVWT 239
Cdd:COG0318 119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPRfD----PERVLELIERERVTVLF 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 240 STPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFpKAKIFNTYGPTEATVAVTsveITNDVISRSESLP 319
Cdd:COG0318 195 GVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVT---VNPEDPGERRPGS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 320 VGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfsHEGqWaYRTGDAGFIQ-DGQIFCQGRLD 398
Cdd:COG0318 271 VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF--RDG-W-LRTGDLGRLDeDGYLYIVGRKK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 399 FQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEE-HEFEKEfqltsAIKKELAASLPAYMIPRK 477
Cdd:COG0318 347 DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPgAELDAE-----ELRAFLRERLARYKVPRR 421
|
490 500
....*....|....*....|....*
3E7X_A 478 FIYQDHIQMTANGKIDRKRIGEEVL 502
Cdd:COG0318 422 VEFVDELPRTASGKIDRRALRERYA 446
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
10-495 |
1.34e-96 |
|
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: 301.18 E-value: 1.34e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 10 HAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGeKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSE 89
Cdd:cd17651 4 QAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVG-PGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 90 RIAKIIESSGAELLIHAAGLSIDAVGQQIQTVSAEELLENEGGSVSQDQWVKEHETFYIIYTSGSTGNPKGVQISAANLQ 169
Cdd:cd17651 83 RLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 170 SFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMCL 249
Cdd:cd17651 163 NLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 250 MDPGFSQDLLPhADTFMFC-GEVLPVSVA-KALLERFPKAKIFNTYGPTEATVaVTSVEITNDVISRSESLPVGFAKPDM 327
Cdd:cd17651 243 EHGRPLGVRLA-ALRYLLTgGEQLVLTEDlREFCAGLPGLRLHNHYGPTETHV-VTALSLPGDPAAWPAPPPIGRPIDNT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 328 NIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSH---EGQWAYRTGD-AGFIQDGQIFCQGRLDFQIKL 403
Cdd:cd17651 321 RVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDpfvPGARMYRTGDlARWLPDGELEFLGRADDQVKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 404 HGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEehefEKEFQLTSAIKKELAASLPAYMIPRKFIYQDH 483
Cdd:cd17651 401 RGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGD----PEAPVDAAELRAALATHLPEYMVPSAFVLLDA 476
|
490
....*....|..
3E7X_A 484 IQMTANGKIDRK 495
Cdd:cd17651 477 LPLTPNGKLDRR 488
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
15-496 |
3.41e-95 |
|
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: 296.90 E-value: 3.41e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 15 PQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGEKkSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKI 94
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPG-DRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 95 IESSGAELLI----HAAGLSIDAVGQQIQTVSAEELLENEGGSVSQDQwvkeheTFYIIYTSGSTGNPKGVQISAANLQS 170
Cdd:cd12116 80 LEDAEPALVLtddaLPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDD------LAYVIYTSGSTGRPKGVVVSHRNLVN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 171 FTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMcLM 250
Cdd:cd12116 154 FLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRM-LL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 251 DPGFSqdllPHADTFMFCG-EVLPVSVAKALLERfpKAKIFNTYGPTEATVAVTSVEITndviSRSESLPVGFAKPDMNI 329
Cdd:cd12116 233 DAGWQ----GRAGLTALCGgEALPPDLAARLLSR--VGSLWNLYGPTETTIWSTAARVT----AAAGPIPIGRPLANTQV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 330 FIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWAYRTGD-AGFIQDGQIFCQGRLDFQIKLH 404
Cdd:cd12116 303 YVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFvpdpFAGPGSRLYRTGDlVRRRADGRLEYLGRADGQVKIR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 405 GYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEyLIAAIVPEEHEFEKefqlTSAIKKELAASLPAYMIPRKFIYQDHI 484
Cdd:cd12116 383 GHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPD----AAALRAHLRATLPAYMVPSAFVRLDAL 457
|
490
....*....|..
3E7X_A 485 QMTANGKIDRKR 496
Cdd:cd12116 458 PLTANGKLDRKA 469
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
3-501 |
5.20e-95 |
|
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: 296.76 E-value: 5.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISG-EKKSPIlvygHME--PHMIVSFLGSVKAGHPY 79
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGpGVFVPL----CFEksKWAVVAMLAVLKAGGAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 80 IPVDLSIPSERIAKIIESSGAELLIhaaglsidavgqqiqtvsaeelleneggsVSQdqwvkEHETFYIIYTSGSTGNPK 159
Cdd:cd05918 77 VPLDPSHPLQRLQEILQDTGAKVVL-----------------------------TSS-----PSDAAYVIFTSGSTGKPK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 160 GVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLhCVTKDA--VNKpkvLFEELKKSGLNv 237
Cdd:cd05918 123 GVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCL-CIPSEEdrLND---LAGFINRLRVT- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 238 WTS-TPSFVQmcLMDPgfsqDLLPHADTFMFCGEVLPVSVakalLERF-PKAKIFNTYGPTEATVAVTSVEITNDVISRS 315
Cdd:cd05918 198 WAFlTPSVAR--LLDP----EDVPSLRTLVLGGEALTQSD----VDTWaDRVRLINAYGPAECTIAATVSPVVPSTDPRN 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 316 ESLPVGfakpdMNIFIMDEE--GQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSHEGQWA----------YRTGD- 382
Cdd:cd05918 268 IGRPLG-----ATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKqegsgrgrrlYRTGDl 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 383 AGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQ-YVRSAVVIPYQPNG--TVEYLIAAIVPEEHE--------- 450
Cdd:cd05918 343 VRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLpGAKEVVVEVVKPKDgsSSPQLVAFVVLDGSSsgsgdgdsl 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
3E7X_A 451 ----FEKEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEEV 501
Cdd:cd05918 423 flepSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
15-495 |
2.23e-94 |
|
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: 295.34 E-value: 2.23e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 15 PQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRiSGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKI 94
Cdd:cd17646 12 PDAPAVVDEGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 95 IESSGAELLIHAAGLSIDAVGQQIQTVSAEELLENEGGSVSQdQWVKEHETFYIIYTSGSTGNPKGVQISAANLQSFTDW 174
Cdd:cd17646 91 LADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPL-VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLW 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 175 ICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPS----FVQMclM 250
Cdd:cd17646 170 MQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSmlrvFLAE--P 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 251 DPGFSQDLlphadTFMFC-GEVLPVSVAKALLERFPkAKIFNTYGPTEATVAVTSVEITNDVisRSESLPVGFAKPDMNI 329
Cdd:cd17646 248 AAGSCASL-----RRVFCsGEALPPELAARFLALPG-AELHNLYGPTEAAIDVTHWPVRGPA--ETPSVPIGRPVPNTRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 330 FIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSH---EGQWAYRTGD-AGFIQDGQIFCQGRLDFQIKLHG 405
Cdd:cd17646 320 YVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDpfgPGSRMYRTGDlARWRPDGALEFLGRSDDQVKIRG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 406 YRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEFEkefQLTSAIKKELAASLPAYMIPRKFIYQDHIQ 485
Cdd:cd17646 400 FRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAG---PDTAALRAHLAERLPEYMVPAAFVVLDALP 476
|
490
....*....|
3E7X_A 486 MTANGKIDRK 495
Cdd:cd17646 477 LTANGKLDRA 486
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
5-497 |
1.56e-91 |
|
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: 286.13 E-value: 1.56e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 5 HAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISgEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDL 84
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGV-VPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 85 SIPSERIAKIIESSGAELLIHAAglsidavgqqiqtvsaeelleneggsvsqdqwvKEHETFYIIYTSGSTGNPKGVQIS 164
Cdd:cd17653 80 KLPSARIQAILRTSGATLLLTTD---------------------------------SPDDLAYIIFTSGSTGIPKGVMVP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 165 AANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLhcVTKDavnkPKVLFEELKKSgLNVWTSTPSF 244
Cdd:cd17653 127 HRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTL--VLAD----PSDPFAHVART-VDALMSTPSI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 245 VQMClmdpgfSQDLLPHADTFMFCGEVLPVSVAKALLERfpkAKIFNTYGPTEATVAVTSVEITNDVisrseSLPVGFAK 324
Cdd:cd17653 200 LSTL------SPQDFPNLKTIFLGGEAVPPSLLDRWSPG---RRLYNAYGPTECTISSTMTELLPGQ-----PVTIGKPI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 325 PDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFS---HEGQWAYRTGDAGFI-QDGQIFCQGRLDFQ 400
Cdd:cd17653 266 PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPdpfWPGSRMYRTGDYGRWtEDGGLEFLGREDNQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 401 IKLHGYRMELEEIEFHVRQSQ-YVRSAVVIpyQPNGTveyLIAAIVPEEHEfekefqlTSAIKKELAASLPAYMIPRKFI 479
Cdd:cd17653 346 VKVRGFRINLEEIEEVVLQSQpEVTQAAAI--VVNGR---LVAFVTPETVD-------VDGLRSELAKHLPSYAVPDRII 413
|
490
....*....|....*...
3E7X_A 480 YQDHIQMTANGKIDRKRI 497
Cdd:cd17653 414 ALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
15-496 |
2.95e-90 |
|
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: 284.16 E-value: 2.95e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 15 PQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRI--SGEkksPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIA 92
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGvrPGD---LVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 93 KIIESSGAELLIhaAGLSIDAVGQQIQTVSAEELLENEGGSVSQDQWVKEHETFYIIYTSGSTGNPKGVQISAANLQSFT 172
Cdd:cd12114 78 AILADAGARLVL--TDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 173 DWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMCLMDP 252
Cdd:cd12114 156 LDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 253 GFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITnDVISRSESLPVGFAKPDMNIFIM 332
Cdd:cd12114 236 EAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPID-EVPPDWRSIPYGRPLANQRYRVL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 333 DEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSH-EGQWAYRTGDAG-FIQDGQI-FCqGRLDFQIKLHGYRME 409
Cdd:cd12114 315 DPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHpDGERLYRTGDLGrYRPDGTLeFL-GRRDGQVKVRGYRIE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 410 LEEIEFHVRQSQYVRSAVVIPYQpNGTVEYLIAAIVPEehefEKEFQLTS-AIKKELAASLPAYMIPRKFIYQDHIQMTA 488
Cdd:cd12114 394 LGEIEAALQAHPGVARAVVVVLG-DPGGKRLAAFVVPD----NDGTPIAPdALRAFLAQTLPAYMIPSRVIALEALPLTA 468
|
....*...
3E7X_A 489 NGKIDRKR 496
Cdd:cd12114 469 NGKVDRAA 476
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
15-495 |
3.09e-90 |
|
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: 283.43 E-value: 3.09e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 15 PQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGeKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKI 94
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVG-PGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 95 IESSGAELLIhaaglsidavgqqiqtvsaeelleneggsvsqdqwVKEHETFYIIYTSGSTGNPKGVQISAAN---LQSF 171
Cdd:cd17643 80 LADSGPSLLL-----------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANvlaLFAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 172 TDWIcadFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPS-FVQMCLM 250
Cdd:cd17643 125 TQRW---FGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSaFYQLVEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 251 DPGFSQDLLPHADTFmFCGEVLPVSVAKALLERF--PKAKIFNTYGPTEATVAVTSVEITNDVISRSESLPVGFAKPDMN 328
Cdd:cd17643 202 ADRDGRDPLALRYVI-FGGEALEAAMLRPWAGRFglDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 329 IFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWAYRTGD-AGFIQDGQIFCQGRLDFQIKL 403
Cdd:cd17643 281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFvanpFGGPGSRMYRTGDlARRLPDGELEYLGRADEQVKI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 404 HGYRMELEEIEFHVRQSQYVRSAVVIP--YQPNGTveYLIAAIVPEEhefEKEfQLTSAIKKELAASLPAYMIPRKFIYQ 481
Cdd:cd17643 361 RGFRIELGEIEAALATHPSVRDAAVIVreDEPGDT--RLVAYVVADD---GAA-ADIAELRALLKELLPDYMVPARYVPL 434
|
490
....*....|....
3E7X_A 482 DHIQMTANGKIDRK 495
Cdd:cd17643 435 DALPLTVNGKLDRA 448
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-495 |
7.62e-89 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 298.61 E-value: 7.62e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 4 LHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGekkSPILV--YGHMEPHMIVSFLGSVKAGHPYIP 81
Cdd:PRK12467 515 HQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVG---PDVLVgiAVERSIEMVVGLLAVLKAGGAYVP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 82 VDLSIPSERIAKIIESSGAELLIH----------AAGLS---IDAVGQQIQTVSAEelleNEGGSVSQDQWVkehetfYI 148
Cdd:PRK12467 592 LDPEYPQDRLAYMLDDSGVRLLLTqshllaqlpvPAGLRslcLDEPADLLCGYSGH----NPEVALDPDNLA------YV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 149 IYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFE 228
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAA 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 229 ELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHadTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEIT 308
Cdd:PRK12467 742 LMADQGVTVLKIVPSHLQALLQASRVALPRPQR--ALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELS 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 309 NDVISRSESlPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWAYRTGD-A 383
Cdd:PRK12467 820 DEERDFGNV-PIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFvpdpFGADGGRLYRTGDlA 898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 384 GFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPyQPNGTVEYLIAAIVPEEHEFEKEFQLTS-AIK 462
Cdd:PRK12467 899 RYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLVPAAVADGAEHQATRdELK 977
|
490 500 510
....*....|....*....|....*....|...
3E7X_A 463 KELAASLPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK12467 978 AQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
25-495 |
6.87e-88 |
|
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: 277.04 E-value: 6.87e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 25 QSLTYQELWEQSDRAAAAIQKRiSGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLi 104
Cdd:cd17650 11 RQLTYRELNERANQLARTLRGL-GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 105 haaglsidavgqqiqtvsaeeLLENEggsvsqdqwvkehETFYIIYTSGSTGNPKGVQISAANLQSFT-----DWICADF 179
Cdd:cd17650 89 ---------------------LTQPE-------------DLAYVIYTSGTTGKPKGVMVEHRNVAHAAhawrrEYELDSF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 180 PVSggkiFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVqMCLMDPGFSQDL- 258
Cdd:cd17650 135 PVR----LLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALI-RPVMAYVYRNGLd 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 259 LPHADTFMFCGEVLPVSVAKALLERF-PKAKIFNTYGPTEATVAVTSVEITNDVISRSESLPVGFAKPDMNIFIMDEEGQ 337
Cdd:cd17650 210 LSAMRLLIVGSDGCKAQDFKTLAARFgQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLDERLQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 338 PLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSH---EGQWAYRTGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELEEI 413
Cdd:cd17650 290 PQPVGVAGELYIGGAGVARGYLNRPELTAERFVENpfaPGERMYRTGDlARWRADGNVELLGRVDHQVKIRGFRIELGEI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 414 EFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEFekefqlTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKID 493
Cdd:cd17650 370 ESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLN------TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443
|
..
3E7X_A 494 RK 495
Cdd:cd17650 444 RR 445
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
15-495 |
1.20e-87 |
|
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: 276.56 E-value: 1.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 15 PQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGEKkspILVYGHME--PHMIVSFLGSVKAGHPYIPVDLSIPSERIA 92
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPE---VRVGIALErsLEMVVALLAILKAGGAYVPLDPEYPAERLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 93 KIIESSGAELLIHAAGLSIDavgqqiqtvsaeelleneggsvsqdqwvkehetfYIIYTSGSTGNPKGVQISAANLQSFT 172
Cdd:cd17649 78 YMLEDSGAGLLLTHHPRQLA----------------------------------YVIYTSGSTGTPKGVAVSHGPLAAHC 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 173 DWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMclmdp 252
Cdd:cd17649 124 QATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQ----- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 253 gFSQDLLPHAD-------TFMFCGEVLPVSvakaLLERFPKA--KIFNTYGPTEATVAVTSVEITNDVISRSESLPVGFA 323
Cdd:cd17649 199 -LAEEADRTGDgrppslrLYIFGGEALSPE----LLRRWLKApvRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 324 KPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWAYRTGD-AGFIQDGQIFCQGRLD 398
Cdd:cd17649 274 LGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpdpFGAPGSRLYRTGDlARWRDDGVIEYLGRVD 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 399 FQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEyLIAAIVPEEHEFEKEfqLTSAIKKELAASLPAYMIPRKF 478
Cdd:cd17649 354 HQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQ-LVAYVVLRAAAAQPE--LRAQLRTALRASLPDYMVPAHL 430
|
490
....*....|....*..
3E7X_A 479 IYQDHIQMTANGKIDRK 495
Cdd:cd17649 431 VFLARLPLTPNGKLDRK 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-495 |
9.68e-85 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 286.85 E-value: 9.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 7 IQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGEKkspILVYGHME--PHMIVSFLGSVKAGHPYIPVDL 84
Cdd:PRK12316 4557 VAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPE---VLVGIAMErsAEMMVGLLAVLKAGGAYVPLDP 4633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 85 SIPSERIAKIIESSGAELLI-HAAGLSIDAVGQQIQTVSAEELLENEGGSvSQDQWVKEH--ETFYIIYTSGSTGNPKGV 161
Cdd:PRK12316 4634 EYPRERLAYMMEDSGAALLLtQSHLLQRLPIPDGLASLALDRDEDWEGFP-AHDPAVRLHpdNLAYVIYTSGSTGRPKGV 4712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 162 QISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHcVTKDAVNKPKVLFEELKKSGLNVWTST 241
Cdd:PRK12316 4713 AVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVV-IRDDSLWDPERLYAEIHEHRVTVLVFP 4791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 242 PSFVQMCLMDPGFSQDLLPhADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVISRSESLPVG 321
Cdd:PRK12316 4792 PVYLQQLAEHAERDGEPPS-LRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIG 4870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 322 FAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWAYRTGD-AGFIQDGQIFCQGR 396
Cdd:PRK12316 4871 TPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpFGAPGGRLYRTGDlARYRADGVIDYLGR 4950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 397 LDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPyQPNGTVEYLIAAIVPEEHEF----EKEFQLTSAIKKELAASLPAY 472
Cdd:PRK12316 4951 VDHQVKIRGFRIELGEIEARLREHPAVREAVVIA-QEGAVGKQLVGYVVPQDPALadadEAQAELRDELKAALRERLPEY 5029
|
490 500
....*....|....*....|...
3E7X_A 473 MIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK12316 5030 MVPAHLVFLARMPLTPNGKLDRK 5052
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
3-497 |
6.14e-83 |
|
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: 264.18 E-value: 6.14e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISG-EKKSPILvyghME--PHMIVSFLGSVKAGHPY 79
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGpESRVGVC----LErtPDLVVALLAVLKAGAAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 80 IPVDLSIPSERIAKIIESSGAELLIhaaglsidavgqqiqtvsaeelleneggsvsqdqwVKEHETFYIIYTSGSTGNPK 159
Cdd:cd12115 77 VPLDPAYPPERLRFILEDAQARLVL-----------------------------------TDPDDLAYVIYTSGSTGRPK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 160 GVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHcvtkdAVNKPKVLFEELKKSGLNVWT 239
Cdd:cd12115 122 GVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVV-----LADNVLALPDLPAAAEVTLIN 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 240 STPSfvqmcLMDPGFSQDLLP-HADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDvisRSESL 318
Cdd:cd12115 197 TVPS-----AAAELLRHDALPaSVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPG---ASGEV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 319 PVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFS---HEGQWAYRTGD-AGFIQDGQIFCQ 394
Cdd:cd12115 269 SIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPdpfGPGARLYRTGDlVRWRPDGLLEFL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 395 GRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPeehEFEKEFQLTsAIKKELAASLPAYMI 474
Cdd:cd12115 349 GRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVA---EPGAAGLVE-DLRRHLGTRLPAYMV 424
|
490 500
....*....|....*....|...
3E7X_A 475 PRKFIYQDHIQMTANGKIDRKRI 497
Cdd:cd12115 425 PSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
15-495 |
1.48e-82 |
|
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: 262.96 E-value: 1.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 15 PQTDAFRSQGQSLTYQELWEQSDRAAAAIQKR-ISGEKKSPILVYGhmEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAK 93
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARgVGPERLVALALPR--SAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 94 IIESSGAELLI----HAAglsidavgqqiqtvsaeelleneggsvsqdqwvkehetfYIIYTSGSTGNPKGVQISAANLQ 169
Cdd:cd17652 79 MLADARPALLLttpdNLA---------------------------------------YVIYTSGSTGRPKGVVVTHRGLA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 170 SFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMcl 249
Cdd:cd17652 120 NLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA-- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 250 MDPgfsqDLLPHADTFMFCGEVLPvsvaKALLERF-PKAKIFNTYGPTEATVAVTSVEITNDvisrSESLPVGFAKPDMN 328
Cdd:cd17652 198 LPP----DDLPDLRTLVVAGEACP----AELVDRWaPGRRMINAYGPTETTVCATMAGPLPG----GGVPPIGRPVPGTR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 329 IFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWAYRTGD-AGFIQDGQIFCQGRLDFQIKL 403
Cdd:cd17652 266 VYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFvadpFGAPGSRMYRTGDlARWRADGQLEFLGRADDQVKI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 404 HGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEehefEKEFQLTSAIKKELAASLPAYMIPRKFIYQDH 483
Cdd:cd17652 346 RGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPA----PGAAPTAAELRAHLAERLPGYMVPAAFVVLDA 421
|
490
....*....|..
3E7X_A 484 IQMTANGKIDRK 495
Cdd:cd17652 422 LPLTPNGKLDRR 433
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
5-495 |
1.55e-82 |
|
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: 263.91 E-value: 1.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 5 HAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQ-KRISGEKKSPILVYGHMEphMIVSFLGSVKAGHPYIPVD 83
Cdd:cd17644 4 QLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQsLGVKSESLVGICVERSLE--MIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 84 LSIPSERIAKIIESSGAELLIhaaglsidavgqqiqtvsaeelleneggsvsqdqwVKEHETFYIIYTSGSTGNPKGVQI 163
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLL-----------------------------------TQPENLAYVIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 164 SAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPS 243
Cdd:cd17644 127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 244 FVQMCLMDPGFSQDLLPHADTFMFCG--EVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVISRSESLPVG 321
Cdd:cd17644 207 YWHLLVLELLLSTIDLPSSLRLVIVGgeAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSVPIG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 322 FAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSH-----EGQWAYRTGD-AGFIQDGQIFCQG 395
Cdd:cd17644 287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHpfnssESERLYKTGDlARYLPDGNIEYLG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 396 RLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEehefEKEFQLTSAIKKELAASLPAYMIP 475
Cdd:cd17644 367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPH----YEESPSTVELRQFLKAKLPDYMIP 442
|
490 500
....*....|....*....|
3E7X_A 476 RKFIYQDHIQMTANGKIDRK 495
Cdd:cd17644 443 SAFVVLEELPLTPNGKIDRR 462
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-495 |
1.05e-80 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 274.73 E-value: 1.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 2 KLLHA-IQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAA-IQKRISGEKKSPILVYGHMEphMIVSFLGSVKAGHPY 79
Cdd:PRK12467 1574 RLVHQlIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRlIALGVGPEVLVGIAVERSLE--MVVGLLAILKAGGAY 1651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 80 IPVDLSIPSERIAKIIESSGAELLI-HAAGLSIDAVGQQIQTV---SAEELLENEGGSVSQDQwVKEHETFYIIYTSGST 155
Cdd:PRK12467 1652 VPLDPEYPRERLAYMIEDSGIELLLtQSHLQARLPLPDGLRSLvldQEDDWLEGYSDSNPAVN-LAPQNLAYVIYTSGST 1730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 156 GNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGL 235
Cdd:PRK12467 1731 GRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQV 1810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 236 NVWTSTPSFVQMCLMDPGfsQDLLPHADTFMFC-GEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVISR 314
Cdd:PRK12467 1811 TTLHFVPSMLQQLLQMDE--QVEHPLSLRRVVCgGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEG 1888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 315 SESLPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWAYRTGD-AGFIQDG 389
Cdd:PRK12467 1889 RDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpFGTVGSRLYRTGDlARYRADG 1968
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 390 QIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQ-PNGTveYLIAAIVPEE----HEFEKEFQLTSAIKKE 464
Cdd:PRK12467 1969 VIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDgANGK--QLVAYVVPTDpglvDDDEAQVALRAILKNH 2046
|
490 500 510
....*....|....*....|....*....|.
3E7X_A 465 LAASLPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK12467 2047 LKASLPEYMVPAHLVFLARMPLTPNGKLDRK 2077
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-495 |
1.37e-80 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 274.53 E-value: 1.37e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGekkSPILVYGHME--PHMIVSFLGSVKAGHPYI 80
Cdd:PRK12316 513 VHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVG---PDVLVGVAMErsIEMVVALLAILKAGGAYV 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 81 PVDLSIPSERIAKIIESSGAELLIH----AAGLSIDAVGQQIQTVSAEELLENEGGSVSQDQWVKEHETfYIIYTSGSTG 156
Cdd:PRK12316 590 PLDPEYPAERLAYMLEDSGVQLLLSqshlGRKLPLAAGVQVLDLDRPAAWLEGYSEENPGTELNPENLA-YVIYTSGSTG 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 157 NPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLN 236
Cdd:PRK12316 669 KPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVD 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 237 VWTSTPSFVQMCLMDPGfSQDLLPhADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVisrSE 316
Cdd:PRK12316 749 TLHFVPSMLQAFLQDED-VASCTS-LRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEG---GD 823
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 317 SLPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSHE---GQWAYRTGD-AGFIQDGQIF 392
Cdd:PRK12316 824 SVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPfvaGERMYRTGDlARYRADGVIE 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 393 CQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPngtvEYLIAAIVPEehefEKEFQLTSAIKKELAASLPAY 472
Cdd:PRK12316 904 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG----KQLVGYVVLE----SEGGDWREALKAHLAASLPEY 975
|
490 500
....*....|....*....|...
3E7X_A 473 MIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK12316 976 MVPAQWLALERLPLTPNGKLDRK 998
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-495 |
3.11e-79 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 270.49 E-value: 3.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 2 KLLHA-IQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAA-IQKRISGEKKSPILVYGHMEphMIVSFLGSVKAGHPY 79
Cdd:PRK12467 3095 RLVHQlIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRlIAIGVGPDVLVGVAVERSVE--MIVALLAVLKAGGAY 3172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 80 IPVDLSIPSERIAKIIESSGAELLIHAAG----LSIDAVGQQ--IQTVSAEELLENEGGSVSQDQWVKehetfYIIYTSG 153
Cdd:PRK12467 3173 VPLDPEYPRERLAYMIEDSGVKLLLTQAHlleqLPAPAGDTAltLDRLDLNGYSENNPSTRVMGENLA-----YVIYTSG 3247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 154 STGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHcVTKDAVNKPKVLFEELKKS 233
Cdd:PRK12467 3248 STGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLV-VRDNDLWDPEELWQAIHAH 3326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 234 GLNVWTSTPSFVQMCLMDPGfSQDLLPhADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVIS 313
Cdd:PRK12467 3327 RISIACFPPAYLQQFAEDAG-GADCAS-LDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVC 3404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 314 RSESLPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWAYRTGD-AGFIQD 388
Cdd:PRK12467 3405 EAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFvadpFSGSGGRLYRTGDlARYRAD 3484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 389 GQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPyQPNGTVEYLIAAIVPEEHEFEkefqLTSAIKKELAAS 468
Cdd:PRK12467 3485 GVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLA-RDGAGGKQLVAYVVPADPQGD----WRETLRDHLAAS 3559
|
490 500
....*....|....*....|....*..
3E7X_A 469 LPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK12467 3560 LPDYMVPAQLLVLAAMPLGPNGKVDRK 3586
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-495 |
3.38e-77 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 264.90 E-value: 3.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 7 IQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGekkSPILVYGHMEP--HMIVSFLGSVKAGHPYIPVDL 84
Cdd:PRK12316 3063 FEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVG---PDVLVGVAVERslEMVVGLLAILKAGGAYVPLDP 3139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 85 SIPSERIAKIIESSGAELLIHAAGLSIDAVgQQIQTVSAEELLENEGGSVSQDQWVKEHETfYIIYTSGSTGNPKGVQIS 164
Cdd:PRK12316 3140 EYPEERLAYMLEDSGAQLLLSQSHLRLPLA-QGVQVLDLDRGDENYAEANPAIRTMPENLA-YVIYTSGSTGKPKGVGIR 3217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 165 AANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSF 244
Cdd:PRK12316 3218 HSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSM 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 245 VQMCLMDPGFSQdlLPHADTFMFCGEVLPVSVAKALLERFPkakIFNTYGPTEATVAVTSVEITNDVISrseSLPVGFAK 324
Cdd:PRK12316 3298 LQAFLEEEDAHR--CTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTHWQCVEEGKD---AVPIGRPI 3369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 325 PDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSH---EGQWAYRTGD-AGFIQDGQIFCQGRLDFQ 400
Cdd:PRK12316 3370 ANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDpfvPGERLYRTGDlARYRADGVIEYIGRVDHQ 3449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 401 IKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPngtvEYLIAAIVPEEHEFEkefqLTSAIKKELAASLPAYMIPRKFIY 480
Cdd:PRK12316 3450 VKIRGFRIELGEIEARLLEHPWVREAVVLAVDG----RQLVAYVVPEDEAGD----LREALKAHLKASLPEYMVPAHLLF 3521
|
490
....*....|....*
3E7X_A 481 QDHIQMTANGKIDRK 495
Cdd:PRK12316 3522 LERMPLTPNGKLDRK 3536
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
15-497 |
5.29e-77 |
|
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: 249.70 E-value: 5.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 15 PQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGeKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKI 94
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVK-KDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 95 IESSGAELLIHAAGLSiDAVGQQIQTVSAEELLENEGGSVSQDQWVKEHETFYIIYTSGSTGNPKGVQI---SAANLQSF 171
Cdd:cd17656 81 MLDSGVRVVLTQRHLK-SKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLehkNMVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 172 T-DWICADFpvsGGKIfLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMCLM 250
Cdd:cd17656 160 ErEKTNINF---SDKV-LQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 251 DPGFSQDLLPHADTFMFCGEVLPVSvaKALLERFPKAKI--FNTYGPTEATVaVTSVEItNDVISRSESLPVGfaKPDMN 328
Cdd:cd17656 236 EREFINRFPTCVKHIITAGEQLVIT--NEFKEMLHEHNVhlHNHYGPSETHV-VTTYTI-NPEAEIPELPPIG--KPISN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 329 --IFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSH---EGQWAYRTGD-AGFIQDGQIFCQGRLDFQIK 402
Cdd:cd17656 310 twIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDpfdPNERMYRTGDlARYLPDGNIEFLGRADHQVK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 403 LHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHefekefQLTSAIKKELAASLPAYMIPRKFIYQD 482
Cdd:cd17656 390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQE------LNISQLREYLAKQLPEYMIPSFFVPLD 463
|
490
....*....|....*
3E7X_A 483 HIQMTANGKIDRKRI 497
Cdd:cd17656 464 QLPLTPNGKVDRKAL 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-495 |
1.85e-75 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 259.89 E-value: 1.85e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 6 AIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGEKkspILVYGHME--PHMIVSFLGSVKAGHPYIPVD 83
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPE---VRVAIAAErsFELVVALLAVLKAGGAYVPLD 2084
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 84 LSIPSERIAKIIESSGAELLIHAAGLSID---AVGQQIQTVSAEELLENEGGSVSQDQwVKEHETFYIIYTSGSTGNPKG 160
Cdd:PRK12316 2085 PNYPAERLAYMLEDSGAALLLTQRHLLERlplPAGVARLPLDRDAEWADYPDTAPAVQ-LAGENLAYVIYTSGSTGLPKG 2163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 161 VQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLhCVTKDAVNKPKVLFEELKKSGLNVWTS 240
Cdd:PRK12316 2164 VAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTILDF 2242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 241 TPSFVQMcLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVISRSESLPV 320
Cdd:PRK12316 2243 PPVYLQQ-LAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPI 2321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 321 GFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWAYRTGD-AGFIQDGQIFCQG 395
Cdd:PRK12316 2322 GRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFvpdpFSASGERLYRTGDlARYRADGVVEYLG 2401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 396 RLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPyQPNGTVEYLIAAIVPEehefEKEFQLTSAIKKELAASLPAYMIP 475
Cdd:PRK12316 2402 RIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA-QDGASGKQLVAYVVPD----DAAEDLLAELRAWLAARLPAYMVP 2476
|
490 500
....*....|....*....|
3E7X_A 476 RKFIYQDHIQMTANGKIDRK 495
Cdd:PRK12316 2477 AHWVVLERLPLNPNGKLDRK 2496
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
11-495 |
2.34e-75 |
|
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: 244.39 E-value: 2.34e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQ-KRISGEKKSPILVYGHMEphMIVSFLGSVKAGHPYIPVDLSIPSE 89
Cdd:cd17645 8 VERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRgKGVKPDDQVGIMLDKSLD--MIAAILGVLKAGGAYVPIDPDYPGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 90 RIAKIIESSGAELLIHAAGlsidavgqqiqtvsaeelleneggsvsqdqwvkehETFYIIYTSGSTGNPKGVQISAANLQ 169
Cdd:cd17645 86 RIAYMLADSSAKILLTNPD-----------------------------------DLAYVIYTSGSTGLPKGVMIEHHNLV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 170 SFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNV-WTSTPSFVQMC 248
Cdd:cd17645 131 NLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIsFLPTGAAEQFM 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 249 LMDpgfSQDLlphaDTFMFCGEVLPVSVAKALlerfpkaKIFNTYGPTEATVAVTSVEITNDvisrSESLPVGFAKPDMN 328
Cdd:cd17645 211 QLD---NQSL----RVLLTGGDKLKKIERKGY-------KLVNNYGPTENTVVATSFEIDKP----YANIPIGKPIDNTR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 329 IFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSH---EGQWAYRTGD-AGFIQDGQIFCQGRLDFQIKLH 404
Cdd:cd17645 273 VYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHpfvPGERMYRTGDlAKFLPDGNIEFLGRLDQQVKIR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 405 GYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEhEFEKEfqltsAIKKELAASLPAYMIPRKFIYQDHI 484
Cdd:cd17645 353 GYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPE-EIPHE-----ELREWLKNDLPDYMIPTYFVHLKAL 426
|
490
....*....|.
3E7X_A 485 QMTANGKIDRK 495
Cdd:cd17645 427 PLTANGKVDRK 437
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-501 |
4.04e-68 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 238.14 E-value: 4.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQ-KRISGEKKSPILVygHMEPHMIVSFLGSVKAGHPYIP 81
Cdd:PRK05691 1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRdKGVGPDVCVAIAA--ERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 82 VDLSIPSERIAKIIESSGAELLIHAAGLsIDAVgQQIQTVSAEELlenegGSVSQDQW--------VKEHETFYIIYTSG 153
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLTQSHL-LERL-PQAEGVSAIAL-----DSLHLDSWpsqapglhLHGDNLAYVIYTSG 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 154 STGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKS 233
Cdd:PRK05691 1284 STGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQY 1363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 234 GLNVWTSTPSFVQMCLMDPGFSQdllPHADTFMFC-GEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVI 312
Cdd:PRK05691 1364 GVTTLHFVPPLLQLFIDEPLAAA---CTSLRRLFSgGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDG 1440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 313 SRSeslPVGfaKPDMNIF--IMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWAYRTGD-AGF 385
Cdd:PRK05691 1441 ERS---PIG--RPLGNVLcrVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFvpdpLGEDGARLYRTGDrARW 1515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 386 IQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQ-PNGT--VEYLIAAIVPEEHefekefqlTSAIK 462
Cdd:PRK05691 1516 NADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREgAAGAqlVGYYTGEAGQEAE--------AERLK 1587
|
490 500 510
....*....|....*....|....*....|....*....
3E7X_A 463 KELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEEV 501
Cdd:PRK05691 1588 AALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPV 1626
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
15-497 |
7.51e-63 |
|
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: 211.88 E-value: 7.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 15 PQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKI 94
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 95 IESSGAELLIhaaglsidavgqqiqtVSAEELLeneggsvsqdqwvkehetfYIIYTSGSTGNPKGVQISAANLQSFTDW 174
Cdd:cd17648 81 LEDTGARVVI----------------TNSTDLA-------------------YAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 175 ICADFPVS--GGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMclmdp 252
Cdd:cd17648 126 LSERYFGRdnGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQ----- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 253 gFSQDLLPHADTFMFCGEVLPVSVAKALLERFPkAKIFNTYGPTEATVavTSVEITNDVISRSESlPVGFAKPDMNIFIM 332
Cdd:cd17648 201 -YDLARLPHLKRVDAAGEEFTAPVFEKLRSRFA-GLIINAYGPTETTV--TNHKRFFPGDQRFDK-SLGRPVRNTKCYVL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 333 DEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWA-------YRTGD-AGFIQDGQIFCQGRLDFQ 400
Cdd:cd17648 276 NDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFlpnpFQTEQERArgrnarlYKTGDlVRWLPSGELEYLGRNDFQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 401 IKLHGYRMELEEIEFHVRQSQYVRSAVVIP-YQPNGTVE----YLIAAIVPEEHEFEKefqltSAIKKELAASLPAYMIP 475
Cdd:cd17648 356 VKIRGQRIEPGEVEAALASYPGVRECAVVAkEDASQAQSriqkYLVGYYLPEPGHVPE-----SDLLSFLRAKLPRYMVP 430
|
490 500
....*....|....*....|..
3E7X_A 476 RKFIYQDHIQMTANGKIDRKRI 497
Cdd:cd17648 431 ARLVRLEGIPVTINGKLDVRAL 452
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
147-493 |
3.37e-62 |
|
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: 206.75 E-value: 3.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 147 YIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDavnKPKVL 226
Cdd:cd04433 4 LILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 227 FEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFpKAKIFNTYGPTEATVAVTSVE 306
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAP-GIKLVNGYGLTETGGTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 307 ITNDVISRSeslPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTekAFFSHEGqWaYRTGDAGFI 386
Cdd:cd04433 160 PDDDARKPG---SVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEAT--AAVDEDG-W-YRTGDLGRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 387 -QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEE-HEFEKEfqltsAIKKE 464
Cdd:cd04433 233 dEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPgADLDAE-----ELRAH 307
|
330 340
....*....|....*....|....*....
3E7X_A 465 LAASLPAYMIPRKFIYQDHIQMTANGKID 493
Cdd:cd04433 308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
15-495 |
9.19e-61 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 216.45 E-value: 9.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 15 PQTDAFRSQGQSLTYQELWEQSdrAAAAIQKRISGEKKSPIL-VYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAK 93
Cdd:PRK10252 472 PDAPALADARYQFSYREMREQV--VALANLLRERGVKPGDSVaVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKM 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 94 IIESSGAELLIHAAGLS---IDAVGQQIQTVSAEeLLENEGGSVSQDQwvkEHETFYIIYTSGSTGNPKGVQISAANLQS 170
Cdd:PRK10252 550 MLEDARPSLLITTADQLprfADVPDLTSLCYNAP-LAPQGAAPLQLSQ---PHHTAYIIFTSGSTGRPKGVMVGQTAIVN 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 171 FTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMCLM 250
Cdd:PRK10252 626 RLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVA 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 251 DPgfSQDLLPHADTFM---FC-GEVLPVSVAKaLLERFPKAKIFNTYGPTEATVAVT----SVEITNDVisRSESLPVGF 322
Cdd:PRK10252 706 SL--TPEGARQSCASLrqvFCsGEALPADLCR-EWQQLTGAPLHNLYGPTEAAVDVSwypaFGEELAAV--RGSSVPIGY 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 323 AKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSH---EGQWAYRTGD-AGFIQDGQIFCQGRLD 398
Cdd:PRK10252 781 PVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfaPGERMYRTGDvARWLDDGAVEYLGRSD 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 399 FQIKLHGYRMELEEIEfHVRQS-----QYVRSAVVIPYQP--NGTVEYLIAAIVPEEHEFEKefqlTSAIKKELAASLPA 471
Cdd:PRK10252 861 DQLKIRGQRIELGEID-RAMQAlpdveQAVTHACVINQAAatGGDARQLVGYLVSQSGLPLD----TSALQAQLRERLPP 935
|
490 500
....*....|....*....|....
3E7X_A 472 YMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK10252 936 HMVPVVLLQLDQLPLSANGKLDRK 959
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
14-495 |
1.27e-60 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 216.19 E-value: 1.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 14 YPQTDAFRSQGQSLTYQELWEQSDRAA-AAIQKRISGEKKSPILVYGHME-PHMIVsflGSVKAGHPYIPVDLSIPSERI 91
Cdd:PRK05691 3733 HPQRIAASCLDQQWSYAELNRAANRLGhALRAAGVGVDQPVALLAERGLDlLGMIV---GSFKAGAGYLPLDPGLPAQRL 3809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 92 AKIIESSGAELLIHAAglsidAVGQQiqtvsAEELLENEGGS----------VSQDQWVKEHETF--------YIIYTSG 153
Cdd:PRK05691 3810 QRIIELSRTPVLVCSA-----ACREQ-----ARALLDELGCAnrprllvweeVQAGEVASHNPGIysgpdnlaYVIYTSG 3879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 154 STGNPKGVQISAA----NLQSFTDWIcadfPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEE 229
Cdd:PRK05691 3880 STGLPKGVMVEQRgmlnNQLSKVPYL----ALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAH 3955
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 230 LKKSGLNVWTSTPSFVQMCLMDPGFSQD----LLPhadtfmfCGEVLPVSVAKALLERFPKAKIFNTYGPTEAT--VAVT 303
Cdd:PRK05691 3956 VQAQGITVLESVPSLIQGMLAEDRQALDglrwMLP-------TGEAMPPELARQWLQRYPQIGLVNAYGPAECSddVAFF 4028
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 304 SVEITNdviSRSESLPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSH----EGQWAYR 379
Cdd:PRK05691 4029 RVDLAS---TRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHpfgaPGERLYR 4105
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 380 TGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQ-PNGtvEYLIAAIVPEEHEFEKEfQL 457
Cdd:PRK05691 4106 TGDlARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEgVNG--KHLVGYLVPHQTVLAQG-AL 4182
|
490 500 510
....*....|....*....|....*....|....*...
3E7X_A 458 TSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRK 4220
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-495 |
9.44e-51 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 187.30 E-value: 9.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGekksPILVYGHMEPH---MIVSFLGSVKAGHPY 79
Cdd:PRK05691 2190 LHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVG----PQVRVGLALERsleMVVGLLAILKAGGAY 2265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 80 IPVDLSIPSERIAKIIESSGAELLIHAAGLsIDAVGQQIQTVsAEELLENEGGS-----------VSQDQwvkeHETfYI 148
Cdd:PRK05691 2266 VPLDPEYPLERLHYMIEDSGIGLLLSDRAL-FEALGELPAGV-ARWCLEDDAAAlaaysdaplpfLSLPQ----HQA-YL 2338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 149 IYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLhcVTK-----DAvnkp 223
Cdd:PRK05691 2339 IYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARV--VLRaqgqwGA---- 2412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 224 kvlfEEL----KKSGLNVWTSTPSFVQMCLMDPGFSQDLLPhadtFMFC---GEVLPVSVAKALLERFPKAKIFNTYGPT 296
Cdd:PRK05691 2413 ----EEIcqliREQQVSILGFTPSYGSQLAQWLAGQGEQLP----VRMCitgGEALTGEHLQRIRQAFAPQLFFNAYGPT 2484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 297 EATVAVTSVEITNDVISRSESLPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSH 372
Cdd:PRK05691 2485 ETVVMPLACLAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFvadpFAA 2564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 373 EGQWAYRTGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQ-PNGT--VEYLIAAIVpeE 448
Cdd:PRK05691 2565 DGGRLYRTGDlVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDtPSGKqlAGYLVSAVA--G 2642
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
3E7X_A 449 HEFEKEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK05691 2643 QDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRR 2689
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
5-497 |
1.29e-49 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 178.77 E-value: 1.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 5 HAIQTHAETYPQTDAFRSQG-----QSLTYQELWEQSDRAAAAIQKRisGEKK-SPILVYGHMEPHMIVSFLGSVKAGHP 78
Cdd:COG0365 13 NCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRAL--GVKKgDRVAIYLPNIPEAVIAMLACARIGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 79 YIPV--DLSIPSerIAKIIESSGAELLIHAAGLS-----------IDAVGQQIQTVSAEELLENEGGSVSQDQWV----- 140
Cdd:COG0365 91 HSPVfpGFGAEA--LADRIEDAEAKVLITADGGLrggkvidlkekVDEALEELPSLEHVIVVGRTGADVPMEGDLdwdel 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 141 -----KEHET--------FYIIYTSGSTGNPKGVQIS----AANLQSFTDWIcadFPVSGGKIFLNQAPFSFdlsVMD-- 201
Cdd:COG0365 169 laaasAEFEPeptdaddpLFILYTSGTTGKPKGVVHThggyLVHAATTAKYV---LDLKPGDVFWCTADIGW---ATGhs 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 202 --LYPCLQSGGTLhcVTKDAV---NKPKVLFEELKKSGLNVWTSTPSFVQMCLmdpGFSQDLLPHAD-----TFMFCGEV 271
Cdd:COG0365 243 yiVYGPLLNGATV--VLYEGRpdfPDPGRLWELIEKYGVTVFFTAPTAIRALM---KAGDEPLKKYDlsslrLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 272 LPVSVAKALLERFpKAKIFNTYGPTEATVAVtsveITNDVIsrsesLPV-----GFAKPDMNIFIMDEEGQPLPEGEKGE 346
Cdd:COG0365 318 LNPEVWEWWYEAV-GVPIVDGWGQTETGGIF----ISNLPG-----LPVkpgsmGKPVPGYDVAVVDEDGNPVPPGEEGE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 347 IVIAGPSVS--RGYLGEPELTEKAFFSHEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEfhvrqSQYV 423
Cdd:COG0365 388 LVIKGPWPGmfRGYWNDPERYRETYFGRFPGW-YRTGDGARRdEDGYFWILGRSDDVINVSGHRIGTAEIE-----SALV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 424 R------SAVV-IPYQPNGTVeyLIAAIVPEEhEFEKEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKR 496
Cdd:COG0365 462 ShpavaeAAVVgVPDEIRGQV--VKAFVVLKP-GVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRL 538
|
.
3E7X_A 497 I 497
Cdd:COG0365 539 L 539
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
11-496 |
1.58e-49 |
|
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: 176.60 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKriSGEKKS-------PILvyghmePHMIVSFLGSVKAGHPYIPVD 83
Cdd:cd05936 9 ARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQN--LGVQPGdrvalmlPNC------PQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 84 LSIPSERIAKIIESSGAELLIhaaglsidavgqqiQTVSAEELLENeGGSVSQDQWVKEHETFYIIYTSGSTGNPKGVQI 163
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALI--------------VAVSFTDLLAA-GAPLGERVALTPEDVAVLQYTSGTTGVPKGAML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 164 S----AANLQSFTDWIcaDFPVSGGKIFLNQAPF--SFDLSVMDLYPcLQSGGTLHCVTKdavNKPKVLFEELKKSGLNV 237
Cdd:cd05936 146 ThrnlVANALQIKAWL--EDLLEGDDVVLAALPLfhVFGLTVALLLP-LALGATIVLIPR---FRPIGVLKEIRKHRVTI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 238 WTSTPSFVQMCLMDPGFSQDLLPhadTFMFC---GEVLPVSVAKALLERFpKAKIFNTYGPTEATVAVTSVEITNDVISR 314
Cdd:cd05936 220 FPGVPTMYIALLNAPEFKKRDFS---SLRLCisgGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVAVNPLDGPRKPG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 315 SESLPVgfakPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfsHEGqWaYRTGDAGFI-QDGQIFC 393
Cdd:cd05936 296 SIGIPL----PGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF--VDG-W-LRTGDIGYMdEDGYFFI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 394 QGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVI--PYQPNGtvEYLIAAIVPEEHEF--EKEfqltsaIKKELAASL 469
Cdd:cd05936 368 VDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVgvPDPYSG--EAVKAFVVLKEGASltEEE------IIAFCREQL 439
|
490 500
....*....|....*....|....*..
3E7X_A 470 PAYMIPRKFIYQDHIQMTANGKIDRKR 496
Cdd:cd05936 440 AGYKVPRQVEFRDELPKSAVGKILRRE 466
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
3-500 |
7.22e-44 |
|
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: 162.26 E-value: 7.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHA-IQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRI--SGEKkspILVYGHMEPHMIVSFLGSVKAGHPY 79
Cdd:TIGR03098 1 LLHHlLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGlaRGER---VAIYLDKRLETVTAMFGAALAGGVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 80 IPVDLSIPSERIAKIIESSGAELLIHAAGL---------SIDAVGQQIQTVSAEELLENEGGSVSQDqWVK--------- 141
Cdd:TIGR03098 78 VPINPLLKAEQVAHILADCNVRLLVTSSERldllhpalpGCHDLRTLIIVGDPAHASEGHPGEEPAS-WPKllalgdadp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 142 EHETF-----YIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLhcVT 216
Cdd:TIGR03098 157 PHPVIdsdmaAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATV--VL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 217 KDAVnKPKVLFEELKKSGLNVWTSTPS-FVQMclmdpgfSQDLLPHADT-----FMFCGEVLPVSVAKALLERFPKAKIF 290
Cdd:TIGR03098 235 HDYL-LPRDVLKALEKHGITGLAAVPPlWAQL-------AQLDWPESAApslryLTNSGGAMPRATLSRLRSFLPNARLF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 291 NTYGPTEATvavtsveitndvisRSESLP----------VGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLG 360
Cdd:TIGR03098 307 LMYGLTEAF--------------RSTYLPpeevdrrpdsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 361 EPELTEKAF--------FSHEGQWAYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPY 431
Cdd:TIGR03098 373 DPEKTAERFrplppfpgELHLPELAVWSGDTVRRdEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGV 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 432 QPNGTVEYLIAAIVPEEH-EFEKEfqltsAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEE 500
Cdd:TIGR03098 453 PDPTLGQAIVLVVTPPGGeELDRA-----ALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAKE 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
10-494 |
8.36e-43 |
|
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: 157.77 E-value: 8.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 10 HAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRisGEKKSP-ILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPS 88
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALRAL--GVAKGDrVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 89 ERIAKIIESSGAELLIHaaglsidavgqqiqtvsaeelleneggsvsqdqwvkehETFYIIYTSGSTGNPKGVQISAANL 168
Cdd:cd17631 82 PEVAYILADSGAKVLFD--------------------------------------DLALLMYTSGTTGRPKGAMLTHRNL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 169 QSFTDWICADFPVSGGKIFLNQAPFsFDLSVMDLY--PCLQSGGTLHCVTKdavNKPKVLFEELKKSGLNVWTSTPSFVQ 246
Cdd:cd17631 124 LWNAVNALAALDLGPDDVLLVVAPL-FHIGGLGVFtlPTLLRGGTVVILRK---FDPETVLDLIERHRVTSFFLVPTMIQ 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 247 MCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERfpKAKIFNTYGPTEATVAVTSVEiTNDVISRSESlpVGFAKPD 326
Cdd:cd17631 200 ALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFLS-PEDHRRKLGS--AGRPVFF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 327 MNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfshEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHG 405
Cdd:cd17631 275 VEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF---RDGW-FHTGDLGRLdEDGYLYIVDRKKDMIISGG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 406 ---YRMELEeiEFHVRQSQYVRSAVV-IPYQPNGtvEYLIAAIVPEEHEFEKEFQLTSAIKKELAaslpAYMIPRKFIYQ 481
Cdd:cd17631 351 envYPAEVE--DVLYEHPAVAEVAVIgVPDEKWG--EAVVAVVVPRPGAELDEDELIAHCRERLA----RYKIPKSVEFV 422
|
490
....*....|...
3E7X_A 482 DHIQMTANGKIDR 494
Cdd:cd17631 423 DALPRNATGKILK 435
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
148-495 |
2.17e-42 |
|
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: 156.83 E-value: 2.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 IIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLhCVTKDAVnKPKVLF 227
Cdd:cd05922 122 LLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATL-VLTNDGV-LDDAFW 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 228 EELKKSGLNVWTSTPSFVQMcLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEi 307
Cdd:cd05922 200 EDLREHGATGLAGVPSTYAM-LTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLP- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 308 TNDVISRSESlpVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYL-GEPELTEKAffshEGQWAYRTGDAGFI 386
Cdd:cd05922 278 PERILEKPGS--IGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWnDPPYRRKEG----RGGGVLHTGDLARR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 387 -QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEfekefqlTSAIKKEL 465
Cdd:cd05922 352 dEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKID-------PKDVLRSL 424
|
330 340 350
....*....|....*....|....*....|
3E7X_A 466 AASLPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:cd05922 425 AERLPPYKVPATVRVVDELPLTASGKVDYA 454
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
26-499 |
8.03e-41 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 153.24 E-value: 8.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 26 SLTYQELWEQSDRAAAAIQKR-IS-GEKKSPILVYGhmePHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELL 103
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALgIKkGDRVAIALPNG---LEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 104 IHAAGLSIDA-----------------VGQQIQTVSAEEL--LENEGGSVSQDQWVKEHETFYIIYTSGSTGNPKGVQIS 164
Cdd:cd05926 91 LTPKGELGPAsraasklglailelaldVGVLIRAPSAESLsnLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 165 AANLQSFTDWICADFPVSGGKIFLNqapfsfdlsVMDLY----------PCLQSGGtlhCVTKDAVNKPKVLFEELKKSG 234
Cdd:cd05926 171 HRNLAASATNITNTYKLTPDDRTLV---------VMPLFhvhglvasllSTLAAGG---SVVLPPRFSASTFWPDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 235 LNVWTSTPSFVQMCLMDPGFSQDLLPHADTFM-FCGEVLPVSVAKALLERFpKAKIFNTYGPTEATVAVTSVEITNDVIS 313
Cdd:cd05926 239 ATWYTAVPTIHQILLNRPEPNPESPPPKLRFIrSCSASLPPAVLEALEATF-GAPVLEAYGMTEAAHQMTSNPLPPGPRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 314 R-SESLPVGfakpdMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFsHEGqWaYRTGDAGFI-QDGQI 391
Cdd:cd05926 318 PgSVGKPVG-----VEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAF-KDG-W-FRTGDLGYLdADGYL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 392 FCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVV--IPYQPNGtvEYLIAAIVPEEHEFEKEFQLTSAIKKELAasl 469
Cdd:cd05926 390 FLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAfgVPDEKYG--EEVAAAVVLREGASVTEEELRAFCRKHLA--- 464
|
490 500 510
....*....|....*....|....*....|
3E7X_A 470 pAYMIPRKFIYQDHIQMTANGKIDRKRIGE 499
Cdd:cd05926 465 -AFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
3-497 |
6.61e-40 |
|
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: 151.67 E-value: 6.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAE-------TYPQTDafrSQGQSLTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEpHMIVSFLGSVKA 75
Cdd:cd05906 12 LLELLLRAAErgptkgiTYIDAD---GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNE-DFIPAFWACVLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 76 GhpYIPVDLSIPS------------ERIAKIIES----SGAELLIHAAGLSIDAVGQQIQTVSAEELLENEGGSVSQDqw 139
Cdd:cd05906 88 G--FVPAPLTVPPtydepnarlrklRHIWQLLGSpvvlTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQ-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 140 vKEHETFYII-YTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPF-----SFDLSVMDLY-PCLQsggtL 212
Cdd:cd05906 164 -SRPDDLALLmLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLdhvggLVELHLRAVYlGCQQ----V 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 213 HCVTKDAVNKPKVLFEELKKSGLNVwTSTPSFVQMCLMD-----PGFSQDLLPhADTFMFCGEVLPVSVAKALLERF--- 284
Cdd:cd05906 239 HVPTEEILADPLRWLDLIDRYRVTI-TWAPNFAFALLNDlleeiEDGTWDLSS-LRYLVNAGEAVVAKTIRRLLRLLepy 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 285 --PKAKIFNTYGPTE--ATVAVTSVEITNDVISRSESLPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLG 360
Cdd:cd05906 317 glPPDAIRPAFGMTEtcSGVIYSRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 361 EPELTEKAFfsHEGQWaYRTGDAGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRS--AVVIPYQPNGTV- 437
Cdd:cd05906 397 NPEANAEAF--TEDGW-FRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAEt 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
3E7X_A 438 EYLIAAIVPEEHEFEKEFQLTSAIKKELAASL---PAYMIPrkfIYQDHIQMTANGKIDRKRI 497
Cdd:cd05906 474 EELAIFFVPEYDLQDALSETLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
10-494 |
9.16e-40 |
|
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: 151.24 E-value: 9.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 10 HAETYPQTDAFR------SQGQSLTYQELWEQSDRAAAAIQKRiSGEKKSPILVYGHmEPHMIVSFLGSVKAGhpYIPVD 83
Cdd:cd05931 2 RAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAV-GKPGDRVLLLAPP-GLDFVAAFLGCLYAG--AIAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 84 LSIPS-----ERIAKIIESSGAELLIHAAGlSIDAVGQQIQTVSA--------EELLENEGGSVSQDQWVKEHETFYIIY 150
Cdd:cd05931 78 LPPPTpgrhaERLAAILADAGPRVVLTTAA-ALAAVRAFAASRPAagtprllvVDLLPDTSAADWPPPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 151 TSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFD--LSVMDLYPcLQSGGTLHCVTKDA-VNKPKVLF 227
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDmgLIGGLLTP-LYSGGPSVLMSPAAfLRRPLRWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 228 EELKKSGLnVWTSTPSFV-QMCLmDPGFSQDLLP---HADTFMFCG-EvlPVSVA--KALLERF------PKAkIFNTYG 294
Cdd:cd05931 236 RLISRYRA-TISAAPNFAyDLCV-RRVRDEDLEGldlSSWRVALNGaE--PVRPAtlRRFAEAFapfgfrPEA-FRPSYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 295 PTEATVAVTSVEITNDVISR---------------------SESLPVGFAKPDMNIFIMDEEG-QPLPEGEKGEIVIAGP 352
Cdd:cd05931 311 LAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpaaRELVSCGRPLPDQEVRIVDPETgRELPDGEVGEIWVRGP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 353 SVSRGYLGEPELTEKAFFSHEGQ----WaYRTGDAGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVR---- 424
Cdd:cd05931 391 SVASGYWGRPEATAETFGALAATdeggW-LRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALrpgc 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 425 -SAVVIpyqPNGTVEYLIAAIVPEEHEFEKEF-QLTSAIKKELAAS----------LPAYMIPRkfiyqdhiqmTANGKI 492
Cdd:cd05931 470 vAAFSV---PDDGEERLVVVAEVERGADPADLaAIAAAIRAAVAREhgvapadvvlVRPGSIPR----------TSSGKI 536
|
..
3E7X_A 493 DR 494
Cdd:cd05931 537 QR 538
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
26-495 |
1.80e-39 |
|
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: 148.77 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 26 SLTYQELWEQSDRAAAAIQKRISGEKKSpILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLih 105
Cdd:cd17654 16 TVSYADLAEKISNLSNFLRKKFQTEERA-IGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 106 aaglsidavgqqiqtvsaeelLENEGGSVSQDQWVKEHETF---------YIIYTSGSTGNPKGVQISAANLQSFTDWIC 176
Cdd:cd17654 93 ---------------------LQNKELDNAPLSFTPEHRHFnirtdeclaYVIHTSGTTGTPKIVAVPHKCILPNIQHFR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 177 ADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTL----HCVTKDAVNKPKVLFeelKKSGLNVWTSTPSFVQMCLMDP 252
Cdd:cd17654 152 SLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLlivpTSVKVLPSKLADILF---KRHRITVLQATPTLFRRFGSQS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 253 GFSQDLLPHAD--TFMFCGEVLPVSVA-KALLERFPKAKIFNTYGPTEatvaVTSVEITNDVISRSESLPVGFAKPDMNI 329
Cdd:cd17654 229 IKSTVLSATSSlrVLALGGEPFPSLVIlSSWRGKGNRTRIFNIYGITE----VSCWALAYKVPEEDSPVQLGSPLLGTVI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 330 FIMDEEGQplpEGEkGEIVIAGpsVSRGYLGEPELTEKaffshEGQWaYRTGDAGFIQDGQIFCQGRLDFQIKLHGYRME 409
Cdd:cd17654 305 EVRDQNGS---EGT-GQVFLGG--LNRVCILDDEVTVP-----KGTM-RATGDFVTVKDGELFFLGRKDSQIKRRGKRIN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 410 LEEIEFHVRQSQYVRSAVVIPYQPngtvEYLIAAIVPEEhefekefqLTSAIKKEL-AASLPAYMIPRKFIYQDHIQMTA 488
Cdd:cd17654 373 LDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGES--------SSSRIHKELqLTLLSSHAIPDTFVQIDKLPLTS 440
|
....*..
3E7X_A 489 NGKIDRK 495
Cdd:cd17654 441 HGKVDKS 447
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
5-501 |
1.36e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 147.64 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 5 HAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKriSGEKKSP-ILVYGHMEPHMIVSFLGSVKAGHPYIPVD 83
Cdd:PRK06187 10 RILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRA--LGVKKGDrVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 84 LSIPSERIAKIIESSGAELLI-HAAGLS-IDAVGQQIQTVSAEELLENEGGSVSQDQW------------------VKEH 143
Cdd:PRK06187 88 IRLKPEEIAYILNDAEDRVVLvDSEFVPlLAAILPQLPTVRTVIVEGDGPAAPLAPEVgeyeellaaasdtfdfpdIDEN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 144 ETFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAP----FSFDLSVMDLYpclqSGGTLhcVTKDA 219
Cdd:PRK06187 168 DAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPmfhvHAWGLPYLALM----AGAKQ--VIPRR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 220 VnKPKVLFEELKKSGLNVWTSTPSFVQMCLmdpgfsQDLLPHADTF-----MFCG-EVLPVSVAKALLERFpKAKIFNTY 293
Cdd:PRK06187 242 F-DPENLLDLIETERVTFFFAVPTIWQMLL------KAPRAYFVDFsslrlVIYGgAALPPALLREFKEKF-GIDLVQGY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 294 GPTEATVAVTSVEITNDVISRSE-SLPVGFAKPDMNIFIMDEEGQPLP--EGEKGEIVIAGPSVSRGYLGEPELTEKAFf 370
Cdd:PRK06187 314 GMTETSPVVSVLPPEDQLPGQWTkRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETI- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 371 shEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHG---YRMELEEIEFHVRQsqyVRSAVVI--PYQPNGtvEYLIAAI 444
Cdd:PRK06187 393 --DGGW-LHTGDVGYIdEDGYLYITDRIKDVIISGGeniYPRELEDALYGHPA---VAEVAVIgvPDEKWG--ERPVAVV 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
3E7X_A 445 VPEEHEfekefQLT-SAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEEV 501
Cdd:PRK06187 465 VLKPGA-----TLDaKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQY 517
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
26-495 |
1.20e-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: 134.91 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 26 SLTYQELWEQSDRAAAAIQkRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLIH 105
Cdd:cd05935 1 SLTYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 106 AAGLSIDAVgqqiqtvsaeelleneggsvsqdqwvkehetfyIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGK 185
Cdd:cd05935 80 GSELDDLAL---------------------------------IPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 186 IFLNQAPFsFDLSVM--DLYPCLQSGGTLhcVTKDAVNKpKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHAD 263
Cdd:cd05935 127 VILACLPL-FHVTGFvgSLNTAVYVGGTY--VLMARWDR-ETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 264 TFMFCGEVLPVSVAKALLERFpkAKIFNT-YGPTEATVAVTSveitnDVISRSESLPVGFAKPDMNIFIMD-EEGQPLPE 341
Cdd:cd05935 203 VLTGGGAPMPPAVAEKLLKLT--GLRFVEgYGLTETMSQTHT-----NPPLRPKLQCLGIP*FGVDARVIDiETGRELPP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 342 GEKGEIVIAGPSVSRGYLGEPELTEKAFFSHEGQWAYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQS 420
Cdd:cd05935 276 NEVGEIVVRGPQIFKGYWNRPEETEESFIEIKGRRFFRTGDLGYMdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3E7X_A 421 QYVRSAVVIPYQPNGTVEYLIAAIV--PEEHEFEKEFQLTSAIKKELAaslpAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:cd05935 356 PAI*EVCVISVPDERVGEEVKAFIVlrPEYRGKVTEEDIIEWAREQMA----AYKYPREVEFVDELPRSASGKILWR 428
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
11-494 |
3.53e-33 |
|
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: 132.11 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIqKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSER 90
Cdd:cd05959 14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGAL-RALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 91 IAKIIESSGAELL---------IHAAGLSIDAVGQQIQTVSAEElleNEGGSVSQDQWVKEHETF------------YII 149
Cdd:cd05959 93 YAYYLEDSRARVVvvsgelapvLAAALTKSEHTLVVLIVSGGAG---PEAGALLLAELVAAEAEQlkpaathaddpaFWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 150 YTSGSTGNPKGVQISAANLQsftdWIC------------ADFPVSGGKIFlnqapFSFDLSVMDLYPcLQSGGTlhCVTK 217
Cdd:cd05959 170 YSSGSTGRPKGVVHLHADIY----WTAelyarnvlgireDDVCFSAAKLF-----FAYGLGNSLTFP-LSVGAT--TVLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 218 DAVNKPKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLphaDTFMFC---GEVLPVSVAKALLERFpKAKIFNTYG 294
Cdd:cd05959 238 PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDL---SSLRLCvsaGEALPAEVGERWKARF-GLDILDGIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 295 PTEAtvavTSVEITN---DVISRSESLPVgfakPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfs 371
Cdd:cd05959 314 STEM----LHIFLSNrpgRVRYGTTGKPV----PGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 372 hEGQWaYRTGDA-GFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEhE 450
Cdd:cd05959 384 -QGEW-TRTGDKyVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRP-G 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....
3E7X_A 451 FEKEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDR 494
Cdd:cd05959 461 YEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQR 504
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
18-495 |
7.82e-33 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 130.10 E-value: 7.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 18 DAFRSQGQSLTYQELWeqsdRAAAAIQKRISGEKKSP----ILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAK 93
Cdd:cd05941 3 IAIVDDGDSITYADLV----ARAARLANRLLALGKDLrgdrVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 94 IIESSGAELLIHAAglsidavgqqiqtvsaeelleneggsvsqdqwvkehetfYIIYTSGSTGNPKGVQISAANLQSFTD 173
Cdd:cd05941 79 VITDSEPSLVLDPA---------------------------------------LILYTSGTTGRPKGVVLTHANLAANVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 174 WICADFPVSGGKIFLNQAPFS-----FDLSVMDLYpclqSGGTLHCVTKDAvnkPKVLFEELKKSGLNVWTSTPSF---- 244
Cdd:cd05941 120 ALVDAWRWTEDDVLLHVLPLHhvhglVNALLCPLF----AGASVEFLPKFD---PKEVAISRLMPSITVFMGVPTIytrl 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 245 ---VQMCLMDPGFSQDLLPHADTFMFCGEV-LPVSV--------AKALLERfpkakifntYGPTEATVAvTSVEITNDVI 312
Cdd:cd05941 193 lqyYEAHFTDPQFARAAAAERLRLMVSGSAaLPVPTleeweaitGHTLLER---------YGMTEIGMA-LSNPLDGERR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 313 SRSeslpVGFAKPDMNIFIMDEE-GQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfsHEGQWaYRTGDAGFI-QDGQ 390
Cdd:cd05941 263 PGT----VGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF--TDDGW-FKTGDLGVVdEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 391 IFCQGRL-DFQIKLHGYRMELEEIEFHVRQSQYVRSAVVI--PYQPNGtvEYLIAAIVPEEHEFEKEFQ-LTSAIKKELA 466
Cdd:cd05941 336 YWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIgvPDPDWG--ERVVAVVVLRAGAAALSLEeLKEWAKQRLA 413
|
490 500
....*....|....*....|....*....
3E7X_A 467 aslpAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:cd05941 414 ----PYKRPRRLILVDELPRNAMGKVNKK 438
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
3-500 |
1.82e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 130.01 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQ-KRISGEKKSPILV---YGHMEPHMIVSFLGSVkaghp 78
Cdd:PRK06145 4 LSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHaRGIGQGDVVALLMknsAAFLELAFAASYLGAV----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 79 YIPVDLSIPSERIAKIIESSGAELLIH-----------AAGLSIDAVGQQIQTVSAEelleneGGSVSQDQWVKEHETFY 147
Cdd:PRK06145 79 FLPINYRLAADEVAYILGDAGAKLLLVdeefdaivaleTPKIVIDAAAQADSRRLAQ------GGLEIPPQAAVAPTDLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 -IIYTSGSTGNPKGVQISAANLQsftdWICADFPVSGG----KIFLNQAPFsFDLSVMDL--YPCLQSGGTLhCVTKDAv 220
Cdd:PRK06145 153 rLMYTSGTTDRPKGVMHSYGNLH----WKSIDHVIALGltasERLLVVGPL-YHVGAFDLpgIAVLWVGGTL-RIHREF- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 221 nKPKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQ-DLlphaDTFMFC---GEVLPVSVAKALLERFPKAKIFNTYGPT 296
Cdd:PRK06145 226 -DPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRfDL----DSLAWCiggGEKTPESRIRDFTRVFTRARYIDAYGLT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 297 EATVAVTSVEITNDvISRSESlpVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFsheGQW 376
Cdd:PRK06145 301 ETCSGDTLMEAGRE-IEKIGS--TGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY---GDW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 377 aYRTGDAGFIQD-GQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEfekef 455
Cdd:PRK06145 375 -FRSGDVGYLDEeGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGA----- 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
3E7X_A 456 QLT-SAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEE 500
Cdd:PRK06145 449 TLTlEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
24-495 |
4.08e-32 |
|
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: 128.89 E-value: 4.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 24 GQSLTYQELWEQSDRAAAAIQKRIsGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVD-LSIPSErIAKIIESSGAEL 102
Cdd:cd05904 30 GRALTYAELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANpLSTPAE-IAKQVKDSGAKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 103 LI---------HAAGLSIDAVGQQIQTVSAEELLENEGGSVSQDQ-WVKEHETFYIIYTSGSTGNPKGVQISAANLQSFT 172
Cdd:cd05904 108 AFttaelaeklASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVvVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 173 DWICADFP--VSGGKIFLNQAPF--SFDLSVMdLYPCLQSGGTLHCVTK-------DAVNKPKVLFeelkksglnVWTST 241
Cdd:cd05904 188 AQFVAGEGsnSDSEDVFLCVLPMfhIYGLSSF-ALGLLRLGATVVVMPRfdleellAAIERYKVTH---------LPVVP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 242 PSFVQMCLMDPGFSQDLLphADTFMFCGEV-LPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVeiTNDVISRSESLPV 320
Cdd:cd05904 258 PIVLALVKSPIVDKYDLS--SLRQIMSGAApLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMC--FAPEKDRAKYGSV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 321 GFAKPDMNIFIMD-EEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFShEGqWaYRTGDAGFI-QDGQIFCQGRLD 398
Cdd:cd05904 334 GRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK-EG-W-LHTGDLCYIdEDGYLFIVDRLK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 399 FQIKLHGYRM---ELEEIEFHVRQsqyVRSAVVIPYQPNGTVEYLIAAIV--PEEHEFEKEfqltsaIKKELAASLPAYM 473
Cdd:cd05904 411 ELIKYKGFQVapaELEALLLSHPE---ILDAAVIPYPDEEAGEVPMAFVVrkPGSSLTEDE------IMDFVAKQVAPYK 481
|
490 500
....*....|....*....|..
3E7X_A 474 IPRKFIYQDHIQMTANGKIDRK 495
Cdd:cd05904 482 KVRKVAFVDAIPKSPSGKILRK 503
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
11-492 |
5.86e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 128.90 E-value: 5.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQkRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSER 90
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALL-DLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 91 IAKIIESSGAELLIHAAGLS--IDAVGQQIQTVSAEELL-----ENEGGSVSQDQWVKEHETFY------------IIYT 151
Cdd:PRK08316 100 LAYILDHSGARAFLVDPALAptAEAALALLPVDTLILSLvlggrEAPGGWLDFADWAEAGSVAEpdveladddlaqILYT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 152 SGSTGNPKGVQIS-AANLQSFTDWIcADFPVSGGKIFLNQAPF--SFDLSVMdLYPCLQSGGTLHCVTKDAvnkPKVLFE 228
Cdd:PRK08316 180 SGTESLPKGAMLThRALIAEYVSCI-VAGDMSADDIPLHALPLyhCAQLDVF-LGPYLYVGATNVILDAPD---PELILR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 229 ELKKSGLN-------VWTSTpsfvqmcLMDPGFSQ-DL--LPHAdtfmFCG-EVLPVSVAKALLERFPKAKIFNTYGPTE 297
Cdd:PRK08316 255 TIEAERITsffapptVWISL-------LRHPDFDTrDLssLRKG----YYGaSIMPVEVLKELRERLPGLRFYNCYGQTE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 298 ----ATVAvtSVEitnDVISRSESLpvgfAKPDMNI--FIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfs 371
Cdd:PRK08316 324 iaplATVL--GPE---EHLRRPGSA----GRPVLNVetRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 372 hEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVI----PYQpngtVEYLIAAIVP 446
Cdd:PRK08316 393 -RGGW-FHSGDLGVMdEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIglpdPKW----IEAVTAVVVP 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
3E7X_A 447 EEHEFEKEFQLTSAIKKELAaslpAYMIPRKFIYQDHIQMTANGKI 492
Cdd:PRK08316 467 KAGATVTEDELIAHCRARLA----GFKVPKRVIFVDELPRNPSGKI 508
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
12-497 |
5.96e-32 |
|
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: 128.79 E-value: 5.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 12 ETYPQTDafrSQGQSLTYQELWEQSDRAAAAIQKRisGEKKSPI-LVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSER 90
Cdd:cd17647 9 ETPSLNS---SKTRSFTYRDINEASNIVAHYLIKT--GIKRGDVvMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 91 iaKIIESSGAE----LLIHAAGLsidAVG-QQIQTVSaeelleneggsvsqdqwvkehetfyiiYTSGSTGNPKGVQISA 165
Cdd:cd17647 84 --QNIYLGVAKprglIVIRAAGV---VVGpDSNPTLS---------------------------FTSGSEGIPKGVLGRH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 166 ANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFV 245
Cdd:cd17647 132 FSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 246 QMCLMDPGFSQDLLPHAdtfMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITndviSRSES-------- 317
Cdd:cd17647 212 QLLTAQATTPFPKLHHA---FFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVP----SRSSDptflknlk 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 318 --LPVGFAKPDMNIFIMD--EEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAF----FSHEGQWA------------ 377
Cdd:cd17647 285 dvMPAGRGMLNVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFvnnwFVEPDHWNyldkdnnepwrq 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 378 ---------YRTGDAG-FIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPE 447
Cdd:cd17647 365 fwlgprdrlYRTGDLGrYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPR 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3E7X_A 448 EHEFEKEF-----------------------QLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRI 497
Cdd:cd17647 445 FDKPDDESfaqedvpkevstdpivkgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
19-497 |
6.07e-32 |
|
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: 127.58 E-value: 6.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 19 AFRSQGQSLTYQELWEQSDRAAAAIQKR-ISGEKKspILVYGHMEPHMIVSFLGSVKAGhpYIPVDLSIPSER--IAKII 95
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLgVSSGDR--VLLLMLDSPELVQLFLGCLARG--AIAVVINPLLHPddYAYIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 96 ESSGAELLIhaaglsidavgqqiqtVSAEELLeneggsvsqdqwvkehetfYIIYTSGSTGNPKGVQISAANLQSFTDWI 175
Cdd:cd05919 79 RDCEARLVV----------------TSADDIA-------------------YLLYSSGTTGPPKGVMHAHRDPLLFADAM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 176 C--------ADFPVSGGKIFlnqapFSFDLSVMDLYPcLQSGGTlhCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQM 247
Cdd:cd05919 124 ArealgltpGDRVFSSAKMF-----FGYGLGNSLWFP-LAVGAS--AVLNPGWPTAERVLATLARFRPTVLYGVPTFYAN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 248 CLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFpKAKIFNTYGPTEatvaVTSVEITN---DVISRSESLPVgfak 324
Cdd:cd05919 196 LLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATE----VGHIFLSNrpgAWRLGSTGRPV---- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 325 PDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfshEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKL 403
Cdd:cd05919 267 PGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF---NGGW-YRTGDKFCRdADGWYTHAGRADDMLKV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 404 HGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEhEFEKEFQLTSAIKKELAASLPAYMIPRKFIYQDH 483
Cdd:cd05919 343 GGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKS-PAAPQESLARDIHRHLLERLSAHKVPRRIAFVDE 421
|
490
....*....|....
3E7X_A 484 IQMTANGKIDRKRI 497
Cdd:cd05919 422 LPRTATGKLQRFKL 435
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
27-494 |
7.11e-32 |
|
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: 127.07 E-value: 7.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 27 LTYQELWEQSDRAAAAIqKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLIha 106
Cdd:cd05972 1 WSFRELKRESAKAANVL-AKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 107 aglsidavgqqiqtvsaeelleneggsvsqdqwVKEHETFYIIYTSGSTGNPKGVQISAANLqsFTDWICADFP--VSGG 184
Cdd:cd05972 78 ---------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYP--LGHIPTAAYWlgLRPD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 185 KIFLNQAPFSFDLSVM-DLYPCLQSGgtLHCVTKDAVN-KPKVLFEELKKSGLNVWTSTPSFVQMcLMDPGFSQDLLPHA 262
Cdd:cd05972 123 DIHWNIADPGWAKGAWsSFFGPWLLG--ATVFVYEGPRfDAERILELLERYGVTSFCGPPTAYRM-LIKQDLSSYKFSHL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 263 DTFMFCGEVLPVSVAKALLERFpKAKIFNTYGPTEaTVAVTSVEITNDVISRSeslpVGFAKPDMNIFIMDEEGQPLPEG 342
Cdd:cd05972 200 RLVVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTE-TGLTVGNFPDMPVKPGS----MGRPTPGYDVAIIDDDGRELPPG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 343 EKGEIVI--AGPSVSRGYLGEPELTEKAFfshEGQWaYRTGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQ 419
Cdd:cd05972 274 EEGDIAIklPPPGLFLGYVGDPEKTEASI---RGDY-YLTGDrAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLE 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3E7X_A 420 SQYVRSAVVIPyQPNGTVEYLIAAIVPEEHEFEKEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDR 494
Cdd:cd05972 350 HPAVAEAAVVG-SPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRR 423
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
25-484 |
3.38e-31 |
|
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: 125.93 E-value: 3.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 25 QSLTYQELWEQSDRAAAAIQKrISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLI 104
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRS-LGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 105 haaglsidavgqqiqtvsaeelLENEGGSVSQdqwvkehetfyIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGG 184
Cdd:cd17640 83 ----------------------VENDSDDLAT-----------IIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 185 KIFLNQAP--FSFDLSVMdlYPCLQSGGTLHCVTkdavnkPKVLFEELKK-------SGLNVWTSTPSFVQMCLMDPGFS 255
Cdd:cd17640 130 DRFLSILPiwHSYERSAE--YFIFACGCSQAYTS------IRTLKDDLKRvkphyivSVPRLWESLYSGIQKQVSKSSPI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 256 QDLLPHadTFMFCGEV-LPVSVAKAL---LERFPKA---KIFNTYGPTEATVAVTSVEITNDVISrseslPVGFAKPDMN 328
Cdd:cd17640 202 KQFLFL--FFLSGGIFkFGISGGGALpphVDTFFEAigiEVLNGYGLTETSPVVSARRLKCNVRG-----SVGRPLPGTE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 329 IFIMDEEGQ-PLPEGEKGEIVIAGPSVSRGYLGEPELTEKAfFSHEGqWaYRTGDAGFI-QDGQIFCQGRLDFQIKL-HG 405
Cdd:cd17640 275 IKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKV-LDSDG-W-FNTGDLGWLtCGGELVLTGRAKDTIVLsNG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 406 YRMELEEIEFHVRQSQYVRSAVVIpyqpnGTVE-YLIAAIVPEEHEFEKEFQLTSAIKKELAASLPAYMIPRKFiYQDHI 484
Cdd:cd17640 352 ENVEPQPIEEALMRSPFIEQIMVV-----GQDQkRLGALIVPNFEELEKWAKESGVKLANDRSQLLASKKVLKL-YKNEI 425
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
4-494 |
4.30e-31 |
|
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: 128.26 E-value: 4.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 4 LHAI-QTHAETYP------QTDAFR---SQGQSLTYQELWEQSDRAAAAIQKriSGEKKSPI-LVYGHMEPHMIVSFLGS 72
Cdd:TIGR03443 238 IHDIfADNAEKHPdrtcvvETPSFLdpsSKTRSFTYKQINEASNILAHYLLK--TGIKRGDVvMIYAYRGVDLVVAVMGV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 73 VKAGHPYIPVDLSIPSERiaKIIESSGAE----LLIHAAGLSIDAVGQQIQ-------TVSAEELLEN---EGGSVSQD- 137
Cdd:TIGR03443 316 LKAGATFSVIDPAYPPAR--QTIYLSVAKpralIVIEKAGTLDQLVRDYIDkelelrtEIPALALQDDgslVGGSLEGGe 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 138 -------QWVKEHETFYII---------YTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMD 201
Cdd:TIGR03443 394 tdvlapyQALKDTPTGVVVgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRD 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 202 LYPCLQSGGTLHCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQmcLMDPGFSQDL--LPHAdtfMFCGEVLPVSVAKA 279
Cdd:TIGR03443 474 MFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQ--LLSAQATTPIpsLHHA---FFVGDILTKRDCLR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 280 LLERFPKAKIFNTYGPTEATVAVTSVEITndviSRSES----------LPVGFAKPDMNIFIMD--EEGQPLPEGEKGEI 347
Cdd:TIGR03443 549 LQTLAENVCIVNMYGTTETQRAVSYFEIP----SRSSDstflknlkdvMPAGKGMKNVQLLVVNrnDRTQTCGVGEVGEI 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 348 VIAGPSVSRGYLGEPELTEKAF----FSHEGQWA---------------------YRTGDAG-FIQDGQIFCQGRLDFQI 401
Cdd:TIGR03443 625 YVRAGGLAEGYLGLPELNAEKFvnnwFVDPSHWIdldkennkperefwlgprdrlYRTGDLGrYLPDGNVECCGRADDQV 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 402 KLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVP--EEHEFEkEFQ---------------------LT 458
Cdd:TIGR03443 705 KIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPqdKSDELE-EFKsevddeessdpvvkglikyrkLI 783
|
570 580 590
....*....|....*....|....*....|....*.
3E7X_A 459 SAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDR 494
Cdd:TIGR03443 784 KDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDK 819
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
11-500 |
1.20e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 124.63 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKriSG-EKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSE 89
Cdd:PRK07656 15 ARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAA--LGiGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 90 RIAKIIESSGAELLIHAAG-LSIDAVGQQ-------IQTVSAEELLENEGGSVSQDQWVKEHETFY------------II 149
Cdd:PRK07656 93 EAAYILARGDAKALFVLGLfLGVDYSATTrlpalehVVICETEEDDPHTEKMKTFTDFLAAGDPAErapevdpddvadIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 150 YTSGSTGNPKGVQISAANLQS-FTDWiCADFPVSGGKIFLNQAPF--SFDLSVMdLYPCLQSGGTLHCVtkdAVNKPKVL 226
Cdd:PRK07656 173 FTSGTTGRPKGAMLTHRQLLSnAADW-AEYLGLTEGDRYLAANPFfhVFGYKAG-VNAPLMRGATILPL---PVFDPDEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 227 FEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVsvakALLERFPKAKIFNT----YGPTEATVAV 302
Cdd:PRK07656 248 FRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPV----ALLERFESELGVDIvltgYGLSEASGVT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 303 TSVEITNDVISRSESlpVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAfFSHEGqWAYrTGD 382
Cdd:PRK07656 324 TFNRLDDDRKTVAGT--IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA-IDADG-WLH-TGD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 383 AGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIE-FHVRQSQYVRSAVV-IPYQPNGtvEYLIAAIVPEEHEFEKEFQLTS 459
Cdd:PRK07656 399 LGRLdEEGYLYIVDRKKDMFIVGGFNVYPAEVEeVLYEHPAVAEAAVIgVPDERLG--EVGKAYVVLKPGAELTEEELIA 476
|
490 500 510 520
....*....|....*....|....*....|....*....|.
3E7X_A 460 AIKKELAaslpAYMIPRKFIYQDHIQMTANGKIDRKRIGEE 500
Cdd:PRK07656 477 YCREHLA----KYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
25-497 |
2.14e-30 |
|
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: 123.09 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 25 QSLTYQELWEQSDRAAAAIQkRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLI 104
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 105 haaglsidavgqqiqtVSAEElleneggsvsqdqwvkehETFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGG 184
Cdd:cd05907 83 ----------------VEDPD------------------DLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 185 KIFLNQAPFSFDL-SVMDLYPCLQSGGTLHCVTKDavnkpKVLFEELKKSGLNVWTSTPSFVQMclMDPGFSQDLLPHAD 263
Cdd:cd05907 129 DRHLSFLPLAHVFeRRAGLYVPLLAGARIYFASSA-----ETLLDDLSEVRPTVFLAVPRVWEK--VYAAIKVKAVPGLK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 264 TFMFCGEVLP-----VS----VAKALLERFPKA--KIFNTYGPTEATVAVTsveitndvISRSESLPVGfakpdmnifim 332
Cdd:cd05907 202 RKLFDLAVGGrlrfaASggapLPAELLHFFRALgiPVYEGYGLTETSAVVT--------LNPPGDNRIG----------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 333 dEEGQPLPE-----GEKGEIVIAGPSVSRGYLGEPELTEKAFFshEGQWaYRTGDAGFI-QDGQIFCQGRL-DFQIKLHG 405
Cdd:cd05907 263 -TVGKPLPGvevriADDGEILVRGPNVMLGYYKNPEATAEALD--ADGW-LHTGDLGEIdEDGFLHITGRKkDLIITSGG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 406 YRMELEEIEFHVRQSQYVRSAVVI----PyqpngtveYLIAAIVPEEHEFEK-------------EFQLTSAIKKELA-- 466
Cdd:cd05907 339 KNISPEPIENALKASPLISQAVVIgdgrP--------FLVALIVPDPEALEAwaeehgiaytdvaELAANPAVRAEIEaa 410
|
490 500 510 520
....*....|....*....|....*....|....*....|..
3E7X_A 467 -----ASLPAYMIPRKFI------YQDHIQMTANGKIDRKRI 497
Cdd:cd05907 411 veaanARLSRYEQIKKFLllpepfTIENGELTPTLKLKRPVI 452
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
140-493 |
3.21e-30 |
|
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: 123.21 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 140 VKEHETFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPF--SFDLSVMDLYPcLQSGGTLHCVTk 217
Cdd:cd05909 144 VQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhSFGLTGCLWLP-LLSGIKVVFHP- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 218 DAVNkPKVLFEELKKSGLNVWTSTPSFVQmclmdpGFSQDLlpHADTF-----MFCG-EVLPVSVAKALLERFPKAkIFN 291
Cdd:cd05909 222 NPLD-YKKIPELIYDKKATILLGTPTFLR------GYARAA--HPEDFsslrlVVAGaEKLKDTLRQEFQEKFGIR-ILE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 292 TYGPTEAT--VAVTSVEITNdvisRSESlpVGFAKPDMNIFIMDEEG-QPLPEGEKGEIVIAGPSVSRGYLGEPELTEKA 368
Cdd:cd05909 292 GYGTTECSpvISVNTPQSPN----KEGT--VGRPLPGMEVKIVSVEThEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 369 FfshEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIE--FHVRQSQYVRSAVV-IPYQPNGtvEYLIAAI 444
Cdd:cd05909 366 F---GDGW-YDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIEdiLSEILPEDNEVAVVsVPDGRKG--EKIVLLT 439
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
3E7X_A 445 VPEEHEFEKefqLTSAIKkelAASLPAYMIPRKFIYQDHIQMTANGKID 493
Cdd:cd05909 440 TTTDTDPSS---LNDILK---NAGISNLAKPSYIHQVEEIPLLGTGKPD 482
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
15-492 |
3.28e-30 |
|
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: 123.09 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 15 PQTDAfrSQGQSLTYQELWEQSDRAAAAIqKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKI 94
Cdd:cd05911 1 AQIDA--DTGKELTYAQLRTLSRRLAAGL-RKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 95 IESSGAELLIhAAGLSIDAV---------GQQIQTVSAEE---------LLENEGGSVSQDQWVKEH---ETFYIIYTSG 153
Cdd:cd05911 78 LKISKPKVIF-TDPDGLEKVkeaakelgpKDKIIVLDDKPdgvlsiedlLSPTLGEEDEDLPPPLKDgkdDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 154 STGNPKGVQISAANLQSFTDWICADFPVSGGK--IFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTK-------DAVNKPK 224
Cdd:cd05911 157 TTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSndVILGFLPLYHIYGLFTTLASLLNGATVIIMPKfdselflDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 225 VLFeelkksgLNVwtsTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTs 304
Cdd:cd05911 237 ITF-------LYL---VPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILT- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 305 veITNDVISRSESlpVGFAKPDMNIFIMDEEG-QPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFsHEGqWaYRTGDA 383
Cdd:cd05911 306 --VNPDGDDKPGS--VGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFD-EDG-W-LHTGDI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 384 GFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVV--IPYQPNGtvEYLIAAIVPEEHEfekefQLTSA 460
Cdd:cd05911 379 GYFdEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVigIPDEVSG--ELPRAYVVRKPGE-----KLTEK 451
|
490 500 510
....*....|....*....|....*....|....*.
3E7X_A 461 -IKKELAASLPAYMIPRK---FIyqDHIQMTANGKI 492
Cdd:cd05911 452 eVKDYVAKKVASYKQLRGgvvFV--DEIPKSASGKI 485
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
24-496 |
4.62e-30 |
|
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: 121.63 E-value: 4.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 24 GQSLTYQELWEQSDRAAAAIQKRisGEKKSP-ILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAEL 102
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAAL--GIRPGDrVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 103 LIhaaglsIDavgqqiqtvsaeelleneggsvsqdqwvkeheTFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVS 182
Cdd:cd05934 79 VV------VD--------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 183 GGKIFLNQAP-FSFDLSVMDLYPCLQSGGTLHCVTKDAVNKpkvLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLlPH 261
Cdd:cd05934 121 EDDVYLTVLPlFHINAQAVSVLAALSVGATLVLLPRFSASR---FWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDR-AH 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 262 ADTFMFCGEVLPvSVAKALLERFpKAKIFNTYGPTEATVAVTSveiTNDVISRSESlpVGFAKPDMNIFIMDEEGQPLPE 341
Cdd:cd05934 197 RLRAAYGAPNPP-ELHEEFEERF-GVRLLEGYGMTETIVGVIG---PRDEPRRPGS--IGRPAPGYEVRIVDDDGQELPA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 342 GEKGEIVI---AGPSVSRGYLGEPELTEKAFfshEGQWaYRTGDAG-FIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHV 417
Cdd:cd05934 270 GEPGELVIrglRGWGFFKGYYNMPEATAEAM---RNGW-FHTGDLGyRDADGFFYFVDRKKDMIRRRGENISSAEVERAI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 418 RQSQYVRSAVVIPY-QPNGTVEYLIAAIVPEEHEFEKEfqltsAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKR 496
Cdd:cd05934 346 LRHPAVREAAVVAVpDEVGEDEVKAVVVLRPGETLDPE-----ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQ 420
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
3-492 |
5.89e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 120.06 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPV 82
Cdd:PRK08314 12 LFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 83 DLSIPSERIAKIIESSGAELLIHAAGLSidavgQQIQTVSAEELLEN-----------EGGSVSQDQWVK---------- 141
Cdd:PRK08314 92 NPMNREEELAHYVTDSGARVAIVGSELA-----PKVAPAVGNLRLRHvivaqysdylpAEPEIAVPAWLRaepplqalap 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 142 -----------------EHETFY-----IIYTSGSTGNPKG-------VQISAAnlqSFTDWicadFPVSGGKIFLNQAP 192
Cdd:PRK08314 167 ggvvawkealaaglappPHTAGPddlavLPYTSGTTGVPKGcmhthrtVMANAV---GSVLW----SNSTPESVVLAVLP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 193 FsFDLSVM--DLYPCLQSGGTLHCVTK-------DAVNKPKVlfeelkksglNVWTSTPSFVQMCLMDPGF-SQDLlpha 262
Cdd:PRK08314 240 L-FHVTGMvhSMNAPIYAGATVVLMPRwdreaaaRLIERYRV----------THWTNIPTMVVDFLASPGLaERDL---- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 263 DTFMFC---GEVLPVSVAKALLERFpKAKIFNTYGPTEaTVAVTsveITNdvisrseslPVGFAK------PDMNI--FI 331
Cdd:PRK08314 305 SSLRYIgggGAAMPEAVAERLKELT-GLDYVEGYGLTE-TMAQT---HSN---------PPDRPKlqclgiPTFGVdaRV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 332 MD-EEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSHEGQWAYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRME 409
Cdd:PRK08314 371 IDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEIDGKRFFRTGDLGRMdEEGYFFITDRLKRMINASGFKVW 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 410 LEEIEFHVRQSQYVRSAVVI----PYqpngTVEYLIAAIVP-EEHEFEKEFQLTSAIKKELAAslpAYMIPRKFIYQDHI 484
Cdd:PRK08314 451 PAEVENLLYKHPAIQEACVIatpdPR----RGETVKAVVVLrPEARGKTTEEEIIAWAREHMA---AYKYPRIVEFVDSL 523
|
....*...
3E7X_A 485 QMTANGKI 492
Cdd:PRK08314 524 PKSGSGKI 531
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-414 |
1.39e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 117.96 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAETYPQTDAFR------SQGQSLTYQELWEQSDRAAAAIQKRIS-GEKKspILVYgHMEPHMIVSFLGSVKA 75
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQARASfGDRA--VLLF-PSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 76 GH---PYIPVDLSIP--SERIAKIIESSGAELLIHAAGLSiDAVGQ--QIQTVSAEELLENEG-GSVSQDQW----VKEH 143
Cdd:PRK05691 88 GViavPAYPPESARRhhQERLLSIIADAEPRLLLTVADLR-DSLLQmeELAAANAPELLCVDTlDPALAEAWqepaLQPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 144 ETFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGG--KIFLNQAPFSFDL--------SVMDLYPCL------- 206
Cdd:PRK05691 167 DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMgliggllqPIFSGVPCVlmspayf 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 207 ------------QSGGTLH---------CVTKDAvnkpKVLFEELKKSGLNVWTSTPsfvqmclmDPGFSQDLLPHADTF 265
Cdd:PRK05691 247 lerplrwleaisEYGGTISggpdfayrlCSERVS----ESALERLDLSRWRVAYSGS--------EPIRQDSLERFAEKF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 266 MFCGevlpvsvakallerFPKAKIFNTYGPTEATVAVT---------SVEITNDVISRSESLP--------VGFAKPDMN 328
Cdd:PRK05691 315 AACG--------------FDPDSFFASYGLAEATLFVSggrrgqgipALELDAEALARNRAEPgtgsvlmsCGRSQPGHA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 329 IFIMD-EEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSHEGQWAYRTGDAGFIQDGQIFCQGRLDFQIKLHGYR 407
Cdd:PRK05691 381 VLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEHDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHN 460
|
....*..
3E7X_A 408 MELEEIE 414
Cdd:PRK05691 461 LYPQDIE 467
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
3-497 |
2.48e-27 |
|
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: 114.73 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKriSG-EKKSPILVYGHMEPHMIVSFLGSVKAGhpYIP 81
Cdd:cd05920 17 LGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRG--LGiRPGDRVVVQLPNVAEFVVLFFALLRLG--AVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 82 VdLSIPSERIAKI---IESSGAELLIHAaglsiDAVGQQIQTVSAEELLEneggsvsqdqwvKEHETFYIIYTSGSTGNP 158
Cdd:cd05920 93 V-LALPSHRRSELsafCAHAEAVAYIVP-----DRHAGFDHRALARELAE------------SIPEVALFLLSGGTTGTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 159 K-----------GVQISA--ANLQSFTDWICAdfpvsggkiflNQAPFSFDLSVMDLYPCLQSGGTLhCVTKDAvnKPKV 225
Cdd:cd05920 155 KliprthndyayNVRASAevCGLDQDTVYLAV-----------LPAAHNFPLACPGVLGTLLAGGRV-VLAPDP--SPDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 226 LFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHAdtfmfcgEVLPVSVAK---ALLERFPKA---KIFNTYGPTEAT 299
Cdd:cd05920 221 AFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSL-------RLLQVGGARlspALARRVPPVlgcTLQQVFGMAEGL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 300 VAVTSVEITNDVISRSESLPVgfaKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAfFSHEGqwAYR 379
Cdd:cd05920 294 LNYTRLDDPDEVIIHTQGRPM---SPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARA-FTPDG--FYR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 380 TGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSA--VVIPYQPNGtvEYLIAAIVPEEHEFEkefq 456
Cdd:cd05920 368 TGDlVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAavVAMPDELLG--ERSCAFVVLRDPPPS---- 441
|
490 500 510 520
....*....|....*....|....*....|....*....|..
3E7X_A 457 lTSAIKKEL-AASLPAYMIPRKFIYQDHIQMTANGKIDRKRI 497
Cdd:cd05920 442 -AAQLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
27-495 |
3.32e-27 |
|
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: 113.75 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 27 LTYQELWEQSDRAAAAIqKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLIha 106
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 107 aglsidavgqqiqtvSAEELLENeggsvsqdqwVKEHETFYIIYTSGSTGNPKGVQISAANLqsFTDWIcadfpvsggki 186
Cdd:cd05969 78 ---------------TTEELYER----------TDPEDPTLLHYTSGTTGTPKGVLHVHDAM--IFYYF----------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 187 flnQAPFSFDLSVMDLYPCLQSGG------------TLHCVTK---DAVNKPKVLFEELKKSGLNVWTSTPSFVQMcLMD 251
Cdd:cd05969 120 ---TGKYVLDLHPDDIYWCTADPGwvtgtvygiwapWLNGVTNvvyEGRFDAESWYGIIERVKVTVWYTAPTAIRM-LMK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 252 PG------FSQDLLPHADTfmfCGEVLPVSVAKALLERFpKAKIFNTYGPTEATvavtSVEITNDVISRSESLPVGFAKP 325
Cdd:cd05969 196 EGdelarkYDLSSLRFIHS---VGEPLNPEAIRWGMEVF-GVPIHDTWWQTETG----SIMIANYPCMPIKPGSMGKPLP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 326 DMNIFIMDEEGQPLPEGEKGEIVI-AG-PSVSRGYLGEPELTEKAFFsheGQWaYRTGDAGFI-QDGQIFCQGRLDFQIK 402
Cdd:cd05969 268 GVKAAVVDENGNELPPGTKGILALkPGwPSMFRGIWNDEERYKNSFI---DGW-YLTGDLAYRdEDGYFWFVGRADDIIK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 403 LHGYRMELEEIEFHVRQSQYVRSAVVIPyQPNGTVEYLIAAIVPEEHEFEKEFQLTSAIKKELAASLPAYMIPRKFIYQD 482
Cdd:cd05969 344 TSGHRVGPFEVESALMEHPAVAEAGVIG-KPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVD 422
|
490
....*....|...
3E7X_A 483 HIQMTANGKIDRK 495
Cdd:cd05969 423 NLPKTRSGKIMRR 435
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1-504 |
8.10e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 113.34 E-value: 8.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 1 MKLLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEphMIVSFLGSVKAGHPYI 80
Cdd:PRK07638 1 MGITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAILLENRIE--FLQLFAGAAMAGWTCV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 81 PVDLSIPSERIAKIIESSGAELLIHAAGLSIDAVGQQIQTVSAEE---LLENEGGSVSQDQWVkEHETFYIIYTSGSTGN 157
Cdd:PRK07638 79 PLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEEGRVIEIDEwkrMIEKYLPTYAPIENV-QNAPFYMGFTSGSTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 158 PKgvqisaANLQSFTDWI----CA--DFPVSGGKIFLnqAPFSFdLSVMDLY---PCLQSGGTLHCVTKDAVNKPKvlfE 228
Cdd:PRK07638 158 PK------AFLRAQQSWLhsfdCNvhDFHMKREDSVL--IAGTL-VHSLFLYgaiSTLYVGQTVHLMRKFIPNQVL---D 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 229 ELKKSGLNVWTSTPSFVQMCLMDPGFsqdlLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVavtsveIT 308
Cdd:PRK07638 226 KLETENISVMYTVPTMLESLYKENRV----IENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF------VT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 309 NDVISRSESLPVGFAKPDMN--IFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAffsHEGQWAyRTGDAGFI 386
Cdd:PRK07638 296 ALVDEESERRPNSVGRPFHNvqVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAREL---NADGWM-TVRDVGYE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 387 -QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVI----PYQPNgtveylIAAIVPEEHEFEKefQLTSAI 461
Cdd:PRK07638 372 dEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIgvpdSYWGE------KPVAIIKGSATKQ--QLKSFC 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
3E7X_A 462 KKELaaslPAYMIPRKFIYQDHIQMTANGKIDR---KRIGEEVLVR 504
Cdd:PRK07638 444 LQRL----SSFKIPKEWHFVDEIPYTNSGKIARmeaKSWIENQEKI 485
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
77-500 |
1.07e-26 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 113.44 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 77 HPYIPVDLSIPSERIAkiiesSGAELLIHaaglsIDAVGQQIQTVSAEELLEneggsvsqdqwvkeHETFYIIYTSGSTG 156
Cdd:PRK05852 134 TRWWPLTVNVGGDSGP-----SGGTLSVH-----LDAATEPTPATSTPEGLR--------------PDDAMIMFTGGTTG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 157 NPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVM-DLYPCLQSGGTlhcVTKDAVNK--PKVLFEELKKS 233
Cdd:PRK05852 190 LPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIaALLATLASGGA---VLLPARGRfsAHTFWDDIKAV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 234 GLNVWTSTPSFVQMCLMDPGF-SQDLLPHADTFM-FCGEVLPVSVAKALLERFpKAKIFNTYGPTEATVAVTSVEITNDV 311
Cdd:PRK05852 267 GATWYTAVPTIHQILLERAATePSGRKPAALRFIrSCSAPLTAETAQALQTEF-AAPVVCAFGMTEATHQVTTTQIEGIG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 312 ISRSESLPVGFAKPD--MNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfsHEGqWaYRTGDAGFI-QD 388
Cdd:PRK05852 346 QTENPVVSTGLVGRStgAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF--TDG-W-LRTGDLGSLsAA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 389 GQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVV--IPYQPNGtvEYLIAAIVPEEHEFEKEFQLTSAIKKELA 466
Cdd:PRK05852 422 GDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVfgVPDQLYG--EAVAAVIVPRESAPPTAEELVQFCRERLA 499
|
410 420 430
....*....|....*....|....*....|....
3E7X_A 467 aslpAYMIPRKFIYQDHIQMTANGKIDRKRIGEE 500
Cdd:PRK05852 500 ----AFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
148-494 |
1.77e-26 |
|
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: 110.04 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 IIYTSGSTGNPKGVQISAANLQSFTD-WICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTlhCVTKDAVNKPKVL 226
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDiLQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGL--CVTGGENTTYKSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 227 FEELKksgLNVWTSTpsfvqmCLMDPGFSQDLLPHADTFMFC--------GEVLPVSVAKALLERFPKAKIFNTYGPTEa 298
Cdd:cd17635 84 FKILT---TNAVTTT------CLVPTLLSKLVSELKSANATVpslrligyGGSRAIAADVRFIEATGLTNTAQVYGLSE- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 299 TVAVTSVEITNDVIsrsESLPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFsheGQWAY 378
Cdd:cd17635 154 TGTALCLPTDDDSI---EINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI---DGWVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 379 rTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEhefEKEFQL 457
Cdd:cd17635 228 -TGDLGERrEDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA---ELDENA 303
|
330 340 350
....*....|....*....|....*....|....*..
3E7X_A 458 TSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDR 494
Cdd:cd17635 304 IRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
7-499 |
2.81e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 111.88 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 7 IQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSI 86
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 87 PSERIAKIIESSGAELLI-----HAAGLSIDAVGQQIQTVSAEELLENEGGSVSQDQWVKEHETFYIIYTSGSTGNPKGV 161
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFvektfQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 162 QISAANL--QSFTDWICADFPVSGGKIFLnqAPFsFDLSVMDLY--PCLQSGGTLHCVTKDAVNKPKVLFEELKksgLNV 237
Cdd:PRK06839 168 VLTQENMfwNALNNTFAIDLTMHDRSIVL--LPL-FHIGGIGLFafPTLFAGGVIIVPRKFEPTKALSMIEKHK---VTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 238 WTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLER-FPKAKifnTYGPTEAtvAVTSVEITNDVISRSe 316
Cdd:PRK06839 242 VMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRgFLFGQ---GFGMTET--SPTVFMLSEEDARRK- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 317 slPVGFAKPDM--NIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfshEGQWAYrTGD-AGFIQDGQIFC 393
Cdd:PRK06839 316 --VGSIGKPVLfcDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI---QDGWLC-TGDlARVDEDGFVYI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 394 QGRLDFQIKLHG---YRMELEEIefhVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEFEKEfqltSAIKKELAASLP 470
Cdd:PRK06839 390 VGRKKEMIISGGeniYPLEVEQV---INKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE----KDVIEHCRLFLA 462
|
490 500
....*....|....*....|....*....
3E7X_A 471 AYMIPRKFIYQDHIQMTANGKIDRKRIGE 499
Cdd:PRK06839 463 KYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
3-499 |
3.24e-26 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 112.50 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAETYPQTDAFRSQG----QSLTYQELWEQSDRAAAA-----IQKrisGEKkspILVYGHMEPHMIVSFLGSV 73
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGllalgVKP---GDR---VAILSDNRPEWVIADLAIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 74 KAGHPYIPVDLSIPSERIAKIIESSGAELLI------------HAAGL-------SIDAVG--QQIQTVSAEELLEnEGG 132
Cdd:COG1022 87 AAGAVTVPIYPTSSAEEVAYILNDSGAKVLFvedqeqldklleVRDELpslrhivVLDPRGlrDDPRLLSLDELLA-LGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 133 SVSQDQWV-------KEHETFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLnqapfSFdLSV------ 199
Cdd:COG1022 166 EVADPAELearraavKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL-----SF-LPLahvfer 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 200 MDLYPCLQSGGTLHCVtkdavNKPKVLFEELKKSGLNVWTSTP-------SFVQMCLMD-PGFSQDLLPHA-------DT 264
Cdd:COG1022 240 TVSYYALAAGATVAFA-----ESPDTLAEDLREVKPTFMLAVPrvwekvyAGIQAKAEEaGGLKRKLFRWAlavgrryAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 265 FMFCGEVLPVS-----------VAKALLERF-PKAK-----------------------IFNTYGPTEATvAVTSVEITN 309
Cdd:COG1022 315 ARLAGKSPSLLlrlkhaladklVFSKLREALgGRLRfavsggaalgpelarffralgipVLEGYGLTETS-PVITVNRPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 310 DVISRSeslpVGFAKPDMNIFImdeegqplpeGEKGEIVIAGPSVSRGYLGEPELTEKAfFSHEGqWaYRTGDAGFI-QD 388
Cdd:COG1022 394 DNRIGT----VGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEA-FDADG-W-LHTGDIGELdED 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 389 GQIFCQGRLDFQIKL-HGYRMELEEIEFHVRQSQYVRSAVVI----PyqpngtveYLIAAIVPEEHEFEK---------- 453
Cdd:COG1022 457 GFLRITGRKKDLIVTsGGKNVAPQPIENALKASPLIEQAVVVgdgrP--------FLAALIVPDFEALGEwaeenglpyt 528
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
3E7X_A 454 ---EF----QLTSAIKKELA---ASLPAYMIPRKFI------YQDHIQMTANGKIDRKRIGE 499
Cdd:COG1022 529 syaELaqdpEVRALIQEEVDranAGLSRAEQIKRFRllpkefTIENGELTPTLKLKRKVILE 590
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
148-499 |
1.12e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 111.55 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 IIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPF--SFDLSVMDLYPcLQSGGTLHCVTK--DAVNKP 223
Cdd:PRK08633 787 IIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTVTLWLP-LLEGIKVVYHPDptDALGIA 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 224 KVLfeelKKSGLNVWTSTPSFVQMCLMDPgfsqdllpHADTFMF-------CG-EVLPVSVAKALLERFPKaKIFNTYGP 295
Cdd:PRK08633 866 KLV----AKHRATILLGTPTFLRLYLRNK--------KLHPLMFaslrlvvAGaEKLKPEVADAFEEKFGI-RILEGYGA 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 296 TE----ATVAVTSVEITNDVI---SRSESlpVGFAKPDMNIFIMD-EEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEK 367
Cdd:PRK08633 933 TEtspvASVNLPDVLAADFKRqtgSKEGS--VGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 368 AFFSHEGQWAYRTGDAGFI-QDGQIFCQGRLDFQIKL------HGyRMElEEIEFHVRQSQYVRSAVVIPYQPNGtvEYL 440
Cdd:PRK08633 1011 VIKDIDGIGWYVTGDKGHLdEDGFLTITDRYSRFAKIggemvpLG-AVE-EELAKALGGEEVVFAVTAVPDEKKG--EKL 1086
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 441 IAAIVPEEHEFEKefqltsaIKKELAAS-LPAYMIPRKFIYQDHIQMTANGKIDRKRIGE 499
Cdd:PRK08633 1087 VVLHTCGAEDVEE-------LKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1-504 |
6.94e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 107.82 E-value: 6.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 1 MKLLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRisGEKK-SPILVYGHMEPHMIVSFLGSVKAGHPY 79
Cdd:PRK07470 7 MNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAAR--GVRKgDRILVHSRNCNQMFESMFAAFRLGAVW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 80 IPVDLSIPSERIAKIIESSGAELLI------------HAAGLSIDAV---GQQIQTVSAEELLENEGGSVSQDQWVKEHE 144
Cdd:PRK07470 85 VPTNFRQTPDEVAYLAEASGARAMIchadfpehaaavRAASPDLTHVvaiGGARAGLDYEALVARHLGARVANAAVDHDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 145 TFYIIYTSGSTGNPKgvqisAANLQ----SF--TDWICADFP-VSGGKIFLNQAPFSfdlsvmdlypclqSGGTLHCVTK 217
Cdd:PRK07470 165 PCWFFFTSGTTGRPK-----AAVLThgqmAFviTNHLADLMPgTTEQDASLVVAPLS-------------HGAGIHQLCQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 218 DAVNKPKVLFEELKKSGLNVWT-----------STPSFVQMCLMDP---GFSQDLLPHAdtfMFCGEVLPVSVAKALLER 283
Cdd:PRK07470 227 VARGAATVLLPSERFDPAEVWAlverhrvtnlfTVPTILKMLVEHPavdRYDHSSLRYV---IYAGAPMYRADQKRALAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 284 FPKaKIFNTYGPTEATVAVT-------SVEITNDV-ISrseslPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVS 355
Cdd:PRK07470 304 LGK-VLVQYFGLGEVTGNITvlppalhDAEDGPDArIG-----TCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 356 RGYLGEPELTEKAFfshEGQWaYRTGDAGFI-QDGQIFCQGRL-DFQIKlHGYRMELEEIEFHVRQSQYVRSAVVIPYqP 433
Cdd:PRK07470 378 AGYYNNPEANAKAF---RDGW-FRTGDLGHLdARGFLYITGRAsDMYIS-GGSNVYPREIEEKLLTHPAVSEVAVLGV-P 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3E7X_A 434 NGTV-EYLIAAIVPEEHEfekefQLT-SAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEEVLVR 504
Cdd:PRK07470 452 DPVWgEVGVAVCVARDGA-----PVDeAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEER 519
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
10-502 |
8.40e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 107.20 E-value: 8.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 10 HAETYPQTDAFR--SQGQSLTYQELWEQSDRAAAAIQKR--ISGEKkspILVYGHMEPHMIVSFLGSVKAGHPYIPVDLS 85
Cdd:PRK09088 4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRgcVDGER---LAVLARNSVWLVALHFACARVGAIYVPLNWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 86 IPSERIAKIIESSGAELLIH-----AAGLSIDAVGQQIQTVSAEELLENEggSVSQDQwvkeheTFYIIYTSGSTGNPKG 160
Cdd:PRK09088 81 LSASELDALLQDAEPRLLLGddavaAGRTDVEDLAAFIASADALEPADTP--SIPPER------VSLILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 161 VQISAANLQSftdwICADFPVSG----GKIFLNQAP-FSFDLSVMDLYPCLQSGGTLhcVTKDAVnKPKVLFEELKKSGL 235
Cdd:PRK09088 153 VMLSERNLQQ----TAHNFGVLGrvdaHSSFLCDAPmFHIIGLITSVRPVLAVGGSI--LVSNGF-EPKRTLGRLGDPAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 236 NV--WTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERfpKAKIFNTYGPTEA-TVAVTSVEItnDVI 312
Cdd:PRK09088 226 GIthYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDD--GIPMVDGFGMSEAgTVFGMSVDC--DVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 313 sRSESLPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAfFSHEGqWaYRTGDAGfIQDGQIF 392
Cdd:PRK09088 302 -RAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARA-FTGDG-W-FRTGDIA-RRDADGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 393 ---CQGRLDFQIKlHGYRMELEEIEFHVRQSQYVRSAVVI--PYQPNGTVEYLiaAIVPEehefEKEFQLTSAIKKELAA 467
Cdd:PRK09088 377 fwvVDRKKDMFIS-GGENVYPAEIEAVLADHPGIRECAVVgmADAQWGEVGYL--AIVPA----DGAPLDLERIRSHLST 449
|
490 500 510
....*....|....*....|....*....|....*
3E7X_A 468 SLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEEVL 502
Cdd:PRK09088 450 RLAKYKVPKHLRLVDALPRTASGKLQKARLRDALA 484
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
4-500 |
1.09e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 107.43 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 4 LHA-IQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKrISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPV 82
Cdd:PRK06710 26 LHKyVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQK-LGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 83 DLSIPSERIAKIIESSGAELLihaagLSIDAVGQQIQTVSAEELLE---------------------------NEGGSVS 135
Cdd:PRK06710 105 NPLYTERELEYQLHDSGAKVI-----LCLDLVFPRVTNVQSATKIEhvivtriadflpfpknllypfvqkkqsNLVVKVS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 136 QDQWVK-------------------EHETFYIIYTSGSTGNPKGVQISAANLQSFT----DWI--CadfpVSGGKIFLNQ 190
Cdd:PRK06710 180 ESETIHlwnsvekevntgvevpcdpENDLALLQYTGGTTGFPKGVMLTHKNLVSNTlmgvQWLynC----KEGEEVVLGV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 191 APFsFDL----SVMDLypCLQSGGTLHCVTKDAVnkpKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFM 266
Cdd:PRK06710 256 LPF-FHVygmtAVMNL--SIMQGYKMVLIPKFDM---KMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 267 FCGEVLPVSVAKALlERFPKAKIFNTYGPTEATvavtSVEITNDVISRSESLPVGFAKPDMNIFIMD-EEGQPLPEGEKG 345
Cdd:PRK06710 330 SGSAPLPVEVQEKF-ETVTGGKLVEGYGLTESS----PVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 346 EIVIAGPSVSRGYLGEPEltEKAFFSHEGqWAYrTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVR 424
Cdd:PRK06710 405 EIVVKGPQIMKGYWNKPE--ETAAVLQDG-WLH-TGDVGYMdEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 425 SAVVI----PYQPngtvEYLIAAIVPEEHEFEKEFQLTSAIKKELAaslpAYMIPRKFIYQDHIQMTANGKIDRKRIGEE 500
Cdd:PRK06710 481 EVVTIgvpdPYRG----ETVKAFVVLKEGTECSEEELNQFARKYLA----AYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
89-499 |
1.45e-24 |
|
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: 105.51 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 89 ERIAKIIESS-GAELLIHAA-GLSIDAVGQQIQtVSAEELLENeggsvSQDQWVKEHETFYIIYTSGSTGNPKGVQI--- 163
Cdd:cd05912 27 DRVALLSKNSiEMILLIHALwLLGAEAVLLNTR-LTPNELAFQ-----LKDSDVKLDDIATIMYTSGTTGKPKGVQQtfg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 164 --------SAANLqSFTD---WICA--DFPVSGGKIFLNQAPFSFDLSVMDLYpclqsggtlhcvtkdavNKPKVLfEEL 230
Cdd:cd05912 101 nhwwsaigSALNL-GLTEddnWLCAlpLFHISGLSILMRSVIYGMTVYLVDKF-----------------DAEQVL-HLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 231 KKSGLNVWTSTPSFVQMCLMDpgFSQDLLPHADTFMFCGEVLPVSVAKALLER-FPkakIFNTYGPTEATVAVTSVEItN 309
Cdd:cd05912 162 NSGKVTIISVVPTMLQRLLEI--LGEGYPNNLRCILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETCSQIVTLSP-E 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 310 DVISRSESlpVGFAKPDMNIFIMDEEGqplPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfshEGQWaYRTGDAGFI-QD 388
Cdd:cd05912 236 DALNKIGS--AGKPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESF---ENGW-FKTGDIGYLdEE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 389 GQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPyQPN---GTVEylIAAIVPEEhEFEKEfQLTSAIKKEL 465
Cdd:cd05912 307 GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVG-IPDdkwGQVP--VAFVVSER-PISEE-ELIAYCSEKL 381
|
410 420 430
....*....|....*....|....*....|....
3E7X_A 466 AaslpAYMIPRKFIYQDHIQMTANGKIDRKRIGE 499
Cdd:cd05912 382 A----KYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
143-497 |
1.49e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 104.67 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 143 HETFYIIYTSGSTGNPKGVQISAANL----------QSFT--DWICADFPvsggkiflnqapfsfdlsvmdLYPCLQS-G 209
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIvnngyfigerLGLTeqDRLCIPVP---------------------LFHCFGSvL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 210 GTLHCVTKDAVN-------KPKVLFEELKKSGLNVWTSTPS-FVQMcLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALL 281
Cdd:cd05917 61 GVLACLTHGATMvfpspsfDPLAVLEAIEKEKCTALHGVPTmFIAE-LEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 282 ERFPKAKIFNTYGPTEATVAVTSVEITNDVISRSESlpVGFAKPDMNIFIMDEEGQPLPE-GEKGEIVIAGPSVSRGYLG 360
Cdd:cd05917 140 EVMNMKDVTIAYGMTETSPVSTQTRTDDSIEKRVNT--VGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 361 EPELTEKAfFSHEGqWaYRTGDAGFI-QDGQIFCQGRL-DFQIKlhG----YRMELEEiEFHvrQSQYVRSAVVI--PYQ 432
Cdd:cd05917 218 DPEKTAEA-IDGDG-W-LHTGDLAVMdEDGYCRIVGRIkDMIIR--GgeniYPREIEE-FLH--THPKVSDVQVVgvPDE 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
3E7X_A 433 PNGtvEYLIAAIVPEEHEfekefQLTSA-IKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRI 497
Cdd:cd05917 290 RYG--EEVCAWIRLKEGA-----ELTEEdIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
7-504 |
9.91e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 104.44 E-value: 9.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 7 IQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGeKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSI 86
Cdd:PRK06164 16 LDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVR-RGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 87 PSERIAKIIESSGAELLIHAAGL-SIDAVGQqIQTVSAEELLENEG----GSVSQD-------QWVKEHETFY------- 147
Cdd:PRK06164 95 RSHEVAHILGRGRARWLVVWPGFkGIDFAAI-LAAVPPDALPPLRAiavvDDAADAtpapapgARVQLFALPDpappaaa 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 -----------IIYT-SGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFS--FDLSVmdLYPCLQSGGTLH 213
Cdd:PRK06164 174 geraadpdagaLLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCgvFGFST--LLGALAGGAPLV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 214 CVtkDAVNKPKVLFEELKKSGLNVWTSTPSFVQMcLMDPGFSQDLlPHADTFMFcGEVLPVS---VAKALLERFPKAKIf 290
Cdd:PRK06164 252 CE--PVFDAARTARALRRHRVTHTFGNDEMLRRI-LDTAGERADF-PSARLFGF-ASFAPALgelAALARARGVPLTGL- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 291 ntYGPTEATVAVTSVEITNDVISRSES--LPvgfAKPDMNIFIMD-EEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEK 367
Cdd:PRK06164 326 --YGSSEVQALVALQPATDPVSVRIEGggRP---ASPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 368 AfFSHEGqWaYRTGDAGFIQ-DGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNG-TVEYliAAIV 445
Cdd:PRK06164 401 A-LTDDG-Y-FRTGDLGYTRgDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGkTVPV--AFVI 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
3E7X_A 446 PEEHEFEKEfqltSAIKKELAASLPAYMIPRKFIYQDHIQMT--ANG-KIDRKRIGEEVLVR 504
Cdd:PRK06164 476 PTDGASPDE----AGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRLREMAQAR 533
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
144-499 |
2.57e-23 |
|
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: 102.46 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 144 ETFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTlHCVTKDAVNKP 223
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGA-PVVLQDIWDPD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 224 KVLfEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFpKAKIFNTYGPTEATVAVT 303
Cdd:cd05903 173 KAL-ALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 304 SVEITN-DVISRSEslpvGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfshEGQWaYRTGD 382
Cdd:cd05903 251 SITPAPeDRRLYTD----GRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA---PEGW-FRTGD 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 383 AGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEE-HEFEKEfQLTSA 460
Cdd:cd05903 323 LARLdEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSgALLTFD-ELVAY 401
|
330 340 350
....*....|....*....|....*....|....*....
3E7X_A 461 IKKELAASlpaYMIPRKFIYQDHIQMTANGKIDRKRIGE 499
Cdd:cd05903 402 LDRQGVAK---QYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
119-502 |
6.35e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 102.00 E-value: 6.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 119 QTVSAEELLENEG---GSVSQDQWVKEHETFYIIYTSGSTGNPKGVQISAANLQSFT----DWIcaDFPVSGGKIFLNQA 191
Cdd:PRK05605 192 GTVPWETLVDAAIggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAaqgkAWV--PGLGDGPERVLAAL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 192 PF--SFDLS-VMDLYPCLqsGGTLhcVTKDAVNKPKVLfEELKKSglnvwtsTPSFVQMC------LMDPGFSQDLLPHA 262
Cdd:PRK05605 270 PMfhAYGLTlCLTLAVSI--GGEL--VLLPAPDIDLIL-DAMKKH-------PPTWLPGVpplyekIAEAAEERGVDLSG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 263 DTFMFCGEV-LPVSVAkALLERFPKAKIFNTYGPTEatvavTS-VEITNDVISRSESLPVGFAKPDMNIFIMDEE--GQP 338
Cdd:PRK05605 338 VRNAFSGAMaLPVSTV-ELWEKLTGGLLVEGYGLTE-----TSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEdpDET 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 339 LPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfsHEGqWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHV 417
Cdd:PRK05605 412 MPDGEEGELLVRGPQVFKGYWNRPEETAKSF--LDG-W-FRTGDVVVMeEDGFIRIVDRIKELIITGGFNVYPAEVEEVL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 418 RQSQYVR-SAVV-IPyQPNGTvEYLIAAIVPEEHE-FEKEfqltsAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDR 494
Cdd:PRK05605 488 REHPGVEdAAVVgLP-REDGS-EEVVAAVVLEPGAaLDPE-----GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
....*...
3E7X_A 495 KRIGEEVL 502
Cdd:PRK05605 561 REVREELL 568
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
147-495 |
9.28e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 101.60 E-value: 9.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 147 YIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMdLYPCLQSGGTLHCVTK-------DA 219
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF-FLPTLLRGGTVIVLAKfdpaevlRA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 220 VNKPKVLFEELkksglnvwtsTPSFVQMcLMD-PGFSQDLLPHADTFMFCGE-VLPVSVAKALlERFpkAKIF-NTYGPT 296
Cdd:PRK06188 251 IEEQRITATFL----------VPTMIYA-LLDhPDLRTRDLSSLETVYYGASpMSPVRLAEAI-ERF--GPIFaQYYGQT 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 297 EATVAVTsveitndVISRSESLPV--------GFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKA 368
Cdd:PRK06188 317 EAPMVIT-------YLRKRDHDPDdpkrltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 369 FfshEGQWaYRTGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVI--PYQPNGtvEYLIAAIV 445
Cdd:PRK06188 390 F---RDGW-LHTGDvAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIgvPDEKWG--EAVTAVVV 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
3E7X_A 446 PEEHEFEKEFQLTSAIkKELAASLPAymiPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK06188 464 LRPGAAVDAAELQAHV-KERKGSVHA---PKQVDFVDSLPLTALGKPDKK 509
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
10-501 |
2.32e-22 |
|
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: 100.22 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 10 HAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRisG-EKKSPILVYGHMEPHMIVSFLGSVKAGhpYIPVdLSIPS 88
Cdd:COG1021 34 RAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLAL--GlRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPV-FALPA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 89 ERIAKI---IESSGAELLI---HAAGLSIDAVGQQIQ-TVSAEE--LLENEGGS-VSQDQWVKEHETFYIIYTS------ 152
Cdd:COG1021 109 HRRAEIshfAEQSEAVAYIipdRHRGFDYRALARELQaEVPSLRhvLVVGDAGEfTSLDALLAAPADLSEPRPDpddvaf 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 153 -----GSTGNPKG-----------VQISAAnlqsftdwICAdfpVSGGKIFLNQAP--FSFDLSvmdlYPCLQsgGTLH- 213
Cdd:COG1021 189 fqlsgGTTGLPKLiprthddylysVRASAE--------ICG---LDADTVYLAALPaaHNFPLS----SPGVL--GVLYa 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 214 --CVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPkAKIFN 291
Cdd:COG1021 252 ggTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALG-CTLQQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 292 TYGPTEATVAVTSVEITNDVISRSESLPVGfakPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAfFS 371
Cdd:COG1021 331 VFGMAEGLVNYTRLDDPEEVILTTQGRPIS---PDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARA-FT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 372 HEGqWaYRTGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYqPNgtvEYLI----AAIVP 446
Cdd:COG1021 407 PDG-F-YRTGDlVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAM-PD---EYLGerscAFVVP 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
3E7X_A 447 EEHEFEkefqlTSAIKKELAAS-LPAYMIPRKFIYQDHIQMTANGKIDRKRIGEEV 501
Cdd:COG1021 481 RGEPLT-----LAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
18-501 |
3.23e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 99.29 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 18 DAFRSQGQSLTYQELWeqsdRAAAAIQKRISGEkkSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSI-PSERiAKIIE 96
Cdd:PRK07787 17 DAVRIGGRVLSRSDLA----GAATAVAERVAGA--RRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSgVAER-RHILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 97 SSGAELLIHAAGLSIDAvgqqiqtvsaeelLENEGGSVSQDQWVKEHE-----TFYIIYTSGSTGNPKGVQIS----AAN 167
Cdd:PRK07787 90 DSGAQAWLGPAPDDPAG-------------LPHVPVRLHARSWHRYPEpdpdaPALIVYTSGTTGPPKGVVLSrraiAAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 168 LQSFTD---WICADFPVSGGKIF----LnqapfsfdlsVMDLYPCLQSGGTLHCVTKDAvnkPKVLFEELKKSGlNVWTS 240
Cdd:PRK07787 157 LDALAEawqWTADDVLVHGLPLFhvhgL----------VLGVLGPLRIGNRFVHTGRPT---PEAYAQALSEGG-TLYFG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 241 TPSFVQMCLMDPGFSQDLLPhADTFMFCGEVLPVSVakalLERFPKA---KIFNTYGPTEaTVAVTSVEITndvisrSES 317
Cdd:PRK07787 223 VPTVWSRIAADPEAARALRG-ARLLVSGSAALPVPV----FDRLAALtghRPVERYGMTE-TLITLSTRAD------GER 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 318 LP--VGFAKPDMNIFIMDEEGQPLP-EGEK-GEIVIAGPSVSRGYLGEPELTEKAFfsHEGQWaYRTGDAGFIQ-DGQIF 392
Cdd:PRK07787 291 RPgwVGLPLAGVETRLVDEDGGPVPhDGETvGELQVRGPTLFDGYLNRPDATAAAF--TADGW-FRTGDVAVVDpDGMHR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 393 CQGR--LDFqIKLHGYRMELEEIEFHVRQSQYVRSAVVI--PYQPNGtvEYLIAAIVPEEHEFEKEfqltsaIKKELAAS 468
Cdd:PRK07787 368 IVGResTDL-IKSGGYRIGAGEIETALLGHPGVREAAVVgvPDDDLG--QRIVAYVVGADDVAADE------LIDFVAQQ 438
|
490 500 510
....*....|....*....|....*....|...
3E7X_A 469 LPAYMIPRKFIYQDHIQMTANGKIDRKRIGEEV 501
Cdd:PRK07787 439 LSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
22-492 |
3.38e-22 |
|
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: 99.96 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 22 SQGQSLTYQELWEQSDRAAAAIqKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAE 101
Cdd:cd17634 80 SQSRTISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 102 LLIHA-----AGLSID-------AVGQQIQTVSAEELLENEGGSV----SQDQWVKE--------HET--------FYII 149
Cdd:cd17634 159 LLITAdggvrAGRSVPlkknvddALNPNVTSVEHVIVLKRTGSDIdwqeGRDLWWRDliakaspeHQPeamnaedpLFIL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 150 YTSGSTGNPKGVQISAANLQSFTDWICAD-FPVSGGKIFLNQApfsfDLSVMDLYPCLQSGGTLHCVT------KDAVNK 222
Cdd:cd17634 239 YTSGTTGKPKGVLHTTGGYLVYAATTMKYvFDYGPGDIYWCTA----DVGWVTGHSYLLYGPLACGATtllyegVPNWPT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 223 PKVLFEELKKSGLNVWTSTPSFVQmCLMDPGfsQDLLPHAD-----TFMFCGEVLPVSVAKALLERFPKAK--IFNTYGP 295
Cdd:cd17634 315 PARMWQVVDKHGVNILYTAPTAIR-ALMAAG--DDAIEGTDrsslrILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 296 TEATVA-VTSVEITNDVISRSESLPVgfakPDMNIFIMDEEGQPLPEGEKGEIVIAG--PSVSRGYLGEPELTEKAFFSH 372
Cdd:cd17634 392 TETGGFmITPLPGAIELKAGSATRPV----FGVQPAVVDNEGHPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFST 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 373 -EGQWAyrTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVV--IPYQPNGTVEYliaAIVPEE 448
Cdd:cd17634 468 fKGMYF--SGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVvgIPHAIKGQAPY---AYVVLN 542
|
490 500 510 520
....*....|....*....|....*....|....*....|....
3E7X_A 449 HEFEKEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKI 492
Cdd:cd17634 543 HGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
146-494 |
3.49e-22 |
|
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: 97.09 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 146 FYIIYTSGSTGNPKgvqisaANLQSFTDWICA------DFPVSGGKIFLNQAPFSFDLSvmdLYPCLQ---SGGTLHCVT 216
Cdd:cd17633 3 FYIGFTSGTTGLPK------AYYRSERSWIESfvcnedLFNISGEDAILAPGPLSHSLF---LYGAISalyLGGTFIGQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 217 KDAVNKPKVLFEELKKSGLNVwtsTPSFVQMCLMdpgfSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPT 296
Cdd:cd17633 74 KFNPKSWIRKINQYNATVIYL---VPTMLQALAR----TLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 297 EATVAVTSVeitNDVISRSESlpVGFAKPDMNIFIMDEEGqplpeGEKGEIVIAGPSVSRGYLGEPeltekafFSHEGQW 376
Cdd:cd17633 147 ELSFITYNF---NQESRPPNS--VGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGG-------FSNPDGW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 377 aYRTGDAGFIQ-DGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEFEkef 455
Cdd:cd17633 210 -MSVGDIGYVDeEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYK--- 285
|
330 340 350
....*....|....*....|....*....|....*....
3E7X_A 456 QLTSAIKKELAAslpaYMIPRKFIYQDHIQMTANGKIDR 494
Cdd:cd17633 286 QLKRFLKQKLSR----YEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
23-494 |
7.52e-22 |
|
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: 98.28 E-value: 7.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 23 QGQSLTYQELWEQSDRAA--AAIQKRISGEKkspILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGA 100
Cdd:cd05914 4 GGEPLTYKDLADNIAKFAllLKINGVGTGDR---VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 101 ELLIhaaglsidavgqqiqtVSAEElleneggsvsqdqwvkehETFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFP 180
Cdd:cd05914 81 KAIF----------------VSDED------------------DVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 181 VSGGKIFLNQAPFS--FDLSVMDLYPcLQSGGTLHCVTKDA-----------------VNKPKVLFEELKKSGLNvwTST 241
Cdd:cd05914 127 LGKGDKILSILPLHhiYPLTFTLLLP-LLNGAHVVFLDKIPsakiialafaqvtptlgVPVPLVIEKIFKMDIIP--KLT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 242 PSFVQMCLMDPGFSQDLLP------------HADTFMFCGEVLPVSVAKALLE-RFPkakIFNTYGPTEatvavTSVEIT 308
Cdd:cd05914 204 LKKFKFKLAKKINNRKIRKlafkkvheafggNIKEFVIGGAKINPDVEEFLRTiGFP---YTIGYGMTE-----TAPIIS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 309 NDVISRSESLPVGFAKPDMNIFIMDeegqPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAfFSHEGqWaYRTGDAG-FIQ 387
Cdd:cd05914 276 YSPPNRIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEA-FDKDG-W-FHTGDLGkIDA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 388 DGQIFCQGRLDFQIKL-HGYRMELEEIEFHVRQSQYVRSAVVIPYQPNgtveyLIAAIVPE-EHEFEKEFQLTSAIKK-- 463
Cdd:cd05914 349 EGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKK-----LVALAYIDpDFLDVKALKQRNIIDAik 423
|
490 500 510
....*....|....*....|....*....|....*..
3E7X_A 464 -----ELAASLPAYMIPRKF-IYQDHIQMTANGKIDR 494
Cdd:cd05914 424 wevrdKVNQKVPNYKKISKVkIVKEEFEKTPKGKIKR 460
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1-501 |
1.21e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 97.73 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 1 MKLLHAIQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKR-ISGEKKSPILVYGHMEPHMIV---SFLGSVKAg 76
Cdd:PRK03640 2 ETMPNWLKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALgVKKGDRVALLMKNGMEMILVIhalQQLGAVAV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 77 hpYIPVDLSIpsERIAKIIESSGAELLIHAAGLSIDAVGQQIQTVSaeELLENEGGSVSQDQWVKEHETFYIIYTSGSTG 156
Cdd:PRK03640 81 --LLNTRLSR--EELLWQLDDAEVKCLITDDDFEAKLIPGISVKFA--ELMNGPKEEAEIQEEFDLDEVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 157 NPKGVQI-----------SAANLqSFTD---WICAD--FPVSGGKIFLNQAPF--------SFDLS-VMDLypcLQSGG- 210
Cdd:PRK03640 155 KPKGVIQtygnhwwsavgSALNL-GLTEddcWLAAVpiFHISGLSILMRSVIYgmrvvlveKFDAEkINKL---LQTGGv 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 211 -TLHCVTKdavnKPKVLFEELKKSGLNvwtstPSFVQMcLMDPGfsqdllphadtfmfcgevlPVSvaKALLE-----RF 284
Cdd:PRK03640 231 tIISVVST----MLQRLLERLGEGTYP-----SSFRCM-LLGGG-------------------PAP--KPLLEqckekGI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 285 PkakIFNTYGPTEAT---VAVTSVEITNDVISrseslpVGfaKP--DMNIFIMDEeGQPLPEGEKGEIVIAGPSVSRGYL 359
Cdd:PRK03640 280 P---VYQSYGMTETAsqiVTLSPEDALTKLGS------AG--KPlfPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 360 GEPELTEKAFfsHEGqWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEfHVRQS-QYVRSAVVI--PYQPNG 435
Cdd:PRK03640 348 NREDATRETF--QDG-W-FKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIE-EVLLShPGVAEAGVVgvPDDKWG 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
3E7X_A 436 TVEYliaAIVPEEHEFEKEfQLTSAIKKELAaslpAYMIPRKFIYQDHIQMTANGKIDRKRIGEEV 501
Cdd:PRK03640 423 QVPV---AFVVKSGEVTEE-ELRHFCEEKLA----KYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
7-500 |
1.32e-21 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 97.91 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 7 IQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQ----KRisGEKkspILVYGHMEPHMIVSFLGSVKAGHPYIPV 82
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAaagvKR--GDR---VALMCGNRIEFLDVFLGCAWLGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 83 DLSIPSERIAKIIESSGAELLIHAAGL--SIDAVGQQIQTVSAEELLENEGGSVSQDQW----------------VKEHE 144
Cdd:PRK06155 102 NTALRGPQLEHILRNSGARLLVVEAALlaALEAADPGDLPLPAVWLLDAPASVSVPAGWstaplppldapapaaaVQPGD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 145 TFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFsFDLSVMD-LYPCLQSGGTLHCVTKDAVNKp 223
Cdd:PRK06155 182 TAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPL-FHTNALNaFFQALLAGATYVLEPRFSASG- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 224 kvLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLlPHADTFMFCGEVlPVSVAKALLERFPKAKIfNTYGPTEatvavt 303
Cdd:PRK06155 260 --FWPAVRRHGATVTYLLGAMVSILLSQPARESDR-AHRVRVALGPGV-PAALHAAFRERFGVDLL-DGYGSTE------ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 304 sveiTNDVI--SRSESLP--VGFAKPDMNIFIMDEEGQPLPEGEKGEIVI--AGP-SVSRGYLGEPELTEKAFfshEGQW 376
Cdd:PRK06155 329 ----TNFVIavTHGSQRPgsMGRLAPGFEARVVDEHDQELPDGEPGELLLraDEPfAFATGYFGMPEKTVEAW---RNLW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 377 aYRTGDAGFIQ-DGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEfEKEF 455
Cdd:PRK06155 402 -FHTGDRVVRDaDGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGT-ALEP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
3E7X_A 456 QltsAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEE 500
Cdd:PRK06155 480 V---ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-495 |
1.73e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 96.73 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 28 TYQELWEQSDRAAAAIqKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLIhaa 107
Cdd:cd05971 8 TFKELKTASNRFANVL-KEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 108 glsidavgqqiqTVSAEELLeneggsvsqdqwvkehetfYIIYTSGSTGNPKGV----QISAANLQsfTDWICADFPVSG 183
Cdd:cd05971 84 ------------TDGSDDPA-------------------LIIYTSGTTGPPKGAlhahRVLLGHLP--GVQFPFNLFPRD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 184 GKIFLNQAPFSFDLSVMD-LYPCLQSGGTL--HCVTKdavNKPKVLFEELKKSGLNVWTSTPSFVQMClmdpGFSQDLLP 260
Cdd:cd05971 131 GDLYWTPADWAWIGGLLDvLLPSLYFGVPVlaHRMTK---FDPKAALDLMSRYGVTTAFLPPTALKMM----RQQGEQLK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 261 HADTFM---FC-----GEVLPVSVAKALlerfpKAKIFNTYGPTEATVAVTSVEITNDVISRSeslpVGFAKPDMNIFIM 332
Cdd:cd05971 204 HAQVKLraiATggeslGEELLGWAREQF-----GVEVNEFYGQTECNLVIGNCSALFPIKPGS----MGKPIPGHRVAIV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 333 DEEGQPLPEGEKGEIVIAGP-SVSR-GYLGEPELTEKAFfshEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRME 409
Cdd:cd05971 275 DDNGTPLPPGEVGEIAVELPdPVAFlGYWNNPSATEKKM---AGDW-LLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 410 LEEIEFHVRQSQYVRSAVVI--PYQPNGTVeylIAAIVPEEHEFEKEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQMT 487
Cdd:cd05971 351 PAEIEECLLKHPAVLMAAVVgiPDPIRGEI---VKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRT 427
|
....*...
3E7X_A 488 ANGKIDRK 495
Cdd:cd05971 428 ATGKIRRR 435
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
60-497 |
5.75e-21 |
|
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: 95.78 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 60 HMEPHMIVSFLGSVKagHPyipVDLSIPSERIAKIIESSGAELLIHAAGLS--IDAVGQQIQTV-------SAEELLENE 130
Cdd:cd12119 63 HLELYYAVPGMGAVL--HT---INPRLFPEQIAYIINHAEDRVVFVDRDFLplLEAIAPRLPTVehvvvmtDDAAMPEPA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 131 GGSV-SQDQWVKEHETFY------------IIYTSGSTGNPKGVQIS--AANLQSFTdwICAD--FPVSGGKIFLNQAPF 193
Cdd:cd12119 138 GVGVlAYEELLAAESPEYdwpdfdentaaaICYTSGTTGNPKGVVYShrSLVLHAMA--ALLTdgLGLSESDVVLPVVPM 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 194 sFDLSVMDL-YPCLQSGGTLhcVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVL 272
Cdd:cd12119 216 -FHVNAWGLpYAAAMVGAKL--VLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 273 PVSVAKALLERFpkAKIFNTYGPTEATVAVTSVEITNDVISRSESLPV------GFAKPDMNIFIMDEEGQPLPE--GEK 344
Cdd:cd12119 293 PRSLIEAFEERG--VRVIHAWGMTETSPLGTVARPPSEHSNLSEDEQLalrakqGRPVPGVELRIVDDDGRELPWdgKAV 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 345 GEIVIAGPSVSRGYLGEPEltEKAFFSHEGqWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHG---YRMELEEIefhVRQS 420
Cdd:cd12119 371 GELQVRGPWVTKSYYKNDE--ESEALTEDG-W-LRTGDVATIdEDGYLTITDRSKDVIKSGGewiSSVELENA---IMAH 443
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3E7X_A 421 QYVRSAVVIPYQPNGTVEYLIAAIVPEEHEfekefQLTS-AIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRI 497
Cdd:cd12119 444 PAVAEAAVIGVPHPKWGERPLAVVVLKEGA-----TVTAeELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
7-386 |
5.76e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 96.00 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 7 IQTHAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGEKKSpILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSI 86
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDR-VLILMLNRTEFVESVLAANMLGAIAVPVNFRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 87 PSERIAKIIESSGAELLIHAAGLS-----IDAVGQQIQTV------------SAEELLeNEGGSVSQDQWVKEHETFYII 149
Cdd:PRK07786 102 TPPEIAFLVSDCGAHVVVTEAALApvataVRDIVPLLSTVvvaggssddsvlGYEDLL-AEAGPAHAPVDIPNDSPALIM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 150 YTSGSTGNPKGVQISAANL--QSFTdWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKVL- 226
Cdd:PRK07786 181 YTSGTTGRPKGAVLTHANLtgQAMT-CLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLd 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 227 -FEELKKSGLNVwtsTPSFVQMCLMDPGFSQDLL----------PHADTFMfcgevlpvsvaKALLERFPKAKIFNTYGP 295
Cdd:PRK07786 260 vLEAEKVTGIFL---VPAQWQAVCAEQQARPRDLalrvlswgaaPASDTLL-----------RQMAATFPEAQILAAFGQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 296 TEATvAVTSVEITNDVISRSESlpVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfshEGQ 375
Cdd:PRK07786 326 TEMS-PVTCMLLGEDAIRKLGS--VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF---AGG 399
|
410
....*....|....*.
3E7X_A 376 WAY-----RTGDAGFI 386
Cdd:PRK07786 400 WFHsgdlvRQDEEGYV 415
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
7-499 |
6.42e-21 |
|
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: 96.03 E-value: 6.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 7 IQTHAETYPQTDAF---RSQGQS--LTYQELWEQSDRAAAAIQKRISGeKKSPILVYGHMEPHMIVSFLGSVKAGHPYIP 81
Cdd:cd05970 23 VDAMAKEYPDKLALvwcDDAGEEriFTFAELADYSDKTANFFKAMGIG-KGDTVMLTLKRRYEFWYSLLALHKLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 82 VDLSIPSERIAKIIESSGAELLIHAAGlsiDAVGQQIQTVSAE----ELLENEGGSVsQDQWVKEHE------------- 144
Cdd:cd05970 102 ATHQLTAKDIVYRIESADIKMIVAIAE---DNIPEEIEKAAPEcpskPKLVWVGDPV-PEGWIDFRKliknaspdferpt 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 145 ---------TFYIIYTSGSTGNPKGVQisaanlQSFTdwicadFP---VSGGKIFLNQAPFSFDLSVMD----------L 202
Cdd:cd05970 178 ansypcgedILLVYFSSGTTGMPKMVE------HDFT------YPlghIVTAKYWQNVREGGLHLTVADtgwgkavwgkI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 203 YPCLQSGGTLHCVTKDAVNkPKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDL--LPHADTfmfCGEVLPVSVakal 280
Cdd:cd05970 246 YGQWIAGAAVFVYDYDKFD-PKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLssLRYCTT---AGEALNPEV---- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 281 LERFPKA---KIFNTYGPTEATVAVTSveitndvISRSESLP--VGFAKPDMNIFIMDEEGQPLPEGEKGEIVI---AGP 352
Cdd:cd05970 318 FNTFKEKtgiKLMEGFGQTETTLTIAT-------FPWMEPKPgsMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 353 SVS--RGYLGEPELTEKAFfsHEGqwAYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVV- 428
Cdd:cd05970 391 PVGlfGGYYKDAEKTAEVW--HDG--YYHTGDAAWMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVt 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3E7X_A 429 -IPYQPNGTVeyLIAAIVpeeheFEKEFQLTSAIKKEL---AASLPA-YMIPRKFIYQDHIQMTANGKIDRKRIGE 499
Cdd:cd05970 467 gVPDPIRGQV--VKATIV-----LAKGYEPSEELKKELqdhVKKVTApYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
25-497 |
1.03e-20 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 95.13 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 25 QSLTYQELWEQSDRAA-----AAIQKrisGEKkspilVYGHME--PHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIES 97
Cdd:PRK08008 36 RRYSYLELNEEINRTAnlfysLGIRK---GDK-----VALHLDncPEFIFCWFGLAKIGAIMVPINARLLREESAWILQN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 98 SGAELL-IHAAGLSI-DAVGQQIQT-----VSAEELLENEGGSVSQDQWVKEH-------------ETFYIIYTSGSTGN 157
Cdd:PRK08008 108 SQASLLvTSAQFYPMyRQIQQEDATplrhiCLTRVALPADDGVSSFTQLKAQQpatlcyapplstdDTAEILFTSGTTSR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 158 PKGVQISAANLQ---SFTDWICAdfpVSGGKIFLNQAP-FSFDLSVMDLYPCLQSGGTLHCVTKDAVNKpkvLFEELKKS 233
Cdd:PRK08008 188 PKGVVITHYNLRfagYYSAWQCA---LRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSARA---FWGQVCKY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 234 GLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFcgeVLPVSVAK--ALLERFpKAKIFNTYGPTEatvavTSVEITNDV 311
Cdd:PRK08008 262 RATITECIPMMIRTLMVQPPSANDRQHCLREVMF---YLNLSDQEkdAFEERF-GVRLLTSYGMTE-----TIVGIIGDR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 312 ISRSESLP----VGF---AKpdmnifIMDEEGQPLPEGEKGEIVI---AGPSVSRGYLGEPELTEKAFfsHEGQWAYrTG 381
Cdd:PRK08008 333 PGDKRRWPsigrPGFcyeAE------IRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVL--EADGWLH-TG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 382 DAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEFEKEFQLTSA 460
Cdd:PRK08008 404 DTGYVdEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAF 483
|
490 500 510 520
....*....|....*....|....*....|....*....|...
3E7X_A 461 IKKELAA-SLPAYM-----IPRkfiyqdhiqmTANGKIDRKRI 497
Cdd:PRK08008 484 CEQNMAKfKVPSYLeirkdLPR----------NCSGKIIKKNL 516
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
25-396 |
1.22e-19 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 91.88 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 25 QSLTYQELWEQSDRAAAAIqkRISGEKKS--------------------------PILVyghmEPHM-IVSFLGSVKAGH 77
Cdd:PRK09274 40 DELSFAELDARSDAIAHGL--NAAGIGRGmravlmvtpsleffaltfalfkagavPVLV----DPGMgIKNLKQCLAEAQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 78 P--YIpvdlSIPSERIAKIIESSGAELLIHAAglsidAVGQQIQT--VSAEELLENEGGSVSQDQWVKEHETFYIIYTSG 153
Cdd:PRK09274 114 PdaFI----GIPKAHLARRLFGWGKPSVRRLV-----TVGGRLLWggTTLATLLRDGAAAPFPMADLAPDDMAAILFTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 154 STGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAP-FS-FDlsvmdlyPCLqsGGTlhCV------TKDAVNKPKV 225
Cdd:PRK09274 185 STGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPlFAlFG-------PAL--GMT--SVipdmdpTRPATVDPAK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 226 LFEELKKSGLnvwtsTPSFVQMCLMDPgfsqdLLPHADTFmfcGEVLP----VSVA-----KALLERF-----PKAKIFN 291
Cdd:PRK09274 254 LFAAIERYGV-----TNLFGSPALLER-----LGRYGEAN---GIKLPslrrVISAgapvpIAVIERFramlpPDAEILT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 292 TYGPTEA--TVAVTSVEITNDVISRSESLP---VGFAKPDMNIFIMD---------EEGQPLPEGEKGEIVIAGPSVSRG 357
Cdd:PRK09274 321 PYGATEAlpISSIESREILFATRAATDNGAgicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
3E7X_A 358 YLGEPELTEKAFFSH-EGQWAYRTGDAGFIQD-GQI-FCqGR 396
Cdd:PRK09274 401 YYNRPEATRLAKIPDgQGDVWHRMGDLGYLDAqGRLwFC-GR 441
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
140-414 |
1.22e-19 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 91.80 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 140 VKEHETFYIIYTSGSTGNPKGVQISAANLQSfTDWICADF--PVSGGKIFLNQAPF-SFDLSVMDLYPCLqSGgtLHCVT 216
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGVPLTHANLLA-NQRACLKFfsPKEDDVMMSFLPPFhAYGFNSCTLFPLL-SG--VPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 217 KDAVNKPKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPT 296
Cdd:PRK06334 256 AYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 297 EATVAVTsveiTNDVISRSESLPVGFAKPDMNIFIMDEEGQ-PLPEGEKGEIVIAGPSVSRGYLGEPEltEKAFFSHEGQ 375
Cdd:PRK06334 336 ECSPVIT----INTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDF--GQGFVELGGE 409
|
250 260 270 280
....*....|....*....|....*....|....*....|
3E7X_A 376 WAYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIE 414
Cdd:PRK06334 410 TWYVTGDLGYVdRHGELFLKGRLSRFVKIGAEMVSLEALE 449
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
148-495 |
4.08e-19 |
|
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: 88.16 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 IIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNKpkvlf 227
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALA----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 228 EELKKSGLnVWTS-TPSFVQMCLMDPGFSQDLlphaDTFmfcGEVL----PVSVakALLERFPKAKI--FNTYGPTEatv 300
Cdd:cd17630 80 EDLAPPGV-THVSlVPTQLQRLLDSGQGPAAL----KSL---RAVLlggaPIPP--ELLERAADRGIplYTTYGMTE--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 301 avTSVEITNDVISRSESLPVGFAKPDMNIFIMDEegqplpegekGEIVIAGPSVSRGYLgEPELTEKAFfshEGQWaYRT 380
Cdd:cd17630 147 --TASQVATKRPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYL-RGQLVPEFN---EDGW-FTT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 381 GDAGFIQ-DGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPyQPNGTV-EYLIAAIVPEEHefekefQLT 458
Cdd:cd17630 210 KDLGELHaDGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVG-VPDEELgQRPVAVIVGRGP------ADP 282
|
330 340 350
....*....|....*....|....*....|....*..
3E7X_A 459 SAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:cd17630 283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1-497 |
4.18e-19 |
|
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: 90.63 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 1 MKLLHA-IQTHAETYPQTDAFRSQGQ-----SLTYQELWEQSDRAAAAIqKRISGEKKSPILVYGHMEPHMIVSFLGSVK 74
Cdd:cd05968 60 MNIVEQlLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFLAVAR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 75 AGHPYIPVDLSIPSERIAKIIESSGAELLIHAAGLS-----------IDAVGQQIQTV--------SAEELLENEGGSVS 135
Cdd:cd05968 139 IGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTrrgrevnlkeeADKACAQCPTVekvvvvrhLGNDFTPAKGRDLS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 136 QDQWVKEH----------ETFYIIYTSGSTGNPKGvqisaanlqsfTDWICADFPVSGGKiflnQAPFSFDLSVMDLY-- 203
Cdd:cd05968 219 YDEEKETAgdgaerteseDPLMIIYTSGTTGKPKG-----------TVHVHAGFPLKAAQ----DMYFQFDLKPGDLLtw 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 204 ---------PCLQSGGTLHCVT---KDAV---NKPKVLFEELKKSGLNVWTSTPSFVQmCLM----DPGFSQDLLP---- 260
Cdd:cd05968 284 ftdlgwmmgPWLIFGGLILGATmvlYDGApdhPKADRLWRMVEDHEITHLGLSPTLIR-ALKprgdAPVNAHDLSSlrvl 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 261 -------HADTFMFCGEVLpvsvakaLLERFPkakIFNTYGPTEatvavTSVEITNDVISRsESLPVGF--AKPDMNIFI 331
Cdd:cd05968 363 gstgepwNPEPWNWLFETV-------GKGRNP---IINYSGGTE-----ISGGILGNVLIK-PIKPSSFngPVPGMKADV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 332 MDEEGQPLPEgEKGEIVIAGP--SVSRGYLGEPELTEKAFFSH-EGQWAYrtGD-AGFIQDGQIFCQGRLDFQIKLHGYR 407
Cdd:cd05968 427 LDESGKPARP-EVGELVLLAPwpGMTRGFWRDEDRYLETYWSRfDNVWVH--GDfAYYDEEGYFYILGRSDDTINVAGKR 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 408 MELEEIEFHVRQSQYVR--SAVVIPYQPNGTVEYLIAAIVPeehefekEFQLTSAIKKELAASLPAYM----IPRKFIYQ 481
Cdd:cd05968 504 VGPAEIESVLNAHPAVLesAAIGVPHPVKGEAIVCFVVLKP-------GVTPTEALAEELMERVADELgkplSPERILFV 576
|
570
....*....|....*.
3E7X_A 482 DHIQMTANGKIDRKRI 497
Cdd:cd05968 577 KDLPKTRNAKVMRRVI 592
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
19-497 |
6.12e-19 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 89.88 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 19 AFRSQGQSLTYQELWEQSDRAAAAIQKR---ISGEK---------KSPILVYGHMEPHMIV--------------SFLGS 72
Cdd:PRK12492 42 AFSNLGVTLSYAELERHSAAFAAYLQQHtdlVPGDRiavqmpnvlQYPIAVFGALRAGLIVvntnplytaremrhQFKDS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 73 VKAGHPYIP-----VDLSIPSERIAKIIESSGAELLIHAAGLSIDAVGQQI----------QTVSAEELLENEGGSVSQD 137
Cdd:PRK12492 122 GARALVYLNmfgklVQEVLPDTGIEYLIEAKMGDLLPAAKGWLVNTVVDKVkkmvpayhlpQAVPFKQALRQGRGLSLKP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 138 QWVKEHETFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSG--GKIFLNQ------AP------FSFDLSVMdly 203
Cdd:PRK12492 202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGpdGQPLMKEgqevmiAPlplyhiYAFTANCM--- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 204 pCLQSGGTLHCVTKDAVNKPKVLfEELKK------SGLNVWtstpsFVqmCLMD-PGFSQDLLPHADTFMFCGEVLpvsv 276
Cdd:PRK12492 279 -CMMVSGNHNVLITNPRDIPGFI-KELGKwrfsalLGLNTL-----FV--ALMDhPGFKDLDFSALKLTNSGGTAL---- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 277 AKALLERFPK---AKIFNTYGPTEATvavtSVEITNDVISRSESLPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPS 353
Cdd:PRK12492 346 VKATAERWEQltgCTIVEGYGLTETS----PVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 354 VSRGYLGEPELTEKAfFSHEGqWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVI--P 430
Cdd:PRK12492 422 VMKGYWQQPEATAEA-LDAEG-W-FKTGDIAVIdPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIgvP 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
3E7X_A 431 YQPNGTVEYLIaaIVPEEHEFEKEfqltsAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRI 497
Cdd:PRK12492 499 DERSGEAVKLF--VVARDPGLSVE-----ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
14-504 |
1.30e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 88.68 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 14 YPQTDA--FRSQGQSLTYQELWEQSDRAAAAIQkRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERI 91
Cdd:PRK12583 31 FPDREAlvVRHQALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 92 AKIIESSGAELLIHAAG-----------------------------------------------LSIDAVGQQIQTVSAE 124
Cdd:PRK12583 110 EYALGQSGVRWVICADAfktsdyhamlqellpglaegqpgalacerlpelrgvvslapapppgfLAWHELQARGETVSRE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 125 ELLENEGGsvsqdqwVKEHETFYIIYTSGSTGNPKGVQISAANL--------QSF----TDWICAdfPVsggkiflnqaP 192
Cdd:PRK12583 190 ALAERQAS-------LDRDDPINIQYTSGTTGFPKGATLSHHNIlnngyfvaESLglteHDRLCV--PV----------P 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 193 F--SFDLsVMDLYPCLQSGGTLhCVTKDAVNKPKVL--FEELKKSGLNvwtSTPSFVQMCLMDPGFSQDLLPHADTFMFC 268
Cdd:PRK12583 251 LyhCFGM-VLANLGCMTVGACL-VYPNEAFDPLATLqaVEEERCTALY---GVPTMFIAELDHPQRGNFDLSSLRTGIMA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 269 GEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVISRSESlpVGFAKPDMNIFIMDEEGQPLPEGEKGEIV 348
Cdd:PRK12583 326 GAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVET--VGRTQPHLEVKVVDPDGATVPRGEIGELC 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 349 IAGPSVSRGYLGEPELTEKAFfsHEGQWAYrTGDAGFIqDGQIFCQ--GRLDFQIKLHG---YRMELEeiEFHVRQSQYV 423
Cdd:PRK12583 404 TRGYSVMKGYWNNPEATAESI--DEDGWMH-TGDLATM-DEQGYVRivGRSKDMIIRGGeniYPREIE--EFLFTHPAVA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 424 RSAVV-IPYQPNGtvEYLIAAIV--PEEHEFEKEfqltsaIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEE 500
Cdd:PRK12583 478 DVQVFgVPDEKYG--EEIVAWVRlhPGHAASEEE------LREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
....
3E7X_A 501 VLVR 504
Cdd:PRK12583 550 SIEE 553
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
11-505 |
1.56e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 88.50 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDAF--RSQGQSLTYQELWEQSDRAAAAIqkRISGEKKSPILVYG--HMEPHMIVSfLGSVKAGHPYIPVDLSI 86
Cdd:PLN02330 38 AELYADKVAFveAVTGKAVTYGEVVRDTRRFAKAL--RSLGLRKGQVVVVVlpNVAEYGIVA-LGIMAAGGVFSGANPTA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 87 PSERIAKIIESSGAELLIHAA---------GLSIDAVGQQ-IQT-VSAEELLE--NEGGSVSQDQWVKEHETFYIIYTSG 153
Cdd:PLN02330 115 LESEIKKQAEAAGAKLIVTNDtnygkvkglGLPVIVLGEEkIEGaVNWKELLEaaDRAGDTSDNEEILQTDLCALPFSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 154 STGNPKGVQISAANLQSFtdwICADFpVSGGKIFLNQapfsfdLSVMDLYPCLQSGGTLHCVTKDAVNKPKVL----FEe 229
Cdd:PLN02330 195 TTGISKGVMLTHRNLVAN---LCSSL-FSVGPEMIGQ------VVTLGLIPFFHIYGITGICCATLRNKGKVVvmsrFE- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 230 lKKSGLNVWTS--------TPSFVQMCLMDPGFSQ-DLLP-HADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEAT 299
Cdd:PLN02330 264 -LRTFLNALITqevsfapiVPPIILNLVKNPIVEEfDLSKlKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHS 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 300 VavtsVEITNDVISRSESLP----VGFAKPDMNI-FIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfsHEG 374
Cdd:PLN02330 343 C----ITLTHGDPEKGHGIAkknsVGFILPNLEVkFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTI--DED 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 375 QWAYrTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEFEK 453
Cdd:PLN02330 417 GWLH-TGDIGYIdDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKES 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
3E7X_A 454 EfqltSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEEVLVRS 505
Cdd:PLN02330 496 E----EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSIN 543
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
24-495 |
1.88e-18 |
|
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: 87.95 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 24 GQSLTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEPHMIVsFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELL 103
Cdd:cd05923 26 GLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIA-LLALHRLGAVPALINPRLKAAELAELIERGEMTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 104 IHA-----------AGLSIDAVGQQIQTVSAE---ELLENEGGSVSQDQWVkehetfyiIYTSGSTGNPKGVQISAANLQ 169
Cdd:cd05923 105 VIAvdaqvmdaifqSGVRVLALSDLVGLGEPEsagPLIEDPPREPEQPAFV--------FYTSGTTGLPKGAVIPQRAAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 170 SFTDWICadfpvsggkiflNQAPFSFD-----LSVMDLY----------PCLQSGGTLHCVTKDAVNKPKVLFEELKKSG 234
Cdd:cd05923 177 SRVLFMS------------TQAGLRHGrhnvvLGLMPLYhvigffavlvAALALDGTYVVVEEFDPADALKLIEQERVTS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 235 LnvwTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIfNTYGPTEAtvaVTSVeITNDVISR 314
Cdd:cd05923 245 L---FATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKV-NIYGTTEA---MNSL-YMRDARTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 315 SESLPvGFAKPDMNIFIMDEEGQPLPEGEKGEIVIA--GPSVSRGYLGEPELTEKAFfsHEGqWaYRTGDAGFIQ-DGQI 391
Cdd:cd05923 317 TEMRP-GFFSEVRIVRIGGSPDEALANGEEGELIVAaaADAAFTGYLNQPEATAKKL--QDG-W-YRTGDVGYVDpSGDV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 392 FCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEFEKEFQLTSAIKKELAaslpA 471
Cdd:cd05923 392 RILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRASELA----D 467
|
490 500
....*....|....*....|....
3E7X_A 472 YMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:cd05923 468 FKRPRRYFFLDELPKNAMNKVLRR 491
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
141-499 |
2.85e-18 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 87.58 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 141 KEHETFYIIYTSGSTGNPKGVQISAANlqsftdwICADFPVSGGKIFLNQ-APFSFDLSVMDL---YPCLQSGGTLHCVT 216
Cdd:cd17642 182 RDEQVALIMNSSGSTGLPKGVQLTHKN-------IVARFSHARDPIFGNQiIPDTAILTVIPFhhgFGMFTTLGYLICGF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 217 KdAVNKPKvlFEE-LKKSGLNVWTstpsfVQMCLMDPGFSQDLLPHA--DTF-------MFCGEVlPVS--VAKALLERF 284
Cdd:cd17642 255 R-VVLMYK--FEEeLFLRSLQDYK-----VQSALLVPTLFAFFAKSTlvDKYdlsnlheIASGGA-PLSkeVGEAVAKRF 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 285 PKAKIFNTYGPTEATVAVTsveITNDVISRSESlpVGFAKPDMNIFIMD-EEGQPLPEGEKGEIVIAGPSVSRGYLGEPE 363
Cdd:cd17642 326 KLPGIRQGYGLTETTSAIL---ITPEGDDKPGA--VGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 364 LTeKAFFSHEGqWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPyQPNGTVEYLIA 442
Cdd:cd17642 401 AT-KALIDKDG-W-LHSGDIAYYdEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAG-IPDEDAGELPA 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
3E7X_A 443 AIVPEEHefekEFQLTSAIKKELAAS--LPAYMIPRKFIYQDHIQMTANGKIDRKRIGE 499
Cdd:cd17642 477 AVVVLEA----GKTMTEKEVMDYVASqvSTAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
8-504 |
7.05e-18 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 86.34 E-value: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 8 QTHAETYPQTDAFR-SQGQSLTYQELWEQSDRAAAaiqkrisgekkspILVYGHMEPHMIVSF------------LGSVK 74
Cdd:PRK06087 30 QQTARAMPDKIAVVdNHGASYTYSALDHAASRLAN-------------WLLAKGIEPGDRVAFqlpgwceftiiyLACLK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 75 AGHPYIPVDLSIPSERIAKIIESSGA--------------ELLIHAAG---------LSIDAVGQQIQTVSAEELLENeG 131
Cdd:PRK06087 97 VGAVSVPLLPSWREAELVWVLNKCQAkmffaptlfkqtrpVDLILPLQnqlpqlqqiVGVDKLAPATSSLSLSQIIAD-Y 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 132 GSVSQDQWVKEHETFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSfdlsvmdlypclQSGGT 211
Cdd:PRK06087 176 EPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLG------------HATGF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 212 LHCVTKDAVNKPKVLFEElkksglnVWTSTPSFVQM------CLM--DPgFSQDLLPHADT---------FMFCG-EVLP 273
Cdd:PRK06087 244 LHGVTAPFLIGARSVLLD-------IFTPDACLALLeqqrctCMLgaTP-FIYDLLNLLEKqpadlsalrFFLCGgTTIP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 274 VSVAKALLERfpKAKIFNTYGPTEATV-AVTSVEitnDVISRSESLPvGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGP 352
Cdd:PRK06087 316 KKVARECQQR--GIKLLSVYGSTESSPhAVVNLD---DPLSRFMHTD-GYAAAGVEIKVVDEARKTLPPGCEGEEASRGP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 353 SVSRGYLGEPELTEKAfFSHEGqWAYrTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPY 431
Cdd:PRK06087 390 NVFMGYLDEPELTARA-LDEEG-WYY-SGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAM 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3E7X_A 432 QPNGTVEYLIAAIVPEEHEFEKEFQ-LTSAIKKElaaSLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEEVLVR 504
Cdd:PRK06087 467 PDERLGERSCAYVVLKAPHHSLTLEeVVAFFSRK---RVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRR 537
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
27-496 |
1.77e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 85.44 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 27 LTYQELWEQsdraAAAIQKRISG---EKKSPILVYGHMEPHMIVSFLGSVKAGhpYIPVDLSIP---------SERIAKI 94
Cdd:PRK09192 50 LPYQTLRAR----AEAGARRLLAlglKPGDRVALIAETDGDFVEAFFACQYAG--LVPVPLPLPmgfggresyIAQLRGM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 95 IESSGAELLIHAAGLS--IDAVGQQIQTV---SAEELLENEGGSVSQDQwVKEHETFYIIYTSGSTGNPKGVQIS----A 165
Cdd:PRK09192 124 LASAQPAAIITPDELLpwVNEATHGNPLLhvlSHAWFKALPEADVALPR-PTPDDIAYLQYSSGSTRFPRGVIIThralM 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 166 ANLQSFT----DWICADFPVSG-------GKIFLNQAPFSFDLSVmDLYPclqsggtlhcvTKDAVNKPKVLFEELKKSG 234
Cdd:PRK09192 203 ANLRAIShdglKVRPGDRCVSWlpfyhdmGLVGFLLTPVATQLSV-DYLP-----------TRDFARRPLQWLDLISRNR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 235 LNVWTStPSF-VQMCLMDPGfSQDllpHADTFMFC-------GEVLPVSVAKALLERFP----KAKIF-NTYGPTEATVA 301
Cdd:PRK09192 271 GTISYS-PPFgYELCARRVN-SKD---LAELDLSCwrvagigADMIRPDVLHQFAEAFApagfDDKAFmPSYGLAEATLA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 302 VTSVEITN-----------------DVISRSESLPV------GFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGY 358
Cdd:PRK09192 346 VSFSPLGSgivveevdrdrleyqgkAVAPGAETRRVrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 359 LGEPElTEKAFFSheGQWaYRTGDAGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRS----AVVIPYQPN 434
Cdd:PRK09192 426 FRDEE-SQDVLAA--DGW-LDTGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSgdaaAFSIAQENG 501
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3E7X_A 435 GTVEYLIAAIV--PEEHEfekefQLTSAIKKELAAS---------LPAYMIPRkfiyqdhiqmTANGKIDRKR 496
Cdd:PRK09192 502 EKIVLLVQCRIsdEERRG-----QLIHALAALVRSEfgveaavelVPPHSLPR----------TSSGKLSRAK 559
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
144-500 |
8.46e-17 |
|
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: 82.92 E-value: 8.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 144 ETFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVM--DLYPCLQSGGTLHCVTKDAVN 221
Cdd:cd05908 107 ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIafHLAPLIAGMNQYLMPTRLFIR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 222 KPKVLFEELKKSGLNVwTSTPSFVQMCLMD---PGFSQDL-LPHADTFMFCGEVLPVSVAKALLERFPKAK-----IFNT 292
Cdd:cd05908 187 RPILWLKKASEHKATI-VSSPNFGYKYFLKtlkPEKANDWdLSSIRMILNGAEPIDYELCHEFLDHMSKYGlkrnaILPV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 293 YGPTEATVAVTS---------VEITND---------VISRSES-----LPVGFAKPDMNIFIMDEEGQPLPEGEKGEIVI 349
Cdd:cd05908 266 YGLAEASVGASLpkaqspfktITLGRRhvthgepepEVDKKDSecltfVEVGKPIDETDIRICDEDNKILPDGYIGHIQI 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 350 AGPSVSRGYLGEPELTEKAfFSHEGqWaYRTGDAGFIQDGQIFCQGRLDFQIKLHG---YRMELEEIEFHVRQSQYVRSA 426
Cdd:cd05908 346 RGKNVTPGYYNNPEATAKV-FTDDG-W-LKTGDLGFIRNGRLVITGREKDIIFVNGqnvYPHDIERIAEELEGVELGRVV 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 427 VVIPYQPNGTVEYLIAAIVPEEHEfEKEFQLTSAIKKEL--------AASLPAYMIPRkfiyqdhiqmTANGKIDRKRIG 498
Cdd:cd05908 423 ACGVNNSNTRNEEIFCFIEHRKSE-DDFYPLGKKIKKHLnkrggwqiNEVLPIRRIPK----------TTSGKVKRYELA 491
|
..
3E7X_A 499 EE 500
Cdd:cd05908 492 QR 493
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
147-497 |
1.17e-16 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 82.62 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 147 YIIYTSGSTGNPKGVQIS----AANLQSFTDWICADFPVSGGK-IFLNQAPFS--FDLSVMDLYpCLQSGGTLHCVTkDA 219
Cdd:PRK08751 212 FLQYTGGTTGVAKGAMLThrnlVANMQQAHQWLAGTGKLEEGCeVVITALPLYhiFALTANGLV-FMKIGGCNHLIS-NP 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 220 VNKPKVLfEELKKSGLNVWTSTPSFVQMCLMDPGFSQdlLPHADTFMFCGEVLpvSVAKALLERFPKAK---IFNTYGPT 296
Cdd:PRK08751 290 RDMPGFV-KELKKTRFTAFTGVNTLFNGLLNTPGFDQ--IDFSSLKMTLGGGM--AVQRSVAERWKQVTgltLVEAYGLT 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 297 EATVAVTSVEITNDVISRSESLPVgfakPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAfFSHEGqW 376
Cdd:PRK08751 365 ETSPAACINPLTLKEYNGSIGLPI----PSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKV-MDADG-W 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 377 aYRTGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEfhvrqsqyvrsaVVIPYQPnGTVEylIAAI-VPEEHEFE-- 452
Cdd:PRK08751 439 -LHTGDiARMDEQGFVYIVDRKKDMILVSGFNVYPNEIE------------DVIAMMP-GVLE--VAAVgVPDEKSGEiv 502
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
3E7X_A 453 ------KEFQLTSA-IKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRI 497
Cdd:PRK08751 503 kvvivkKDPALTAEdVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
25-399 |
1.17e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 82.12 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 25 QSLTYQELWEQSDRAAAAIqkrisgekkspiLVYGhMEPHMIVSFLgsVKAGHPYIPVDLSIpseriakiiESSGAELLI 104
Cdd:cd05910 1 SRLSFRELDERSDRIAQGL------------TAYG-IRRGMRAVLM--VPPGPDFFALTFAL---------FKAGAVPVL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 105 HAAGLSIDAVGQQIQTVSAEELLenegGSVSQDqwvkehETFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGG 184
Cdd:cd05910 57 IDPGMGRKNLKQCLQEAEPDAFI----GIPKAD------EPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 185 KI----FLNQAPFSFDLSVMDLYPCLQSggtlhcvTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMcLMDPGFSQDL-L 259
Cdd:cd05910 127 EVdlatFPLFALFGPALGLTSVIPDMDP-------TRPARADPQKLVGAIRQYGVSIVFGSPALLER-VARYCAQHGItL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 260 PHADTFMFCGEVLPVsvakALLERF-----PKAKIFNTYGPTEAtVAVTSVEiTNDVISRSESLP-------VGFAKP-- 325
Cdd:cd05910 199 PSLRRVLSAGAPVPI----ALAARLrkmlsDEAEILTPYGATEA-LPVSSIG-SRELLATTTAATsggagtcVGRPIPgv 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 326 DMNIFIMDEEGQP-------LPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSHEGQ--WaYRTGDAGFIQDgqifcQGR 396
Cdd:cd05910 273 RVRIIEIDDEPIAewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEgfW-HRMGDLGYLDD-----EGR 346
|
...
3E7X_A 397 LDF 399
Cdd:cd05910 347 LWF 349
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
11-497 |
1.69e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 82.40 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKR--ISGEKkspilVYGHME--PHMIVSFLGSVKAGHPYIPVD-LS 85
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRgvGAGDR-----VAVFLPncPQFHIVFFGILKLGAVHVPVSpLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 86 IPSErIAKIIESSGAELLIhaaglSIDAVGQQIQTVSAEELLEN----------------------EGGSVSQDQWVKEH 143
Cdd:PRK06178 118 REHE-LSYELNDAGAEVLL-----ALDQLAPVVEQVRAETSLRHvivtsladvlpaeptlplpdslRAPRLAAAGAIDLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 144 ETFY------------------IIYTSGSTGNPKGVQISAANLQsftdWICADF-PVSGGK----IFLNQAPfSF----- 195
Cdd:PRK06178 192 PALRactapvplpppaldalaaLNYTGGTTGMPKGCEHTQRDMV----YTAAAAyAVAVVGgedsVFLSFLP-EFwiage 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 196 DLSVmdLYPcLQSGGTLHCVTK-DAVnkpkVLFEELKKSGLNVWTST-PSFVQmcLMD-PGFSQ-DL--LPHADTFMFCG 269
Cdd:PRK06178 267 NFGL--LFP-LFSGATLVLLARwDAV----AFMAAVERYRVTRTVMLvDNAVE--LMDhPRFAEyDLssLRQVRVVSFVK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 270 EVLPvsvakALLERFPKAK---IFNT-YGPTEATVA--VTSVEITNDVISRSESLPVGFAKPDMNIFIMDEE-GQPLPEG 342
Cdd:PRK06178 338 KLNP-----DYRQRWRALTgsvLAEAaWGMTETHTCdtFTAGFQDDDFDLLSQPVFVGLPVPGTEFKICDFEtGELLPLG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 343 EKGEIVIAGPSVSRGYLGEPELTEKAFfshEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQ 421
Cdd:PRK06178 413 AEGEIVVRTPSLLKGYWNKPEATAEAL---RDGW-LHTGDIGKIdEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHP 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 422 YVRSAVVIPYQPNGTVEYLIAAIVPEEhefekEFQLTSAikkELAA----SLPAYMIPRKFIyQDHIQMTANGKIDRKRI 497
Cdd:PRK06178 489 AVLGSAVVGRPDPDKGQVPVAFVQLKP-----GADLTAA---ALQAwcreNMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
148-501 |
2.89e-16 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 81.64 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 IIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMD--LYPcLQSGGTLhcVTKDAVNKPKV 225
Cdd:PRK13295 202 LIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYglMMP-VMLGATA--VLQDIWDPARA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 226 LfEELKKSGLNvWT--STPsFvqmcLMDPGFSQDL----LPHADTFMFCGEVLPVSVAKALLERFpKAKIFNTYGPTE-A 298
Cdd:PRK13295 279 A-ELIRTEGVT-FTmaSTP-F----LTDLTRAVKEsgrpVSSLRTFLCAGAPIPGALVERARAAL-GAKIVSAWGMTEnG 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 299 TVAVTSVEITNDVISRSESLPVgfakPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfshEGqWaY 378
Cdd:PRK13295 351 AVTLTKLDDPDERASTTDGCPL----PGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA---DG-W-F 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 379 RTGDAGFIQ-DGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEE-HEFEKEfq 456
Cdd:PRK13295 422 DTGDLARIDaDGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPgQSLDFE-- 499
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
3E7X_A 457 ltsAIKKEL-AASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEEV 501
Cdd:PRK13295 500 ---EMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREML 542
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
11-492 |
2.97e-16 |
|
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: 81.19 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKR-ISGEKKSPIL---VYGHMEPHMIVSFLGSVkaghpYIPVDLSI 86
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALgISRGDTVAVLapnTPAMYELHFGVPMAGAV-----LNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 87 PSERIAKIIESSGAELLIhaaglsidaVGQQIQTvsaEELLEnEGGSVSQDQWVK-EHETFYIIYTSGSTGNPKGVQIS- 164
Cdd:cd12118 89 DAEEIAFILRHSEAKVLF---------VDREFEY---EDLLA-EGDPDFEWIPPAdEWDPIALNYTSGTTGRPKGVVYHh 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 165 -AANLQSFTDWIcaDFPVSGGKIFLNQAP--------FSFDLSVmdlypclqSGGTLHCVTKdaVNkPKVLFEELKKSGL 235
Cdd:cd12118 156 rGAYLNALANIL--EWEMKQHPVYLWTLPmfhcngwcFPWTVAA--------VGGTNVCLRK--VD-AKAIYDLIEKHKV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 236 NVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLER-FpkaKIFNTYGPTE----ATVAVTSVEitnd 310
Cdd:cd12118 223 THFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELgF---DVTHVYGLTEtygpATVCAWKPE---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 311 visrSESLPVG-----FAKPDMNIFIMDEE-------GQPLP-EGEK-GEIVIAGPSVSRGYLGEPELTEKAFfshEGQW 376
Cdd:cd12118 296 ----WDELPTEerarlKARQGVRYVGLEEVdvldpetMKPVPrDGKTiGEIVFRGNIVMKGYLKNPEATAEAF---RGGW 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 377 aYRTGDAGFIQ-DGQIFCQGRLDFQIKLHGYRM---ELEEIEFHVRQsqyVRSAVVIPyQPNGT-VEYLIAAIVPEEHEF 451
Cdd:cd12118 369 -FHSGDLAVIHpDGYIEIKDRSKDIIISGGENIssvEVEGVLYKHPA---VLEAAVVA-RPDEKwGEVPCAFVELKEGAK 443
|
490 500 510 520
....*....|....*....|....*....|....*....|.
3E7X_A 452 EKEFQLTSAIKKElaasLPAYMIPRKFIYqDHIQMTANGKI 492
Cdd:cd12118 444 VTEEEIIAFCREH----LAGFMVPKTVVF-GELPKTSTGKI 479
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
19-497 |
5.31e-16 |
|
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: 80.21 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 19 AFRSQGQSLTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESS 98
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 99 GAellihAAGLSIDAVgqqiqtvsaeelleneggSVSQDqwvkeheTFYIIYTSGSTGNPKG-VQISAANLQSFTDWICA 177
Cdd:cd05958 83 RI-----TVALCAHAL------------------TASDD-------ICILAFTSGTTGAPKAtMHFHRDPLASADRYAVN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 178 DFPVSGGKIFLNQAP--FSFDLSVMDLYPclQSGGTLHCVTKDAVnkPKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFS 255
Cdd:cd05958 133 VLRLREDDRFVGSPPlaFTFGLGGVLLFP--FGVGASGVLLEEAT--PDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 256 QDLLPHADTFMFCGEVLPvsvaKALLERFPKA---KIFNTYGPTEATvavtSVEITN---DVISRSESLPVgfakPDMNI 329
Cdd:cd05958 209 GPDLSSLRKCVSAGEALP----AALHRAWKEAtgiPIIDGIGSTEMF----HIFISArpgDARPGATGKPV----PGYEA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 330 FIMDEEGQPLPEGEKGEIVIAGPSVSRgYLGEPelTEKAFFshEGQWAYrTGDAGFIQ-DGQIFCQGRLDFQIKLHGYRM 408
Cdd:cd05958 277 KVVDDEGNPVPDGTIGRLAVRGPTGCR-YLADK--RQRTYV--QGGWNI-TGDTYSRDpDGYFRHQGRSDDMIVSGGYNI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 409 ELEEIEFHVRQSQYVRSAVVI--PYQPNGTVeyLIAAIVPEEHEFEKEfQLTSAIKKELAASLPAYMIPRKFIYQDHIQM 486
Cdd:cd05958 351 APPEVEDVLLQHPAVAECAVVghPDESRGVV--VKAFVVLRPGVIPGP-VLARELQDHAKAHIAPYKYPRAIEFVTELPR 427
|
490
....*....|.
3E7X_A 487 TANGKIDRKRI 497
Cdd:cd05958 428 TATGKLQRFAL 438
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
21-499 |
6.51e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 80.13 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 21 RSQGQSLTYQELWEQSDRAAAAIQKRISGEKKSpILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGA 100
Cdd:PRK12406 6 ISGDRRRSFDELAQRAARAAGGLAALGVRPGDC-VALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 101 ELLI-HA---AGLSiDAVGQQIQTVSAE---ELLENEG----------GSVSQDQWVKEHETF---------YIIYTSGS 154
Cdd:PRK12406 85 RVLIaHAdllHGLA-SALPAGVTVLSVPtppEIAAAYRispalltppaGAIDWEGWLAQQEPYdgppvpqpqSMIYTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 155 TGNPKGVQISAAN---LQSFTDWICADFPVSGGKIFL------NQAPFSFDL------SVMDLYPCLQSGGTLHCVTKDA 219
Cdd:PRK12406 164 TGHPKGVRRAAPTpeqAAAAEQMRALIYGLKPGIRALltgplyHSAPNAYGLragrlgGVLVLQPRFDPEELLQLIERHR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 220 VNKPKV---LFEELKKSGLNVW----TSTPSFVQmclmdpgfsqdllpHAdtfmfcGEVLPVSVAKALLERFPKAkIFNT 292
Cdd:PRK12406 244 ITHMHMvptMFIRLLKLPEEVRakydVSSLRHVI--------------HA------AAPCPADVKRAMIEWWGPV-IYEY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 293 YGPTEATVAVTSVeiTNDVISRSESlpVGFAKPDMNIFIMDEEGQPLPEGEKGEIV--IAG-PSVSrgYLGEPEltEKAF 369
Cdd:PRK12406 303 YGSTESGAVTFAT--SEDALSHPGT--VGKAAPGAELRFVDEDGRPLPQGEIGEIYsrIAGnPDFT--YHNKPE--KRAE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 370 FSHEGQWAyrTGDAGFI-QDGQIF-CQGRLDFQIKlHGYRMELEEIEFHVRQSQYVRSAVV--IPYQPNGtvEYLIAAIV 445
Cdd:PRK12406 375 IDRGGFIT--SGDVGYLdADGYLFlCDRKRDMVIS-GGVNIYPAEIEAVLHAVPGVHDCAVfgIPDAEFG--EALMAVVE 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
3E7X_A 446 PEEhefEKEFQLtSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGE 499
Cdd:PRK12406 450 PQP---GATLDE-ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
66-397 |
7.54e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 80.37 E-value: 7.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 66 IVSFLGSVKAGhpYIPVDLSIPS-----ERI-AKIIESSGAELLIHAAglSIDAVGQQIQTVSAE--------ELLENEG 131
Cdd:PRK05850 73 IVAFLGALQAG--LIAVPLSVPQggahdERVsAVLRDTSPSVVLTTSA--VVDDVTEYVAPQPGQsappvievDLLDLDS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 132 GSVSQDQWVKEHETFYIIYTSGSTGNPKGVQISAANLQSFTDWICAD-FPVSGGKIFLNQA-----PFSFDLSVMdLYPC 205
Cdd:PRK05850 149 PRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDyFGDTGGVPPPDTTvvswlPFYHDMGLV-LGVC 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 206 LQSGGTLHCVTKDAV---NKPKVLFEELKKSGLnVWTSTPSFvqmclmdpGFS--------QDL----LPHADTFMFCGE 270
Cdd:PRK05850 228 APILGGCPAVLTSPVaflQRPARWMQLLASNPH-AFSAAPNF--------AFElavrktsdDDMagldLGGVLGIISGSE 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 271 -VLPVSVaKALLERFPKakiFN--------TYGPTEATVAV-TSVEITNDVISR--SESLPVGFAKP------------- 325
Cdd:PRK05850 299 rVHPATL-KRFADRFAP---FNlretairpSYGLAEATVYVaTREPGQPPESVRfdYEKLSAGHAKRcetgggtplvsyg 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 326 ---DMNIFIMD-EEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFFSH---------EGQWaYRTGDAGFIQDGQIF 392
Cdd:PRK05850 375 sprSPTVRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATlvdpspgtpEGPW-LRTGDLGFISEGELF 453
|
....*
3E7X_A 393 CQGRL 397
Cdd:PRK05850 454 IVGRI 458
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
146-494 |
1.01e-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: 78.08 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 146 FYIIYTSGSTGNPKGVQISAANLqsftdwICADFP------VSGGKIFLNQAPFsFDLSVMDL-YPCLQSGGTLHCVTKD 218
Cdd:cd17637 3 FVIIHTAAVAGRPRGAVLSHGNL------IAANLQlihamgLTEADVYLNMLPL-FHIAGLNLaLATFHAGGANVVMEKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 219 AvnkPKVLFEELKKSGLNVWTSTPSFVQM---CLMDPGFSQDLLPHAdtfmfCGEVLPVSVAKalLERFPKAKIFNTYGP 295
Cdd:cd17637 76 D---PAEALELIEEEKVTLMGSFPPILSNlldAAEKSGVDLSSLRHV-----LGLDAPETIQR--FEETTGATFWSLYGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 296 TEATVAVTsveitndvISRSESLP--VGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfshE 373
Cdd:cd17637 146 TETSGLVT--------LSPYRERPgsAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---R 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 374 GQWaYRTGDAG-FIQDGQIFCQGR-----LdfqIKLHGYRMELEEIEFHVRQSQYVRSAVVI--PYQPNGtvEYLIAAIV 445
Cdd:cd17637 215 NGW-HHTGDLGrFDEDGYLWYAGRkpekeL---IKPGGENVYPAEVEKVILEHPAIAEVCVIgvPDPKWG--EGIKAVCV 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
3E7X_A 446 PEEHEFEKEFQLTSAIKKELAaslpAYMIPRKFIYQDHIQMTANGKIDR 494
Cdd:cd17637 289 LKPGATLTADELIEFVGSRIA----RYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
26-495 |
1.40e-15 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 79.42 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 26 SLTYQELWEQSDRAAAAIQKRISGEKKS-PILVYGHMepHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLI 104
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVvGIMCRNHR--GFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 105 H---------------AAGLSIDAVGQQIQTVSAEELLENEGGsvsQDQWVKEHETFYIIYTSGSTGNPKGVQISAAN-- 167
Cdd:PRK13382 146 YdeefsatvdraladcPQATRIVAWTDEDHDLTVEVLIAAHAG---QRPEPTGRKGRVILLTSGTTGTPKGARRSGPGgi 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 168 --LQSFTDWIcadfPVSGGKIFLNQAP------FSfdlsvmdlypCLQSGGTLHC--VTK------DAVNkpkvLFEELK 231
Cdd:PRK13382 223 gtLKAILDRT----PWRAEEPTVIVAPmfhawgFS----------QLVLAASLACtiVTRrrfdpeATLD----LIDRHR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 232 KSGLNVwtsTPSFVQ--MCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAkIFNTYGPTEATVAVTSveiTN 309
Cdd:PRK13382 285 ATGLAV---VPVMFDriMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEAGMIATA---TP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 310 DVISRSeslPVGFAKPDM--NIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEpelTEKAFfsHEGQWAyrTGDAGFIQ 387
Cdd:PRK13382 358 ADLRAA---PDTAGRPAEgtEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDF--HDGFMA--SGDVGYLD 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 388 D-GQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEhefekEFQLT-SAIKKEL 465
Cdd:PRK13382 428 EnGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-----GASATpETLKQHV 502
|
490 500 510
....*....|....*....|....*....|
3E7X_A 466 AASLPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK13382 503 RDNLANYKVPRDIVVLDELPRGATGKILRR 532
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
27-494 |
2.46e-15 |
|
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: 77.94 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 27 LTYQELWEQSDRAAAAIQKRISGEKKspiLVYGHM--EPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLI 104
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGD---VVAGLLprTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 105 haaglsidavgqqiqtvsaeelleneggsVSQDQWVK-EHETFYIIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSG 183
Cdd:cd05973 78 -----------------------------TDAANRHKlDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 184 GKIFLNQAP--FSFDLSVMDLYPCLQSGGTLhcvTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMcLMDPGFSQDLLPH 261
Cdd:cd05973 129 EDSFWNAADpgWAYGLYYAITGPLALGHPTI---LLEGGFSVESTWRVIERLGVTNLAGSPTAYRL-LMAAGAEVPARPK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 262 adtfmfcGEVLPVSVAKALLE----RFPKAK----IFNTYGPTEATVAVTSVEITNDVIsRSESLpvGFAKPDMNIFIMD 333
Cdd:cd05973 205 -------GRLRRVSSAGEPLTpeviRWFDAAlgvpIHDHYGQTELGMVLANHHALEHPV-HAGSA--GRAMPGWRVAVLD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 334 EEGQPLPEGEKGEIVI---AGPSVS-RGYLGEPElteKAFfshEGQWaYRTGDAG-FIQDGQIFCQGRLDFQIKLHGYRM 408
Cdd:cd05973 275 DDGDELGPGEPGRLAIdiaNSPLMWfRGYQLPDT---PAI---DGGY-YLTGDTVeFDPDGSFSFIGRADDVITMSGYRI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 409 ELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEH-----EFEKEFQLTsaIKKELAASlpAYmiPRKFIYQDH 483
Cdd:cd05973 348 GPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGhegtpALADELQLH--VKKRLSAH--AY--PRTIHFVDE 421
|
490
....*....|.
3E7X_A 484 IQMTANGKIDR 494
Cdd:cd05973 422 LPKTPSGKIQR 432
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
27-453 |
1.16e-14 |
|
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: 76.49 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 27 LTYQELWEQSDRAAAAIQKR-ISGEKKSPILVYGHMEPHMIVSFLGSVkaGHPYIPVDL--SIPSERIAKIIESSGAELL 103
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLgGKPAPASFVGIYSINRPEWIISELACY--AYSLVTVPLydTLGPEAIEYILNHAEISIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 104 IHAAGlsidavgqqIQTVSAEELlENEGGSVSQDQWVKEHETFY-IIYTSGSTGNPKGVQISAANLQSFTDWICaDFPVS 182
Cdd:cd05927 84 FCDAG---------VKVYSLEEF-EKLGKKNKVPPPPPKPEDLAtICYTSGTTGNPKGVMLTHGNIVSNVAGVF-KILEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 183 GGKIFLNQAPFSFdLS-------VMDLYpCLQSGGTLHCVTKDavnkPKVLFEELKKSGLNVWTSTP------------- 242
Cdd:cd05927 153 LNKINPTDVYISY-LPlahiferVVEAL-FLYHGAKIGFYSGD----IRLLLDDIKALKPTVFPGVPrvlnriydkifnk 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 243 ----SFVQMCLMDPGFSQDLL------PHADTF-----------MFCGEV-LPVSVAKAL---LERFPKA----KIFNTY 293
Cdd:cd05927 227 vqakGPLKRKLFNFALNYKLAelrsgvVRASPFwdklvfnkikqALGGNVrLMLTGSAPLspeVLEFLRValgcPVLEGY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 294 GPTEATVAVT-SVEITNDVISRSESLPVGFAK----PDMNIFIMDEEGqplpegeKGEIVIAGPSVSRGYLGEPELTEKA 368
Cdd:cd05927 307 GQTECTAGATlTLPGDTSVGHVGGPLPCAEVKlvdvPEMNYDAKDPNP-------RGEVCIRGPNVFSGYYKDPEKTAEA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 369 FFShEGqWaYRTGDAGFIQ-DGQIFCQGRLDFQIKL-HGYRMELEEIEFHVRQSQYVRSAVVI--PYQPngtveYLIAAI 444
Cdd:cd05927 380 LDE-DG-W-LHTGDIGEWLpNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVYgdSLKS-----FLVAIV 451
|
....*....
3E7X_A 445 VPEEHEFEK 453
Cdd:cd05927 452 VPDPDVLKE 460
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
24-492 |
1.47e-14 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 76.07 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 24 GQSLTYQELWEQSDRAAAAIQKRisGEKK-SPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAEL 102
Cdd:PRK07514 26 GLRYTYGDLDAASARLANLLVAL--GVKPgDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 103 LI----HAAGLSidAVGQQIQTVSAEELLENEGGSVSQ--DQWVKEHETF--------YIIYTSGSTGNPKGVQISAANL 168
Cdd:PRK07514 104 VVcdpaNFAWLS--KIAAAAGAPHVETLDADGTGSLLEaaAAAPDDFETVprgaddlaAILYTSGTTGRSKGAMLSHGNL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 169 QS----------FTD---WICAdFPV---------------SGGK-IFLNQapfsFDlsvmdlypclqsggtlhcvtkda 219
Cdd:PRK07514 182 LSnaltlvdywrFTPddvLIHA-LPIfhthglfvatnvallAGASmIFLPK----FD----------------------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 220 vnkPKVLFEELKKSglNVWTSTPSFVQMCLMDPGFSQDLLPH------------ADTFMFCGEVlpvsVAKALLERfpka 287
Cdd:PRK07514 234 ---PDAVLALMPRA--TVMMGVPTFYTRLLQEPRLTREAAAHmrlfisgsapllAETHREFQER----TGHAILER---- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 288 kifntYGPTEaTVAVTSVEITNDVISRSeslpVGFAKPDMNIFIMD-EEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTe 366
Cdd:PRK07514 301 -----YGMTE-TNMNTSNPYDGERRAGT----VGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKT- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 367 KAFFSHEGqWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHV-RQSQYVRSAVV-IPYQPNGtvEYLIAA 443
Cdd:PRK07514 370 AEEFRADG-F-FITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPKEVEGEIdELPGVVESAVIgVPHPDFG--EGVTAV 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
3E7X_A 444 IVPeehefEKEFQLT-SAIKKELAASLPAYMIPRKFIYQDHIQMTANGKI 492
Cdd:PRK07514 446 VVP-----KPGAALDeAAILAALKGRLARFKQPKRVFFVDELPRNTMGKV 490
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
27-497 |
3.00e-14 |
|
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: 74.94 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 27 LTYQELWEQSDRAAAAIQKrISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPyipvdlsipserIAKIIESSGAELLIHA 106
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVE-LGLKPGDKVAIFAETRAEWLITALGCWSQNIP------------IVTVYATLGEDALIHS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 107 aglsidavgqqIQTVSAEELLENEGGSvsqdqwvkehETFYIIYTSGSTGNPKGVQISAANLQSF--------------T 172
Cdd:cd17639 73 -----------LNETECSAIFTDGKPD----------DLACIMYTSGSTGNPKGVMLTHGNLVAGiaglgdrvpellgpD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 173 DWICADFPVSggKIFlnqaPFSFDLSvmdlypCLQSGG--------TLHCVTK-----DAVN-KPKVL------FEELKK 232
Cdd:cd17639 132 DRYLAYLPLA--HIF----ELAAENV------CLYRGGtigygsprTLTDKSKrgckgDLTEfKPTLMvgvpaiWDTIRK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 233 sGLNVWTSTPSFVQMCLMDPGFS--QDLLPHADTFMFCGEVLPVSVAKALLERF-----------PKAKIF-NT------ 292
Cdd:cd17639 200 -GVLAKLNPMGGLKRTLFWTAYQskLKALKEGPGTPLLDELVFKKVRAALGGRLrymlsggaplsADTQEFlNIvlcpvi 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 293 --YGPTEaTVAVTSVEITNDVISRSeslpVGFAKPDMNIFIMD-EEG-----QPLPegeKGEIVIAGPSVSRGYLGEPEL 364
Cdd:cd17639 279 qgYGLTE-TCAGGTVQDPGDLETGR----VGPPLPCCEIKLVDwEEGgystdKPPP---RGEILIRGPNVFKGYYKNPEK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 365 TEKAFFshEGQWaYRTGDAG-FIQDGQIFCQGRLDFQIKL-HGYRMELEEIEFHVRQSQYVRS--AVVIPYQPngtveYL 440
Cdd:cd17639 351 TKEAFD--GDGW-FHTGDIGeFHPDGTLKIIDRKKDLVKLqNGEYIALEKLESIYRSNPLVNNicVYADPDKS-----YP 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 441 IAAIVP---------EEH-----EFE-----KEFQltSAIKKEL-----AASLPAYMIPRKFIYQDHI------QMTANG 490
Cdd:cd17639 423 VAIVVPnekhltklaEKHgvinsEWEelcedKKLQ--KAVLKSLaetarAAGLEKFEIPQGVVLLDEEwtpengLVTAAQ 500
|
....*..
3E7X_A 491 KIDRKRI 497
Cdd:cd17639 501 KLKRKEI 507
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
10-492 |
3.29e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 74.96 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 10 HAETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKR-ISGEKKSPILVYGHMEphMIVSFLGSVKAGHPYIPVDLSIPS 88
Cdd:PRK07788 58 AARRAPDRAALIDERGTLTYAELDEQSNALARGLLALgVRAGDGVAVLARNHRG--FVLALYAAGKVGARIILLNTGFSG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 89 ERIAKIIESSGAELLIH-------AAGLSIDAVGQQIQTVSAEELLENEGGSVSQDQWVKEHET----------FYIIYT 151
Cdd:PRK07788 136 PQLAEVAAREGVKALVYddeftdlLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTaplpkppkpgGIVILT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 152 SGSTGNPKGVQISAANlqSFTdwicadfPVSGgkiFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVN---------K 222
Cdd:PRK07788 216 SGTTGTPKGAPRPEPS--PLA-------PLAG---LLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGstvvlrrrfD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 223 PKVLFEELKKSGLNVWTSTPSFVQMCLmdpgfsqDLLPHA----DT----FMFC-GEVLPVSVAKALLERFPKAkIFNTY 293
Cdd:PRK07788 284 PEATLEDIAKHKATALVVVPVMLSRIL-------DLGPEVlakyDTsslkIIFVsGSALSPELATRALEAFGPV-LYNLY 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 294 GPTEATVAVtsveitndvISRSESL---P--VGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYL-GEPELTEK 367
Cdd:PRK07788 356 GSTEVAFAT---------IATPEDLaeaPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTdGRDKQIID 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 368 AFFShegqwayrTGDAGFI-QDGQIFCQGRLDFQIKLHG---YRMELEE-IEFHvrqsQYVRSAVVIPYQPNGTVEYLIA 442
Cdd:PRK07788 427 GLLS--------SGDVGYFdEDGLLFVDGRDDDMIVSGGenvFPAEVEDlLAGH----PDVVEAAVIGVDDEEFGQRLRA 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
3E7X_A 443 AIVPEEHEFEKEFQLTSAIKKELAaslpAYMIPRKFIYQDHIQMTANGKI 492
Cdd:PRK07788 495 FVVKAPGAALDEDAIKDYVRDNLA----RYKVPRDVVFLDELPRNPTGKV 540
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
148-492 |
3.34e-14 |
|
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: 73.69 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 IIYTSGSTGNPKGVQisAANLQS---FTDWiCADFPVSGGKIFLNQAPF--SFDLSVmDLYPCLQSGGTlhcVTKDAVNK 222
Cdd:cd17638 5 IMFTSGTTGRSKGVM--CAHRQTlraAAAW-ADCADLTEDDRYLIINPFfhTFGYKA-GIVACLLTGAT---VVPVAVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 223 PKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAv 302
Cdd:cd17638 78 VDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 303 TSVEITNDVISRSESlpVGFAKPDMNIFIMDEegqplpegekGEIVIAGPSVSRGYLGEPELTEKAFfsHEGQWAYrTGD 382
Cdd:cd17638 157 TMCRPGDDAETVATT--CGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI--DADGWLH-TGD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 383 AG-FIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVI--PYQPNGTVEYliAAIVPEEHEFEKEFQLTS 459
Cdd:cd17638 222 VGeLDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIgvPDERMGEVGK--AFVVARPGVTLTEEDVIA 299
|
330 340 350
....*....|....*....|....*....|...
3E7X_A 460 AIKKELAaslpAYMIPRKFIYQDHIQMTANGKI 492
Cdd:cd17638 300 WCRERLA----NYKVPRFVRFLDELPRNASGKV 328
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
147-493 |
3.61e-14 |
|
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: 73.96 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 147 YIIYTSGSTGNPKGV----------QISAANL----QSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTL 212
Cdd:cd05924 7 YILYTGGTTGMPKGVmwrqedifrmLMGGADFgtgeFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 213 hcVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMCLMDPgfSQDLLPHADTFMFC----GEVLPVSVAKALLERFPKAK 288
Cdd:cd05924 87 --VLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDA--LRDAGPYDLSSLFAissgGALLSPEVKQGLLELVPNIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 289 IFNTYGPTEATVAVTSVEITNDVISRSeslpvgFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPS-VSRGYLGEPELTEK 367
Cdd:cd05924 163 LVDAFGSSETGFTGSGHSAGSGPETGP------FTRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 368 AFFSHEGQ-WAYrTGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPyQPNGTVEYLIAAIV 445
Cdd:cd05924 237 TFPEVDGVrYAV-PGDrATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVG-RPDERWGQEVVAVV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
3E7X_A 446 peehEFEKEFQLTSA-IKKELAASLPAYMIPRKFIYQDHIQMTANGKID 493
Cdd:cd05924 315 ----QLREGAGVDLEeLREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
142-497 |
3.68e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 75.06 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 142 EHETFYIIYTSGSTGNPKGVQIS-----AANLQSFTDWICADFPVsggkiFLNQAP------FSFDLSVMdlypclQSGG 210
Cdd:PLN03102 185 EHDPISLNYTSGTTADPKGVVIShrgayLSTLSAIIGWEMGTCPV-----YLWTLPmfhcngWTFTWGTA------ARGG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 211 TLHCVTKdaVNKPKVlFEELKKSGLNVWTSTPSFVQMCLmdPGFSQDLLPHADTF-MFCGEVLPVSVAKALLERFpKAKI 289
Cdd:PLN03102 254 TSVCMRH--VTAPEI-YKNIEMHNVTHMCCVPTVFNILL--KGNSLDLSPRSGPVhVLTGGSPPPAALVKKVQRL-GFQV 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 290 FNTYGPTEATVAVTSVEITND-----------VISRSESLPVGFAKPDMNifiMDEEGQPLPEGEK--GEIVIAGPSVSR 356
Cdd:PLN03102 328 MHAYGLTEATGPVLFCEWQDEwnrlpenqqmeLKARQGVSILGLADVDVK---NKETQESVPRDGKtmGEIVIKGSSIMK 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 357 GYLGEPELTEKAFfshEGQWaYRTGDAGFIQ-DGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVI--PYQP 433
Cdd:PLN03102 405 GYLKNPKATSEAF---KHGW-LNTGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVamPHPT 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 434 NGtvEYLIAAIVPEEHEFEKEFQLTSAIKKE------LAASLPAYMIPRKFIYQDHIQMTANGKIDRKRI 497
Cdd:PLN03102 481 WG--ETPCAFVVLEKGETTKEDRVDKLVTRErdlieyCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
28-497 |
3.97e-14 |
|
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: 74.81 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 28 TYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLIhaa 107
Cdd:cd05928 43 SFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIV--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 108 glSIDAVGQQIQTVSAE------ELLENEGgsvSQDQWV------------------KEHETFYIIYTSGSTGNPKGVQI 163
Cdd:cd05928 120 --TSDELAPEVDSVASEcpslktKLLVSEK---SRDGWLnfkellneastehhcvetGSQEPMAIYFTSGTTGSPKMAEH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 164 SAANLqsftdwicadfpvsGGKIFLNqAPFSFDLSVMDLYPCLQSGGTLH--------------CVTKDAVNK--PKVLF 227
Cdd:cd05928 195 SHSSL--------------GLGLKVN-GRYWLDLTASDIMWNTSDTGWIKsawsslfepwiqgaCVFVHHLPRfdPLVIL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 228 EELKKSGLNVWTSTPSFVQMCLMDpGFSQDLLPHADTFMFCGEVLPVSVakalLERFpKAK----IFNTYGPTEaTVAVT 303
Cdd:cd05928 260 KTLSSYPITTFCGAPTVYRMLVQQ-DLSSYKFPSLQHCVTGGEPLNPEV----LEKW-KAQtgldIYEGYGQTE-TGLIC 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 304 SVEITNDVISRSeslpVGFAKPDMNIFIMDEEGQPLPEGEKGEIVI-AGP----SVSRGYLGEPELTEKAFfshEGQWaY 378
Cdd:cd05928 333 ANFKGMKIKPGS----MGKASPPYDVQIIDDNGNVLPPGTEGDIGIrVKPirpfGLFSGYVDNPEKTAATI---RGDF-Y 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 379 RTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFH-VRQSQYVRSAVV-IPYQPNGTVEYLIAAIVPEEHEFEKEf 455
Cdd:cd05928 405 LTGDRGIMdEDGYFWFMGRADDVINSSGYRIGPFEVESAlIEHPAVVESAVVsSPDPIRGEVVKAFVVLAPQFLSHDPE- 483
|
490 500 510 520
....*....|....*....|....*....|....*....|..
3E7X_A 456 QLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRI 497
Cdd:cd05928 484 QLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
151-494 |
7.77e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 73.88 E-value: 7.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 151 TSGSTGNPKGVQISAANLQSFTDWIC--ADFPVSGGkIFLNQAPFSFDLSVMD-LYPCLQSGGTLHCVTK-DAVNKPKVL 226
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFvaAEFDVETD-VMVSWLPLFHDMGMVGfLTVPMYFGAELVKVTPmDFLRDPLLW 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 227 FEELKKSGLNVwTSTPSFV------QMCLMDPGFSQDLlpHADTFMFCG-EVLPVSVAKALLE---RF--PKAKIFNTYG 294
Cdd:PRK07768 239 AELISKYRGTM-TAAPNFAyallarRLRRQAKPGAFDL--SSLRFALNGaEPIDPADVEDLLDagaRFglRPEAILPAYG 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 295 PTEATVAVTSVE----ITNDVIS------RSESLPV-----------GFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPS 353
Cdd:PRK07768 316 MAEATLAVSFSPcgagLVVDEVDadllaaLRRAVPAtkgntrrlatlGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGES 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 354 VSRGYL---GEPELTEkaffshEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRS--AV 427
Cdd:PRK07768 396 VTPGYLtmdGFIPAQD------ADGW-LDTGDLGYLtEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPgnAV 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 428 VIPYQPNGTVEYLiaAIVPEEHEFEKEFQLTsAIKKELAAS--------------LPAYMIPRkfiyqdhiqmTANGKID 493
Cdd:PRK07768 469 AVRLDAGHSREGF--AVAVESNAFEDPAEVR-RIRHQVAHEvvaevgvrprnvvvLGPGSIPK----------TPSGKLR 535
|
.
3E7X_A 494 R 494
Cdd:PRK07768 536 R 536
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
26-479 |
9.32e-14 |
|
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: 73.64 E-value: 9.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 26 SLTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELL-- 103
Cdd:cd17632 67 TITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLav 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 104 -------------------------------IHAAGLSI--DAVGQQIQTVSAEELLENEGGSVSQDQWVKEHET----F 146
Cdd:cd17632 147 saehldlaveavleggtpprlvvfdhrpevdAHRAALESarERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDddplA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 147 YIIYTSGSTGNPKGVQISAANLQSF---TDWICADFPVSGgkIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTKDAVNkp 223
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYTERLVATFwlkVSSIQDIRPPAS--ITLNFMPMSHIAGRISLYGTLARGGTAYFAAASDMS-- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 224 kVLFEELKKSGLNVWTSTPSFVQMCL--------------MDPG---------FSQDLLPHADTFMFCGEVLPVSVAKAL 280
Cdd:cd17632 303 -TLFDDLALVRPTELFLVPRVCDMLFqryqaeldrrsvagADAEtlaervkaeLRERVLGGRLLAAVCGSAPLSAEMKAF 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 281 LERFPKAKIFNTYGPTEATVAvtsveITNDVISRSeslPVGFAK----PDMNIFIMDeegQPLPegeKGEIVIAGPSVSR 356
Cdd:cd17632 382 MESLLDLDLHDGYGSTEAGAV-----ILDGVIVRP---PVLDYKlvdvPELGYFRTD---RPHP---RGELLVKTDTLFP 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 357 GYLGEPELTEKaFFSHEGqwAYRTGD--AGFIQDGQIFCQGRLDFqiklhgyrMELEEIEFhVRQSQ----YVRSAVV-- 428
Cdd:cd17632 448 GYYKRPEVTAE-VFDEDG--FYRTGDvmAELGPDRLVYVDRRNNV--------LKLSQGEF-VTVARleavFAASPLVrq 515
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
3E7X_A 429 IPYQPNGTVEYLIAAIVP--EEHEFEKEFQLTSAIKKELA-----ASLPAYMIPRKFI 479
Cdd:cd17632 516 IFVYGNSERAYLLAVVVPtqDALAGEDTARLRAALAESLQriareAGLQSYEIPRDFL 573
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
3-497 |
2.09e-13 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 72.33 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAEtyPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEPHMIVsFLGSVKAGhpYIPV 82
Cdd:PRK10946 27 LTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYIT-FFALLKLG--VAPV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 83 ---------DLSIPSERI--AKIIESSGAELLihAAGLSIDAVGQQIQTVSAEeLLENEGGSVSQDQWVKEHETFYIIYT 151
Cdd:PRK10946 102 nalfshqrsELNAYASQIepALLIADRQHALF--SDDDFLNTLVAEHSSLRVV-LLLNDDGEHSLDDAINHPAEDFTATP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 152 S------------GSTGNPK-----------GVQISA--ANLQSFTDWICAdFPvsggkiflnqAPFSFDLSVMDLYPCL 206
Cdd:PRK10946 179 SpadevaffqlsgGSTGTPKliprthndyyySVRRSVeiCGFTPQTRYLCA-LP----------AAHNYPMSSPGALGVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 207 QSGGtlhCVTKDAVNKPKVLFEELKKSGLNVWTSTPSFVQMCL---MDPGFSQDL--LphadtfmfcgEVLPVSVAK--- 278
Cdd:PRK10946 248 LAGG---TVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLqaiAEGGSRAQLasL----------KLLQVGGARlse 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 279 ALLERFPK---AKIFNTYGPTEATVAVTSVEITNDVISRSESLPVgfaKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVS 355
Cdd:PRK10946 315 TLARRIPAelgCQLQQVFGMAEGLVNYTRLDDSDERIFTTQGRPM---SPDDEVWVADADGNPLPQGEVGRLMTRGPYTF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 356 RGYLGEPELTEKAF----FSHEGQWAYRTgdagfiQDGQIFCQGRLDFQIKLHGYRMELEEIEfhvrqSQYVRSAVVIPy 431
Cdd:PRK10946 392 RGYYKSPQHNASAFdangFYCSGDLVSID------PDGYITVVGREKDQINRGGEKIAAEEIE-----NLLLRHPAVIH- 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3E7X_A 432 qpngtveyliAAIV--PEEHEFEKE--FQLTS------AIKKELAASLPA-YMIPRKFIYQDHIQMTANGKIDRKRI 497
Cdd:PRK10946 460 ----------AALVsmEDELMGEKScaFLVVKeplkavQLRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
19-502 |
3.34e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 71.72 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 19 AFRSQGQSLTYQELWEQSDRAAAAIQK--------RISGEKKS----PILVYGHMEPHMIVsflgsVKAGHPYIPVDLS- 85
Cdd:PRK05677 42 AFSNLGKTLTYGELYKLSGAFAAWLQQhtdlkpgdRIAVQLPNvlqyPVAVFGAMRAGLIV-----VNTNPLYTAREMEh 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 86 -----------------------IPSERIAKIIESSGAELLIHAAGLSIDAVGQQI----------QTVSAEELLENEGG 132
Cdd:PRK05677 117 qfndsgakalvclanmahlaekvLPKTGVKHVIVTEVADMLPPLKRLLINAVVKHVkkmvpayhlpQAVKFNDALAKGAG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 133 SVSQDQWVKEHETFYIIYTSGSTGNPKGVQISAANLQSF---TDWICADFPVSGGKIFLnqAPfsfdLSVMDLYPClqsg 209
Cdd:PRK05677 197 QPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGSNLNEGCEILI--AP----LPLYHIYAF---- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 210 gTLHCVTKDAVNKPKVLF----------EELKKS------GLNVWtstpsFVQMClMDPGFSQDLLPHADTFMFCGEVLP 273
Cdd:PRK05677 267 -TFHCMAMMLIGNHNILIsnprdlpamvKELGKWkfsgfvGLNTL-----FVALC-NNEAFRKLDFSALKLTLSGGMALQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 274 VSVAKaLLERFPKAKIFNTYGPTEaTVAVTSVEITNDVISRSESLPVgfakPDMNIFIMDEEGQPLPEGEKGEIVIAGPS 353
Cdd:PRK05677 340 LATAE-RWKEVTGCAICEGYGMTE-TSPVVSVNPSQAIQVGTIGIPV----PSTLCKVIDDDGNELPLGEVGELCVKGPQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 354 VSRGYLGEPELTEKAFFShEGqWaYRTGDAGFIQ-DGQIFCQGRLDFQIKLHGYRMELEEIEfhvrqsqyvrsaVVIPYQ 432
Cdd:PRK05677 414 VMKGYWQRPEATDEILDS-DG-W-LKTGDIALIQeDGYMRIVDRKKDMILVSGFNVYPNELE------------DVLAAL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 433 PnGTVEylIAAI-VPEEHEFE--KEF-------QLT-SAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEEV 501
Cdd:PRK05677 479 P-GVLQ--CAAIgVPDEKSGEaiKVFvvvkpgeTLTkEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEE 555
|
.
3E7X_A 502 L 502
Cdd:PRK05677 556 L 556
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
5-495 |
4.52e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 71.46 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 5 HAIQTHAETyPQTD--AFR----SQGQSLTYQELWEQSDRAAAAIqKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHP 78
Cdd:PRK04319 47 EAIDRHADG-GRKDkvALRyldaSRKEKYTYKELKELSNKFANVL-KELGVEKGDRVFIFMPRIPELYFALLGALKNGAI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 79 YIPVDLSIPSERIAKIIESSGAELLIH---------AAGLS-------IDAVGQQI-QTVSAEELLEneggSVSQD---Q 138
Cdd:PRK04319 125 VGPLFEAFMEEAVRDRLEDSEAKVLITtpallerkpADDLPslkhvllVGEDVEEGpGTLDFNALME----QASDEfdiE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 139 WVKEHETFYIIYTSGSTGNPKGV----------QISAANLQSFTD----WICADfP--VSG---GkIFlnqAPFsfdlsv 199
Cdd:PRK04319 201 WTDREDGAILHYTSGSTGKPKGVlhvhnamlqhYQTGKYVLDLHEddvyWCTAD-PgwVTGtsyG-IF---APW------ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 200 mdlypclqsggtLHCVTK--DAVN-KPKVLFEELKKSGLNVWTSTPSFVQMcLMDPG---FSQDLLPHADTFMFCGEVLP 273
Cdd:PRK04319 270 ------------LNGATNviDGGRfSPERWYRILEDYKVTVWYTAPTAIRM-LMGAGddlVKKYDLSSLRHILSVGEPLN 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 274 VSVAKALLERFPKaKIFNTYGPTEaTVAVTsveITN----DVISRSESLPVgfakPDMNIFIMDEEGQPLPEGEKGEIVI 349
Cdd:PRK04319 337 PEVVRWGMKVFGL-PIHDNWWMTE-TGGIM---IANypamDIKPGSMGKPL----PGIEAAIVDDQGNELPPNRMGNLAI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 350 -AG-PSVSRGYLGEPELTEKAFfshEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSA 426
Cdd:PRK04319 408 kKGwPSMMRGIWNNPEKYESYF---AGDW-YVSGDSAYMdEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEA 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3E7X_A 427 VVIPyQPNGTVEYLIAAIVpeehEFEKEFQLTSAIKKELAA----SLPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK04319 484 GVIG-KPDPVRGEIIKAFV----ALRPGYEPSEELKEEIRGfvkkGLGAHAAPREIEFKDKLPKTRSGKIMRR 551
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
148-504 |
6.36e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 70.98 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 IIYTSGSTGNPKGVQIS--AANLQSFtdwicADFPVSGgkiflnqapfsfdLSVMDLY----PCLQSGGTLHCVTKDAVN 221
Cdd:PLN02860 177 ICFTSGTTGRPKGVTIShsALIVQSL-----AKIAIVG-------------YGEDDVYlhtaPLCHIGGLSSALAMLMVG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 222 KPKVL---------FEELKKSGLNVWTSTP-------SFVQMCLMDPGFsqdllPHADTFMFCGEVLPVSVAKALLERFP 285
Cdd:PLN02860 239 ACHVLlpkfdakaaLQAIKQHNVTSMITVPammadliSLTRKSMTWKVF-----PSVRKILNGGGSLSSRLLPDAKKLFP 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 286 KAKIFNTYGPTEATVAVT------------------SVEITNDVISRSESLPVGFAKPDMNIFIMDEEGQPLpegekGEI 347
Cdd:PLN02860 314 NAKLFSAYGMTEACSSLTfmtlhdptlespkqtlqtVNQTKSSSVHQPQGVCVGKPAPHVELKIGLDESSRV-----GRI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 348 VIAGPSVSRGYLGEPelTEKAFFSHEGQWaYRTGDAGFIQD-GQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSA 426
Cdd:PLN02860 389 LTRGPHVMLGYWGQN--SETASVLSNDGW-LDTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASV 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 427 VVIPYQPNGTVEYLIAAI--------VPEEHE-FEKEFQLTSAIKKELAA--SLPAYMIPRKFI-YQDHIQMTANGKIDR 494
Cdd:PLN02860 466 VVVGVPDSRLTEMVVACVrlrdgwiwSDNEKEnAKKNLTLSSETLRHHCRekNLSRFKIPKLFVqWRKPFPLTTTGKIRR 545
|
410
....*....|
3E7X_A 495 KRIGEEVLVR 504
Cdd:PLN02860 546 DEVRREVLSH 555
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
140-495 |
7.13e-13 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 71.03 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 140 VKEHETFYIIYTSGSTGNPKGVQISAANL----QSFTDWICADFPVSGGK-IFLNQAP----FSFDLSVMDLypcLQSGG 210
Cdd:PLN02574 195 IKQDDVAAIMYSSGTTGASKGVVLTHRNLiamvELFVRFEASQYEYPGSDnVYLAALPmfhiYGLSLFVVGL---LSLGS 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 211 TLHCVTK----DAVNK------------PKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLphaDTFmfcgevlpv 274
Cdd:PLN02574 272 TIVVMRRfdasDMVKVidrfkvthfpvvPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFI---QDF--------- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 275 svakalLERFPKAKIFNTYGPTEATvAVTSVEITNDVISRSESlpVGFAKPDMNIFIMD-EEGQPLPEGEKGEIVIAGPS 353
Cdd:PLN02574 340 ------VQTLPHVDFIQGYGMTEST-AVGTRGFNTEKLSKYSS--VGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPG 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 354 VSRGYLGEPELTEKAFFshEGQWaYRTGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQ 432
Cdd:PLN02574 411 VMKGYLNNPKATQSTID--KDGW-LRTGDiAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVP 487
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
3E7X_A 433 PNGTVEYLIAAIVPEEHEFEKEFQLTSAIKKELAaslpAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PLN02574 488 DKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVA----PYKKVRKVVFVQSIPKSPAGKILRR 546
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
124-499 |
1.18e-12 |
|
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: 70.14 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 124 EELLENEGGSVSqdqwvkehetfYIIYTSGSTGNPKGVQISAANLQSF-TDWICADfPVSGGKIFLNQAPFSFDLS-VMD 201
Cdd:cd17641 150 REVAAGKGEDVA-----------VLCTTSGTTGKPKLAMLSHGNFLGHcAAYLAAD-PLGPGDEYVSVLPLPWIGEqMYS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 202 LYPCLQSGGTLHCVtkdavNKPKVLFEELKKSGLN-------VWTSTPSFVQMCLMDPG-FSQDLLPHA----------- 262
Cdd:cd17641 218 VGQALVCGFIVNFP-----EEPETMMEDLREIGPTfvllpprVWEGIAADVRARMMDATpFKRFMFELGmklglraldrg 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 263 --DTFMFCGEVLPVSVAKALLER-------FPKAKIFNT-----------------------YGPTEATVAVTsVEITND 310
Cdd:cd17641 293 krGRPVSLWLRLASWLADALLFRplrdrlgFSRLRSAATggaalgpdtfrffhaigvplkqlYGQTELAGAYT-VHRDGD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 311 VisRSESlpVGFAKPDMNIFImdeegqplpeGEKGEIVIAGPSVSRGYLGEPELTEKAFFshEGQWaYRTGDAGFI-QDG 389
Cdd:cd17641 372 V--DPDT--VGVPFPGTEVRI----------DEVGEILVRSPGVFVGYYKNPEATAEDFD--EDGW-LHTGDAGYFkENG 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 390 QIFCQGRL-DFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIpyqpNGTVEYLIA------AIVPEEHE-----FEKEFQL 457
Cdd:cd17641 435 HLVVIDRAkDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVL----GAGRPYLTAficidyAIVGKWAEqrgiaFTTYTDL 510
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
3E7X_A 458 TS------AIKKELA---ASLPAYMIPRKFI--YQ----DHIQMTANGKIDRKRIGE 499
Cdd:cd17641 511 ASrpevyeLIRKEVEkvnASLPEAQRIRRFLllYKeldaDDGELTRTRKVRRGVIAE 567
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
275-495 |
1.95e-12 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 69.28 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 275 SVAKALLERFPK---AKIFNTYGPTEATVAVTSVEITNDVISRSESLPVgfakPDMNIFIMDEEGQPLPEGEKGEIVIAG 351
Cdd:PRK07059 338 AVQRPVAERWLEmtgCPITEGYGLSETSPVATCNPVDATEFSGTIGLPL----PSTEVSIRDDDGNDLPLGEPGEICIRG 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 352 PSVSRGYLGEPELTEKA-----FFshegqwayRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEfhvrqsqyvrs 425
Cdd:PRK07059 414 PQVMAGYWNRPDETAKVmtadgFF--------RTGDVGVMdERGYTKIVDRKKDMILVSGFNVYPNEIE----------- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 426 aVVIPYQPnGTVEylIAAI-VPEEHEFE--------KEFQLTSA-IKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK07059 475 -EVVASHP-GVLE--VAAVgVPDEHSGEavklfvvkKDPALTEEdVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRR 550
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
27-493 |
2.51e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 69.14 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 27 LTYQELWEQSDRAAAAIQKRisGEKK-SPILVYGHMEPHMIVSFLGSVKAGhpYIPVDLS---IPSErIAKIIESSGAEL 102
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQ--GLGPgDHVGIYARNRIEYVEAMLGAFKAR--AVPVNVNyryVEDE-LRYLLDDSDAVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 103 LIHAAGLSiDAVGQ------------QIQTVSAEELLeneGGSVSQDQWVKEHET-----------FYIIYTSGSTGNPK 159
Cdd:PRK07798 104 LVYEREFA-PRVAEvlprlpklrtlvVVEDGSGNDLL---PGAVDYEDALAAGSPerdfgerspddLYLLYTGGTTGMPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 160 GV-----QISAANLQSfTDWICADFPVS-----------GGKIFLNQAPFSFDLSVMDLYPCLQSGGT--LHCVTK---- 217
Cdd:PRK07798 180 GVmwrqeDIFRVLLGG-RDFATGEPIEDeeelakraaagPGMRRFPAPPLMHGAGQWAAFAALFSGQTvvLLPDVRfdad 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 218 ------------------DAVNKPkvLFEELKK------SGLNVWTSTpsfvqmclmdpgfsqdllphadtfmfcGEVLP 273
Cdd:PRK07798 259 evwrtierekvnvitivgDAMARP--LLDALEArgpydlSSLFAIASG---------------------------GALFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 274 VSVAKALLERFPKAKIFNTYGPTEATVAVTSVeitndviSRSESLPVGFAK--PDMNIFIMDEEGQPLPEGEKGEIVIA- 350
Cdd:PRK07798 310 PSVKEALLELLPNVVLTDSIGSSETGFGGSGT-------VAKGAVHTGGPRftIGPRTVVLDEDGNPVEPGSGEIGWIAr 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 351 GPSVSRGYLGEPELTEKAFFSHEGQ-WAYrTGDAGFIQ-DGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVV 428
Cdd:PRK07798 383 RGHIPLGYYKDPEKTAETFPTIDGVrYAI-PGDRARVEaDGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALV 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3E7X_A 429 IPyQPNGTVEYLIAAIV-------PEEHEfekefqltsaIKKELAASLPAYMIPRKFIYQDHIQMTANGKID 493
Cdd:PRK07798 462 VG-VPDERWGQEVVAVVqlregarPDLAE----------LRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
147-494 |
3.84e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 68.91 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 147 YIIYTSGSTGNPKGVQISAANLQSFTDWIC--------ADFPVSGGKIFlnqapFSFDLSVMDLYPcLQSGGTLHC---- 214
Cdd:PRK06060 149 YATYTSGTTGPPKAAIHRHADPLTFVDAMCrkalrltpEDTGLCSARMY-----FAYGLGNSVWFP-LATGGSAVInsap 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 215 VTKDAVNKPKVLFEElkksglNVWTSTPSF----VQMClmdpgfSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIF 290
Cdd:PRK06060 223 VTPEAAAILSARFGP------SVLYGVPNFfarvIDSC------SPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPIL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 291 NTYGPTEatvaVTSVEITNDVIS-RSESLpvGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPEltekAF 369
Cdd:PRK06060 291 DGIGSTE----VGQTFVSNRVDEwRLGTL--GRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD----SP 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 370 FSHEGqWAYRTGDAGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEH 449
Cdd:PRK06060 361 VANEG-WLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSG 439
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
3E7X_A 450 EFEKEfQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDR 494
Cdd:PRK06060 440 ATIDG-SVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVR 483
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
24-495 |
9.92e-12 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 67.31 E-value: 9.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 24 GQSLTYQELWEQSDRAAAAIQKrISGEKKSPILVYGHMEPHMIVSFLGSVKAG------HPyipvdLSIPSErIAKIIES 97
Cdd:PLN02246 48 GRVYTYADVELLSRRVAAGLHK-LGIRQGDVVMLLLPNCPEFVLAFLGASRRGavtttaNP-----FYTPAE-IAKQAKA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 98 SGAELLI-------------HAAGLSIDAVGQQIQ-TVSAEELLENEGGSVSQdqwVKEH--ETFYIIYTSGSTGNPKGV 161
Cdd:PLN02246 121 SGAKLIItqscyvdklkglaEDDGVTVVTIDDPPEgCLHFSELTQADENELPE---VEISpdDVVALPYSSGTTGLPKGV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 162 QISAANL-QSFTDWICADFP---VSGGKIFLNQAP----FSFDlSVMdlyPC-LQSGGTLHCVTKDAVNKpkvLFEELKK 232
Cdd:PLN02246 198 MLTHKGLvTSVAQQVDGENPnlyFHSDDVILCVLPmfhiYSLN-SVL---LCgLRVGAAILIMPKFEIGA---LLELIQR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 233 SGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEAtvavtsveitNDVI 312
Cdd:PLN02246 271 HKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEA----------GPVL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 313 SRSeslpVGFAK----------------PDMNIfIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAfFSHEGqW 376
Cdd:PLN02246 341 AMC----LAFAKepfpvksgscgtvvrnAELKI-VDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANT-IDKDG-W 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 377 AYrTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEhefekEF 455
Cdd:PLN02246 414 LH-TGDIGYIdDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSN-----GS 487
|
490 500 510 520
....*....|....*....|....*....|....*....|.
3E7X_A 456 QLTS-AIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PLN02246 488 EITEdEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRK 528
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
9-492 |
1.45e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 9 THAETYPQTDAF--RSQGQSLTYQELWEQSdrAAAAIQKRISGEKKSPILVY-GHMEPHMIVSFLGSVKAGHPYIPVDLS 85
Cdd:PRK13390 5 THAQIAPDRPAVivAETGEQVSYRQLDDDS--AALARVLYDAGLRTGDVVALlSDNSPEALVVLWAALRSGLYITAINHH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 86 IPSERIAKIIESSGAELLIHAAGLS-------------------IDAVGQQIQTVSAE--ELLENEGGSVsqdqwvkehe 144
Cdd:PRK13390 83 LTAPEADYIVGDSGARVLVASAALDglaakvgadlplrlsfggeIDGFGSFEAALAGAgpRLTEQPCGAV---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 145 tfyIIYTSGSTGNPKGVQ--ISAANLQSFTDWICAdfpVSGGkiflnqapfSFDLSVMDLY----PCLQSGGTLHCVTKD 218
Cdd:PRK13390 153 ---MLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVA---IARA---------FYDISESDIYyssaPIYHAAPLRWCSMVH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 219 AVNKPKVL---------FEELKKSGLNVWTSTPS-FVQMCLMDPGF-SQDLLPHADTFMFCGEVLPVSVAKALLERFPKA 287
Cdd:PRK13390 218 ALGGTVVLakrfdaqatLGHVERYRITVTQMVPTmFVRLLKLDADVrTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 288 kIFNTYGPTEATvAVTSVEiTNDVISRSESlpVGFAKPDmNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEK 367
Cdd:PRK13390 298 -VYEYYSSTEAH-GMTFID-SPDWLAHPGS--VGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 368 AFFSHEGQWAyRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVI--PYQPNG----TVEYL 440
Cdd:PRK13390 372 AQHPAHPFWT-TVGDLGSVdEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIgvPDPEMGeqvkAVIQL 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
3E7X_A 441 IAAIVPEEhEFEKEfqLTSAIKKELAaslpAYMIPRKFIYQDHIQMTANGKI 492
Cdd:PRK13390 451 VEGIRGSD-ELARE--LIDYTRSRIA----HYKAPRSVEFVDELPRTPTGKL 495
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
11-492 |
1.63e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 66.37 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDA--FRSQGQSLTYQELWEQSDRAAAA-----IQKrisGEKkspILVYGHMEPHMIVSFLGSVKAGHPYIPVD 83
Cdd:PRK08315 26 AARYPDREAlvYRDQGLRWTYREFNEEVDALAKGllalgIEK---GDR---VGIWAPNVPEWVLTQFATAKIGAILVTIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 84 lsiPSERIAK---IIESSGAELLIHAAGLS-------IDAVGQQIQTVSAEEL--------------------------- 126
Cdd:PRK08315 100 ---PAYRLSEleyALNQSGCKALIAADGFKdsdyvamLYELAPELATCEPGQLqsarlpelrrviflgdekhpgmlnfde 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 127 LENEGGSVSQDQW------VKEHETFYIIYTSGSTGNPKGVQISAANL----------QSFT--DWICadFPVsggkifl 188
Cdd:PRK08315 177 LLALGRAVDDAELaarqatLDPDDPINIQYTSGTTGFPKGATLTHRNIlnngyfigeaMKLTeeDRLC--IPV------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 189 nqaPFsfdlsvmdlYPCLqsG---GTLHCVTK--------DAVNKPKVL--FEELKKSGL-NVWTStpsFVQMcLMDPGF 254
Cdd:PRK08315 248 ---PL---------YHCF--GmvlGNLACVTHgatmvypgEGFDPLATLaaVEEERCTALyGVPTM---FIAE-LDHPDF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 255 SQDLLPHADTFMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVISRSESlpVGFAKPDMNIFIMDE 334
Cdd:PRK08315 310 ARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTETSPVSTQTRTDDPLEKRVTT--VGRALPHLEVKIVDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 335 E-GQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAfFSHEGqWaYRTGDAGfIQDGQIFCQ--GRL-DFQIKlhG----Y 406
Cdd:PRK08315 388 EtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDADG-W-MHTGDLA-VMDEEGYVNivGRIkDMIIR--GgeniY 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 407 RMELEEIEFHVRQSQYVrsAVV-IPYQPNGtvEYLIAAIVPEEHEfekefQLT-SAIKKELAASLPAYMIPRKFIYQDHI 484
Cdd:PRK08315 462 PREIEEFLYTHPKIQDV--QVVgVPDEKYG--EEVCAWIILRPGA-----TLTeEDVRDFCRGKIAHYKIPRYIRFVDEF 532
|
....*...
3E7X_A 485 QMTANGKI 492
Cdd:PRK08315 533 PMTVTGKI 540
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
275-504 |
2.13e-11 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 66.23 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 275 SVAKALLERFPKA---KIFNTYGPTEATVAVTSVEITNDVISRSESLPVgfakPDMNIFIMDEEGQPLPEGEKGEIVIAG 351
Cdd:PRK08974 336 AVQQAVAERWVKLtgqYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPV----PSTEIKLVDDDGNEVPPGEPGELWVKG 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 352 PSVSRGYLGEPELTEKAFfsHEGQWAyrTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIP 430
Cdd:PRK08974 412 PQVMLGYWQRPEATDEVI--KDGWLA--TGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVG 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3E7X_A 431 yQPNGTVEYLIAAIVpeeheFEKEFQLT-SAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEEVLVR 504
Cdd:PRK08974 488 -VPSEVSGEAVKIFV-----VKKDPSLTeEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
28-391 |
2.79e-11 |
|
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: 65.92 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 28 TYQELWEQSDRAAAAIQKR-ISGEKKSPILVYGHMEpHMIVSFlGSVKAGHPYIPVD-----LSIPSERIAKIIE----- 96
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLgLSAERPLLILSGNSIE-HALMAL-AAMYAGVPAAPVSpayslMSQDLAKLKHLFEllkpg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 97 ------------SSGAELLIHAAGLSIDAVGQQIQTVSAEELLENEGG--------SVSQDQWVKehetfyIIYTSGSTG 156
Cdd:cd05921 105 lvfaqdaapfarALAAIFPLGTPLVVSRNAVAGRGAISFAELAATPPTaavdaafaAVGPDTVAK------FLFTSGSTG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 157 NPKGVQISAANLQSFTDWICADFPVSGGKI--FLNQAPFSFDLSV-MDLYPCLQSGGTLHCvtkDAvNKPKV-LFEE--- 229
Cdd:cd05921 179 LPKAVINTQRMLCANQAMLEQTYPFFGEEPpvLVDWLPWNHTFGGnHNFNLVLYNGGTLYI---DD-GKPMPgGFEEtlr 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 230 -LKKSGLNVWTSTP----SFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALL--------ERFPkakIFNTYGPT 296
Cdd:cd05921 255 nLREISPTVYFNVPagweMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQalavatvgERIP---MMAGLGAT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 297 EatvavTSVEITNDVISRSESLPVGFAKPDMnifimdeEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAfFSHEGqw 376
Cdd:cd05921 332 E-----TAPTATFTHWPTERSGLIGLPAPGT-------ELKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQA-FDEEG-- 396
|
410 420
....*....|....*....|....*.
3E7X_A 377 AYRTGDA-----------GFIQDGQI 391
Cdd:cd05921 397 FYCLGDAakladpddpakGLVFDGRV 422
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
16-401 |
2.82e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 65.84 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 16 QTDAFRSQGQSLTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEPHMIVSfLGSVKAGHPYIPVD--LSIPSERIAK 93
Cdd:PRK12582 70 QREPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMT-LAAMQAGVPAAPVSpaYSLMSHDHAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 94 ------------IIESSGA--ELLIHAAGL------SIDAVGQQIQTVSAEELLENE-GGSVSQDQWVKEHETF-YIIYT 151
Cdd:PRK12582 149 lkhlfdlvkprvVFAQSGApfARALAALDLldvtvvHVTGPGEGIASIAFADLAATPpTAAVAAAIAAITPDTVaKYLFT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 152 SGSTGNPKGV----QISAANL----QSFTDWICADFPV----------SGGKIFLNqapfsfdlsvmdlyPCLQSGGTLH 213
Cdd:PRK12582 229 SGSTGMPKAVintqRMMCANIamqeQLRPREPDPPPPVsldwmpwnhtMGGNANFN--------------GLLWGGGTLY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 214 CvtkDAvNKP-KVLFEE----LKKSGLNVWTSTPSFVQMCL----MDPGFSQDLLPHADTFMFCGEVLPVSV-------- 276
Cdd:PRK12582 295 I---DD-GKPlPGMFEEtirnLREISPTVYGNVPAGYAMLAeameKDDALRRSFFKNLRLMAYGGATLSDDLyermqala 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 277 AKALLERFPkakIFNTYGPTEATVAVTSVEItndvISRSESLpVGFAKPDMnifimdeEGQPLPEGEKGEIVIAGPSVSR 356
Cdd:PRK12582 371 VRTTGHRIP---FYTGYGATETAPTTTGTHW----DTERVGL-IGLPLPGV-------ELKLAPVGDKYEVRVKGPNVTP 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
3E7X_A 357 GYLGEPELTEKAfFSHEGqwAYRTGDAG-FIQD-----GQIFcQGRL--DFQI 401
Cdd:PRK12582 436 GYHKDPELTAAA-FDEEG--FYRLGDAArFVDPddpekGLIF-DGRVaeDFKL 484
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
142-497 |
3.71e-11 |
|
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: 65.09 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 142 EHETFYIIYTSGSTGNPKGVQ--ISAANLQSFTDWICAD-FPVSGGKIFLN------QAPFSFDLSVmdlypcLQSGGTL 212
Cdd:cd05929 124 EAAGWKMLYSGGTTGRPKGIKrgLPGGPPDNDTLMAAALgFGPGADSVYLSpaplyhAAPFRWSMTA------LFMGGTL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 213 HCVTK-------DAVNKPKVLFEELkksglnvwtsTPS-FVQMcLMDPGFSQDL--LPHADTFMFCGEVLPVSVAKALLE 282
Cdd:cd05929 198 VLMEKfdpeeflRLIERYRVTFAQF----------VPTmFVRL-LKLPEAVRNAydLSSLKRVIHAAAPCPPWVKEQWID 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 283 RFPKaKIFNTYGPTEAtVAVTsveitndVISRSESL--PVGFAKPDM-NIFIMDEEGQPLPEGEKGEIVIAGPSvSRGYL 359
Cdd:cd05929 267 WGGP-IIWEYYGGTEG-QGLT-------IINGEEWLthPGSVGRAVLgKVHILDEDGNEVPPGEIGEVYFANGP-GFEYT 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 360 GEPELTEKAffSHEGQWAyRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVV--IPYQPNGt 436
Cdd:cd05929 337 NDPEKTAAA--RNEGGWS-TLGDVGYLdEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVvgVPDEELG- 412
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
3E7X_A 437 vEYLIAAIVPEEHEFEKEfQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRI 497
Cdd:cd05929 413 -QRVHAVVQPAPGADAGT-ALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
26-461 |
3.96e-11 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 65.45 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 26 SLTYQELWEQSDRAAAAIQKRISGEKKSPI-LVYGHMEpHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLI 104
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQKKVGLKPGDRVaLMYPDPL-DFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 105 HAAGLSIDAVGQQIQTVSAEELLENEGGSVSQDqWVKEHE-------------------TFYIIYTSGSTGNPKGVQISA 165
Cdd:cd05905 93 TVEACLKGLPKKLLKSKTAAEIAKKKGWPKILD-FVKIPKskrsklkkwgphpptrdgdTAYIEYSFSSDGSLSGVAVSH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 166 ANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMdlYPCLQSGGTLHCVT----KDAVNKPKVLFEELKKSGLNVWTST 241
Cdd:cd05905 172 SSLLAHCRALKEACELYESRPLVTVLDFKSGLGLW--HGCLLSVYSGHHTIlippELMKTNPLLWLQTLSQYKVRDAYVK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 242 PSFVQMCLMDPGFSQDLLPHAD-------TFMF-CGEVLPVSVAKALLERF----PKAKIFNT--------------YGP 295
Cdd:cd05905 250 LRTLHWCLKDLSSTLASLKNRDvnlsslrMCMVpCENRPRISSCDSFLKLFqtlgLSPRAVSTefgtrvnpficwqgTSG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 296 TE-ATVAVTSVEITNDVI-------SRSESL-PVGFAKPDMNIFIMDEEGQPL-PEGEKGEIVIAGPSVSRGYL---GEP 362
Cdd:cd05905 330 PEpSRVYLDMRALRHGVVrlderdkPNSLPLqDSGKVLPGAQVAIVNPETKGLcKDGEIGEIWVNSPANASGYFlldGET 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 363 ELTEKAFFSHEGQ-------WAyRTGDAGFIQDGQIFCQG--RLDFQIKLhGYRMELEEIEFHVRQSQYVRSAV--VIPY 431
Cdd:cd05905 410 NDTFKVFPSTRLStgitnnsYA-RTGLLGFLRPTKCTDLNveEHDLLFVV-GSIDETLEVRGLRHHPSDIEATVmrVHPY 487
|
490 500 510
....*....|....*....|....*....|....*
3E7X_A 432 QPNGTV----EYL-IAAIVPEEHEfEKEFQLTSAI 461
Cdd:cd05905 488 RGRCAVfsitGLVvVVAEQPPGSE-EEALDLVPLV 521
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
66-495 |
5.94e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 64.75 E-value: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 66 IVSFLGSVKAGHpyIPVDLSIPSE-----RIAKIIESSGAELLIHAAGlSIDAVGQQIQTVSAEE--------LLENEGG 132
Cdd:PRK07769 93 LIAFFGALYAGR--IAVPLFDPAEpghvgRLHAVLDDCTPSAILTTTD-SAEGVRKFFRARPAKErprviavdAVPDEVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 133 SVSQDQWVKEHETFYIIYTSGSTGNPKGVQIS----AANLQSFTDWICADFPVSGgkifLNQAPFSFDLS-VMDLYPCLq 207
Cdd:PRK07769 170 ATWVPPEANEDTIAYLQYTSGSTRIPAGVQIThlnlPTNVLQVIDALEGQEGDRG----VSWLPFFHDMGlITVLLPAL- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 208 SGGTLHCVTKDA-VNKPKVLFEELKKSG---LNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEV---LPVSVAKal 280
Cdd:PRK07769 245 LGHYITFMSPAAfVRRPGRWIRELARKPggtGGTFSAAPNFAFEHAAARGLPKDGEPPLDLSNVKGLLngsEPVSPAS-- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 281 LERF---------PKAKIFNTYGPTEATVAVTSVEITND--VIS--RSESLPVGFAKPDMN------------------I 329
Cdd:PRK07769 323 MRKFneafapyglPPTAIKPSYGMAEATLFVSTTPMDEEptVIYvdRDELNAGRFVEVPADapnavaqvsagkvgvsewA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 330 FIMD-EEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFF---------SH-EG-----QWaYRTGDAGFIQDGQIFC 393
Cdd:PRK07769 403 VIVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQnilksrlseSHaEGapddaLW-VRTGDYGVYFDGELYI 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 394 QGRLDFQIKLHGYRMELEEIEFHVRQ-SQYVRSAVV---------------------IPYQPNGTVEYLIaaIVPEE--- 448
Cdd:PRK07769 482 TGRVKDLVIIDGRNHYPQDLEYTAQEaTKALRTGYVaafsvpanqlpqvvfddshagLKFDPEDTSEQLV--IVAERapg 559
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
3E7X_A 449 -HEFEKEfQLTSAIKKELAAS----------LPAYMIPRkfiyqdhiqmTANGKIDRK 495
Cdd:PRK07769 560 aHKLDPQ-PIADDIRAAIAVRhgvtvrdvllVPAGSIPR----------TSSGKIARR 606
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
139-497 |
6.47e-11 |
|
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: 64.64 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 139 WVKEHETFYIIYTSGSTGNPKGVQ--------ISAANLQSFTD------WICA-DFPVSGGKIFLNQAPFsfdlsvmdly 203
Cdd:cd05967 226 PVAATDPLYILYTSGTTGKPKGVVrdngghavALNWSMRNIYGikpgdvWWAAsDVGWVVGHSYIVYGPL---------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 204 pclqsggtLHCVTK-------DAVNKPKVLFEELKKSGLNVWTSTPSFVQMCLMDPgfsqdllPHAD-----------TF 265
Cdd:cd05967 296 --------LHGATTvlyegkpVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKED-------PDGKyikkydlsslrTL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 266 MFCGEVLPVSVAKALLERFPKAkIFNTYGPTEATVAVTsveiTNDVISRSESLPVGFA-KPDM--NIFIMDEEGQPLPEG 342
Cdd:cd05967 361 FLAGERLDPPTLEWAENTLGVP-VIDHWWQTETGWPIT----ANPVGLEPLPIKAGSPgKPVPgyQVQVLDEDGEPVGPN 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 343 EKGEIVIAGPsVSRGYL----GEPELTEKAFFSHEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHV 417
Cdd:cd05967 436 ELGNIVIKLP-LPPGCLltlwKNDERFKKLYLSKFPGY-YDTGDAGYKdEDGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 418 RQSQYVRSAVVIpyqpnGTVEYL-----IAAIVPEEHEFEKEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKI 492
Cdd:cd05967 514 LSHPAVAECAVV-----GVRDELkgqvpLGLVVLKEGVKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKI 588
|
....*
3E7X_A 493 DRKRI 497
Cdd:cd05967 589 LRRTL 593
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
148-403 |
9.65e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 64.13 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 IIYTSGSTGNPKGVQIS----AANLQSFTDwiCADFPVSGGKIFLNQAPFS------FDLSVMdlypcLQSGGTLHCvtk 217
Cdd:PRK08180 214 FLFTSGSTGLPKAVINThrmlCANQQMLAQ--TFPFLAEEPPVLVDWLPWNhtfggnHNLGIV-----LYNGGTLYI--- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 218 DAvNKPKV-LFEE----LKKSGLNVWTSTPSFVQMCL----MDPGFSQDLLPHADTFMFCGEVLPVSVAKALlERFPKAK 288
Cdd:PRK08180 284 DD-GKPTPgGFDEtlrnLREISPTVYFNVPKGWEMLVpaleRDAALRRRFFSRLKLLFYAGAALSQDVWDRL-DRVAEAT 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 289 I-----FNT-YGPTEATVAVTSVEITND---VISrsesLPVgfakPDMNIFImdeegqpLPEGEKGEIVIAGPSVSRGYL 359
Cdd:PRK08180 362 CgerirMMTgLGMTETAPSATFTTGPLSragNIG----LPA----PGCEVKL-------VPVGGKLEVRVKGPNVTPGYW 426
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
3E7X_A 360 GEPELTEKAfFSHEGqwAYRTGDAGFIQD------GQIFcQGRL--DFqiKL 403
Cdd:PRK08180 427 RAPELTAEA-FDEEG--YYRSGDAVRFVDpadperGLMF-DGRIaeDF--KL 472
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
27-428 |
1.39e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 63.61 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 27 LTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEphMIVSFLGSVKAGHpyIPVDLSIP-----SERIAKIIESSGAE 101
Cdd:PRK12476 69 LTWTQLGVRLRAVGARLQQVAGPGDRVAILAPQGID--YVAGFFAAIKAGT--IAVPLFAPelpghAERLDTALRDAEPT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 102 LLIHAAGLSiDAVGQQIQTVSA---------EELLENEGGSVSQDQwVKEHETFYIIYTSGSTGNPKGVQIS----AANL 168
Cdd:PRK12476 145 VVLTTTAAA-EAVEGFLRNLPRlrrprviaiDAIPDSAGESFVPVE-LDTDDVSHLQYTSGSTRPPVGVEIThravGTNL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 169 QSFTdwicadfpVSGGKIFLNQ-----APFSFDLSV-MDLYPCLqSGGTLHCVTKDA-VNKPKVLFEELKKSGL--NVWT 239
Cdd:PRK12476 223 VQMI--------LSIDLLDRNThgvswLPLYHDMGLsMIGFPAV-YGGHSTLMSPTAfVRRPQRWIKALSEGSRtgRVVT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 240 STPSFV-----QMCLMDPGFSQDLlphADTFMFCGEVlPVSVAKalLERF---------PKAKIFNTYGPTEATVAVTS- 304
Cdd:PRK12476 294 AAPNFAyewaaQRGLPAEGDDIDL---SNVVLIIGSE-PVSIDA--VTTFnkafapyglPRTAFKPSYGIAEATLFVATi 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 305 --------VEITNDVISRSESLPVGFAKPDMNI-------------FIMDEE-GQPLPEGEKGEIVIAGPSVSRGYLGEP 362
Cdd:PRK12476 368 apdaepsvVYLDREQLGAGRAVRVAADAPNAVAhvscgqvarsqwaVIVDPDtGAELPDGEVGEIWLHGDNIGRGYWGRP 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 363 ELTEKAFF----------SH------EGQWaYRTGDAGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQ-SQYVRS 425
Cdd:PRK12476 448 EETERTFGaklqsrlaegSHadgaadDGTW-LRTGDLGVYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMVRR 526
|
...
3E7X_A 426 AVV 428
Cdd:PRK12476 527 GYV 529
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
136-494 |
1.85e-10 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 63.32 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 136 QDQWvkehETFYIIYTSGSTGNPKGVQIS--AANLQSFTDWICADFPVsgGKIFLNQAP--------FSFDLSVMdlypC 205
Cdd:PLN02479 192 ADEW----QSIALGYTSGTTASPKGVVLHhrGAYLMALSNALIWGMNE--GAVYLWTLPmfhcngwcFTWTLAAL----C 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 206 lqsgGTLHC---VTKDAVnkpkvlFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDL-LPHADTFMFCGEVLPVSVAKALL 281
Cdd:PLN02479 262 ----GTNIClrqVTAKAI------YSAIANYGVTHFCAAPVVLNTIVNAPKSETILpLPRVVHVMTAGAAPPPSVLFAMS 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 282 ERfpKAKIFNTYGPTE----ATVAVTSVEItndvisrsESLP---------------VGFAKPDMnifIMDEEGQPLPEG 342
Cdd:PLN02479 332 EK--GFRVTHTYGLSEtygpSTVCAWKPEW--------DSLPpeeqarlnarqgvryIGLEGLDV---VDTKTMKPVPAD 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 343 EK--GEIVIAGPSVSRGYLGEPELTEKAFfshEGQWaYRTGDAGFIQ-DGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQ 419
Cdd:PLN02479 399 GKtmGEIVMRGNMVMKGYLKNPKANEEAF---ANGW-FHSGDLGVKHpDGYIEIKDRSKDIIISGGENISSLEVENVVYT 474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3E7X_A 420 SQYVRSAVVIPYQPNGTVEYLIAAIVP-EEHEFEKEFQLTSAIKKELAASLPAYMIPRKFIYQDhIQMTANGKIDR 494
Cdd:PLN02479 475 HPAVLEASVVARPDERWGESPCAFVTLkPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQK 549
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
22-497 |
2.67e-10 |
|
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: 62.65 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 22 SQGQSLTYQELWEQSDRAAAAIQKRisGEKK-SPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGA 100
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSL--GVKKgDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 101 ELLIHA-----AGLSI-------DAVGQQIQTVSA----------------------EELLENEGGSVSQDQWVKEHETF 146
Cdd:TIGR02188 162 KLVITAdeglrGGKVIplkaivdEALEKCPVSVEHvlvvrrtgnpvvpwvegrdvwwHDLMAKASAYCEPEPMDSEDPLF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 147 yIIYTSGSTGNPKGVQISaanlqsftdwicadfpvSGGkiFLNQAPFS----FDLSVMDLYPC----------------- 205
Cdd:TIGR02188 242 -ILYTSGSTGKPKGVLHT-----------------TGG--YLLYAAMTmkyvFDIKDGDIFWCtadvgwitghsyivygp 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 206 LQSGGTlhCVTKDAV-NKPKV--LFEELKKSGLNVWTSTPSFVQMcLMDPG---------FSQDLL--------PHAdtF 265
Cdd:TIGR02188 302 LANGAT--TVMFEGVpTYPDPgrFWEIIEKHKVTIFYTAPTAIRA-LMRLGdewvkkhdlSSLRLLgsvgepinPEA--W 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 266 MFCGEVlpvsVAKallERFPkakIFNTYGPTEATVAVTSveitndvisrseSLPVGF-AKPDMNIF--------IMDEEG 336
Cdd:TIGR02188 377 MWYYKV----VGK---ERCP---IVDTWWQTETGGIMIT------------PLPGATpTKPGSATLpffgiepaVVDEEG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 337 QPLP-EGEKGEIVIAG--PSVSRGYLGEPELTEKAFFSH-EGQwaYRTGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELE 411
Cdd:TIGR02188 435 NPVEgPGEGGYLVIKQpwPGMLRTIYGDHERFVDTYFSPfPGY--YFTGDgARRDKDGYIWITGRVDDVINVSGHRLGTA 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 412 EIEFH-VRQSQYVRSAVV-IPYQPNGTVeylIAAIVPEEHEFEKEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTAN 489
Cdd:TIGR02188 513 EIESAlVSHPAVAEAAVVgIPDDIKGQA---IYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRS 589
|
....*...
3E7X_A 490 GKIDRkRI 497
Cdd:TIGR02188 590 GKIMR-RL 596
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
265-396 |
3.13e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 62.67 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 265 FMFCGEV-LPVSVAKALLERfPKAKIFNTYGPTEATVAVTSVEITNDVISRSESLPVGFAkpDMNIFIMDEEG---QPLP 340
Cdd:PRK07529 337 YALCGAApLPVEVFRRFEAA-TGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQ--RVRVVILDDAGrylRDCA 413
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
3E7X_A 341 EGEKGEIVIAGPSVSRGYLgEPELTEKAFFshEGQWaYRTGDAGFI-QDGQIFCQGR 396
Cdd:PRK07529 414 VDEVGVLCIAGPNVFSGYL-EAAHNKGLWL--EDGW-LNTGDLGRIdADGYFWLTGR 466
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
140-497 |
8.97e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 61.30 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 140 VKEHETFYIIYTSGSTGNPKGVQIS-AANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLhCVTKD 218
Cdd:PTZ00237 251 VESSHPLYILYTSGTTGNSKAVVRSnGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTF-VMFEG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 219 AVNKPKV----LFEELKKSGLNVWTSTPSFVQMCL-MDPG----FSQDLLPHADTFMFCGEVLPVSVAKALLERFpKAKI 289
Cdd:PTZ00237 330 GIIKNKHieddLWNTIEKHKVTHTLTLPKTIRYLIkTDPEatiiRSKYDLSNLKEIWCGGEVIEESIPEYIENKL-KIKS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 290 FNTYGPTEATVAVTSVEITNDVISRSESLPVGFAKPDmnifIMDEEGQPLPEGEKGEIVIA---GPSVSRGYLGEPELTE 366
Cdd:PTZ00237 409 SRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPS----ILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFK 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 367 KAFFSHEGQwaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIV 445
Cdd:PTZ00237 485 QLFSKFPGY--YNSGDLGFKdENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLV 562
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
3E7X_A 446 ---PEEHEFEKEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRI 497
Cdd:PTZ00237 563 lkqDQSNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
331-497 |
9.15e-10 |
|
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: 61.04 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 331 IMDEEGQPLPEGEKGEIVI--AGPSVSRGYLGEPELTEKAFFSHEgQWAYRTGD-AGFIQDGQIFCQGRLDFQIKLHGYR 407
Cdd:cd05966 423 ILDEEGNEVEGEVEGYLVIkrPWPGMARTIYGDHERYEDTYFSKF-PGYYFTGDgARRDEDGYYWITGRVDDVINVSGHR 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 408 MELEEIEFHVRQSQYV-RSAVV-IPYQPNGTVeylIAAIVPEEHEFEKEFQLTSAIKKELAASLPAYMIPRKFIYQDHIQ 485
Cdd:cd05966 502 LGTAEVESALVAHPAVaEAAVVgRPHDIKGEA---IYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLP 578
|
170
....*....|..
3E7X_A 486 MTANGKIDRkRI 497
Cdd:cd05966 579 KTRSGKIMR-RI 589
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
335-497 |
1.05e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 60.06 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 335 EGQPLPEG----EKGEIVIAGPSVSRGYLGEPElteKAFFSHEGqWaYRTGDAGFIQDGQIFCQGRLDFQIKLHGYRMEL 410
Cdd:PRK07824 194 DGVPLDGVrvrvEDGRIALGGPTLAKGYRNPVD---PDPFAEPG-W-FRTDDLGALDDGVLTVLGRADDAISTGGLTVLP 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 411 EEIEFHVRQSQYVRSAVV--IPYQPNGtvEYLIAAIVPEEHEFEkefqLTSAIKKELAASLPAYMIPRKFIYQDHIQMTA 488
Cdd:PRK07824 269 QVVEAALATHPAVADCAVfgLPDDRLG--QRVVAAVVGDGGPAP----TLEALRAHVARTLDRTAAPRELHVVDELPRRG 342
|
....*....
3E7X_A 489 NGKIDRKRI 497
Cdd:PRK07824 343 IGKVDRRAL 351
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
327-504 |
1.27e-09 |
|
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: 60.75 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 327 MNIFIMDEEGQPLPeGEKGEIVIAGPSVSR--GYLGEPELT--EKAFFS-HEGQWAYrtGDagFIQ---DGQIFCQGRLD 398
Cdd:cd05943 433 MAVEAFDEEGKPVW-GEKGELVCTKPFPSMpvGFWNDPDGSryRAAYFAkYPGVWAH--GD--WIEitpRGGVVILGRSD 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 399 FQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVEYLIAAIV-PEEHEFEKEfqLTSAIKKELAASLPAYMIPRK 477
Cdd:cd05943 508 GTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKlREGVELDDE--LRKRIRSTIRSALSPRHVPAK 585
|
170 180
....*....|....*....|....*..
3E7X_A 478 FIYQDHIQMTANGKIdrkrigEEVLVR 504
Cdd:cd05943 586 IIAVPDIPRTLSGKK------VEVAVK 606
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
148-384 |
2.16e-09 |
|
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: 58.85 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 IIYTSGSTGNPKGVQIS-----AANLQSFtdWICAdfpVSGGKIFLNQAPFsFDLSV-MDLYPCLQSGGT---LHCVtkD 218
Cdd:cd17636 5 AIYTAAFSGRPNGALLShqallAQALVLA--VLQA---IDEGTVFLNSGPL-FHIGTlMFTLATFHAGGTnvfVRRV--D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 219 AVNKPKVLFEELKKSGlnvWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLERFPKAkifntYGPTEA 298
Cdd:cd17636 77 AEEVLELIEAERCTHA---FLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPGG-----YGQTEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 299 TVAVTSVEITNDVISRSeslpvGFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKaffSHEGQWaY 378
Cdd:cd17636 149 MGLATFAALGGGAIGGA-----GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNAR---RTRGGW-H 219
|
....*.
3E7X_A 379 RTGDAG 384
Cdd:cd17636 220 HTNDLG 225
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
3-494 |
2.35e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 59.64 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 3 LLHAIQTHAETYPQTDAFR-SQGQS-LTYQELWEQSDRAAAAIQKRiSGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYI 80
Cdd:PRK05857 16 VLDRVFEQARQQPEAIALRrCDGTSaLRYRELVAEVGGLAADLRAQ-SVSRGSRVLVISDNGPETYLSVLACAKLGAIAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 81 PVDLSIPSERIAKIIESSGAELLIHAAGLSIDAVGQQIQTVSAEELLENEGGSVSQDQWVKE------------HETFYI 148
Cdd:PRK05857 95 MADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDaaslagnadqgsEDPLAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 149 IYTSGSTGNPKGV-----------QISAANLQSFTDWICADF---PVSGGKI-----FLNqapfsfdlsvmdlypCLQSG 209
Cdd:PRK05857 175 IFTSGTTGEPKAVllanrtffavpDILQKEGLNWVTWVVGETtysPLPATHIgglwwILT---------------CLMHG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 210 GTlhCVTKDavNKPKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGevlpvSVAKALLERFPKAKI 289
Cdd:PRK05857 240 GL--CVTGG--ENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG-----SRAIAADVRFIEATG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 290 FNT---YGPTEATVAVTSVEITNDVISRSESLPVGFAKPDMNIFIMDEEG------QPLPEGEKGEIVIAGPSVSRGYLG 360
Cdd:PRK05857 311 VRTaqvYGLSETGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 361 EPELTEKAFFshEGqWAyRTGD-AGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVV--IPYQPNGTV 437
Cdd:PRK05857 391 NPERTAEVLI--DG-WV-NTGDlLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACyeIPDEEFGAL 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
3E7X_A 438 EYLiaAIVPEEhefEKEFQLTSAIKKELAASL----PAYMIPRKFIYQDHIQMTANGKIDR 494
Cdd:PRK05857 467 VGL--AVVASA---ELDESAARALKHTIAARFrresEPMARPSTIVIVTDIPRTQSGKVMR 522
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
6-414 |
3.65e-09 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 59.19 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 6 AIQTHAETYPQTDAF------RSQGQSLTYQELWEQSDRAAAAIQkRISGEKKSPILVYGHM------------------ 61
Cdd:PRK10524 58 AVDRHLAKRPEQLALiavsteTDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMiaeaafamlacarigaih 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 62 -------------------EPHMIVSFLGSVKAGH--PYIP-VDLSIpseriaKIIESSGAELLIHAAGLSiDAVGQQIQ 119
Cdd:PRK10524 137 svvfggfashslaariddaKPVLIVSADAGSRGGKvvPYKPlLDEAI------ALAQHKPRHVLLVDRGLA-PMARVAGR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 120 TVSAEELLENEGGSVSQDQWVKEHETFYIIYTSGSTGNPKGVQisaanlqsfTDwicadfpVSGGKIFLNqapfsfdlSV 199
Cdd:PRK10524 210 DVDYATLRAQHLGARVPVEWLESNEPSYILYTSGTTGKPKGVQ---------RD-------TGGYAVALA--------TS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 200 MDLYPCLQSGGTLHCvTKDA---------VNKP------KVLFEEL-------------KKSGLNVWTSTPSFVQMcL-- 249
Cdd:PRK10524 266 MDTIFGGKAGETFFC-ASDIgwvvghsyiVYAPllagmaTIMYEGLptrpdagiwwrivEKYKVNRMFSAPTAIRV-Lkk 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 250 MDPgfsqDLLPHAD-----TFMFCGEVLPVSVAKALLERFPKAKIFNtYGPTEATVAVTSveITNDVisrsESLPVGFAK 324
Cdd:PRK10524 344 QDP----ALLRKHDlsslrALFLAGEPLDEPTASWISEALGVPVIDN-YWQTETGWPILA--IARGV----EDRPTRLGS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 325 PDM-----NIFIMDEE-GQPLPEGEKGEIVIAGPsVSRGYL----GEPELTEKAFFSHEGQWAYRTGDAGFI-QDGQIFC 393
Cdd:PRK10524 413 PGVpmygyNVKLLNEVtGEPCGPNEKGVLVIEGP-LPPGCMqtvwGDDDRFVKTYWSLFGRQVYSTFDWGIRdADGYYFI 491
|
490 500
....*....|....*....|.
3E7X_A 394 QGRLDFQIKLHGYRMELEEIE 414
Cdd:PRK10524 492 LGRTDDVINVAGHRLGTREIE 512
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
24-497 |
4.70e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 58.76 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 24 GQSLTYQELWEQSDRAAAAIqkRISGEKKSPILVyGHME--PHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAE 101
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGL--RALGLREGDVVA-ILLEnnPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 102 LLIHAAGLSiDAVGQQIQTVSAE-ELLENEGGSV----SQDQWVKEHETFYI---------IYTSGSTGNPKGVQISA-- 165
Cdd:PRK08276 86 VLIVSAALA-DTAAELAAELPAGvPLLLVVAGPVpgfrSYEEALAAQPDTPIadetagadmLYSSGTTGRPKGIKRPLpg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 166 ----ANLQSFTDWICADFPVSGGKIFLNQAPF------SFDLSVmdlypcLQSGGTLHCVTK-------DAVNKPKVLFE 228
Cdd:PRK08276 165 ldpdEAPGMMLALLGFGMYGGPDSVYLSPAPLyhtaplRFGMSA------LALGGTVVVMEKfdaeealALIERYRVTHS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 229 ELkksglnVWTstpSFVQMCLMDPGFSQ--DL--LPHAdtfMFCGEVLPVSVAKALLERF-PkaKIFNTYGPTEA---TV 300
Cdd:PRK08276 239 QL------VPT---MFVRMLKLPEEVRAryDVssLRVA---IHAAAPCPVEVKRAMIDWWgP--IIHEYYASSEGggvTV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 301 AvTSVeitnDVISRSESlpVGfaKP-DMNIFIMDEEGQPLPEGEKGEIVIAGPSVSRGYLGEPELTEKAFfsHEGQWAyR 379
Cdd:PRK08276 305 I-TSE----DWLAHPGS--VG--KAvLGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAAR--NPHGWV-T 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 380 TGDAGFI-QDGQIFCQGRLDFQIKLHG---YRMELE-EIEFHVRqsqyVRSAVV--IPYQPNGtvEYLIAAIVPEE-HEF 451
Cdd:PRK08276 373 VGDVGYLdEDGYLYLTDRKSDMIISGGvniYPQEIEnLLVTHPK----VADVAVfgVPDEEMG--ERVKAVVQPADgADA 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
3E7X_A 452 EKEfqLTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRI 497
Cdd:PRK08276 447 GDA--LAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
11-391 |
1.41e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 57.26 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKR-IS-GEKKSPIL--VYGHMEPHMIVSFLGSVKAGhpyIPVDLSI 86
Cdd:PRK08162 28 AEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRgIGrGDTVAVLLpnIPAMVEAHFGVPMAGAVLNT---LNTRLDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 87 PSerIAKIIESSGAELLI---------HAAG--------LSIDAV------GQQIQTVSAEELLEnEG-----GSVSQDQ 138
Cdd:PRK08162 105 AS--IAFMLRHGEAKVLIvdtefaevaREALallpgpkpLVIDVDdpeypgGRFIGALDYEAFLA-SGdpdfaWTLPADE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 139 WvkehETFYIIYTSGSTGNPKGV--QISAANLQSFTDWICADFPvsggkiflnqaPFSFDLSVMDLYPC---------LQ 207
Cdd:PRK08162 182 W----DAIALNYTSGTTGNPKGVvyHHRGAYLNALSNILAWGMP-----------KHPVYLWTLPMFHCngwcfpwtvAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 208 SGGTLHCVTKdavNKPKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKALLER-Fpk 286
Cdd:PRK08162 247 RAGTNVCLRK---VDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIgF-- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 287 aKIFNTYGPTE----ATVAVTSVEItndvisrsESLPVGfAKPDMN------------IFIMD-EEGQPLP-EGEK-GEI 347
Cdd:PRK08162 322 -DLTHVYGLTEtygpATVCAWQPEW--------DALPLD-ERAQLKarqgvryplqegVTVLDpDTMQPVPaDGETiGEI 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
3E7X_A 348 VIAGPSVSRGYLGEPELTEKAFfshEGQWaYRTGDAGFIQ-DGQI 391
Cdd:PRK08162 392 MFRGNIVMKGYLKNPKATEEAF---AGGW-FHTGDLAVLHpDGYI 432
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
336-494 |
1.46e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 56.93 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 336 GQPLP-------EGEKGEIVIAGPSVSRGYLgePELTEKAFFshegqwaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYR 407
Cdd:PRK07445 286 GQVLPhaqitipANQTGNITIQAQSLALGYY--PQILDSQGI-------FETDDLGYLdAQGYLHILGRNSQKIITGGEN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 408 MELEEIEFHVRQSQYVRSAVVI--PYQPNGtvEYLIAAIVPEEHEFEKEfQLTSAIKKELAAslpaYMIPRKFIYQDHIQ 485
Cdd:PRK07445 357 VYPAEVEAAILATGLVQDVCVLglPDPHWG--EVVTAIYVPKDPSISLE-ELKTAIKDQLSP----FKQPKHWIPVPQLP 429
|
....*....
3E7X_A 486 MTANGKIDR 494
Cdd:PRK07445 430 RNPQGKINR 438
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
292-429 |
2.41e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 56.31 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 292 TYGPTEATVAVTSVE-----ITNDVISRSESLP-----VGFAKPDMNIFIMDEEGQ-PLPEGEKGEIVIAGPSVSRGYLG 360
Cdd:PRK05851 309 SYGLAESTCAVTVPVpgiglRVDEVTTDDGSGArrhavLGNPIPGMEVRISPGDGAaGVAGREIGEIEIRGASMMSGYLG 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3E7X_A 361 EPELtekaffsHEGQWaYRTGDAGFIQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVI 429
Cdd:PRK05851 389 QAPI-------DPDDW-FPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVV 449
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
148-500 |
9.04e-08 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 54.36 E-value: 9.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 IIYTSGSTGNPKGVQISAANLQSfTDWicadfPVSGGkifLNQAPFSFDLSVMDLY----------PCLQSGGTLHCVTK 217
Cdd:cd05937 92 LIYTSGTTGLPKAAAISWRRTLV-TSN-----LLSHD---LNLKNGDRTYTCMPLYhgtaaflgacNCLMSGGTLALSRK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 218 DAVNKpkvLFEELKKSGLNVWTSTPSFVQMCLMDPGfSQDLLPHADTFMFcGEVLPVSVAKALLERFPKAKIFNTYGPTE 297
Cdd:cd05937 163 FSASQ---FWKDVRDSGATIIQYVGELCRYLLSTPP-SPYDRDHKVRVAW-GNGLRPDIWERFRERFNVPEIGEFYAATE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 298 ATVAVT---SVEITNDVISRSESLPVGFAKPDMNIFIMD-EEGQPL-----------PEGEKGEIVIAGPSVSR----GY 358
Cdd:cd05937 238 GVFALTnhnVGDFGAGAIGHHGLIRRWKFENQVVLVKMDpETDDPIrdpktgfcvraPVGEPGEMLGRVPFKNReafqGY 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 359 LGEPELTEKAFFS---HEGQWAYRTGDAgFIQD--GQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQ- 432
Cdd:cd05937 318 LHNEDATESKLVRdvfRKGDIYFRTGDL-LRQDadGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKv 396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3E7X_A 433 PNGTVEYLIAAI-VPEEHEFEKEFQLtSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRKRIGEE 500
Cdd:cd05937 397 PGHDGRAGCAAItLEESSAVPTEFTK-SLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
265-453 |
9.05e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 54.74 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 265 FMFCGEVlPVSvakALLERFPK----AKIFNTYGPTEATVAVTSVEITNDVISR-SESLPVGFAKpdmniFIMDEEG--- 336
Cdd:PLN02387 424 FMLSGGA-PLS---GDTQRFINiclgAPIGQGYGLTETCAGATFSEWDDTSVGRvGPPLPCCYVK-----LVSWEEGgyl 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 337 ---QPLPegeKGEIVIAGPSVSRGYLGEPELTEKAFFSHEG--QWAYrTGDAG-FIQDGQIFCQGRLDFQIKL-HGYRME 409
Cdd:PLN02387 495 isdKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVDERgmRWFY-TGDIGqFHPDGCLEIIDRKKDIVKLqHGEYVS 570
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
3E7X_A 410 LEEIEFHVRQSQYVRSAVVI--PYQpngtvEYLIAAIVPEEHEFEK 453
Cdd:PLN02387 571 LGKVEAALSVSPYVDNIMVHadPFH-----SYCVALVVPSQQALEK 611
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
25-405 |
2.77e-07 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 53.13 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 25 QSLTYQELWEQSDRAAAAIQKrISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLI 104
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLK-LGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 105 ---HAAGLSIDAVGQQIQTVSA-----EELLENE------------GGSVSQDQW------VKEHETFYIIYTSGSTGNP 158
Cdd:cd05933 86 venQKQLQKILQIQDKLPHLKAiiqykEPLKEKEpnlyswdefmelGRSIPDEQLdaiissQKPNQCCTLIYTSGTTGMP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 159 KGVQISAANLQSFTDWICADF----PVSGGKIFLNQAPFSF-DLSVMDLYPCLQSGGTLHCVTKDAVN----------KP 223
Cdd:cd05933 166 KGVMLSHDNITWTAKAASQHMdlrpATVGQESVVSYLPLSHiAAQILDIWLPIKVGGQVYFAQPDALKgtlvktlrevRP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 224 KVLF----------EELKKSG---------LNVWTSTPSF-VQMCLMDPGFSQDLLPH-ADTFMF-----------CGEV 271
Cdd:cd05933 246 TAFMgvprvwekiqEKMKAVGaksgtlkrkIASWAKGVGLeTNLKLMGGESPSPLFYRlAKKLVFkkvrkalgldrCQKF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 272 L----PVSvaKALLERFPKA--KIFNTYGPTEATVAVTsveITNDVISRSESLPVGFAKPDMNIFIMDEEGQplpegekG 345
Cdd:cd05933 326 FtgaaPIS--RETLEFFLSLniPIMELYGMSETSGPHT---ISNPQAYRLLSCGKALPGCKTKIHNPDADGI-------G 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
3E7X_A 346 EIVIAGPSVSRGYLGEPELTEKAfFSHEGqWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHG 405
Cdd:cd05933 394 EICFWGRHVFMGYLNMEDKTEEA-IDEDG-W-LHSGDLGKLdEDGFLYITGRIKELIITAG 451
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
8-492 |
2.84e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 53.16 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 8 QTHAETYPQTDAF--RSQGQSLTYQELWEQSDRAAAAIQKRisGEKKS---PILVYGHmePHMIVSFLGSVKAGHPYIPV 82
Cdd:PRK13391 4 GIHAQTTPDKPAVimASTGEVVTYRELDERSNRLAHLFRSL--GLKRGdhvAIFMENN--LRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 83 DLSIPSERIAKIIESSGAELLI--HAAG----------------LSIDAVGQQIQTVSAEELLENEGGSVSQDQWVKEHe 144
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALItsAAKLdvarallkqcpgvrhrLVLDGDGELEGFVGYAEAVAGLPATPIADESLGTD- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 145 tfyIIYTSGSTGNPKGV--QISAANLQ---SFTDWICADFPVSGGKIFLNQAPF------SFDLSVMDLypclqsGGT-- 211
Cdd:PRK13391 159 ---MLYSSGTTGRPKGIkrPLPEQPPDtplPLTAFLQRLWGFRSDMVYLSPAPLyhsapqRAVMLVIRL------GGTvi 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 212 ----------LHCVTKDAVNKPKVLfeelkksglnvwtstPS-FVQMcLMDPGFSQDLLPHA--DTFMFCGEVLPVSVAK 278
Cdd:PRK13391 230 vmehfdaeqyLALIEEYGVTHTQLV---------------PTmFSRM-LKLPEEVRDKYDLSslEVAIHAAAPCPPQVKE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 279 ALLERFPKAkIFNTYGPTEAtVAVTsveitndVISRSESL--PVGFAKPDMNIF-IMDEEGQPLPEGEKGEIVIAGPSvS 355
Cdd:PRK13391 294 QMIDWWGPI-IHEYYAATEG-LGFT-------ACDSEEWLahPGTVGRAMFGDLhILDDDGAELPPGEPGTIWFEGGR-P 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 356 RGYLGEPELTEKAfFSHEGQWAyRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVI--PYQ 432
Cdd:PRK13391 364 FEYLNDPAKTAEA-RHPDGTWS-TVGDIGYVdEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFgvPNE 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
3E7X_A 433 PNGtvEYLIAAIVPEEhefekEFQLTSAIKKELAA----SLPAYMIPRKFIYQDHIQMTANGKI 492
Cdd:PRK13391 442 DLG--EEVKAVVQPVD-----GVDPGPALAAELIAfcrqRLSRQKCPRSIDFEDELPRLPTGKL 498
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
24-498 |
6.44e-07 |
|
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: 51.59 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 24 GQSLTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHmEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELL 103
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMEN-RPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 104 IhaaglsIDAVgqqiqtvsaeelleneggsvsqdqwvkehetFYIiYTSGSTGNPKGVQISAANLQSFTDWICADFPVSG 183
Cdd:cd05940 80 V------VDAA-------------------------------LYI-YTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 184 GKIFLNQAPFSFDLSVM-DLYPCLQSGGTLhcvtkdAVNKpkvlfeelKKSGLNVW--------TSTPSFVQMC--LMDP 252
Cdd:cd05940 122 SDVLYTCLPLYHSTALIvGWSACLASGATL------VIRK--------KFSASNFWddirkyqaTIFQYIGELCryLLNQ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 253 GFSQDLLPHADTfMFCGEVLPVSVAKALLERFPKAKIFNTYGPTEATVAVTSVEITNDVISRSESL-----PVGFAK--P 325
Cdd:cd05940 188 PPKPTERKHKVR-MIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLlrkvaPLALVKydL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 326 DMNIFIMDEEG--QPLPEGEKGEIV--IAGPSVSRGYLGEPELTEK----AFfsHEGQWAYRTGDAGFIQD-GQIFCQGR 396
Cdd:cd05940 267 ESGEPIRDAEGrcIKVPRGEPGLLIsrINPLEPFDGYTDPAATEKKilrdVF--KKGDAWFNTGDLMRLDGeGFWYFVDR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 397 LDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQ-PNGTVEYLIAAI-VPEEHEFEkefqlTSAIKKELAASLPAYMI 474
Cdd:cd05940 345 LGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPGTDGRAGMAAIvLQPNEEFD-----LSALAAHLEKNLPGYAR 419
|
490 500
....*....|....*....|....*..
3E7X_A 475 PRKFIYQDHIQMTAN---GKIDRKRIG 498
Cdd:cd05940 420 PLFLRLQPEMEITGTfkqQKVDLRNEG 446
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
24-399 |
7.18e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 51.91 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 24 GQSLTYQELWEQSDRAAAAIQKRISGEKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELL 103
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 104 IHAAGL----------------------------SIDAVGQQIQTVSAEELleneggSVSQDQWVKEHETFYIIYTSGST 155
Cdd:cd05938 83 VVAPELqeaveevlpalradgvsvwylshtsnteGVISLLDKVDAASDEPV------PASLRAHVTIKSPALYIYTSGTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 156 GNPKGVQISAANLqsftdWICADF-PVSGGK----IFLNQAPFSFDLSVMDLYPCLQSGGTLhcvtkdaVNKPKVlfeel 230
Cdd:cd05938 157 GLPKAARISHLRV-----LQCSGFlSLCGVTaddvIYITLPLYHSSGFLLGIGGCIELGATC-------VLKPKF----- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 231 kksglnvwtstpSFVQmclmdpgFSQDLLPHADT-FMFCGEVL------PVS-------------------VAKALLERF 284
Cdd:cd05938 220 ------------SASQ-------FWDDCRKHNVTvIQYIGELLrylcnqPQSpndrdhkvrlaignglradVWREFLRRF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 285 PKAKIFNTYGPTEATVAVTSVEITNDVISRSESL-----PVGFAKPDMNIF--IMDEEGQ--PLPEGEKGEIV--IAGPS 353
Cdd:cd05938 281 GPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLykllfPFELIKFDVEKEepVRDAQGFciPVAKGEPGLLVakITQQS 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
3E7X_A 354 VSRGYLGEPELTEKAFFSHegqwAYRTGDAGFiQDGQIFCQGRLDF 399
Cdd:cd05938 361 PFLGYAGDKEQTEKKLLRD----VFKKGDVYF-NTGDLLVQDQQNF 401
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
11-430 |
7.78e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 51.41 E-value: 7.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 11 AETYPQTDAFRSQGQSLTYQELWEQSDRAAAAIQKRisG-EKKSPILVYGHMEPHMIVSFLGSVKAGHPYIPVDLSIPSE 89
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQ--GvVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 90 RIAKIIESSGAELLIHAAGlsidavGQQIQTVSAEELLENEGgsVSQDQWvkEHETFY-IIYTSGSTGNPKGVQ------ 162
Cdd:PRK09029 91 LLEELLPSLTLDFALVLEG------ENTFSALTSLHLQLVEG--AHAVAW--QPQRLAtMTLTSGSTGLPKAAVhtaqah 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 163 -ISAANLQSFTDWICAD--------FPVSGGKIflnqapfsfdlsvmdLYPCLQSGGTLHcvtkdaVNKPKVLFEELKKs 233
Cdd:PRK09029 161 lASAEGVLSLMPFTAQDswllslplFHVSGQGI---------------VWRWLYAGATLV------VRDKQPLEQALAG- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 234 glnvwTSTPSFV--QMC-LMDPGFSQDLLPHadtFMFCGEVLPVSVAKALLERfpKAKIFNTYGPTEATVAVTSVeitnd 310
Cdd:PRK09029 219 -----CTHASLVptQLWrLLDNRSEPLSLKA---VLLGGAAIPVELTEQAEQQ--GIRCWCGYGLTEMASTVCAK----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 311 visRSESLP-VgfakpdmnifimdeeGQPLPEGE----KGEIVIAGPSVSRGYLGEPELTekAFFSHEGqWaYRTGDAGF 385
Cdd:PRK09029 284 ---RADGLAgV---------------GSPLPGREvklvDGEIWLRGASLALGYWRQGQLV--PLVNDEG-W-FATRDRGE 341
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
3E7X_A 386 IQDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIP 430
Cdd:PRK09029 342 WQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVP 386
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
140-497 |
1.14e-06 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 50.89 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 140 VKEHETFYIIYTSGSTGNPKGVQIS--AANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMDLYPCLQSGGTLHCVTK 217
Cdd:cd05915 150 VPERAACGMAYTTGTTGLPKGVVYShrALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGP 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 218 daVNKPKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHADTFMFCGEVLPVSVAKalLERFPKAKIFNTYGPTE 297
Cdd:cd05915 230 --RLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSLIA--RFERMGVEVRQGYGLTE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 298 ----ATVAVTSVEItnDVISRSESLPVGfAKPDMNIF-----IMDEEGQPLPEGEKGEIVIA--GPSVSRGYLGEPELTE 366
Cdd:cd05915 306 tspvVVQNFVKSHL--ESLSEEEKLTLK-AKTGLPIPlvrlrVADEEGRPVPKDGKALGEVQlkGPWITGGYYGNEEATR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 367 KAFFshEGQWaYRTGDAGFIQ-DGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPyQPNGTVEYLIAAIV 445
Cdd:cd05915 383 SALT--PDGF-FRTGDIAVWDeEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA-IPHPKWQERPLAVV 458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
3E7X_A 446 PEEHEFEKEFQLTSAIKKELAAslpAYMIPRKFIYQDHIQMTANGKIdRKRI 497
Cdd:cd05915 459 VPRGEKPTPEELNEHLLKAGFA---KWQLPDAYVFAEEIPRTSAGKF-LKRA 506
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
331-414 |
2.18e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 50.14 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 331 IMDEEGQPLPEGEKGEIVIAG--PSVSRGYLGEPELTEKAFFSHEgQWAYRTGD-AGFIQDGQIFCQGRLDFQIKLHGYR 407
Cdd:PRK00174 437 VVDEEGNPLEGGEGGNLVIKDpwPGMMRTIYGDHERFVKTYFSTF-KGMYFTGDgARRDEDGYYWITGRVDDVLNVSGHR 515
|
....*..
3E7X_A 408 MELEEIE 414
Cdd:PRK00174 516 LGTAEIE 522
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
64-495 |
2.24e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 50.03 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 64 HMIVSFLGSVKAGHPYIPVDLSIPSERIAKIIESSGAELLIHAaglSIDAVGQQIQTVSAEEllenegGSVSQdqwvkeh 143
Cdd:PRK08308 44 DIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLLYG---ESDFTKLEAVNYLAEE------PSLLQ------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 144 etfyiiYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPFSFDLSVMdlypClqsgGTLHCVTKDAvnKP 223
Cdd:PRK08308 108 ------YSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLI----C----GVLAALTRGS--KP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 224 KVLFEELKKSGLNVWTSTPsfVQMCLMDPGFSQ---DLLPHADTF---MFCGEVLPVSVAKALLERfpKAKIFNTYGPTE 297
Cdd:PRK08308 172 VIITNKNPKFALNILRNTP--QHILYAVPLMLHilgRLLPGTFQFhavMTSGTPLPEAWFYKLRER--TTYMMQQYGCSE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 298 ATVavtsVEITNDVisrSESLPVGFAKPDMNIFIMDEEGQPlpegekGEIVIagpsvsrgylgepeltekaffsHEGQWA 377
Cdd:PRK08308 248 AGC----VSICPDM---KSHLDLGNPLPHVSVSAGSDENAP------EEIVV----------------------KMGDKE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 378 YRTGDAGFI-QDGQIFCQGRLDFQIKLHG---YRMELEEIefhVRQSQYVRSAVVIPYQPNGTVEyLIAAIVPEEHEFEk 453
Cdd:PRK08308 293 IFTKDLGYKsERGTLHFMGRMDDVINVSGlnvYPIEVEDV---MLRLPGVQEAVVYRGKDPVAGE-RVKAKVISHEEID- 367
|
410 420 430 440
....*....|....*....|....*....|....*....|..
3E7X_A 454 efqlTSAIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK08308 368 ----PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRK 405
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
150-494 |
3.37e-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: 49.02 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 150 YTSGSTGNPKGVQISAANlQSFTDWICADFPVSG-GKIFLNQAP-FSFDLSVMDLYPCLQSGGTLHCVTKDAVNKPKV-- 225
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDpDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAGYRNPGLfd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 226 ----LFEELKKSGLnvwTSTPSFVQMCLMDPGfsqdllpHADT----FMFCGEV-LPVSVAKALlERFPKAKIFNTYGPT 296
Cdd:cd05944 88 nfwkLVERYRITSL---STVPTVYAALLQVPV-------NADIsslrFAMSGAApLPVELRARF-EDATGLPVVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 297 EATVAVTSVEITNDVISRSESLPVGFAKpdMNIFIMDEEGQPLPE---GEKGEIVIAGPSVSRGYLgEPELTEKAFFshE 373
Cdd:cd05944 157 EATCLVAVNPPDGPKRPGSVGLRLPYAR--VRIKVLDGVGRLLRDcapDEVGEICVAGPGVFGGYL-YTEGNKNAFV--A 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 374 GQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVI----PYQ---PNGTVEYLIAAIV 445
Cdd:cd05944 232 DGW-LNTGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVgqpdAHAgelPVAYVQLKPGAVV 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
3E7X_A 446 PEEHEFEkefqLTSAIKKELAAslpaymIPRKFIYQDHIQMTANGKIDR 494
Cdd:cd05944 311 EEEELLA----WARDHVPERAA------VPKHIEVLEELPVTAVGKVFK 349
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
88-495 |
9.09e-06 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 48.24 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 88 SERIAKII-ESSGAELLIHAAGLSIDA----VGQQIQTVSAEELLEneGGSVSQDqW--VKEHETFYIIYTSGSTGNPKG 160
Cdd:PRK05620 122 AEQLGEILkECPCVRAVVFIGPSDADSaaahMPEGIKVYSYEALLD--GRSTVYD-WpeLDETTAAAICYSTGTTGAPKG 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 161 VQIS--AANLQSFTDWICADFPVSGGKIFLNQAPFSFDLS-------VMDLYPCLQSGGTLhcvtkDAVNKPKVLFEELK 231
Cdd:PRK05620 199 VVYShrSLYLQSLSLRTTDSLAVTHGESFLCCVPIYHVLSwgvplaaFMSGTPLVFPGPDL-----SAPTLAKIIATAMP 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 232 KSGLNVWTSTPSFVQMCLMDPGFSQDLlphaDTFMFCGEVLPVSVAKALLERFpKAKIFNTYGPTEaTVAVTSVE----- 306
Cdd:PRK05620 274 RVAHGVPTLWIQLMVHYLKNPPERMSL----QEIYVGGSAVPPILIKAWEERY-GVDVVHVWGMTE-TSPVGTVArppsg 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 307 ---ITNDVISRSES-LPVGfakpdMNIFIMDEeGQPLPEGEK--GEIVIAGPSVSRGYL---------------GEPELT 365
Cdd:PRK05620 348 vsgEARWAYRVSQGrFPAS-----LEYRIVND-GQVMESTDRneGEIQVRGNWVTASYYhspteegggaastfrGEDVED 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 366 EKAFFSHEGqWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIPYQPNGTVE-----Y 439
Cdd:PRK05620 422 ANDRFTADG-W-LRTGDVGSVtRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGErplavT 499
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
3E7X_A 440 LIAAIVPEEHEFEKEfqltsaIKKELAASLPAYMIPRKFIYQDHIQMTANGKIDRK 495
Cdd:PRK05620 500 VLAPGIEPTRETAER------LRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKK 549
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
223-430 |
1.38e-05 |
|
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: 47.56 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 223 PKVLFEELKKSGLNVWTSTPSFVQMCLMDPGFSQDLLPHAdtfmFCGEVLPVSvaKALLERFPKA---KIFNTYGPTEAT 299
Cdd:cd05974 165 AKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLRE----VVGAGEPLN--PEVIEQVRRAwglTIRDGYGQTETT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 300 VavtsveitndVISRSESLPV-----GFAKPDMNIFIMDEEGQPLPEGEKGEIVIAGPSVS--RGYLGEPELTEKAFfsh 372
Cdd:cd05974 239 A----------LVGNSPGQPVkagsmGRPLPGYRVALLDPDGAPATEGEVALDLGDTRPVGlmKGYAGDPDKTAHAM--- 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
3E7X_A 373 EGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEFHVRQSQYVRSAVVIP 430
Cdd:cd05974 306 RGGY-YRTGDIAMRdEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVP 363
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
293-435 |
1.46e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 47.66 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 293 YGPTEaTVAVTSVEITNDVisrsESLPVGFAKPDMNIFIMDEEG-----QPLPegeKGEIVIAGPSVSRGYLGEPELTEK 367
Cdd:PTZ00216 459 WGLTE-TVCCGGIQRTGDL----EPNAVGQLLKGVEMKLLDTEEykhtdTPEP---RGEILLRGPFLFKGYYKQEELTRE 530
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 368 AFfsHEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIK-LHGYRMELEEIEfhvrqSQYVRSAVVipyQPNG 435
Cdd:PTZ00216 531 VL--DEDGW-FHTGDVGSIaANGTLRIIGRVKALAKnCLGEYIALEALE-----ALYGQNELV---VPNG 589
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
148-493 |
4.33e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.50 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 IIYTSGSTGNPKGVQISAANLQSFTDWICADFPVSGGKIFLNQAPF--SFDLSVMDLYPCLqSG-------GTLHCvtkd 218
Cdd:PRK06814 798 ILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVfhSFGLTGGLVLPLL-SGvkvflypSPLHY---- 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 219 avnkpKVLFEELKKSGLNVWTSTPSFvqmcLMdpGFSQdlLPHADTF-----MFCG-EVLPVSVAKALLERFpKAKIFNT 292
Cdd:PRK06814 873 -----RIIPELIYDTNATILFGTDTF----LN--GYAR--YAHPYDFrslryVFAGaEKVKEETRQTWMEKF-GIRILEG 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 293 YGPTEatvavtsveiTNDVIS-----RSESLPVGFAKPDMNIFIMDEEGqpLPEGekGEIVIAGPSVSRGYLgepeLTEK 367
Cdd:PRK06814 939 YGVTE----------TAPVIAlntpmHNKAGTVGRLLPGIEYRLEPVPG--IDEG--GRLFVRGPNVMLGYL----RAEN 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 368 --AFFSHEGQWaYRTGDAGFI-QDGQIFCQGRLDFQIKLHGYRMELEEIEfhvrqsqyvrsAVVIPYQPNgtveYLIAAI 444
Cdd:PRK06814 1001 pgVLEPPADGW-YDTGDIVTIdEEGFITIKGRAKRFAKIAGEMISLAAVE-----------ELAAELWPD----ALHAAV 1064
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
3E7X_A 445 -VPEEHEFEKEFQLTSA--------IKKELAASLPAYMIPRKFIYQDHIQMTANGKID 493
Cdd:PRK06814 1065 sIPDARKGERIILLTTAsdatraafLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
148-382 |
7.22e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 45.48 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 148 IIYTSGSTGNPKGVQISAANLQSftdwicADFPVSGGKIFLNQAP---FSFdLSVMDLYP------CLQSGGTLHCVTKD 218
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYN------TVVPLCKHSIFKKYNPkthLSY-LPISHIYErviaylSFMLGGTINIWSKD 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 219 AVNKPKVLFEelkkSGLNVWTSTP-----------------SFVQMCL-----------MDPGFSQDLL----------- 259
Cdd:PTZ00342 382 INYFSKDIYN----SKGNILAGVPkvfnriytnimteinnlPPLKRFLvkkilslrksnNNGGFSKFLEgithisskikd 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 260 ---PHADTFMFCGEVLPVSVAKAlLERFPKAKIFNTYGPTEATVAVTsVEITNDVISRSESLPVGfakPDMNIFIMDEE- 335
Cdd:PTZ00342 458 kvnPNLEVILNGGGKLSPKIAEE-LSVLLNVNYYQGYGLTETTGPIF-VQHADDNNTESIGGPIS---PNTKYKVRTWEt 532
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
3E7X_A 336 ---GQPLPegeKGEIVIAGPSVSRGYLGEPELTEKAfFSHEGqwAYRTGD 382
Cdd:PTZ00342 533 ykaTDTLP---KGELLIKSDSIFSGYFLEKEQTKNA-FTEDG--YFKTGD 576
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
86-168 |
5.90e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 42.39 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 86 IPSERIAKIIESSGAELLIHAAGlsidaVGQQIQTVSAeelLENEGGSvSQDQWV--KEHETFYIIYTSGSTGNPKGVQI 163
Cdd:PLN02736 171 IPSVRLIVVVGGADEPLPSLPSG-----TGVEIVTYSK---LLAQGRS-SPQPFRppKPEDVATICYTSGTTGTPKGVVL 241
|
....*
3E7X_A 164 SAANL 168
Cdd:PLN02736 242 THGNL 246
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
142-162 |
6.94e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 42.44 E-value: 6.94e-04
10 20
....*....|....*....|.
3E7X_A 142 EHETFyIIYTSGSTGNPKGVQ 162
Cdd:PRK00174 245 EDPLF-ILYTSGSTGKPKGVL 264
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
409-491 |
5.73e-03 |
|
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: 35.60 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3E7X_A 409 ELEEIefhVRQSQYVRSAVVIPYQPNGTVEYLIAAIVPEEHEFEkefqLTSAIKKELAASLPAYMIPRKFIYQDHIQMTA 488
Cdd:pfam13193 1 EVESA---LVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVEL----LEEELVAHVREELGPYAVPKEVVFVDELPKTR 73
|
...
3E7X_A 489 NGK 491
Cdd:pfam13193 74 SGK 76
|
|
| |
