|
Name |
Accession |
Description |
Interval |
E-value |
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
24-470 |
3.27e-148 |
|
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: 430.52 E-value: 3.27e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLREIC 103
Cdd:cd05945 5 PDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 104 HLASAPYyydvatrqFIATGEpgkvleeqDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFS 183
Cdd:cd05945 85 DAAKPAL--------LIADGD--------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 184 FDLSLIPLLANLAMGGHIVLNAKEDIQK-ENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNK 262
Cdd:cd05945 149 FDLSVMDLYPALASGATLVPVPRDATADpKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 263 ALVKQLRRRFPQAKIINSYGPTEATIATTVVEITDAILNsDSAVLPVGVMMPESKMEISTD----------GELIIWGKN 332
Cdd:cd05945 229 KTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLD-GYDRLPIGYAKPGAKLVILDEdgrpvppgekGELVISGPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 333 VMRGYLGLPQENAAKLlrREDEAFRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLP 410
Cdd:cd05945 308 VSKGYLNNPEKTAAAF--FPDEGQRAYRTGDLVRleADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVP 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658547412 411 LMKScGSVLRIAAFCVTDMA-----PDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05945 386 KYKG-EKVTELIAFVVPKPGaeaglTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
22-470 |
7.30e-131 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 388.10 E-value: 7.30e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLRE 101
Cdd:PRK04813 14 TQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 102 ICHLASAPYYydVATRQFIATGEPGKVLEEQDLA---------------------YIMFTSGSTGKPKGVQIGRESVWHF 160
Cdd:PRK04813 94 IIEVAKPSLI--IATEELPLEILGIPVITLDELKdifatgnpydfdhavkgddnyYIIFTSGTTGKPKGVQISHDNLVSF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 161 MKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWL-ERLKSNAVSAWVSTPSFAYQQLLS 239
Cdd:PRK04813 172 TNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLfETLPQLPINVWVSTPSFADMCLLD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 240 PQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATTVVEITDAILNS-DSavLPVGVMMPESKM 318
Cdd:PRK04813 252 PSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEITDEMLDQyKR--LPIGYAKPDSPL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 319 EIST----------DGELIIWGKNVMRGYLGLPQenaakllrREDEAF------RGYRTGDLGY-EAGLIYCQGRNDSQV 381
Cdd:PRK04813 330 LIIDeegtklpdgeQGEIVISGPSVSKGYLNNPE--------KTAEAFftfdgqPAYHTGDAGYlEDGLLFYQGRIDFQI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 382 KLNGYRIEINEIENRLLAMSGINEAVVLPLMKScGSVLRIAAFCV---TDMAPD-----TIKTSLSKVVPHYMVPSQIIV 453
Cdd:PRK04813 402 KLNGYRIELEEIEQNLRQSSYVESAVVVPYNKD-HKVQYLIAYVVpkeEDFEREfeltkAIKKELKERLMEYMIPRKFIY 480
|
490
....*....|....*..
gi 658547412 454 KDALPLNPNGKIDRKLL 470
Cdd:PRK04813 481 RDSLPLTPNGKIDRKAL 497
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
22-470 |
5.78e-126 |
|
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: 375.64 E-value: 5.78e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLRE 101
Cdd:TIGR01734 12 TYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPSERIEM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 102 ICHLASAPYYYDVA------TRQFIATGEPGKVLEEQ-------------DLAYIMFTSGSTGKPKGVQIGRESVWHFMK 162
Cdd:TIGR01734 92 IIEAAGPELVIHTAelsidaVGTQIITLSALEQAETSggpvsfdhavkgdDNYYIIYTSGSTGNPKGVQISHDNLVSFTN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 163 WVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWL-ERLKSNAVSAWVSTPSFAYQQLLSPQ 241
Cdd:TIGR01734 172 WMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLfEELPKTGLNVWVSTPSFVDMCLLDPN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 242 FNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATTVVEITDAILnSDSAVLPVGVMMPESKMEI- 320
Cdd:TIGR01734 252 FNQENYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEIL-DQYPRLPIGFAKPDMNLFIm 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 321 ---------STDGELIIWGKNVMRGYLGLPQENAAKLLrrEDEAFRGYRTGDLG-YEAGLIYCQGRNDSQVKLNGYRIEI 390
Cdd:TIGR01734 331 deegeplpeGEKGEIVIVGPSVSKGYLNNPEKTAEAFF--SHEGQPAYRTGDAGtITDGQLFYQGRLDFQIKLHGYRIEL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 391 NEIENRLLAMSGINEAVVLPLMKSCGSVLRIAAFCVTD--------MAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPN 462
Cdd:TIGR01734 409 EDIEFNLRQSSYIESAVVVPKYNKDHKVEYLIAAIVPEtedfekefQLTKAIKKELKKSLPAYMIPRKFIYRDQLPLTAN 488
|
....*...
gi 658547412 463 GKIDRKLL 470
Cdd:TIGR01734 489 GKIDRKAL 496
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
24-470 |
3.73e-105 |
|
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: 320.24 E-value: 3.73e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLREIc 103
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 104 hLAsapyyyDVATRQFIATGEpgkvleeqDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFS 183
Cdd:cd05930 80 -LE------DSGAKLVLTDPD--------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 184 FDLSLIPLLANLAMGGHIVL---NAKEDIQKenWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSeyLPALNVFIFIGEVL 260
Cdd:cd05930 145 FDVSVWEIFGALLAGATLVVlpeEVRKDPEA--LADLLAEEGITVLHLTPSLLRLLLQELELAA--LPSLRLVLVGGEAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 261 NKALVKQLRRRFPQAKIINSYGPTEATIATTVVEITDA-------------------ILNSDSAVLPVGVMmpeskmeis 321
Cdd:cd05930 221 PPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDdeedgrvpigrpipntrvyVLDENLRPVPPGVP--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 322 tdGELIIWGKNVMRGYLGLPQENAAKLLR-REDEAFRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLL 398
Cdd:cd05930 292 --GELYIGGAGLARGYLNRPELTAERFVPnPFGPGERMYRTGDLVRwlPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658547412 399 AMSGINEAVVLPLMKSCGSVlRIAAFCVTDMAPD----TIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05930 370 AHPGVREAAVVAREDGDGEK-RLVAYVVPDEGGEldeeELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
10-470 |
1.96e-84 |
|
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: 267.06 E-value: 1.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 10 LQDFLRAALCdpASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIP 89
Cdd:COG0318 1 LADLLRRAAA--RHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 90 VDCIYPQERLREICHLASApyyydvatRQFIAtgepgkvleeqdlAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFS 169
Cdd:COG0318 79 LNPRLTAEELAYILEDSGA--------RALVT-------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 170 LPEKPVLMNHAVFSFDLSLI-PLLANLAMGGHIVLNAKEDIqkENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLP 248
Cdd:COG0318 138 LTPGDVVLVALPLFHVFGLTvGLLAPLLAGATLVLLPRFDP--ERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 249 ALNVFIFIGEVLNKALVKQLRRRFpQAKIINSYGPTEATIATTV-------------------VEItdAILNSDSAVLPV 309
Cdd:COG0318 216 SLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVnpedpgerrpgsvgrplpgVEV--RIVDEDGRELPP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 310 GvmmpeskmeisTDGELIIWGKNVMRGYLGLPQENAakllrredEAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNG 385
Cdd:COG0318 293 G-----------EVGEIVVRGPNVMKGYWNDPEATA--------EAFRDgwLRTGDLGRldEDGYLYIVGRKKDMIISGG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 386 YRIEINEIENRLLAMSGINEAVVLPLM-KSCGSvlRIAAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLN 460
Cdd:COG0318 354 ENVYPAEVEEVLAAHPGVAEAAVVGVPdEKWGE--RVVAFVVlrpgAELDAEELRAFLRERLARYKVPRRVEFVDELPRT 431
|
490
....*....|
gi 658547412 461 PNGKIDRKLL 470
Cdd:COG0318 432 ASGKIDRRAL 441
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
59-408 |
2.78e-84 |
|
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: 265.28 E-value: 2.78e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 59 AGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLREIC------HLASAPYYYDVATRQFIATGEPGKVLEE- 131
Cdd:TIGR01733 24 PGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILedagarLLLTDSALASRLAGLVLPVILLDPLELAa 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 132 ----------------QDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANL 195
Cdd:TIGR01733 104 lddapappppdapsgpDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 196 AMGGHIVLNAKEDIQ--KENWLERLKSNAVSAWVSTPSFAyqQLLSPQfNSEYLPALNVFIFIGEVLNKALVKQLRRRFP 273
Cdd:TIGR01733 184 LAGATLVVPPEDEERddAALLAALIAEHPVTVLNLTPSLL--ALLAAA-LPPALASLRLVILGGEALTPALVDRWRARGP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 274 QAKIINSYGPTEATIATTVVEITDAILNSDSAVlPVGVMMPESKMEISTD----------GELIIWGKNVMRGYLGLPQE 343
Cdd:TIGR01733 261 GARLINLYGPTETTVWSTATLVDPDDAPRESPV-PIGRPLANTRLYVLDDdlrpvpvgvvGELYIGGPGVARGYLNRPEL 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 344 NAAKLL---RREDEAFRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVV 408
Cdd:TIGR01733 340 TAERFVpdpFAGGDGARLYRTGDLVRylPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
22-470 |
2.54e-79 |
|
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: 254.82 E-value: 2.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLRE 101
Cdd:cd12117 9 RTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 102 ICHLASA------------------PYYYDVATRQFiATGEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKw 163
Cdd:cd12117 89 MLADAGAkvlltdrslagragglevAVVIDEALDAG-PAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 164 vSQDF-SLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWL-ERLKSNAVSA-WVSTPSFayQQLLsp 240
Cdd:cd12117 167 -NTNYvTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALgALIAEEGVTVlWLTAALF--NQLA-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 241 QFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATTVVEITDA-------------------ILN 301
Cdd:cd12117 242 DEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELdevagsipigrpiantrvyVLD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 302 SDSAVLPVGVMmpeskmeistdGELIIWGKNVMRGYLGLPQENAAKLLrrEDEAFRG---YRTGDLGY--EAGLIYCQGR 376
Cdd:cd12117 322 EDGRPVPPGVP-----------GELYVGGDGLALGYLNRPALTAERFV--ADPFGPGerlYRTGDLARwlPDGRLEFLGR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 377 NDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSvLRIAAFCVTDMAPDT--IKTSLSKVVPHYMVPSQIIVK 454
Cdd:cd12117 389 IDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGD-KRLVAYVVAEGALDAaeLRAFLRERLPAYMVPAAFVVL 467
|
490
....*....|....*.
gi 658547412 455 DALPLNPNGKIDRKLL 470
Cdd:cd12117 468 DELPLTANGKVDRRAL 483
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
22-472 |
1.46e-78 |
|
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: 266.72 E-value: 1.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLRE 101
Cdd:COG1020 488 RTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAY 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 102 ICHLASAPY-------------------YYDVATRQFIATGEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMK 162
Cdd:COG1020 568 MLEDAGARLvltqsalaarlpelgvpvlALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLA 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 163 WVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLnAKEDIQK--ENWLERLKSNAVSAWVSTPSFaYQQLLsp 240
Cdd:COG1020 648 WMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVL-APPEARRdpAALAELLARHRVTVLNLTPSL-LRALL-- 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 241 QFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATTVVEITDAILNSDSA------------VL- 307
Cdd:COG1020 724 DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSVpigrpiantrvyVLd 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 308 ------PVGVMmpeskmeistdGELIIWGKNVMRGYLGLPQENAakllrredEAF----------RGYRTGDLGY--EAG 369
Cdd:COG1020 804 ahlqpvPVGVP-----------GELYIGGAGLARGYLNRPELTA--------ERFvadpfgfpgaRLYRTGDLARwlPDG 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 370 LIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVlRIAAFCVT----DMAPDTIKTSLSKVVPHY 445
Cdd:COG1020 865 NLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDK-RLVAYVVPeagaAAAAALLRLALALLLPPY 943
|
490 500
....*....|....*....|....*..
gi 658547412 446 MVPSQIIVKDALPLNPNGKIDRKLLDA 472
Cdd:COG1020 944 MVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
24-470 |
1.66e-77 |
|
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: 249.90 E-value: 1.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLREIC 103
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 104 H-------------LASAPYYYDVATRQFIATGEPGKVLEEQ----DLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQ 166
Cdd:cd12116 81 EdaepalvltddalPDRLPAGLPVLLLALAAAAAAPAAPRTPvspdDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 167 DFSL-PEKPVLmnhAV--FSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWLERLKSNAVSAWV-STPSFaYQQLLSPQF 242
Cdd:cd12116 161 RLGLgPGDRLL---AVttYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMqATPAT-WRMLLDAGW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 243 -NSEYLPALNVfifiGEVLNKALVKQLRRRfpQAKIINSYGPTEATIATTVVEITDA---------ILNSDSAVL----- 307
Cdd:cd12116 237 qGRAGLTALCG----GEALPPDLAARLLSR--VGSLWNLYGPTETTIWSTAARVTAAagpipigrpLANTQVYVLdaalr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 308 --PVGVMmpeskmeistdGELIIWGKNVMRGYLGLPQENAAKLLR--REDEAFRGYRTGDLGY--EAGLIYCQGRNDSQV 381
Cdd:cd12116 311 pvPPGVP-----------GELYIGGDGVAQGYLGRPALTAERFVPdpFAGPGSRLYRTGDLVRrrADGRLEYLGRADGQV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 382 KLNGYRIEINEIENRLLAMSGINEAVVlpLMKSCGSVLRIAAFCV--TDMAPDT--IKTSLSKVVPHYMVPSQIIVKDAL 457
Cdd:cd12116 380 KIRGHRIELGEIEAALAAHPGVAQAAV--VVREDGGDRRLVAYVVlkAGAAPDAaaLRAHLRATLPAYMVPSAFVRLDAL 457
|
490
....*....|...
gi 658547412 458 PLNPNGKIDRKLL 470
Cdd:cd12116 458 PLTANGKLDRKAL 470
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
10-470 |
1.38e-71 |
|
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: 233.75 E-value: 1.38e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 10 LQDFLRAALcdPASPQQLAISGSDEALSWLQLS--AAVTDWAQRYQRCQPvaGTPVVLYGHQQAEFAVAIYSCLLHNIPY 87
Cdd:cd12115 1 LHDLVEAQA--ARTPDAIALVCGDESLTYAELNrrANRLAARLRAAGVGP--ESRVGVCLERTPDLVVALLAVLKAGAAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 88 IPVDCIYPQERLREIchlasapyyydvatrqfIATGEPGKVL-EEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQ 166
Cdd:cd12115 77 VPLDPAYPPERLRFI-----------------LEDAQARLVLtDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 167 DFSLPE-KPVLMNHAVfSFDLSLIPLLANLAMGGHIVLnakediqKENWLErLKSNAVSAWVS----TPSfAYQQLLspq 241
Cdd:cd12115 140 AFSAEElAGVLASTSI-CFDLSVFELFGPLATGGKVVL-------ADNVLA-LPDLPAAAEVTlintVPS-AAAELL--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 242 fNSEYLPA-LNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEAT---------------------IATTVVEITDAI 299
Cdd:cd12115 207 -RHDALPAsVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTtystvapvppgasgevsigrpLANTQAYVLDRA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 300 LNSdsavLPVGVMmpeskmeistdGELIIWGKNVMRGYLGLPQENAAKLL-RREDEAFRGYRTGDLG-YEA-GLIYCQGR 376
Cdd:cd12115 286 LQP----VPLGVP-----------GELYIGGAGVARGYLGRPGLTAERFLpDPFGPGARLYRTGDLVrWRPdGLLEFLGR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 377 NDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSvLRIAAFCVTD----MAPDTIKTSLSKVVPHYMVPSQII 452
Cdd:cd12115 351 ADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGE-RRLVAYIVAEpgaaGLVEDLRRHLGTRLPAYMVPSRFV 429
|
490
....*....|....*...
gi 658547412 453 VKDALPLNPNGKIDRKLL 470
Cdd:cd12115 430 RLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
24-470 |
5.75e-71 |
|
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: 231.97 E-value: 5.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLreic 103
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 104 hlasapyyydvatrQFIAT--GEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPV-LMNHA 180
Cdd:cd17650 77 --------------QYMLEdsGAKLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVrLLQMA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 181 VFSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWLER-LKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEV 259
Cdd:cd17650 143 SFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDlILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 260 LNKALVKQLRRRFPQA-KIINSYGPTEATIATTVVEITDAILnSDSAVLPVGVMMPESKMEISTD----------GELII 328
Cdd:cd17650 223 CKAQDFKTLAARFGQGmRIINSYGVTEATIDSTYYEEGRDPL-GDSANVPIGRPLPNTAMYVLDErlqpqpvgvaGELYI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 329 WGKNVMRGYLGLPQENAAKLLRREDEAF-RGYRTGDLG--YEAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINE 405
Cdd:cd17650 302 GGAGVARGYLNRPELTAERFVENPFAPGeRMYRTGDLArwRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658547412 406 AVVLpLMKSCGSVLRIAAFCVTDMAPDT--IKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd17650 382 AVVA-VREDKGGEARLCAYVVAAATLNTaeLRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
22-470 |
1.19e-70 |
|
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: 232.62 E-value: 1.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLRE 101
Cdd:cd17651 7 RTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 102 I-------CHLASAPYYYDVATRQF------------IATGEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMK 162
Cdd:cd17651 87 MladagpvLVLTHPALAGELAVELVavtlldqpgaaaGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 163 WVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLnAKEDIqkenwleRLKSNAVSAWVST--------PSFAY 234
Cdd:cd17651 167 WQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVL-PPEEV-------RTDPPALAAWLDEqrisrvflPTVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 235 QQLL-SPQFNSEYLPALNVFIFIGEVLN-KALVKQLRRRFPQAKIINSYGPTEATIATtvVEITDAILNSDSAVLPVGVM 312
Cdd:cd17651 239 RALAeHGRPLGVRLAALRYLLTGGEQLVlTEDLREFCAGLPGLRLHNHYGPTETHVVT--ALSLPGDPAAWPAPPPIGRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 313 MPESKMEISTD----------GELIIWGKNVMRGYLGLPQENAAKLLrreDEAFRG----YRTGDLGY--EAGLIYCQGR 376
Cdd:cd17651 317 IDNTRVYVLDAalrpvppgvpGELYIGGAGLARGYLNRPELTAERFV---PDPFVPgarmYRTGDLARwlPDGELEFLGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 377 NDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSvLRIAAFCVTDMA----PDTIKTSLSKVVPHYMVPSQII 452
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGE-KRLVAYVVGDPEapvdAAELRAALATHLPEYMVPSAFV 472
|
490
....*....|....*...
gi 658547412 453 VKDALPLNPNGKIDRKLL 470
Cdd:cd17651 473 LLDALPLTPNGKLDRRAL 490
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
22-474 |
2.23e-70 |
|
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: 231.28 E-value: 2.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAqRYQRCQPV-AGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLR 100
Cdd:cd05918 11 SQPDAPAVCAWDGSLTYAELDRLSSRLA-HHLRSLGVgPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 101 EICHLASAPyyydvatrqFIATGEPgkvleeQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSL-PEKPVLmNH 179
Cdd:cd05918 90 EILQDTGAK---------VVLTSSP------SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLtSESRVL-QF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 180 AVFSFDLSLIPLLANLAMGGHIVLNAKEDIqKEN---WLERLKSNAVSAwvsTPSFAyqQLLSPqfnsEYLPALNVFIFI 256
Cdd:cd05918 154 ASYTFDVSILEIFTTLAAGGCLCIPSEEDR-LNDlagFINRLRVTWAFL---TPSVA--RLLDP----EDVPSLRTLVLG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 257 GEVLNKALVKQLRRRfpqAKIINSYGPTEATIATTVVEITDailNSDSAVL--PVGVMM-------PESKMEISTDGELI 327
Cdd:cd05918 224 GEALTQSDVDTWADR---VRLINAYGPAECTIAATVSPVVP---STDPRNIgrPLGATCwvvdpdnHDRLVPIGAVGELL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 328 IWGKNVMRGYLGLPQENAAKL------LRREDEAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRL 397
Cdd:cd05918 298 IEGPILARGYLNDPEKTAAAFiedpawLKQEGSGRGRrlYRTGDLVRynPDGSLEYVGRKDTQVKIRGQRVELGEIEHHL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 398 LA-MSGINEAVVLPLMKSCGSVL-RIAAFCVTD-------------MAPD--------TIKTSLSKVVPHYMVPSQIIVK 454
Cdd:cd05918 378 RQsLPGAKEVVVEVVKPKDGSSSpQLVAFVVLDgsssgsgdgdslfLEPSdefralvaELRSKLRQRLPSYMVPSVFLPL 457
|
490 500
....*....|....*....|
gi 658547412 455 DALPLNPNGKIDRKLLDAYA 474
Cdd:cd05918 458 SHLPLTASGKIDRRALRELA 477
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
24-470 |
2.88e-69 |
|
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: 228.31 E-value: 2.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLREIC 103
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 104 HLASA--------PYYYDVATRQFIATG---------EPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQ 166
Cdd:cd12114 81 ADAGArlvltdgpDAQLDVAVFDVLILDldalaapapPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 167 DFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKEN-WLERLKSNAVSAWVSTPsfAYQQLL--SPQFN 243
Cdd:cd12114 161 RFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAhWAELIERHGVTLWNSVP--ALLEMLldVLEAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 244 SEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATTVVEITDAilNSDSAVLPVGVMMPESKMEISTD 323
Cdd:cd12114 239 QALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEV--PPDWRSIPYGRPLANQRYRVLDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 324 ----------GELIIWGKNVMRGYLGLPQENAAKLLRREDEAfRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEIN 391
Cdd:cd12114 317 rgrdcpdwvpGELWIGGRGVALGYLGDPELTAARFVTHPDGE-RLYRTGDLGRyrPDGTLEFLGRRDGQVKVRGYRIELG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 392 EIENRLLAMSGINEAVVLPLMKSCGSvlRIAAFCVTD-----MAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKID 466
Cdd:cd12114 396 EIEAALQAHPGVARAVVVVLGDPGGK--RLAAFVVPDndgtpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVD 473
|
....
gi 658547412 467 RKLL 470
Cdd:cd12114 474 RAAL 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
22-470 |
2.63e-68 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 237.75 E-value: 2.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERL-- 99
Cdd:PRK12467 524 QHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLay 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 100 -------REICH-------------LASAPYYYDVATRQFIATGEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWH 159
Cdd:PRK12467 604 mlddsgvRLLLTqshllaqlpvpagLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALAN 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 160 FMKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQK-ENWLERLKSNAVSAWVSTPSfAYQQLL 238
Cdd:PRK12467 684 YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDaEAFAALMADQGVTVLKIVPS-HLQALL 762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 239 SPQFNSEYLPALNVfIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATTVVEITDAilNSDSAVLPVGVMMPESKM 318
Cdd:PRK12467 763 QASRVALPRPQRAL-VCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDE--ERDFGNVPIGQPLANLGL 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 319 EI----------STDGELIIWGKNVMRGYLGLPQENAAKLLRREDEA--FRGYRTGDLG-YEA-GLIYCQGRNDSQVKLN 384
Cdd:PRK12467 840 YIldhylnpvpvGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdgGRLYRTGDLArYRAdGVIEYLGRMDHQVKIR 919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 385 GYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLriAAFCVTDMAP---------DTIKTSLSKVVPHYMVPSQIIVKD 455
Cdd:PRK12467 920 GFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQL--VAYLVPAAVAdgaehqatrDELKAQLRQVLPDYMVPAHLLLLD 997
|
490
....*....|....*
gi 658547412 456 ALPLNPNGKIDRKLL 470
Cdd:PRK12467 998 SLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
23-470 |
3.80e-68 |
|
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: 225.67 E-value: 3.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 23 SPQQLAISGSDEALSWLQLS--AAVTDWAQRYQRCQPvaGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLR 100
Cdd:cd17655 10 TPDHTAVVFEDQTLTYRELNerANQLARTLREKGVGP--DTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 101 EICH-------LASAPYYYDVATRQFIATGEPGKVLEE-----------QDLAYIMFTSGSTGKPKGVQIGRESVWHFMK 162
Cdd:cd17655 88 YILEdsgadilLTQSHLQPPIAFIGLIDLLDEDTIYHEesenlepvsksDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 163 WVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWLER-LKSNAVSAWVSTPsfAYQQLLSPQ 241
Cdd:cd17655 168 WANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQyIRQNRITIIDLTP--AHLKLLDAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 242 FNSEYLPaLNVFIFIGEVLNKALVKQLRRRF-PQAKIINSYGPTEATIATTVVEITDA-------------------ILN 301
Cdd:cd17655 246 DDSEGLS-LKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYEPEtdqqvsvpigkplgntriyILD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 302 SDSAVLPVGVMmpeskmeistdGELIIWGKNVMRGYLGLPQENAAKLLrreDEAF----RGYRTGDLG--YEAGLIYCQG 375
Cdd:cd17655 325 QYGRPQPVGVA-----------GELYIGGEGVARGYLNRPELTAEKFV---DDPFvpgeRMYRTGDLArwLPDGNIEFLG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 376 RNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLrIAAFCVTD--MAPDTIKTSLSKVVPHYMVPSQIIV 453
Cdd:cd17655 391 RIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNY-LCAYIVSEkeLPVAQLREFLARELPDYMIPSYFIK 469
|
490
....*....|....*..
gi 658547412 454 KDALPLNPNGKIDRKLL 470
Cdd:cd17655 470 LDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
24-470 |
4.51e-67 |
|
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: 221.86 E-value: 4.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLREIC 103
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 104 HLASAPyyydvatrqFIATGEPgkvleeQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFS 183
Cdd:cd17649 81 EDSGAG---------LLLTHHP------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 184 FDLSLIPLLANLAMGGHIVLNAKEDIQKENWLERL-KSNAVSAWVSTPSFAYQQLL-SPQFNSEYLPALNVFIFIGEVLN 261
Cdd:cd17649 146 FDGAHEQLLPPLICGACVVLRPDELWASADELAEMvRELGVTVLDLPPAYLQQLAEeADRTGDGRPPSLRLYIFGGEALS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 262 kalVKQLRRRFPQAK-IINSYGPTEATIATTVVEI--------------------TDAILNSDSAVLPVGVMmpeskmei 320
Cdd:cd17649 226 ---PELLRRWLKAPVrLFNAYGPTEATVTPLVWKCeagaaragasmpigrplggrSAYILDADLNPVPVGVT-------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 321 stdGELIIWGKNVMRGYLGLPQENAAKLLRRED--EAFRGYRTGDL--GYEAGLIYCQGRNDSQVKLNGYRIEINEIENR 396
Cdd:cd17649 295 ---GELYIGGEGLARGYLGRPELTAERFVPDPFgaPGSRLYRTGDLarWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 397 LLAMSGINEAVVLPLMKSCGSvlRIAAFCVTDMA------PDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd17649 372 LLEHPGVREAAVVALDGAGGK--QLVAYVVLRAAaaqpelRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
24-470 |
4.60e-65 |
|
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: 216.79 E-value: 4.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAavtdWAQRYQRC---QPV-AGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERL 99
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDA----RANRLARTlraEGVgPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 100 REIchLAsapyyyDVATRQFIATGEpgkvleeqDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPV-LMN 178
Cdd:cd17643 77 AFI--LA------DSGPSLLLTDPD--------DLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVwTLF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 179 HAvFSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWLERL-KSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIG 257
Cdd:cd17643 141 HS-YAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLlRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 258 EVLNKALVKQLRRRF--PQAKIINSYGPTEATIATTVVEITDAILnSDSAVLPVGVMMPESKMEISTD----------GE 325
Cdd:cd17643 220 EALEAAMLRPWAGRFglDRPQLVNMYGITETTVHVTFRPLDAADL-PAAAASPIGRPLPGLRVYVLDAdgrpvppgvvGE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 326 LIIWGKNVMRGYLGLPQENAAKLLRRED--EAFRGYRTGDLGYEAG---LIYcQGRNDSQVKLNGYRIEINEIENRLLAM 400
Cdd:cd17643 299 LYVSGAGVARGYLGRPELTAERFVANPFggPGSRMYRTGDLARRLPdgeLEY-LGRADEQVKIRGFRIELGEIEAALATH 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658547412 401 SGINEAVVLPLMKSCGSvLRIAAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd17643 378 PSVRDAAVIVREDEPGD-TRLVAYVVaddgAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
24-470 |
5.47e-65 |
|
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: 215.96 E-value: 5.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLReic 103
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 104 HLASapyyyDVATRQFIATGEpgkvleeqDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFS 183
Cdd:cd17652 78 YMLA-----DARPALLLTTPD--------NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 184 FDLSLIPLLANLAMGGHIVLNAKEDIQKENWLER-LKSNAVSAWVSTPSfayqqLLSPqFNSEYLPALNVFIFIGEVLNK 262
Cdd:cd17652 145 FDASVWELLMALLAGATLVLAPAEELLPGEPLADlLREHRITHVTLPPA-----ALAA-LPPDDLPDLRTLVVAGEACPA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 263 ALVKQL--RRRFpqakiINSYGPTEATIATTVVEITdailnSDSAVLPVGVMMPESKMEISTD----------GELIIWG 330
Cdd:cd17652 219 ELVDRWapGRRM-----INAYGPTETTVCATMAGPL-----PGGGVPPIGRPVPGTRVYVLDArlrpvppgvpGELYIAG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 331 KNVMRGYLGLPQENAAKLLRRE--DEAFRGYRTGDLG-YEA-GLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEA 406
Cdd:cd17652 289 AGLARGYLNRPGLTAERFVADPfgAPGSRMYRTGDLArWRAdGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658547412 407 VVLpLMKSCGSVLRIAAFCVT--DMAPDT--IKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd17652 369 VVV-VRDDRPGDKRLVAYVVPapGAAPTAaeLRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
24-470 |
2.33e-64 |
|
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: 214.48 E-value: 2.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLREIc 103
Cdd:cd17653 11 PDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAI- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 104 hlasapyyYDVATRQFIATGEPGkvleeQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSL-PEKPVLmNHAVF 182
Cdd:cd17653 90 --------LRTSGATLLLTTDSP-----DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVgPGSRVA-QVLSI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 183 SFDLSLIPLLANLAMGGHIVLNAKEDiqkeNWLERLKSnaVSAWVSTPSFAyqQLLSPQfnsEYlPALNVFIFIGEVLNK 262
Cdd:cd17653 156 AFDACIGEIFSTLCNGGTLVLADPSD----PFAHVART--VDALMSTPSIL--STLSPQ---DF-PNLKTIFLGGEAVPP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 263 ALvkqLRRRFPQAKIINSYGPTEATIATTVVEITDA---------------ILNSDSAVLPVGVMmpeskmeistdGELI 327
Cdd:cd17653 224 SL---LDRWSPGRRLYNAYGPTECTISSTMTELLPGqpvtigkpipnstcyILDADLQPVPEGVV-----------GEIC 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 328 IWGKNVMRGYLGLPQENAAKLLRREDE-AFRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENrllamsgin 404
Cdd:cd17653 290 ISGVQVARGYLGNPALTASKFVPDPFWpGSRMYRTGDYGRwtEDGGLEFLGREDNQVKVRGFRINLEEIEE--------- 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658547412 405 eavvlPLMKSCGSVLRIAAFCVTD-----MAPDTI-----KTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd17653 361 -----VVLQSQPEVTQAAAIVVNGrlvafVTPETVdvdglRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
22-472 |
1.61e-62 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 220.98 E-value: 1.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERL-- 99
Cdd:PRK12316 523 RTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLay 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 100 -----------------------REICHLAsapyyYDVATRQFIA--TGEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGR 154
Cdd:PRK12316 603 mledsgvqlllsqshlgrklplaAGVQVLD-----LDRPAAWLEGysEENPGTELNPENLAYVIYTSGSTGKPKGAGNRH 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 155 ESVWHFMKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQK-ENWLERLKSNAVSAWVSTPSFA 233
Cdd:PRK12316 678 RALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDpAKLVELINREGVDTLHFVPSML 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 234 yqQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATT----VVEITDA----------- 298
Cdd:PRK12316 758 --QAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVThwtcVEEGGDSvpigrpianla 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 299 --ILNSDSAVLPVGVMmpeskmeistdGELIIWGKNVMRGYLGLPQENAAKLLRRE-DEAFRGYRTGDLG-YEA-GLIYC 373
Cdd:PRK12316 836 cyILDANLEPVPVGVL-----------GELYLAGRGLARGYHGRPGLTAERFVPSPfVAGERMYRTGDLArYRAdGVIEY 904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 374 QGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLmkscgSVLRIAAFCVTDMA----PDTIKTSLSKVVPHYMVPS 449
Cdd:PRK12316 905 AGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGKQLVGYVVLESEggdwREALKAHLAASLPEYMVPA 979
|
490 500
....*....|....*....|...
gi 658547412 450 QIIVKDALPLNPNGKIDRKLLDA 472
Cdd:PRK12316 980 QWLALERLPLTPNGKLDRKALPA 1002
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
22-470 |
7.02e-59 |
|
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: 201.35 E-value: 7.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQRYqRCQPV-AGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLR 100
Cdd:cd17646 10 RTPDAPAVVDEGRTLTYRELDERANRLAHLL-RARGVgPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 101 EIchLASA---------------PYYYDVATRQFIATGE-----PGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHF 160
Cdd:cd17646 89 YM--LADAgpavvlttadlaarlPAGGDVALLGDEALAAppatpPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 161 MKWVSQDFSL-PEKPVLMNhAVFSFDLSLIPLLANLAMGGHIVLnAKEDIQKE-NWLERL-KSNAVSAWVSTPSFAYQQL 237
Cdd:cd17646 167 LLWMQDEYPLgPGDRVLQK-TPLSFDVSVWELFWPLVAGARLVV-ARPGGHRDpAYLAALiREHGVTTCHFVPSMLRVFL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 238 LSPQfnSEYLPALNVFIFIGEVLNKALVKQLRRRFPqAKIINSYGPTEATIATTVVEITDAilnSDSAVLPVGVMMPESK 317
Cdd:cd17646 245 AEPA--AGSCASLRRVFCSGEALPPELAARFLALPG-AELHNLYGPTEAAIDVTHWPVRGP---AETPSVPIGRPVPNTR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 318 MEISTD----------GELIIWGKNVMRGYLGLPQENAAKLLrreDEAF----RGYRTGDLGY--EAGLIYCQGRNDSQV 381
Cdd:cd17646 319 LYVLDDalrpvpvgvpGELYLGGVQLARGYLGRPALTAERFV---PDPFgpgsRMYRTGDLARwrPDGALEFLGRSDDQV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 382 KLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVlRIAAFCV-----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDA 456
Cdd:cd17646 396 KIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAA-RLVGYVVpaagaAGPDTAALRAHLAERLPEYMVPAAFVVLDA 474
|
490
....*....|....
gi 658547412 457 LPLNPNGKIDRKLL 470
Cdd:cd17646 475 LPLTANGKLDRAAL 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
22-472 |
6.36e-58 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 207.32 E-value: 6.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAvtdwAQRYQRCQPVAG-TPVVLYG---HQQAEFAVAIYSCLLHNIPYIPVDCIYPQE 97
Cdd:PRK12467 1586 ATPEAVALVFGEQELTYGELNRR----ANRLAHRLIALGvGPEVLVGiavERSLEMVVGLLAILKAGGAYVPLDPEYPRE 1661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 98 RL---------------REIC-HLASAPYYYDVATRQFIATGE------PGKVLEEQDLAYIMFTSGSTGKPKGVQIGRE 155
Cdd:PRK12467 1662 RLaymiedsgiellltqSHLQaRLPLPDGLRSLVLDQEDDWLEgysdsnPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHG 1741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 156 SVWHFMKWVSQDFSL-PEKPVLMNHAvFSFDLSLIPLLANLAMGGHIVLNA-KEDIQKENWLERLKSNAVSAWVSTPSfA 233
Cdd:PRK12467 1742 ALVNRLCATQEAYQLsAADVVLQFTS-FAFDVSVWELFWPLINGARLVIAPpGAHRDPEQLIQLIERQQVTTLHFVPS-M 1819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 234 YQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATTVVEITDAILNSDSAVlPVGVMM 313
Cdd:PRK12467 1820 LQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDSV-PIGQPI 1898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 314 PESK----------MEISTDGELIIWGKNVMRGYLGLPQENAAKLLRREDEAF--RGYRTGDLG-YEA-GLIYCQGRNDS 379
Cdd:PRK12467 1899 ANLStyildaslnpVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTVgsRLYRTGDLArYRAdGVIEYLGRIDH 1978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 380 QVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLriAAFCVTDMAP------------DTIKTSLSKVVPHYMV 447
Cdd:PRK12467 1979 QVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQL--VAYVVPTDPGlvdddeaqvalrAILKNHLKASLPEYMV 2056
|
490 500
....*....|....*....|....*
gi 658547412 448 PSQIIVKDALPLNPNGKIDRKLLDA 472
Cdd:PRK12467 2057 PAHLVFLARMPLTPNGKLDRKALPA 2081
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
24-470 |
1.55e-56 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 203.08 E-value: 1.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYqrCQPVAGtPVVLYG---HQQAEFAVAIYSCLLHNIPYIPVDCIYPQERL- 99
Cdd:PRK12467 3109 PEAPALVFGDQQLSYAELNRRANRLAHRL--IAIGVG-PDVLVGvavERSVEMIVALLAVLKAGGAYVPLDPEYPRERLa 3185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 100 ---------------REICHLASAPYYYDVATRQFIATGE----PGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHF 160
Cdd:PRK12467 3186 ymiedsgvkllltqaHLLEQLPAPAGDTALTLDRLDLNGYsennPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANH 3265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 161 MKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWLERLKSNAVSAWVSTPSfAYQQLLSP 240
Cdd:PRK12467 3266 LCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPA-YLQQFAED 3344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 241 QFNSEYlPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATTVVEIT-DAIlnSDSAVLPVGVMMPESKME 319
Cdd:PRK12467 3345 AGGADC-ASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGgDAV--CEAPYAPIGRPVAGRSIY 3421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 320 I----------STDGELIIWGKNVMRGYLGLPQENAAKLLRR--EDEAFRGYRTGDLG-YEA-GLIYCQGRNDSQVKLNG 385
Cdd:PRK12467 3422 VldgqlnpvpvGVAGELYIGGVGLARGYHQRPSLTAERFVADpfSGSGGRLYRTGDLArYRAdGVIEYLGRIDHQVKIRG 3501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 386 YRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLriAAFCVTDmAP-----DTIKTSLSKVVPHYMVPSQIIVKDALPLN 460
Cdd:PRK12467 3502 FRIELGEIEARLLQHPSVREAVVLARDGAGGKQL--VAYVVPA-DPqgdwrETLRDHLAASLPDYMVPAQLLVLAAMPLG 3578
|
490
....*....|
gi 658547412 461 PNGKIDRKLL 470
Cdd:PRK12467 3579 PNGKVDRKAL 3588
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
23-470 |
6.84e-56 |
|
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: 192.65 E-value: 6.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 23 SPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLREI 102
Cdd:cd17644 13 TPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 103 CHlasapyyyDVATRQFIATGEpgkvleeqDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVF 182
Cdd:cd17644 93 LE--------DAQISVLLTQPE--------NLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 183 SFDLSLIPLLANLAMGGHIVLNAKEDIQK-ENWLERLKSNAVSAWVSTPsfAYQQLLSPQFNSEYLP---ALNVFIFIGE 258
Cdd:cd17644 157 AFDVAAEEIYVTLLSGATLVLRPEEMRSSlEDFVQYIQQWQLTVLSLPP--AYWHLLVLELLLSTIDlpsSLRLVIVGGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 259 VLNKALVKQLR---RRFPQakIINSYGPTEATIATTVVEITDA--------------------ILNSDSAVLPVGVMmpe 315
Cdd:cd17644 235 AVQPELVRQWQknvGNFIQ--LINVYGPTEATIAATVCRLTQLternitsvpigrpiantqvyILDENLQPVPVGVP--- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 316 skmeistdGELIIWGKNVMRGYLGLPQENAAKLLR---REDEAFRGYRTGDLG-YEA-GLIYCQGRNDSQVKLNGYRIEI 390
Cdd:cd17644 310 --------GELHIGGVGLARGYLNRPELTAEKFIShpfNSSESERLYKTGDLArYLPdGNIEYLGRIDNQVKIRGFRIEL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 391 NEIENRLLAMSGINEAVVLPLMKSCGSVlRIAAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKID 466
Cdd:cd17644 382 GEIEAVLSQHNDVKTAVVIVREDQPGNK-RLVAYIVphyeESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKID 460
|
....
gi 658547412 467 RKLL 470
Cdd:cd17644 461 RRAL 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
22-470 |
9.56e-56 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 200.95 E-value: 9.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLRE 101
Cdd:PRK12316 4563 MTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAY 4642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 102 ICH-------------LASAPYYYDVATRQFIATGE--------PGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHF 160
Cdd:PRK12316 4643 MMEdsgaallltqshlLQRLPIPDGLASLALDRDEDwegfpahdPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNH 4722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 161 MKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWLERLKSNAVSAWVSTPSfAYQQLLSP 240
Cdd:PRK12316 4723 LHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPV-YLQQLAEH 4801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 241 QFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATTVVEITDAILnSDSAVLPVGVMMPESK--- 317
Cdd:PRK12316 4802 AERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDA-CGAAYMPIGTPLGNRSgyv 4880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 318 -------MEISTDGELIIWGKNVMRGYLGLPQENAAKLLRR--EDEAFRGYRTGDLG-YEA-GLIYCQGRNDSQVKLNGY 386
Cdd:PRK12316 4881 ldgqlnpLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfGAPGGRLYRTGDLArYRAdGVIDYLGRVDHQVKIRGF 4960
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 387 RIEINEIENRLLAMSGINEAVVLPLMKSCGSVLriAAFCVTD---MAPDT---------IKTSLSKVVPHYMVPSQIIVK 454
Cdd:PRK12316 4961 RIELGEIEARLREHPAVREAVVIAQEGAVGKQL--VGYVVPQdpaLADADeaqaelrdeLKAALRERLPEYMVPAHLVFL 5038
|
490
....*....|....*.
gi 658547412 455 DALPLNPNGKIDRKLL 470
Cdd:PRK12316 5039 ARMPLTPNGKLDRKAL 5054
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
22-472 |
1.21e-55 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 200.57 E-value: 1.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLR- 100
Cdd:PRK12316 2015 RAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAy 2094
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 101 --EICHLASAPYYYDVATRQFIATG------------------EPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHF 160
Cdd:PRK12316 2095 mlEDSGAALLLTQRHLLERLPLPAGvarlpldrdaewadypdtAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAH 2174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 161 MKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWLERLKSNAVSAWVSTPSFaYQQLLSP 240
Cdd:PRK12316 2175 CQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVY-LQQLAEH 2253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 241 QFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIaTTVVEITDAILNSDSAVLPVGVMMPESKMEI 320
Cdd:PRK12316 2254 AERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVV-TPLLWKCRPQDPCGAAYVPIGRALGNRRAYI 2332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 321 ----------STDGELIIWGKNVMRGYLGLPQENAAKLLRREDEAF--RGYRTGDL--GYEAGLIYCQGRNDSQVKLNGY 386
Cdd:PRK12316 2333 ldadlnllapGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASgeRLYRTGDLarYRADGVVEYLGRIDHQVKIRGF 2412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 387 RIEINEIENRLLAMSGINEAVVLPLMKSCGSvlRIAAFCVTDMA----PDTIKTSLSKVVPHYMVPSQIIVKDALPLNPN 462
Cdd:PRK12316 2413 RIELGEIEARLQAHPAVREAVVVAQDGASGK--QLVAYVVPDDAaedlLAELRAWLAARLPAYMVPAHWVVLERLPLNPN 2490
|
490
....*....|
gi 658547412 463 GKIDRKLLDA 472
Cdd:PRK12316 2491 GKLDRKALPK 2500
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
87-470 |
1.10e-54 |
|
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: 189.15 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 87 YIPVDCIYPQERLREICHlasapyyyDVATRQFIAtgepgkvlEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQ 166
Cdd:cd17648 65 YVPIDPSYPDERIQFILE--------DTGARVVIT--------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 167 DFSL--PEKPVLMNHAVFSFDLSLIPLLANLaMGGH--IVLNAKEDIQKENWLERLKSNAVSAWVSTPSfayqqLLSpQF 242
Cdd:cd17648 129 RYFGrdNGDEAVLFFSNYVFDFFVEQMTLAL-LNGQklVVPPDEMRFDPDRFYAYINREKVTYLSGTPS-----VLQ-QY 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 243 NSEYLPALNVFIFIGEVLNKALVKQLRRRFPqAKIINSYGPTEATIATTVVE-----------------ITDAILNSDSA 305
Cdd:cd17648 202 DLARLPHLKRVDAAGEEFTAPVFEKLRSRFA-GLIINAYGPTETTVTNHKRFfpgdqrfdkslgrpvrnTKCYVLNDAMK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 306 VLPVGVMmpeskmeistdGELIIWGKNVMRGYLGLPQENAAKLL----RREDEAFRG-----YRTGDL---GYEAGLIYC 373
Cdd:cd17648 281 RVPVGAV-----------GELYLGGDGVARGYLNRPELTAERFLpnpfQTEQERARGrnarlYKTGDLvrwLPSGELEYL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 374 qGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLRIAAFCVTDMAPDT-------IKTSLSKVVPHYM 446
Cdd:cd17648 350 -GRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQKYLVGYYLPEPghvpesdLLSFLRAKLPRYM 428
|
410 420
....*....|....*....|....
gi 658547412 447 VPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd17648 429 VPARLVRLEGIPVTINGKLDVRAL 452
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
24-470 |
2.10e-54 |
|
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: 188.15 E-value: 2.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLReic 103
Cdd:cd17645 12 PDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIA--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 104 hlasapyyydvatrqFIATGEPGKVLEEQ--DLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAV 181
Cdd:cd17645 89 ---------------YMLADSSAKILLTNpdDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 182 FSFDLSLIPLLANLAMGG--HIVLNA-KEDIQKENwlERLKSNAVS-AWVSTPsfayqqlLSPQFNSEYLPALNVFIFIG 257
Cdd:cd17645 154 FSFDASAWEIFPHLTAGAalHVVPSErRLDLDALN--DYFNQEGITiSFLPTG-------AAEQFMQLDNQSLRVLLTGG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 258 EVLNKALVKQLrrrfpqaKIINSYGPTEATIATTVVEITDA----------------ILNSDSAVLPVGVMmpeskmeis 321
Cdd:cd17645 225 DKLKKIERKGY-------KLVNNYGPTENTVVATSFEIDKPyanipigkpidntrvyILDEALQLQPIGVA--------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 322 tdGELIIWGKNVMRGYLGLPQENAAKLLRR-EDEAFRGYRTGDLG--YEAGLIYCQGRNDSQVKLNGYRIEINEIENRLL 398
Cdd:cd17645 289 --GELCIAGEGLARGYLNRPELTAEKFIVHpFVPGERMYRTGDLAkfLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLM 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658547412 399 AMSGINEAVVLPlMKSCGSVLRIAAFCV--TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd17645 367 NHPLIELAAVLA-KEDADGRKYLVAYVTapEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
22-472 |
1.39e-50 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 185.93 E-value: 1.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLR- 100
Cdd:PRK12316 3069 RTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAy 3148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 101 ----------------EICHLASAPYYYDVATRQFIATGEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWV 164
Cdd:PRK12316 3149 mledsgaqlllsqshlRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWM 3228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 165 SQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWLERL-KSNAVSAWVSTPSFAYQQLLSPQFN 243
Cdd:PRK12316 3229 QQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELiNSEGVDVLHAYPSMLQAFLEEEDAH 3308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 244 SeyLPALNVFIFIGEVLNKALVKQLrrrFPQAKIINSYGPTEATIATTVVEITDailnSDSAVLPVGVMMPESKMEISTD 323
Cdd:PRK12316 3309 R--CTSLKRIVCGGEALPADLQQQV---FAGLPLYNLYGPTEATITVTHWQCVE----EGKDAVPIGRPIANRACYILDG 3379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 324 ----------GELIIWGKNVMRGYLGLPQENAAKLLRRE-DEAFRGYRTGDLG-YEA-GLIYCQGRNDSQVKLNGYRIEI 390
Cdd:PRK12316 3380 slepvpvgalGELYLGGEGLARGYHNRPGLTAERFVPDPfVPGERLYRTGDLArYRAdGVIEYIGRVDHQVKIRGFRIEL 3459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 391 NEIENRLLAMSGINEAVVLPLMKScgsvlRIAAFCVTDM----APDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKID 466
Cdd:PRK12316 3460 GEIEARLLEHPWVREAVVLAVDGR-----QLVAYVVPEDeagdLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLD 3534
|
....*.
gi 658547412 467 RKLLDA 472
Cdd:PRK12316 3535 RKALPR 3540
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
23-470 |
1.60e-49 |
|
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: 176.13 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 23 SPQQLAISGSDEALSWLQLSAAVTDWAqRYQRCQPV-AGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLRE 101
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLA-RFLREKGVkKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 102 IC------------HLASAPYY--------YDVATRQfiATGEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFM 161
Cdd:cd17656 80 IMldsgvrvvltqrHLKSKLSFnkstilleDPSISQE--DTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 162 KWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGG--HIVLN-AKEDIQKENwlERLKSNAVSAwVSTPSFAYQQLL 238
Cdd:cd17656 158 HFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGtlYIIREeTKRDVEQLF--DLVKRHNIEV-VFLPVAFLKFIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 239 SP-QFNSEYLPALNVFIFIGE--VLNKALVKQLRRRfpQAKIINSYGPTEATIATT------------------VVEITD 297
Cdd:cd17656 235 SErEFINRFPTCVKHIITAGEqlVITNEFKEMLHEH--NVHLHNHYGPSETHVVTTytinpeaeipelppigkpISNTWI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 298 AILNSDSAVLPVGVMmpeskmeistdGELIIWGKNVMRGYLGLPQENAAKLLRRE-DEAFRGYRTGDLG--YEAGLIYCQ 374
Cdd:cd17656 313 YILDQEQQLQPQGIV-----------GELYISGASVARGYLNRQELTAEKFFPDPfDPNERMYRTGDLAryLPDGNIEFL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 375 GRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLRIAAFCVTDMAPDT-IKTSLSKVVPHYMVPSQIIV 453
Cdd:cd17656 382 GRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISqLREYLAKQLPEYMIPSFFVP 461
|
490
....*....|....*..
gi 658547412 454 KDALPLNPNGKIDRKLL 470
Cdd:cd17656 462 LDQLPLTPNGKVDRKAL 478
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
31-383 |
8.41e-49 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 172.50 E-value: 8.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 31 GSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLREICHLASA-- 108
Cdd:pfam00501 17 GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAkv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 109 ------------------------PYYYDVA----TRQFIATGEPGKVLEEQ-------DLAYIMFTSGSTGKPKGVQIG 153
Cdd:pfam00501 97 litddalkleellealgklevvklVLVLDRDpvlkEEPLPEEAKPADVPPPPppppdpdDLAYIIYTSGTTGKPKGVMLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 154 RESVWHFMKWVSQ----DFSLPEKPVLMNHAVFSFDLSLIP-LLANLAMGGHIVLNAKEDIQK-ENWLERLKSNAVSAWV 227
Cdd:pfam00501 177 HRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPGFPALDpAALLELIERYKVTVLY 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 228 STPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAkIINSYGPTEATIATTVVEITDAILNSDSAvl 307
Cdd:pfam00501 257 GVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVTTPLPLDEDLRSLGS-- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 308 pVGVMMPESKMEISTD-----------GELIIWGKNVMRGYLGLPQENAAKLLrredeAFRGYRTGDLGY--EAGLIYCQ 374
Cdd:pfam00501 334 -VGRPLPGTEVKIVDDetgepvppgepGELCVRGPGVMKGYLNDPELTAEAFD-----EDGWYRTGDLGRrdEDGYLEIV 407
|
....*....
gi 658547412 375 GRNDSQVKL 383
Cdd:pfam00501 408 GRKKDQIKL 416
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
22-470 |
3.91e-48 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 178.44 E-value: 3.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERL-- 99
Cdd:PRK05691 1143 QTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLay 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 100 --------------REICHLASAPYYYDVATRQFIATG----EPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFM 161
Cdd:PRK05691 1223 mladsgvellltqsHLLERLPQAEGVSAIALDSLHLDSwpsqAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERL 1302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 162 KWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKEnwlERLKSNAVSAWVSTPSFAyQQLLSpQ 241
Cdd:PRK05691 1303 QWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDP---QRIAELVQQYGVTTLHFV-PPLLQ-L 1377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 242 FNSEYLPA----LNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATT--VVEITDA---------------IL 300
Cdd:PRK05691 1378 FIDEPLAAactsLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVThwQCQAEDGerspigrplgnvlcrVL 1457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 301 NSDSAVLPVGVMmpeskmeistdGELIIWGKNVMRGYLGLPQENAAKLLRRE--DEAFRGYRTGDLG---YEAGLIYCqG 375
Cdd:PRK05691 1458 DAELNLLPPGVA-----------GELCIGGAGLARGYLGRPALTAERFVPDPlgEDGARLYRTGDRArwnADGALEYL-G 1525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 376 RNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLrIAAFCVT---DMAPDTIKTSLSKVVPHYMVPSQII 452
Cdd:PRK05691 1526 RLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQL-VGYYTGEagqEAEAERLKAALAAELPEYMVPAQLI 1604
|
490
....*....|....*...
gi 658547412 453 VKDALPLNPNGKIDRKLL 470
Cdd:PRK05691 1605 RLDQMPLGPSGKLDRRAL 1622
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
133-466 |
5.18e-48 |
|
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: 168.23 E-value: 5.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKe 212
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 213 nWLERLKSNAVSAWVSTPSFaYQQLL-SPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPqAKIINSYGPTEATIATT 291
Cdd:cd04433 80 -ALELIEREKVTILLGVPTL-LARLLkAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG-IKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 292 VVEITDAILNSDSAVLPVgvmmPESKMEI-STD---------GELIIWGKNVMRGYLGLPQENAakllrredEAFRG--Y 359
Cdd:cd04433 157 TGPPDDDARKPGSVGRPV----PGVEVRIvDPDggelppgeiGELVVRGPSVMKGYWNNPEATA--------AVDEDgwY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 360 RTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPL-MKSCGSvlRIAAFCVT----DMAPD 432
Cdd:cd04433 225 RTGDLGRldEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVpDPEWGE--RVVAVVVLrpgaDLDAE 302
|
330 340 350
....*....|....*....|....*....|....
gi 658547412 433 TIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKID 466
Cdd:cd04433 303 ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
22-472 |
1.13e-45 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 171.50 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTD--WAQRYQRCQPvaGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERL 99
Cdd:PRK05691 2200 RTPQAPALTFAGQTLSYAELDARANRlaRALRERGVGP--QVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERL 2277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 100 REICHLASAPYYYDVAtRQFIATGE-PGKV----LEE-------------------QDLAYIMFTSGSTGKPKGVQIGRE 155
Cdd:PRK05691 2278 HYMIEDSGIGLLLSDR-ALFEALGElPAGVarwcLEDdaaalaaysdaplpflslpQHQAYLIYTSGSTGKPKGVVVSHG 2356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 156 SVWHFMKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWLERLKSNAVSAWVSTPSFAYQ 235
Cdd:PRK05691 2357 EIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQ 2436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 236 --QLLSPQfnSEYLPaLNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEaTIATTVVEITDAILNSDSAVLPVGVMM 313
Cdd:PRK05691 2437 laQWLAGQ--GEQLP-VRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTE-TVVMPLACLAPEQLEEGAASVPIGRVV 2512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 314 PESKMEISTD----------GELIIWGKNVMRGYLGLPQENAAKLLRR--EDEAFRGYRTGDLGYEA--GLIYCQGRNDS 379
Cdd:PRK05691 2513 GARVAYILDAdlalvpqgatGELYVGGAGLAQGYHDRPGLTAERFVADpfAADGGRLYRTGDLVRLRadGLVEYVGRIDH 2592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 380 QVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLriAAFCVTDMAP----------DTIKTSLSKVVPHYMVPS 449
Cdd:PRK05691 2593 QVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQL--AGYLVSAVAGqddeaqaalrEALKAHLKQQLPDYMVPA 2670
|
490 500
....*....|....*....|...
gi 658547412 450 QIIVKDALPLNPNGKIDRKLLDA 472
Cdd:PRK05691 2671 HLILLDSLPLTANGKLDRRALPA 2693
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
122-470 |
1.97e-43 |
|
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: 159.14 E-value: 1.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 122 TGEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHI 201
Cdd:cd05922 107 ASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 202 VLNAKEDIQKENWlERLKSNAVSAWVSTPSFaYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSY 281
Cdd:cd05922 187 VLTNDGVLDDAFW-EDLREHGATGLAGVPST-YAMLTRLGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMY 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 282 GPTEATIATTVVEiTDAILNSDSAVlpvGVMMPESKMEISTD----------GELIIWGKNVMRGYLGLPQEnaaklLRR 351
Cdd:cd05922 265 GQTEATRRMTYLP-PERILEKPGSI---GLAIPGGEFEILDDdgtptppgepGEIVHRGPNVMKGYWNDPPY-----RRK 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 352 EDEAFRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLRIAAFCVTDM 429
Cdd:cd05922 336 EGRGGGVLHTGDLARrdEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKI 415
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 658547412 430 APDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05922 416 DPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
22-472 |
4.23e-43 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 163.80 E-value: 4.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAvtdwAQRYQRCQPVAGT----PVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQE 97
Cdd:PRK05691 3732 AHPQRIAASCLDQQWSYAELNRA----ANRLGHALRAAGVgvdqPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQ 3807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 98 RLREICHLASAPY----------------------------YYDVATRQfIATGEPGKVLEEQDLAYIMFTSGSTGKPKG 149
Cdd:PRK05691 3808 RLQRIIELSRTPVlvcsaacreqaralldelgcanrprllvWEEVQAGE-VASHNPGIYSGPDNLAYVIYTSGSTGLPKG 3886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 150 VQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGH--IVLNA-KEDIQkeNWLERLKSNAVSAW 226
Cdd:PRK05691 3887 VMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARveIVPNAiAHDPQ--GLLAHVQAQGITVL 3964
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 227 VSTPSFAYQQLLSPQfnsEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATTVVEITDAilNSDSAV 306
Cdd:PRK05691 3965 ESVPSLIQGMLAEDR---QALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLA--STRGSY 4039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 307 LPVGVMMPESKMEISTD----------GELIIWGKNVMRGYLGLPQENAAKLLRREDEAF--RGYRTGDLGYEA--GLIY 372
Cdd:PRK05691 4040 LPIGSPTDNNRLYLLDEalelvplgavGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPgeRLYRTGDLARRRsdGVLE 4119
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 373 CQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVL---RIAAFCVTDMAP--DTIKTSLSKVVPHYMV 447
Cdd:PRK05691 4120 YVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLvgyLVPHQTVLAQGAllERIKQRLRAELPDYMV 4199
|
490 500
....*....|....*....|....*
gi 658547412 448 PSQIIVKDALPLNPNGKIDRKLLDA 472
Cdd:PRK05691 4200 PLHWLWLDRLPLNANGKLDRKALPA 4224
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
22-470 |
6.12e-43 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 162.91 E-value: 6.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 22 ASPQQLAISGSDEALSWLQLSAAVTDWAQ--RYQRCQPvaGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERL 99
Cdd:PRK10252 470 KTPDAPALADARYQFSYREMREQVVALANllRERGVKP--GDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 100 REIchLASA----------------------PYYYDVAtrQFIATGEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESV 157
Cdd:PRK10252 548 KMM--LEDArpsllittadqlprfadvpdltSLCYNAP--LAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 158 WHFMKWVSQDFSLPEKPVLMNHAVFSFDLSL----IPLLAnlamGGHIVLnAKEDIQKE-NWLERLksnaVSAW-VSTPS 231
Cdd:PRK10252 624 VNRLLWMQNHYPLTADDVVLQKTPCSFDVSVweffWPFIA----GAKLVM-AEPEAHRDpLAMQQF----FAEYgVTTTH 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 232 F------AYQQLLSPQFNSEYLPAL-NVFIfIGEvlnkALVKQLRRRFPQ---AKIINSYGPTEATiattvVEIT----- 296
Cdd:PRK10252 695 FvpsmlaAFVASLTPEGARQSCASLrQVFC-SGE----ALPADLCREWQQltgAPLHNLYGPTEAA-----VDVSwypaf 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 297 -DAILNSDSAVLPVGVMMPESKMEISTD----------GELIIWGKNVMRGYLGLPQENAAKLLrreDEAF----RGYRT 361
Cdd:PRK10252 765 gEELAAVRGSSVPIGYPVWNTGLRILDArmrpvppgvaGDLYLTGIQLAQGYLGRPDLTASRFI---ADPFapgeRMYRT 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 362 GDLG--YEAGLI-YCqGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLM-----KSCGSVLRIAAFCV--TDMAP 431
Cdd:PRK10252 842 GDVArwLDDGAVeYL-GRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVinqaaATGGDARQLVGYLVsqSGLPL 920
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 658547412 432 DT--IKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK10252 921 DTsaLQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
60-470 |
1.83e-35 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 138.03 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 60 GTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERlreichlasAPYYYDVAT-RQFIATGEPGKVLEEQDLAYIM 138
Cdd:cd17647 45 GDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR---------QNIYLGVAKpRGLIVIRAAGVVVGPDSNPTLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 139 FTSGSTGKPKGVqIGRE-SVWHFMKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDI----QKEN 213
Cdd:cd17647 116 FTSGSEGIPKGV-LGRHfSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIgtpgRLAE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 214 WLERLKsnavsAWVSTPSFAYQQLLSPQFNSEYLPALNVFiFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATTVV 293
Cdd:cd17647 195 WMAKYG-----ATVTHLTPAMGQLLTAQATTPFPKLHHAF-FVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 294 EIT-----DAILNSDSAVLPVGVMMPESKM------------EISTDGELIIWGKNVMRGYLGLPQENAAKLLRR----- 351
Cdd:cd17647 269 EVPsrssdPTFLKNLKDVMPAGRGMLNVQLlvvnrndrtqicGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvep 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 352 -----EDEAF-------------RGYRTGDLG--YEAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLpL 411
Cdd:cd17647 349 dhwnyLDKDNnepwrqfwlgprdRLYRTGDLGryLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITL-V 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 412 MKSCGSVLRIAAFCVTDMAP-------------------------------DTIKTSLSKVVPHYMVPSQIIVKDALPLN 460
Cdd:cd17647 428 RRDKDEEPTLVSYIVPRFDKpddesfaqedvpkevstdpivkgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLN 507
|
490
....*....|
gi 658547412 461 PNGKIDRKLL 470
Cdd:cd17647 508 PNGKVDKPKL 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
23-467 |
7.64e-34 |
|
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: 132.35 E-value: 7.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 23 SPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDciypqERL--R 100
Cdd:cd17631 8 HPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN-----FRLtpP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 101 EICHLasapyyydvatrqfIATGEPGKVLEeqDLAYIMFTSGSTGKPKGVQIG-RESVWHFMKWVSqDFSLPEKPVLMNH 179
Cdd:cd17631 83 EVAYI--------------LADSGAKVLFD--DLALLMYTSGTTGRPKGAMLThRNLLWNAVNALA-ALDLGPDDVLLVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 180 A-VFSFDLSLIPLLANLAMGGHIVLNAKEDIqkENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGE 258
Cdd:cd17631 146 ApLFHIGGLGVFTLPTLLRGGTVVILRKFDP--ETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 259 VLNKALVKQLRRRFPqaKIINSYGPTEATIATTVVEITDA-----------------ILNSDSAVLPVGvmmpeskmEIs 321
Cdd:cd17631 224 PMPERLLRALQARGV--KFVQGYGMTETSPGVTFLSPEDHrrklgsagrpvffvevrIVDPDGREVPPG--------EV- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 322 tdGELIIWGKNVMRGYLGLPQENAakllrredEAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRL 397
Cdd:cd17631 293 --GEIVVRGPHVMAGYWNRPEATA--------AAFRDgwFHTGDLGRldEDGYLYIVDRKKDMIISGGENVYPAEVEDVL 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658547412 398 LAMSGINEAVV--LPLMKsCGSVlrIAAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDR 467
Cdd:cd17631 363 YEHPAVAEVAVigVPDEK-WGEA--VVAVVVprpgAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
65-470 |
1.12e-33 |
|
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: 131.83 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 65 LYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLREI------------CHLASAPYYYDVATRQF-IATGEPgkvlee 131
Cdd:cd17654 46 LRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVmkkchvsyllqnKELDNAPLSFTPEHRHFnIRTDEC------ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 132 qdLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQK 211
Cdd:cd17654 120 --LAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 212 ENWLERL--KSNAVSAWVSTPSFaYQQLLSPQFNSEYLPA---LNVFIFIGEVL-NKALVKQLRRRFPQAKIINSYGPTE 285
Cdd:cd17654 198 PSKLADIlfKRHRITVLQATPTL-FRRFGSQSIKSTVLSAtssLRVLALGGEPFpSLVILSSWRGKGNRTRIFNIYGITE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 286 ATIATTVVEITDailnsDSAVLPVGVMMPESKMEI------STDGELIIWGKN---VMRGYLGLPQENAakllrredeaf 356
Cdd:cd17654 277 VSCWALAYKVPE-----EDSPVQLGSPLLGTVIEVrdqngsEGTGQVFLGGLNrvcILDDEVTVPKGTM----------- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 357 rgYRTGDL-GYEAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKScgsvlRIAAFCVTDMAPDTIK 435
Cdd:cd17654 341 --RATGDFvTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQ-----RLIAFIVGESSSSRIH 413
|
410 420 430
....*....|....*....|....*....|....*.
gi 658547412 436 TSLSK-VVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd17654 414 KELQLtLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
72-465 |
1.12e-32 |
|
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: 129.64 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 72 EFAVAIYSCLLHNIPYIPVDCIYPQ----------------------ERLREICHLA-----------SAPYYYDVATRQ 118
Cdd:cd05911 47 YYPPVFLGCLFAGGIFSAANPIYTAdelahqlkiskpkviftdpdglEKVKEAAKELgpkdkiivlddKPDGVLSIEDLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 119 FIATGEPGKVLEEQ------DLAYIMFTSGSTGKPKGVQIGRESV--WHFMKWVSQDFSLPEKPVLMNHAVFSFDLSLIP 190
Cdd:cd05911 127 SPTLGEEDEDLPPPlkdgkdDTAAILYSSGTTGLPKGVCLSHRNLiaNLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 191 LLANLAMGGHIVLNAKEDIqkENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRR 270
Cdd:cd05911 207 TLASLLNGATVIIMPKFDS--ELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAK 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 271 RFPQAKIINSYGPTEATIATTVVEITDAILNSdsavlpVGVMMPESKMEISTD-----------GELIIWGKNVMRGYLG 339
Cdd:cd05911 285 RFPNATIKQGYGMTETGGILTVNPDGDDKPGS------VGRLLPNVEAKIVDDdgkdslgpnepGEICVRGPQVMKGYYN 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 340 LPQENAAklLRREDeafrG-YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMK-SC 415
Cdd:cd05911 359 NPEATKE--TFDED----GwLHTGDIGYfdEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDeVS 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 658547412 416 GSVLRiaAFCV----TDMAPDTIKTSL-SKVVPHYMVPSQIIVKDALPLNPNGKI 465
Cdd:cd05911 433 GELPR--AYVVrkpgEKLTEKEVKDYVaKKVASYKQLRGGVVFVDEIPKSASGKI 485
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
10-470 |
2.51e-31 |
|
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: 125.75 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 10 LQDFLRAALCDPasPQQLAISGSDEALSWLQLSAAVTDWAQRYQR--CQPvaGTPVVLYGHQQAEFAVAIYSCLLHNIPY 87
Cdd:cd05936 1 LADLLEEAARRF--PDKTALIFMGRKLTYRELDALAEAFAAGLQNlgVQP--GDRVALMLPNCPQFPIAYFGALKAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 88 IPVDCIYPQERLREICHLASAPYYYDVATRQ-FIATGEPGK---VLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFM-- 161
Cdd:cd05936 77 VPLNPLYTPRELEHILNDSGAKALIVAVSFTdLLAAGAPLGervALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANAlq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 162 -KWVSQDFSLPEKPVL----MNHaVFSFDLSlipLLANLAMGGHIVL-------NAKEDIQKENwlerlksnaVSAWVST 229
Cdd:cd05936 157 iKAWLEDLLEGDDVVLaalpLFH-VFGLTVA---LLLPLALGATIVLiprfrpiGVLKEIRKHR---------VTIFPGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 230 PSFaYQQLL-SPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFpQAKIINSYGPTEATIATTVVEITD----------- 297
Cdd:cd05936 224 PTM-YIALLnAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVAVNPLDGprkpgsigipl 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 298 -----AILNSDSAVLPVGvmmpeskmeisTDGELIIWGKNVMRGYLGLPQENAakllrredEAFRG--YRTGDLGY--EA 368
Cdd:cd05936 302 pgtevKIVDDDGEELPPG-----------EVGELWVRGPQVMKGYWNRPEETA--------EAFVDgwLRTGDIGYmdED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 369 GLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVV--LPLMKScGSVlrIAAFCV--TDMAPDT--IKTSLSKVV 442
Cdd:cd05936 363 GYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVvgVPDPYS-GEA--VKAFVVlkEGASLTEeeIIAFCREQL 439
|
490 500
....*....|....*....|....*...
gi 658547412 443 PHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05936 440 AGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
139-470 |
6.25e-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: 127.10 E-value: 6.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 139 FTSGSTGKPKGVqIGRE-SVWHFMKWVSQDFSLPEkpvlmnHAVFSFdLSLIP-------LLANLAMGGHIVLNAKEDIQ 210
Cdd:TIGR03443 422 FTSGSEGIPKGV-LGRHfSLAYYFPWMAKRFGLSE------NDKFTM-LSGIAhdpiqrdMFTPLFLGAQLLVPTADDIG 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 211 KE----NWLERLKsnavsAWVS--TPsfAYQQLLSPQfNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPT 284
Cdd:TIGR03443 494 TPgrlaEWMAKYG-----ATVThlTP--AMGQLLSAQ-ATTPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTT 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 285 EATIATTVVEITDaiLNSDSA-------VLPVGVMMPESKM---------------EIstdGELIIWGKNVMRGYLGLPQ 342
Cdd:TIGR03443 566 ETQRAVSYFEIPS--RSSDSTflknlkdVMPAGKGMKNVQLlvvnrndrtqtcgvgEV---GEIYVRAGGLAEGYLGLPE 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 343 ENAAKLLR----------REDEAF-------------RGYRTGDLG-Y-EAGLIYCQGRNDSQVKLNGYRIEINEI---- 393
Cdd:TIGR03443 641 LNAEKFVNnwfvdpshwiDLDKENnkperefwlgprdRLYRTGDLGrYlPDGNVECCGRADDQVKIRGFRIELGEIdthl 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 394 -------ENRLLAMSGINEAVVL-----PLMKSCG-SVLRIAAFCVTDMAP------------DTIKTSLSKVVPHYMVP 448
Cdd:TIGR03443 721 sqhplvrENVTLVRRDKDEEPTLvsyivPQDKSDElEEFKSEVDDEESSDPvvkglikyrkliKDIREYLKKKLPSYAIP 800
|
410 420
....*....|....*....|..
gi 658547412 449 SQIIVKDALPLNPNGKIDRKLL 470
Cdd:TIGR03443 801 TVIVPLKKLPLNPNGKVDKPAL 822
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
36-470 |
4.35e-30 |
|
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: 121.30 E-value: 4.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 36 LSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDC-IYPQERLREIchLASAPYYYDV 114
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTrLTPNELAFQL--KDSDVKLDDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 115 ATrqfiatgepgkvleeqdlayIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEK-----PVLMNHAVfsfDLSLi 189
Cdd:cd05912 80 AT--------------------IMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDdnwlcALPLFHIS---GLSI- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 190 pLLANLAMGGHIVLNAKEDIQKEnwLERLKSNAVSAwVSTPSFAYQQLLSpQFNSEYLPALNVFIFIGEVLNKALVKQLR 269
Cdd:cd05912 136 -LMRSVIYGMTVYLVDKFDAEQV--LHLINSGKVTI-ISVVPTMLQRLLE-ILGEGYPNNLRCILLGGGPAPKPLLEQCK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 270 RR-FPqakIINSYGPTEATIATTVVEITDAILNSDSA---VLPVGVMMPESKMEISTDGELIIWGKNVMRGYLGLPQENA 345
Cdd:cd05912 211 EKgIP---VYQSYGMTETCSQIVTLSPEDALNKIGSAgkpLFPVELKIEDDGQPPYEVGEILLKGPNVTKGYLNRPDATE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 346 AKLlrrEDEAFrgyRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLM-KSCGSVLRIA 422
Cdd:cd05912 288 ESF---ENGWF---KTGDIGYldEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPdDKWGQVPVAF 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 658547412 423 AFCVTDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05912 362 VVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
125-470 |
6.43e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 122.22 E-value: 6.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 125 PGKVLEEQDLAYIMFTSGSTGKPKGVQIG-RESVWH------FMKWVSQDFSLPEKPvlMNHaVFSFDLSLIPLLAnlam 197
Cdd:PRK06187 160 DFPDIDENDAAAMLYTSGTTGHPKGVVLShRNLFLHslavcaWLKLSRDDVYLVIVP--MFH-VHAWGLPYLALMA---- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 198 GGHIVLNAKedIQKENWLE--RLKSNAVSAWVSTpsfAYQQLLS-PQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFpQ 274
Cdd:PRK06187 233 GAKQVIPRR--FDPENLLDliETERVTFFFAVPT---IWQMLLKaPRAYFVDFSSLRLVIYGGAALPPALLREFKEKF-G 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 275 AKIINSYGPTEATIATTVVEITDAILNSDSAVLPVGVMMP--------ESKMEISTD----GELIIWGKNVMRGYLGLPQ 342
Cdd:PRK06187 307 IDLVQGYGMTETSPVVSVLPPEDQLPGQWTKRRSAGRPLPgvearivdDDGDELPPDggevGEIIVRGPWLMQGYWNRPE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 343 ENAakllrredEAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVL--PLMKScG 416
Cdd:PRK06187 387 ATA--------ETIDGgwLHTGDVGYidEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIgvPDEKW-G 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 658547412 417 SvlRIAAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK06187 458 E--RPVAVVVlkpgATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
72-470 |
8.60e-29 |
|
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: 117.87 E-value: 8.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 72 EFAVAIYSCLLHNIPYIPVDCIYPQERLREICHLASApyyydvatRQFIATGEPGK---VLEEQDLAYIMFTSGSTGKPK 148
Cdd:cd05903 38 EFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA--------KVFVVPERFRQfdpAAMPDAVALLLFTSGTTGEPK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 149 GVQIGRESVWHFMKWVSQDFSLPEKPVL-----MNHAVFSFDLSLIPLLanlamgghivLNAKEDIQkENW-----LERL 218
Cdd:cd05903 110 GVMHSHNTLSASIRQYAERLGLGPGDVFlvaspMAHQTGFVYGFTLPLL----------LGAPVVLQ-DIWdpdkaLALM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 219 KSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFpQAKIINSYGPTEATIATTVVEIT-- 296
Cdd:cd05903 179 REHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSITPApe 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 297 DAILNSDSAVLPvGVMM-----PESKMEISTDGELIIWGKNVMRGYLGLPQENAAKLlrreDEAFrgYRTGDLGY--EAG 369
Cdd:cd05903 258 DRRLYTDGRPLP-GVEIkvvddTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA----PEGW--FRTGDLARldEDG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 370 LIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLM-KSCGSvlRIAAFCVTD----MAPDTIKTSLSKV-VP 443
Cdd:cd05903 331 YLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPdERLGE--RACAVVVTKsgalLTFDELVAYLDRQgVA 408
|
410 420
....*....|....*....|....*..
gi 658547412 444 HYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05903 409 KQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
118-470 |
1.35e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 118.47 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 118 QFIATGEPGKV---LEEQDLAYIMFTSGSTGKPKGV-----QIGR--ESVWHFMKWVSQDFSLPEKPvlMNHaVFSFDLS 187
Cdd:PRK07656 149 DFLAAGDPAERapeVDPDDVADILFTSGTTGRPKGAmlthrQLLSnaADWAEYLGLTEGDRYLAANP--FFH-VFGYKAG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 188 LiplLANLAMGGHIVLNAKEDIqkENWLERLKSNAVSAWVSTPSFaYQQLLS-PQFNSEYLPALNVFIFIGEVLNKALVK 266
Cdd:PRK07656 226 V---NAPLMRGATILPLPVFDP--DEVFRLIETERITVLPGPPTM-YNSLLQhPDRSAEDLSSLRLAVTGAASMPVALLE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 267 QLRRRFPQAKIINSYGPTEA--------------TIATTV------VEItdAILNSDSAVLPVGVmmpeskmeistDGEL 326
Cdd:PRK07656 300 RFESELGVDIVLTGYGLSEAsgvttfnrldddrkTVAGTIgtaiagVEN--KIVNELGEEVPVGE-----------VGEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 327 IIWGKNVMRGYLGLPQENAAKLlrREDeafrGY-RTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGI 403
Cdd:PRK07656 367 LVRGPNVMKGYYDDPEATAAAI--DAD----GWlHTGDLGRldEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAV 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 404 NEAVVL----PLMKSCGS---VLR---------IAAFCVTDMApdtiktslskvvpHYMVPSQIIVKDALPLNPNGKIDR 467
Cdd:PRK07656 441 AEAAVIgvpdERLGEVGKayvVLKpgaelteeeLIAYCREHLA-------------KYKVPRSIEFLDELPKNATGKVLK 507
|
...
gi 658547412 468 KLL 470
Cdd:PRK07656 508 RAL 510
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
128-470 |
3.45e-28 |
|
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: 115.90 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 128 VLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMN--------HAVFSFdlsliplLANLAMGG 199
Cdd:cd05972 77 VTDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNiadpgwakGAWSSF-------FGPWLLGA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 200 HIVLNAKEDIQKENWLERLKSNAVSAWVSTPSfAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFpQAKIIN 279
Cdd:cd05972 150 TVFVYEGPRFDAERILELLERYGVTSFCGPPT-AYRMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAAT-GLPIRD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 280 SYGPTEATIATTVVEITD---------------AILNSDSAVLPVGvmmpeskmeisTDGELIIWGKNV--MRGYLGLPQ 342
Cdd:cd05972 228 GYGQTETGLTVGNFPDMPvkpgsmgrptpgydvAIIDDDGRELPPG-----------EEGDIAIKLPPPglFLGYVGDPE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 343 ENAAKllrredeaFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSC-GS 417
Cdd:cd05972 297 KTEAS--------IRGdyYLTGDRAYrdEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVrGE 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 418 VLRiaAFCV-TDMAPDT------IKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05972 369 VVK--AFVVlTSGYEPSeelaeeLQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
125-470 |
3.75e-28 |
|
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: 116.64 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 125 PGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMN-------HAVfsfdlsLIPLLANLAM 197
Cdd:cd05926 142 SEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVvmplfhvHGL------VASLLSTLAA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 198 GGHIVLNAKEDIQK-ENWLERLKSNAVSAwVSTpsfAYQQLLS---PQFNSEYlPALNvfiFI---GEVLNKALVKQLRR 270
Cdd:cd05926 216 GGSVVLPPRFSASTfWPDVRDYNATWYTA-VPT---IHQILLNrpePNPESPP-PKLR---FIrscSASLPPAVLEALEA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 271 RFpQAKIINSYGPTEATIATT------------------VVEItdAILNSDSAVLPVGVMmpeskmeistdGELIIWGKN 332
Cdd:cd05926 288 TF-GAPVLEAYGMTEAAHQMTsnplppgprkpgsvgkpvGVEV--RILDEDGEILPPGVV-----------GEICLRGPN 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 333 VMRGYLGLPQENAAkllrredEAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVV 408
Cdd:cd05926 354 VTRGYLNNPEANAE-------AAFKDgwFRTGDLGYldADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVA 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658547412 409 --LPLMK-----SCGSVLRIAAfcvtDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05926 427 fgVPDEKygeevAAAVVLREGA----SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
36-470 |
1.03e-27 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 114.88 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 36 LSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDciyPQERLREICHLASapyyyDVA 115
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPIN---PMLKERELEYILN-----DSG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 116 TRQFIATGEpgkvLEeqDLAYIMFTSGSTGKPKGVQIGRESVW-------HFMKWVSQDFSLPEKPVLmnHaVFSFDLSl 188
Cdd:cd05935 74 AKVAVVGSE----LD--DLALIPYTSGTTGLPKGCMHTHFSAAanalqsaVWTGLTPSDVILACLPLF--H-VTGFVGS- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 189 ipLLANLAMGGHIVLNAKEDiqKENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQL 268
Cdd:cd05935 144 --LNTAVYVGGTYVLMARWD--RETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 269 RRRFpQAKIINSYGPTEATIATTV--------------VEITDA--ILNSDSAVLPVGVmmpeskmeistDGELIIWGKN 332
Cdd:cd05935 220 LKLT-GLRFVEGYGLTETMSQTHTnpplrpklqclgip*FGVDArvIDIETGRELPPNE-----------VGEIVVRGPQ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 333 VMRGYLGLPQENAAKLLrrEDEAFRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLP 410
Cdd:cd05935 288 IFKGYWNRPEETEESFI--EIKGRRFFRTGDLGYmdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658547412 411 LMKScGSVLRIAAFCVTD------MAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05935 366 VPDE-RVGEEVKAFIVLRpeyrgkVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
133-467 |
1.34e-27 |
|
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: 112.50 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLP-EKPVLMNHAVfSFDLSLIPLLANLAMGGHIVLNAKEDIQk 211
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISgEDAILAPGPL-SHSLFLYGAISALYLGGTFIGQRKFNPK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 212 eNWLERLKSNAVSAWVSTPSFAyQQLLSpqfnsEYLPALNVFIFI--GEVLNKALVKQLRRRFPQAKIINSYGPTEATIA 289
Cdd:cd17633 79 -SWIRKINQYNATVIYLVPTML-QALAR-----TLEPESKIKSIFssGQKLFESTKKKLKNIFPKANLIEFYGTSELSFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 290 TtvveitdAILNSDSA-VLPVGVMMPESKMEI-STDGELI--IWGKNVMR--GYLGLPQENAAKLlrredeafrgYRTGD 363
Cdd:cd17633 152 T-------YNFNQESRpPNSVGRPFPNVEIEIrNADGGEIgkIFVKSEMVfsGYVRGGFSNPDGW----------MSVGD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 364 LGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLRIAAFCVTDMAPDTIKTSLSKV 441
Cdd:cd17633 215 IGYvdEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYKQLKRFLKQK 294
|
330 340
....*....|....*....|....*.
gi 658547412 442 VPHYMVPSQIIVKDALPLNPNGKIDR 467
Cdd:cd17633 295 LSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
31-376 |
1.52e-25 |
|
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: 109.64 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 31 GSDEALSWLQLSAAVTDWAQRYQRCQPvAGTPVVLYGHQQAEFAVAIYSCLLHNIpyIPVDCIYP-----QERLREI--- 102
Cdd:cd05931 20 GREETLTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGA--IAVPLPPPtpgrhAERLAAIlad 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 103 CH----LASAPYyyDVATRQFIATGE---------------------PGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESV 157
Cdd:cd05931 97 AGprvvLTTAAA--LAAVRAFAASRPaagtprllvvdllpdtsaadwPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 158 WHFMKWVSQDFSLPEKPVLMN-----HavfsfDLSLIP-LLANLAMGGHIVLNAKED-IQK-ENWLERL-KSNAVsaWVS 228
Cdd:cd05931 175 LANVRQIRRAYGLDPGDVVVSwlplyH-----DMGLIGgLLTPLYSGGPSVLMSPAAfLRRpLRWLRLIsRYRAT--ISA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 229 TPSFAYqQLLSPQFNSEYLPALN----VFIFIG-EVLNKALVKQLRRRF------PQAkIINSYGPTEATIATT------ 291
Cdd:cd05931 248 APNFAY-DLCVRRVRDEDLEGLDlsswRVALNGaEPVRPATLRRFAEAFapfgfrPEA-FRPSYGLAEATLFVSggppgt 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 292 --VVEITDAILNSDSAVLP----------VGVMMPESKMEIS-------------TDGEliIW--GKNVMRGYLGLPQEN 344
Cdd:cd05931 326 gpVVLRVDRDALAGRAVAVaaddpaarelVSCGRPLPDQEVRivdpetgrelpdgEVGE--IWvrGPSVASGYWGRPEAT 403
|
410 420 430
....*....|....*....|....*....|....
gi 658547412 345 AAKLLRREDEAFRGY-RTGDLGYEA-GLIYCQGR 376
Cdd:cd05931 404 AETFGALAATDEGGWlRTGDLGFLHdGELYITGR 437
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
27-470 |
1.12e-24 |
|
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: 106.22 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 27 LAISGSDEALSWLQLSAAVTDWAQRYQR-CQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLReichl 105
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLAlGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELE----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 106 asapyyydvatrQFIATGEPGKVLeeqDLAYIMFTSGSTGKPKGVQIGRESV----------WhfmKWVSQDFSLPEKPV 175
Cdd:cd05941 78 ------------YVITDSEPSLVL---DPALILYTSGTTGRPKGVVLTHANLaanvralvdaW---RWTEDDVLLHVLPL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 176 LMNHAVFsfdlslIPLLANLAMGGHIVLNAKEDIQKENWLERLKSnaVSAWVSTPSFaYQQLLS-PQFNSEYLPALNVFI 254
Cdd:cd05941 140 HHVHGLV------NALLCPLFAGASVEFLPKFDPKEVAISRLMPS--ITVFMGVPTI-YTRLLQyYEAHFTDPQFARAAA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 255 FIGEVLN----KALVKQLRRRFPQA---KIINSYGPTEATIATTVVeitdaiLNSDSAVLPVGVMMPESKMEISTD---- 323
Cdd:cd05941 211 AERLRLMvsgsAALPVPTLEEWEAItghTLLERYGMTEIGMALSNP------LDGERRPGTVGMPLPGVQARIVDEetge 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 324 -------GELIIWGKNVMRGYLGLPQENAakllrredEAFRG---YRTGDLGY--EAGLIYCQGR-NDSQVKLNGYRIEI 390
Cdd:cd05941 285 plprgevGEIQVRGPSVFKEYWNKPEATK--------EEFTDdgwFKTGDLGVvdEDGYYWILGRsSVDIIKSGGYKVSA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 391 NEIENRLLAMSGINEAVVLPLM-KSCGSvlRIAAFCVTD-----MAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGK 464
Cdd:cd05941 357 LEIERVLLAHPGVSECAVIGVPdPDWGE--RVVAVVVLRagaaaLSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGK 434
|
....*.
gi 658547412 465 IDRKLL 470
Cdd:cd05941 435 VNKKEL 440
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
128-467 |
1.19e-24 |
|
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: 106.01 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 128 VLEEQDLAYIMFTSGSTGKPKGV-QIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFSFDLSL-IPLLANLAMGGHIVLNA 205
Cdd:cd05919 87 VTSADDIAYLLYSSGTTGPPKGVmHAHRDPLLFADAMAREALGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 206 kEDIQKENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFpQAKIINSYGPTE 285
Cdd:cd05919 167 -GWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 286 aTIATTVVEITDAI-LNSDSAVLP---VGVMMPESK-MEISTDGELIIWGKNVMRGYLGLPQENAAkllrredeAFRG-- 358
Cdd:cd05919 245 -VGHIFLSNRPGAWrLGSTGRPVPgyeIRLVDEEGHtIPPGEEGDLLVRGPSAAVGYWNNPEKSRA--------TFNGgw 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 359 YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGsVLRIAAFCV--TDMAPD-- 432
Cdd:cd05919 316 YRTGDKFCrdADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTG-LSRLTAFVVlkSPAAPQes 394
|
330 340 350
....*....|....*....|....*....|....*...
gi 658547412 433 ---TIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDR 467
Cdd:cd05919 395 larDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
15-470 |
1.37e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 106.20 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 15 RAALcdpaSPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSC-------LLHNIPY 87
Cdd:PRK03640 11 RAFL----TPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALqqlgavaVLLNTRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 88 IPVDCIYPQERLREICHLASAPYYYDVATRQFI-------ATGEPGKVLEEQDL---AYIMFTSGSTGKPKGVQIGRESv 157
Cdd:PRK03640 87 SREELLWQLDDAEVKCLITDDDFEAKLIPGISVkfaelmnGPKEEAEIQEEFDLdevATIMYTSGTTGKPKGVIQTYGN- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 158 wHFMKWVSQDFSLPekpvLMNH-----AVFSFDLS-LIPLLANLAMGGHIVLNAKEDIQKEN-WLERLKSNAVSAwVSTp 230
Cdd:PRK03640 166 -HWWSAVGSALNLG----LTEDdcwlaAVPIFHISgLSILMRSVIYGMRVVLVEKFDAEKINkLLQTGGVTIISV-VST- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 231 sfAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRR-FPqakIINSYGPTE--ATIATtvveitdaiLNSDSAVL 307
Cdd:PRK03640 239 --MLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKgIP---VYQSYGMTEtaSQIVT---------LSPEDALT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 308 PVG-VMMPESKMEI-----------STDGELIIWGKNVMRGYLGLPQENAakllrredEAFRG--YRTGDLGY--EAGLI 371
Cdd:PRK03640 305 KLGsAGKPLFPCELkiekdgvvvppFEEGEIVVKGPNVTKGYLNREDATR--------ETFQDgwFKTGDIGYldEEGFL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 372 YCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLM-KSCGSVlrIAAFCVTDMAP--DTIKTSLSKVVPHYMVP 448
Cdd:PRK03640 377 YVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPdDKWGQV--PVAFVVKSGEVteEELRHFCEEKLAKYKVP 454
|
490 500
....*....|....*....|..
gi 658547412 449 SQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK03640 455 KRFYFVEELPRNASGKLLRHEL 476
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
132-467 |
5.65e-23 |
|
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: 99.64 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 132 QDLAYIMFTSGSTGKPKGVQIGRESVW--------HFMKWVSQDFSLpekpvLMNHAVFSFDLSLIplLANLAMGGHIVL 203
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFavpdilqkEGLNWVVGDVTY-----LPLPATHIGGLWWI--LTCLIHGGLCVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 204 nAKEDIQKENWLERLKSNAVSAWVSTPSfAYQQLLSPQFNS-EYLPALNVFIFIGE-VLNKAlvKQLRRRFPQAKIINSY 281
Cdd:cd17635 74 -GGENTTYKSLFKILTTNAVTTTCLVPT-LLSKLVSELKSAnATVPSLRLIGYGGSrAIAAD--VRFIEATGLTNTAQVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 282 GPTEATIATTVVEITDAI-LNSDSAVLP-VGVMMPESK-MEISTDGELIIWGKN--VMRGYLGLPQENAAKLLrreDEAF 356
Cdd:cd17635 150 GLSETGTALCLPTDDDSIeINAVGRPYPgVDVYLAATDgIAGPSASFGTIWIKSpaNMLGYWNNPERTAEVLI---DGWV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 357 rgyRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLRIAAFCVTDM----A 430
Cdd:cd17635 227 ---NTGDLGErrEDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAEldenA 303
|
330 340 350
....*....|....*....|....*....|....*..
gi 658547412 431 PDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDR 467
Cdd:cd17635 304 IRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
133-470 |
1.72e-22 |
|
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: 99.29 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNH-AVFSFDLSLIPLLANLAMGGHIVLNAKEDIqK 211
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVlPLFHINAQAVSVLAALSVGATLVLLPRFSA-S 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 212 ENWLERLKSNAvsAWVST----PSFAYQQLLSPQFNSEYLPAlnvfIFIGEVlNKALVKQLRRRFpQAKIINSYGPTEaT 287
Cdd:cd05934 161 RFWSDVRRYGA--TVTNYlgamLSYLLAQPPSPDDRAHRLRA----AYGAPN-PPELHEEFEERF-GVRLLEGYGMTE-T 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 288 IATTVVEITDAIlnsdsAVLPVGVMMPESKMEISTD----------GELII---WGKNVMRGYLGLPQENAakllrredE 354
Cdd:cd05934 232 IVGVIGPRDEPR-----RPGSIGRPAPGYEVRIVDDdgqelpagepGELVIrglRGWGFFKGYYNMPEATA--------E 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 355 AFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGS-------VLR--- 420
Cdd:cd05934 299 AMRNgwFHTGDLGYrdADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEdevkavvVLRpge 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 658547412 421 ------IAAFCVTDMAPdtiktslskvvphYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05934 379 tldpeeLFAFCEGQLAY-------------FKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
89-470 |
2.19e-22 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 100.21 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 89 PVDCIYP-QERLREICHLA----SAPYYYDVATRQFIATGEPgkvLEE------QDLAYIMFTSGSTGKPKGVQIGRESV 157
Cdd:PRK06087 136 PVDLILPlQNQLPQLQQIVgvdkLAPATSSLSLSQIIADYEP---LTTaitthgDELAAVLFTSGTEGLPKGVMLTHNNI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 158 W----HFMKWV---SQDFSLPEKPvlMNHAVFSFDLSLIPLLAnlamGGHIVLnaKEDIQKENWLERLKSNAVSaWV--S 228
Cdd:PRK06087 213 LaserAYCARLnltWQDVFMMPAP--LGHATGFLHGVTAPFLI----GARSVL--LDIFTPDACLALLEQQRCT-CMlgA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 229 TPsFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRfpQAKIINSYGPTEAT-------------------IA 289
Cdd:PRK06087 284 TP-FIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESSphavvnlddplsrfmhtdgYA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 290 TTVVEItdAILNSDSAVLPVGVmmpeskmeistDGELIIWGKNVMRGYLGLPQENAAKLlrrEDEAFrgYRTGDLGY--E 367
Cdd:PRK06087 361 AAGVEI--KVVDEARKTLPPGC-----------EGEEASRGPNVFMGYLDEPELTARAL---DEEGW--YYSGDLCRmdE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 368 AGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLM-KSCGSvlRIAAFCVtdMAPDTIKTSLSKV----- 441
Cdd:PRK06087 423 AGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPdERLGE--RSCAYVV--LKAPHHSLTLEEVvaffs 498
|
410 420 430
....*....|....*....|....*....|..
gi 658547412 442 ---VPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK06087 499 rkrVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
133-470 |
3.10e-22 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 99.80 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGVQIGRES--VWH--FMKWVsqdFSLPEKPVLMNHAvfsfDLSLI-----PLLANLAMGGHIVL 203
Cdd:COG0365 185 DPLFILYTSGTTGKPKGVVHTHGGylVHAatTAKYV---LDLKPGDVFWCTA----DIGWAtghsyIVYGPLLNGATVVL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 204 -NAKED-IQKENWLERLKSNAVSAWVSTPSfAYQQLLS--PQFNSEY-LPALNVFIFIGEVLNKALVKQLRRRFpQAKII 278
Cdd:COG0365 258 yEGRPDfPDPGRLWELIEKYGVTVFFTAPT-AIRALMKagDEPLKKYdLSSLRLLGSAGEPLNPEVWEWWYEAV-GVPIV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 279 NSYGPTEAT--IATTV----------------VEItdAILNSDSAVLPVGVMmpeskmeistdGELII---W-GknVMRG 336
Cdd:COG0365 336 DGWGQTETGgiFISNLpglpvkpgsmgkpvpgYDV--AVVDEDGNPVPPGEE-----------GELVIkgpWpG--MFRG 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 337 YLGLPQENAAKLLrredEAFRG-YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPL-- 411
Cdd:COG0365 401 YWNDPERYRETYF----GRFPGwYRTGDGARrdEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVpd 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658547412 412 -MKscGSVlrIAAFCV-------TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:COG0365 477 eIR--GQV--VKAFVVlkpgvepSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
133-470 |
1.28e-21 |
|
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: 97.31 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGV--------------------QIGRESVwhFMkwvsqdFSLPekpvlMNHavfSFDLSLIpLL 192
Cdd:cd05904 159 DVAALLYSSGTTGRSKGVmlthrnliamvaqfvagegsNSDSEDV--FL------CVLP-----MFH---IYGLSSF-AL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 193 ANLAMGGHIVLNAKEDIqkENWLERLKSNAVS-AWVSTPSFAyqQLL-SPQFNSEYLPALnVFIFIGEV-LNKALVKQLR 269
Cdd:cd05904 222 GLLRLGATVVVMPRFDL--EELLAAIERYKVThLPVVPPIVL--ALVkSPIVDKYDLSSL-RQIMSGAApLGKELIEAFR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 270 RRFPQAKIINSYGPTEATIATTVveiTDAILNSDSAVLPVGVMMPESKMEI-----------STDGELIIWGKNVMRGYL 338
Cdd:cd05904 297 AKFPNVDLGQGYGMTESTGVVAM---CFAPEKDRAKYGSVGRLVPNVEAKIvdpetgeslppNQTGELWIRGPSIMKGYL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 339 GLPQENAAKLlrREDeafrGY-RTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLM-KS 414
Cdd:cd05904 374 NNPEATAATI--DKE----GWlHTGDLCYidEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPdEE 447
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 415 CGSVlrIAAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05904 448 AGEV--PMAFVVrkpgSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
133-465 |
1.97e-21 |
|
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: 94.88 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGVQIG-RESVWHFMKWVS-QDFSLPEKPVLMNHAVFSFDLSlIPLLANLAMGGHIVLNAKEDIQ 210
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAhRQTLRAAAAWADcADLTEDDRYLIINPFFHTFGYK-AGIVACLLTGATVVPVAVFDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 211 KEnwLERLKSNAVSAWVSTPSFaYQQLLS-PQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIA 289
Cdd:cd17638 80 AI--LEAIERERITVLPGPPTL-FQSLLDhPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 290 TTVVEITDAILNSDSavlpVGVMMPESKMEISTDGELIIWGKNVMRGYLGLPQENAAKLlrreDEafRGY-RTGDLGY-- 366
Cdd:cd17638 157 TMCRPGDDAETVATT----CGRACPGFEVRIADDGEVLVRGYNVMQGYLDDPEATAEAI----DA--DGWlHTGDVGEld 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 367 EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPL----MKSCGSVLRIAAFCVTDMAPDTIKTSLSKVV 442
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVpderMGEVGKAFVVARPGVTLTEEDVIAWCRERLA 306
|
330 340
....*....|....*....|...
gi 658547412 443 pHYMVPSQIIVKDALPLNPNGKI 465
Cdd:cd17638 307 -NYKVPRFVRFLDELPRNASGKV 328
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
130-474 |
2.01e-21 |
|
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: 96.63 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 130 EEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMN-----HAvFSFDLSLI-PLLanlaMGGHIV- 202
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGalpffHS-FGLTGCLWlPLL----SGIKVVf 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 203 ----LNAKEDIqkenwlERLKSNAVSAWVSTPSFAYQQLLSpqFNSEYLPALNVFIFIGEVLNKALVKQLRRRFpQAKII 278
Cdd:cd05909 220 hpnpLDYKKIP------ELIYDKKATILLGTPTFLRGYARA--AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRIL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 279 NSYGPTEAT--IATTVVEiTDAILNSDSAVLP---VGVMMPESKMEIST--DGELIIWGKNVMRGYLGLPQENaakllrr 351
Cdd:cd05909 291 EGYGTTECSpvISVNTPQ-SPNKEGTVGRPLPgmeVKIVSVETHEEVPIgeGGLLLVRGPNVMLGYLNEPELT------- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 352 eDEAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMkSCGSVLRIAAFCVT 427
Cdd:cd05909 363 -SFAFGDgwYDTGDIGKidGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSV-PDGRKGEKIVLLTT 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 658547412 428 --DMAPDTIKTSLSKV-VPHYMVPSQIIVKDALPLNPNGKIDRKLLDAYA 474
Cdd:cd05909 441 ttDTDPSSLNDILKNAgISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
125-470 |
3.79e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 96.11 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 125 PGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWhfmkWVSQD------FSLPEKPVLMN--HAVFSFDLsliPLLANLA 196
Cdd:PRK06145 142 PQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLH----WKSIDhvialgLTASERLLVVGplYHVGAFDL---PGIAVLW 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 197 MGGhiVLNAKEDIQKENWLERLKSNAVS-AWVStPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQA 275
Cdd:PRK06145 215 VGG--TLRIHREFDPEAVLAAIERHRLTcAWMA-PVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 276 KIINSYGPTEATIATTVVEITDAILNSDSAvlpvGVMMPESKMEISTD----------GELIIWGKNVMRGYLGLPQENA 345
Cdd:PRK06145 292 RYIDAYGLTETCSGDTLMEAGREIEKIGST----GRALAHVEIRIADGagrwlppnmkGEICMRGPKVTKGYWKDPEKTA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 346 akllrredEAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKS-CGSvlR 420
Cdd:PRK06145 368 --------EAFYGdwFRSGDVGYldEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDrWGE--R 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 658547412 421 IAAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK06145 438 ITAVVVlnpgATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
24-476 |
7.24e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 95.38 E-value: 7.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSC----LLH----------NIPYI- 88
Cdd:PRK08316 25 PDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACaragAVHvpvnfmltgeELAYIl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 89 -------------------PVDCIYPQERLREICHLASAPY------YYDVATRQfiATGEPGKVLEEQDLAYIMFTSGS 143
Cdd:PRK08316 105 dhsgaraflvdpalaptaeAALALLPVDTLILSLVLGGREApggwldFADWAEAG--SVAEPDVELADDDLAQILYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 144 TGKPKGVQIGRESVWHfmKWVSQ----DFSLPEKPVlmnHA----------VFsfdlsLIPLlanLAMGGHIVLNAKEDI 209
Cdd:PRK08316 183 ESLPKGAMLTHRALIA--EYVSCivagDMSADDIPL---HAlplyhcaqldVF-----LGPY---LYVGATNVILDAPDP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 210 qkENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPAL-----NVFIFIGEVLnkalvKQLRRRFPQAKIINSYGPT 284
Cdd:PRK08316 250 --ELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLrkgyyGASIMPVEVL-----KELRERLPGLRFYNCYGQT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 285 E-ATIAtTVVEITDAILNSDSAVLPvgVMMPESKMEISTD--------GELIIWGKNVMRGYLGLPQENAakllrredEA 355
Cdd:PRK08316 323 EiAPLA-TVLGPEEHLRRPGSAGRP--VLNVETRVVDDDGndvapgevGEIVHRSPQLMLGYWDDPEKTA--------EA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 356 FRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVV--LPLMKSCGSVlriAAFCV--- 426
Cdd:PRK08316 392 FRGgwFHSGDLGVmdEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVigLPDPKWIEAV---TAVVVpka 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 658547412 427 -TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKI-DRKLLDAYART 476
Cdd:PRK08316 469 gATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKIlKRELRERYAGA 520
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
8-470 |
8.47e-21 |
|
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: 94.88 E-value: 8.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 8 QELQDFLRAALCDPASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCllHNIPY 87
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLAL--HRLGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 88 IPV------------DCIYPQErLREICHLASAPYYYDVATR--------QFIATGEP---GKVLE------EQDlAYIM 138
Cdd:cd05923 79 VPAlinprlkaaelaELIERGE-MTAAVIAVDAQVMDAIFQSgvrvlalsDLVGLGEPesaGPLIEdpprepEQP-AFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 139 FTSGSTGKPKGVQI---GRESVWHFMKWVSQDFSLPEKPVL----MNHAVFSFDLslipLLANLAMGGHIVLnaKEDIQK 211
Cdd:cd05923 157 YTSGTTGLPKGAVIpqrAAESRVLFMSTQAGLRHGRHNVVLglmpLYHVIGFFAV----LVAALALDGTYVV--VEEFDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 212 ENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKiINSYGPTEA---TI 288
Cdd:cd05923 231 ADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEK-VNIYGTTEAmnsLY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 289 ATTVVEITD--AILNSDSAVLPVGVmMPESKMEISTDGELII--WGKNVMRGYLGLPQENAAKLlrredeAFRGYRTGDL 364
Cdd:cd05923 310 MRDARTGTEmrPGFFSEVRIVRIGG-SPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKL------QDGWYRTGDV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 365 GY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLM-KSCGSvlRIAAFCVTDMAPDTI----KTS 437
Cdd:cd05923 383 GYvdPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVAdERWGQ--SVTACVVPREGTLSAdeldQFC 460
|
490 500 510
....*....|....*....|....*....|...
gi 658547412 438 LSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05923 461 RASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
24-472 |
1.46e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 94.28 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAE-FAVAIYSCL-------LH------------ 83
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvLMAIGAAQLaglrrtaLHplgslddhayvl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 84 ---NIPYIPVDCIYPQER----------LREICHLASAPYYYDVATRqfIATGEPGKVLEEQ---DLAYIMFTSGSTGKP 147
Cdd:PRK06188 106 edaGISTLIVDPAPFVERalallarvpsLKHVLTLGPVPDGVDLLAA--AAKFGPAPLVAAAlppDIAGLAYTGGTTGKP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 148 KGVQIGRESVWHFMKWVSQDFSLPEKP-VLM----NHAVFSFdlslipLLANLAMGGHIVLNAKEDIqkENWLERLKSNA 222
Cdd:PRK06188 184 KGVMGTHRSIATMAQIQLAEWEWPADPrFLMctplSHAGGAF------FLPTLLRGGTVIVLAKFDP--AEVLRAIEEQR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 223 VSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAkIINSYGPTEATIATTVVEITDAILNS 302
Cdd:PRK06188 256 ITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPI-FAQYYGQTEAPMVITYLRKRDHDPDD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 303 DSAVLPVGVMMP--------ESKMEISTD--GELIIWGKNVMRGYLGLPQENAakllrredEAFRG--YRTGDLGY--EA 368
Cdd:PRK06188 335 PKRLTSCGRPTPglrvalldEDGREVAQGevGEICVRGPLVMDGYWNRPEETA--------EAFRDgwLHTGDVARedED 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 369 GLIYCQGRNDSQVKLNGYRIEINEIENRL-----LAMSGI--------NEAVvlplmKSCgSVLRiaafcvTDMAPDT-- 433
Cdd:PRK06188 407 GFYYIVDRKKDMIVTGGFNVFPREVEDVLaehpaVAQVAVigvpdekwGEAV-----TAV-VVLR------PGAAVDAae 474
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 658547412 434 ----IKTSlsKVVPHymVPSQIIVKDALPLNPNGKIDRKLLDA 472
Cdd:PRK06188 475 lqahVKER--KGSVH--APKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
36-409 |
1.93e-20 |
|
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: 93.43 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 36 LSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPvdcIYPQERLREICHLASapyyyDVA 115
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVP---IYPTSSAEQIAYILN-----DSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 116 TRQFIaTGEPgkvleeQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLmnhavfsfdLSLIPL---L 192
Cdd:cd05907 78 AKALF-VEDP------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRH---------LSFLPLahvF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 193 AN-------LAMGGHIVLNAKEDIQKENwLERLK--------------SNAVSAwVSTPSFayQQLLspqFNSEYLPALN 251
Cdd:cd05907 142 ERraglyvpLLAGARIYFASSAETLLDD-LSEVRptvflavprvwekvYAAIKV-KAVPGL--KRKL---FDLAVGGRLR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 252 VFIFIGEVLNKALVkqlrrRFPQA---KIINSYGPTEATIATTVVEITDAILNSdsavlpVGVMMPESKMEISTDGELII 328
Cdd:cd05907 215 FAASGGAPLPAELL-----HFFRAlgiPVYEGYGLTETSAVVTLNPPGDNRIGT------VGKPLPGVEVRIADDGEILV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 329 WGKNVMRGYLGLPQENAAKLLrrEDEAFrgyRTGDLGY--EAGLIYCQGR-NDSQVKLNGYRIEINEIENRLLAMSGINE 405
Cdd:cd05907 284 RGPNVMLGYYKNPEATAEALD--ADGWL---HTGDLGEidEDGFLHITGRkKDLIITSGGKNISPEPIENALKASPLISQ 358
|
....
gi 658547412 406 AVVL 409
Cdd:cd05907 359 AVVI 362
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
133-474 |
2.20e-20 |
|
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: 91.62 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQdfslPEKPVLMNHAVFSFDLSLI----PLLANLAMGGHIVLnaked 208
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHS----RLGFGGGDSWLLSLPLYHVgglaILVRSLLAGAELVL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 209 iqkenwLERLKSNAVSA------WVSTPSFAYQQLLSPQFNSEYLPALNVfIFIGevlNKALVKQLRRRFPQAKI--INS 280
Cdd:cd17630 72 ------LERNQALAEDLappgvtHVSLVPTQLQRLLDSGQGPAALKSLRA-VLLG---GAPIPPELLERAADRGIplYTT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 281 YGPTE--ATIATTVVEITDAILnsdsavlpVGVMMPESKMEISTDGELIIWGKNVMRGYLGLPQENaaklLRREDEAFRg 358
Cdd:cd17630 142 YGMTEtaSQVATKRPDGFGRGG--------VGVLLPGRELRIVEDGEIWVGGASLAMGYLRGQLVP----EFNEDGWFT- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 359 yrTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLM-KSCGSvlRIAAFCVTDM--APDT 433
Cdd:cd17630 209 --TKDLGElhADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPdEELGQ--RPVAVIVGRGpaDPAE 284
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 658547412 434 IKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLLDAYA 474
Cdd:cd17630 285 LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
14-470 |
1.34e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 88.12 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 14 LRAALCDPASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVA--GTPVvlyghqqAEFAVAIYSCLLHNIPYIPVD 91
Cdd:PRK07787 4 LNPAAVAAAADIADAVRIGGRVLSRSDLAGAATAVAERVAGARRVAvlATPT-------LATVLAVVGALIAGVPVVPVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 92 ciyPQERLREICH----------LASAPYYY--------DVATRQFIATGEPgkvlEEQDLAYIMFTSGSTGKPKGVQIG 153
Cdd:PRK07787 77 ---PDSGVAERRHiladsgaqawLGPAPDDPaglphvpvRLHARSWHRYPEP----DPDAPALIVYTSGTTGPPKGVVLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 154 RESV----------WhfmKWVSQDfslpekpVLMnHAVFSFDL-SLI-PLLANLAMGGHIVLNAKEDiqKENWLERLKSN 221
Cdd:PRK07787 150 RRAIaadldalaeaW---QWTADD-------VLV-HGLPLFHVhGLVlGVLGPLRIGNRFVHTGRPT--PEAYAQALSEG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 222 AvSAWVSTPS--------------FAYQQLLSPqfNSEYLPAlNVFifigevlnkalvKQLRRRFPQAkIINSYGPTEAT 287
Cdd:PRK07787 217 G-TLYFGVPTvwsriaadpeaaraLRGARLLVS--GSAALPV-PVF------------DRLAALTGHR-PVERYGMTETL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 288 IATTVveitdailNSDSAVLP--VGVMMP--------ESKMEISTDGELI----IWGKNVMRGYLGLPQENAAkllrred 353
Cdd:PRK07787 280 ITLST--------RADGERRPgwVGLPLAgvetrlvdEDGGPVPHDGETVgelqVRGPTLFDGYLNRPDATAA------- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 354 eAFRG---YRTGDLGY--EAGLIYCQGRNDSQ-VKLNGYRIEINEIENRLLAMSGINEAVVLPLMKS-CGSvlRIAAFCV 426
Cdd:PRK07787 345 -AFTAdgwFRTGDVAVvdPDGMHRIVGRESTDlIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDdLGQ--RIVAYVV 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 658547412 427 --TDMAPDT----IKTSLSkvvPHYMvPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK07787 422 gaDDVAADElidfVAQQLS---VHKR-PREVRFVDALPRNAMGKVLKKQL 467
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
31-470 |
4.50e-18 |
|
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: 86.34 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 31 GSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLReichlasapY 110
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVH---------H 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 111 YYDVATRQFIATGEpgkvleEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLmnhavfsfdLSLIP 190
Cdd:cd05914 74 ILNHSEAKAIFVSD------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKI---------LSILP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 191 L----------LANLAMGGHIVL-----NAKEDIQKENwleRLKSNAVSA--WV------------STPSFAYQQLLSPQ 241
Cdd:cd05914 139 LhhiypltftlLLPLLNGAHVVFldkipSAKIIALAFA---QVTPTLGVPvpLViekifkmdiipkLTLKKFKFKLAKKI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 242 FNSEYLPAL----------NVFIFI--GEVLNKALVKQLRR-RFPqakIINSYGPTEAT--IATTVVEITdaILNSDSAV 306
Cdd:cd05914 216 NNRKIRKLAfkkvheafggNIKEFVigGAKINPDVEEFLRTiGFP---YTIGYGMTETApiISYSPPNRI--RLGSAGKV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 307 LPVGVMMPESKMEISTDGELIIWGKNVMRGYLGLPQENAAKLLrrEDEAFrgyRTGDLGY--EAGLIYCQGRNDSQVKL- 383
Cdd:cd05914 291 IDGVEVRIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFD--KDGWF---HTGDLGKidAEGYLYIRGRKKEMIVLs 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 384 NGYRIEINEIENRLLAMSGINEAVVLPLMKScgSVLRI-----AAFCVTDMAPDTIKTSLSKV-------VPHYMVPSQI 451
Cdd:cd05914 366 SGKNIYPEEIEAKINNMPFVLESLVVVQEKK--LVALAyidpdFLDVKALKQRNIIDAIKWEVrdkvnqkVPNYKKISKV 443
|
490 500
....*....|....*....|
gi 658547412 452 -IVKDALPLNPNGKIDRKLL 470
Cdd:cd05914 444 kIVKEEFEKTPKGKIKRFLY 463
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
120-474 |
1.32e-17 |
|
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: 84.86 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 120 IATGEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESV--------WHF------MKWVSQDfslPEKPVLMNHAVFSfd 185
Cdd:cd05969 77 ITTEELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMifyyftgkYVLdlhpddIYWCTAD---PGWVTGTVYGIWA-- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 186 lsliPLLANLAMgghIVLNAKEDIqkENWLERLKSNAVSAWVSTPSfAYQQL------LSPQFNseyLPALNVFIFIGEV 259
Cdd:cd05969 152 ----PWLNGVTN---VVYEGRFDA--ESWYGIIERVKVTVWYTAPT-AIRMLmkegdeLARKYD---LSSLRFIHSVGEP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 260 LNKALVKQLRRRFpQAKIINSYGPTE-ATIattvveitdAILNSDSAVLPVGVM-MP------------ESKMEISTDGE 325
Cdd:cd05969 219 LNPEAIRWGMEVF-GVPIHDTWWQTEtGSI---------MIANYPCMPIKPGSMgKPlpgvkaavvdenGNELPPGTKGI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 326 LII---WgKNVMRGYLGLPQenaakllrREDEAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLL 398
Cdd:cd05969 289 LALkpgW-PSMFRGIWNDEE--------RYKNSFIDgwYLTGDLAYrdEDGYFWFVGRADDIIKTSGHRVGPFEVESALM 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 399 AMSGINEAVVL----PLMKScgsvlRIAAFCV--TDMAP-DTIKTSLSKVVPH----YMVPSQIIVKDALPLNPNGKIDR 467
Cdd:cd05969 360 EHPAVAEAGVIgkpdPLRGE-----IIKAFISlkEGFEPsDELKEEIINFVRQklgaHVAPREIEFVDNLPKTRSGKIMR 434
|
....*..
gi 658547412 468 KLLDAYA 474
Cdd:cd05969 435 RVLKAKE 441
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
131-470 |
4.47e-17 |
|
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: 83.73 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 131 EQDLAYIMFTSGSTGKPKGVQIGRESvwhfmkwVSQDFSLPEKPVLMNHAVFSFD-LSLIP---------LLANLAMGGH 200
Cdd:cd17642 183 DEQVALIMNSSGSTGLPKGVQLTHKN-------IVARFSHARDPIFGNQIIPDTAiLTVIPfhhgfgmftTLGYLICGFR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 201 IVLNAKedIQKENWLERLKSNAV-SAWVSTPSFAYQQlLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIIN 279
Cdd:cd17642 256 VVLMYK--FEEELFLRSLQDYKVqSALLVPTLFAFFA-KSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQ 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 280 SYGPTEATIATTVVEITDAILNSDSAVLP---VGVMMPESKMEISTD--GELIIWGKNVMRGYLGLPQenAAKLLRREDe 354
Cdd:cd17642 333 GYGLTETTSAILITPEGDDKPGAVGKVVPffyAKVVDLDTGKTLGPNerGELCVKGPMIMKGYVNNPE--ATKALIDKD- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 355 afrGY-RTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLRiAAFCVTdmap 431
Cdd:cd17642 410 ---GWlHSGDIAYydEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELP-AAVVVL---- 481
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 658547412 432 DTIKTSLSKVVPHYmVPSQ----------IIVKDALPLNPNGKIDRKLL 470
Cdd:cd17642 482 EAGKTMTEKEVMDY-VASQvstakrlrggVKFVDEVPKGLTGKIDRRKI 529
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
30-473 |
8.45e-17 |
|
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: 82.72 E-value: 8.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 30 SGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHN-IPYI-PVDCIY--PQERLREICHL 105
Cdd:cd05906 34 DGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGfVPAPlTVPPTYdePNARLRKLRHI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 106 -------------ASAPYYYDVATRQFI--------------ATGEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVW 158
Cdd:cd05906 114 wqllgspvvltdaELVAEFAGLETLSGLpgirvlsieelldtAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNIL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 159 HFMKWVSQDFSLPEKPVLMN-----HAVFSFDLSLIPLLAnlamGGHIVLNAKEDIQKE--NWLERLKSNAVS-AWvsTP 230
Cdd:cd05906 194 ARSAGKIQHNGLTPQDVFLNwvpldHVGGLVELHLRAVYL----GCQQVHVPTEEILADplRWLDLIDRYRVTiTW--AP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 231 SFAY----QQLLSPQFNSEYLPALNVFIFIGEVLN----KALVKQLRRR-FPQAKIINSYGPTE--ATIATTVVEITDAI 299
Cdd:cd05906 268 NFAFallnDLLEEIEDGTWDLSSLRYLVNAGEAVVaktiRRLLRLLEPYgLPPDAIRPAFGMTEtcSGVIYSRSFPTYDH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 300 LNSDSAVlPVGVMMPESKMEI----------STDGELIIWGKNVMRGYLGLPQENAakllrredEAFRG---YRTGDLGY 366
Cdd:cd05906 348 SQALEFV-SLGRPIPGVSMRIvddegqllpeGEVGRLQVRGPVVTKGYYNNPEANA--------EAFTEdgwFRTGDLGF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 367 -EAGLIYCQGRNDSQVKLNGYRIEINEIEnrllamSGINEA-VVLPLMKSCGSVL-------RIAAFCVTDMAPDT---- 433
Cdd:cd05906 419 lDNGNLTITGRTKDTIIVNGVNYYSHEIE------AAVEEVpGVEPSFTAAFAVRdpgaeteELAIFFVPEYDLQDalse 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 658547412 434 ----IKTSLSK---VVPHYMVPsqiIVKDALPLNPNGKIDR-KLLDAY 473
Cdd:cd05906 493 tlraIRSVVSRevgVSPAYLIP---LPKEEIPKTSLGKIQRsKLKAAF 537
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
133-465 |
9.14e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 82.70 E-value: 9.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGVQIGRESVWH----FMKWVSqdfSLPEkpvlmnhAVFsfdLSLIP----------LLANLAMG 198
Cdd:PRK08314 191 DLAVLPYTSGTTGVPKGCMHTHRTVMAnavgSVLWSN---STPE-------SVV---LAVLPlfhvtgmvhsMNAPIYAG 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 199 GHIVLNAKEDiqKENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFpQAKII 278
Cdd:PRK08314 258 ATVVLMPRWD--REAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELT-GLDYV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 279 NSYGPTEaTIATTVVEITD---------AILNSDSAV--------LPVGVMmpeskmeistdGELIIWGKNVMRGYLGLP 341
Cdd:PRK08314 335 EGYGLTE-TMAQTHSNPPDrpklqclgiPTFGVDARVidpetleeLPPGEV-----------GEIVVHGPQVFKGYWNRP 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 342 QENAAKLLRREDEAFrgYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEA------------- 406
Cdd:PRK08314 403 EATAEAFIEIDGKRF--FRTGDLGRmdEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEAcviatpdprrget 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658547412 407 ----VVL-PLMKSCGSVLRIAAFCVTDMAPdtiktslskvvphYMVPSQIIVKDALPLNPNGKI 465
Cdd:PRK08314 481 vkavVVLrPEARGKTTEEEIIAWAREHMAA-------------YKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
117-470 |
1.94e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 81.90 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 117 RQFIATGEPGKV-LEEQDLAYIMFTSGSTGKPKGVQIGR----ESVWHFMKWVSqdFSLPEKPVL---MNHAvfsfdLSL 188
Cdd:PRK07788 191 DDLIAGSSTAPLpKPPKPGGIVILTSGTTGTPKGAPRPEpsplAPLAGLLSRVP--FRAGETTLLpapMFHA-----TGW 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 189 IPLLANLAMGGHIVLNAKEDiqKENWLERLKSNAVSAWVSTPSFAYQQL-LSPQFNSEY-LPALNvFIFI-GEVLNKALV 265
Cdd:PRK07788 264 AHLTLAMALGSTVVLRRRFD--PEATLEDIAKHKATALVVVPVMLSRILdLGPEVLAKYdTSSLK-IIFVsGSALSPELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 266 KQLRRRFpqAKII-NSYGPTE---ATIAT-------------TVVEITDAILNSDSAVLPVGVM--------MPeskMEI 320
Cdd:PRK07788 341 TRALEAF--GPVLyNLYGSTEvafATIATpedlaeapgtvgrPPKGVTVKILDENGNEVPRGVVgrifvgngFP---FEG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 321 STDGEliiwGKNVMRGYLglpqenaakllrredeafrgyRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLL 398
Cdd:PRK07788 416 YTDGR----DKQIIDGLL---------------------SSGDVGYfdEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLA 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 399 AMSGINEAVVLPLM-KSCGSvlRIAAFCVT--------DMAPDTIKTSLSKvvphYMVPSQIIVKDALPLNPNGKIDRKL 469
Cdd:PRK07788 471 GHPDVVEAAVIGVDdEEFGQ--RLRAFVVKapgaaldeDAIKDYVRDNLAR----YKVPRDVVFLDELPRNPTGKVLKRE 544
|
.
gi 658547412 470 L 470
Cdd:PRK07788 545 L 545
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
121-468 |
4.07e-16 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 80.70 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 121 ATGEPGKVLE-----EQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWV-------SQDFSLPEKPVLMNHAVfsfdlsL 188
Cdd:PRK05852 160 AATEPTPATStpeglRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIitgyrlsPRDATVAVMPLYHGHGL------I 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 189 IPLLANLAMGGHIVLNAKEDIQKENWLERLKSNAVSAWVSTPSFaYQQLL---SPQFNSEYLPALNVFIFIGEVLNKALV 265
Cdd:PRK05852 234 AALLATLASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTI-HQILLeraATEPSGRKPAALRFIRSCSAPLTAETA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 266 KQLRRRFpQAKIINSYGPTEAT--IATTVVEITDAILNSDSAVLPVG--------VMMPESK-MEISTDGELIIWGKNVM 334
Cdd:PRK05852 313 QALQTEF-AAPVVCAFGMTEAThqVTTTQIEGIGQTENPVVSTGLVGrstgaqirIVGSDGLpLPAGAVGEVWLRGTTVV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 335 RGYLGLPQENAAkllrredeAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINE----- 405
Cdd:PRK05852 392 RGYLGDPTITAA--------NFTDgwLRTGDLGSlsAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEaavfg 463
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658547412 406 -----------AVVLPLMKSCGSVLRIAAFCVTDMAPdtiktslskvvphYMVPSQIIVKDALPLNPNGKIDRK 468
Cdd:PRK05852 464 vpdqlygeavaAVIVPRESAPPTAEELVQFCRERLAA-------------FEIPASFQEASGLPHTAKGSLDRR 524
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
24-470 |
8.32e-16 |
|
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: 79.68 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIpyIPVDCIyPQERLREIC 103
Cdd:cd05920 29 PDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPVLAL-PSHRRSELS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 104 HLASA--PYYYDVATRQ--FIATGEPGKVLEEQ-DLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLM- 177
Cdd:cd05920 106 AFCAHaeAVAYIVPDRHagFDHRALARELAESIpEVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLa 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 178 -NHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKENWL-ERLKSNAVSAwvsTPSFAYQQLLSPQFNSEYLPALNVFIF 255
Cdd:cd05920 186 vLPAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFPLiEREGVTVTAL---VPALVSLWLDAAASRRADLSSLRLLQV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 256 IGEVLNKALVKQLRRRFpQAKIINSYGPTEATIATTVVEITDAI--------LNSDSAVLPV---GVMMPESKMeistdG 324
Cdd:cd05920 263 GGARLSPALARRVPPVL-GCTLQQVFGMAEGLLNYTRLDDPDEViihtqgrpMSPDDEIRVVdeeGNPVPPGEE-----G 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 325 ELIIWGKNVMRGYLGLPQENAAKLlrrEDEAFrgYRTGDLG--YEAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSG 402
Cdd:cd05920 337 ELLTRGPYTIRGYYRAPEHNARAF---TPDGF--YRTGDLVrrTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPA 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658547412 403 INEA--VVLPlmkscGSVL--RIAAFCV-TDMAPDTIKtsLSKV-----VPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05920 412 VHDAavVAMP-----DELLgeRSCAFVVlRDPPPSAAQ--LRRFlrergLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
137-467 |
1.00e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 78.47 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 137 IMFTSGSTGKPKGVQIGRESVW-------HFMKWVSQDfslpeK---PVLMNHAvfsFDLSLiPLLANLAMGGHIVLNAK 206
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVnngyfigERLGLTEQD-----RlciPVPLFHC---FGSVL-GVLACLTHGATMVFPSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 207 --------EDIQKEnwlerlKSNAVSAwvsTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKII 278
Cdd:cd05917 78 sfdplavlEAIEKE------KCTALHG---VPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 279 NSYGPTEATIATTVVEITDAIlnsDSAVLPVGVMMPESKMEI-----------STDGELIIWGKNVMRGYLGLPQENAAK 347
Cdd:cd05917 149 IAYGMTETSPVSTQTRTDDSI---EKRVNTVGRIMPHTEAKIvdpeggivppvGVPGELCIRGYSVMKGYWNDPEKTAEA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 348 LLRRedeafRGYRTGDLGY--EAGliYCQ--GRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLM-KSCGSVlrIA 422
Cdd:cd05917 226 IDGD-----GWLHTGDLAVmdEDG--YCRivGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPdERYGEE--VC 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 658547412 423 AFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDR 467
Cdd:cd05917 297 AWIRlkegAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
104-465 |
1.75e-15 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 78.94 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 104 HLASAPYYYDVATRQFIATGEPGKvleeQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVL-----MN 178
Cdd:PRK13295 173 LLITPAWEQEPDAPAILARLRPGP----DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVIlmaspMA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 179 HAV-FSFDLsLIPLLanlaMGGHIVLnakEDI-QKENWLERLKSNAVS-AWVSTPsFAYQQLLSPQFNSEYLPALNVFIF 255
Cdd:PRK13295 249 HQTgFMYGL-MMPVM----LGATAVL---QDIwDPARAAELIRTEGVTfTMASTP-FLTDLTRAVKESGRPVSSLRTFLC 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 256 IGEVLNKALVKQLRRRFpQAKIINSYGPTEATIATT--------VVEITDA---------ILNSDSAVLPVGvmmpeskm 318
Cdd:PRK13295 320 AGAPIPGALVERARAAL-GAKIVSAWGMTENGAVTLtklddpdeRASTTDGcplpgvevrVVDADGAPLPAG-------- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 319 eisTDGELIIWGKNVMRGYLGLPQENAakllrreDEAFRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENR 396
Cdd:PRK13295 391 ---QIGRLQVRGCSNFGGYLKRPQLNG-------TDADGWFDTGDLARidADGYIRISGRSKDVIIRGGENIPVVEIEAL 460
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658547412 397 LLAMSGINE-AVVLPLMKSCGSvlRIAAFCVT---------DMApDTIKTslSKVVPHYMvPSQIIVKDALPLNPNGKI 465
Cdd:PRK13295 461 LYRHPAIAQvAIVAYPDERLGE--RACAFVVPrpgqsldfeEMV-EFLKA--QKVAKQYI-PERLVVRDALPRTPSGKI 533
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
117-409 |
3.08e-15 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 77.92 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 117 RQFIATGEPGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVwhfmkwVSQDfslpekpvLMNHAVFSFD-----LSLIPL 191
Cdd:PLN02860 157 QRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSAL------IVQS--------LAKIAIVGYGeddvyLHTAPL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 192 ---------LANLAMGGHIVLNAKEDIQKEnwLERLKSNAVSAWVSTPSFaYQQLLSPQFNSEylpALNVFIFIGEVLNK 262
Cdd:PLN02860 223 chigglssaLAMLMVGACHVLLPKFDAKAA--LQAIKQHNVTSMITVPAM-MADLISLTRKSM---TWKVFPSVRKILNG 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 263 A------LVKQLRRRFPQAKIINSYGPTEATIATTVVEITDAIL-------------NSDSAVLPVGVMM--PESKMEI- 320
Cdd:PLN02860 297 GgslssrLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLHDPTLespkqtlqtvnqtKSSSVHQPQGVCVgkPAPHVELk 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 321 ------STDGELIIWGKNVMRGYLGLPQENAAKllrREDEAFrgYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINE 392
Cdd:PLN02860 377 igldesSRVGRILTRGPHVMLGYWGQNSETASV---LSNDGW--LDTGDIGWidKAGNLWLIGRSNDRIKTGGENVYPEE 451
|
330
....*....|....*..
gi 658547412 393 IENRLLAMSGINEAVVL 409
Cdd:PLN02860 452 VEAVLSQHPGVASVVVV 468
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
130-474 |
6.17e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 77.16 E-value: 6.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 130 EEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMN-----HAvFSFD-LSLIPLLanlaMGGHIVL 203
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSflppfHA-YGFNsCTLFPLL----SGVPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 204 nAKEDIQKENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGP 283
Cdd:PRK06334 256 -AYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGT 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 284 TEatiATTVVEITDAilNS---DSAV------LPVGVMMPESKMEISTD--GELIIWGKNVMRGYLGlpQENAAKLLRRE 352
Cdd:PRK06334 335 TE---CSPVITINTV--NSpkhESCVgmpirgMDVLIVSEETKVPVSSGetGLVLTRGTSLFSGYLG--EDFGQGFVELG 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 353 DEAFrgYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSC---GSVLRIAAFC-- 425
Cdd:PRK06334 408 GETW--YVTGDLGYvdRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAADHAGPLVVCglpGEKVRLCLFTtf 485
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 658547412 426 ------VTDMAPDTIKTSLSKVVPHYMVpsqiivkDALPLNPNGKIDRKLLDAYA 474
Cdd:PRK06334 486 ptsiseVNDILKNSKTSSILKISYHHQV-------ESIPMLGTGKPDYCSLNALA 533
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
136-467 |
9.07e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 76.36 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 136 YIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSL-PEKPVLMNHAVFSfDLSLIPLLANLAMGGHIVLNAKedIQKENW 214
Cdd:PRK07638 147 YMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMkREDSVLIAGTLVH-SLFLYGAISTLYVGQTVHLMRK--FIPNQV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 215 LERLKSNAVSAWVSTPSFayqqLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGPTEATIATTVVE 294
Cdd:PRK07638 224 LDKLETENISVMYTVPTM----LESLYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTALVD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 295 itdailnSDSAVLPVGVMMPESKMEI---STDGELI-------IWGKNVMR--GYLglpqeNAAKLLRREDEafRGYRT- 361
Cdd:PRK07638 300 -------EESERRPNSVGRPFHNVQVricNEAGEEVqkgeigtVYVKSPQFfmGYI-----IGGVLARELNA--DGWMTv 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 362 GDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKS-CGSvlrIAAFCVTDMA-PDTIKTS 437
Cdd:PRK07638 366 RDVGYedEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSyWGE---KPVAIIKGSAtKQQLKSF 442
|
330 340 350
....*....|....*....|....*....|
gi 658547412 438 LSKVVPHYMVPSQIIVKDALPLNPNGKIDR 467
Cdd:PRK07638 443 CLQRLSSFKIPKEWHFVDEIPYTNSGKIAR 472
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
132-474 |
1.67e-14 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 76.50 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 132 QDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVF--SFDLS---LIPLLANLAMGGHI-VLNA 205
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTvtlWLPLLEGIKVVYHPdPTDA 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 206 KEdIQKenwleRLKSNAVSAWVSTPSF--AYQQllSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFpQAKIINSYGP 283
Cdd:PRK08633 862 LG-IAK-----LVAKHRATILLGTPTFlrLYLR--NKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKF-GIRILEGYGA 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 284 TEATIATTV----VEITDAILNSDSAVLPVGVMMPESKMEIS-----------TDGELIIWGKNVMRGYLGLPQENAAKL 348
Cdd:PRK08633 933 TETSPVASVnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVdpetfeelppgEDGLILIGGPQVMKGYLGDPEKTAEVI 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 349 lrREDEAFRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGineavvlplmkscGSVLRIAAFCV 426
Cdd:PRK08633 1013 --KDIDGIGWYVTGDKGHldEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALG-------------GEEVVFAVTAV 1077
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658547412 427 TD---------------MAPDTIKTSLSKV-VPHYMVPSQIIVKDALPLNPNGKIDRKLLDAYA 474
Cdd:PRK08633 1078 PDekkgeklvvlhtcgaEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELA 1141
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
129-470 |
4.83e-14 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 74.33 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 129 LEEQDLAYIMFTSGSTGKPKGVQIGRESVW---HFMKWVSQdfsLPEKPVLMN-HAVFSFDLSLIPLLANLAMGGHIVLN 204
Cdd:PRK08008 170 LSTDDTAEILFTSGTTSRPKGVVITHYNLRfagYYSAWQCA---LRDDDVYLTvMPAFHIDCQCTAAMAAFSAGATFVLL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 205 AKEDIQKeNWLERLKSNA-VSAwvSTPSFAYQQLLSPQFNSEYLPALNVFIFIgevLNkaLVKQLRRRFPQ---AKIINS 280
Cdd:PRK08008 247 EKYSARA-FWGQVCKYRAtITE--CIPMMIRTLMVQPPSANDRQHCLREVMFY---LN--LSDQEKDAFEErfgVRLLTS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 281 YGPTEatiaTTVVEITDA--------------------ILNSDSAVLPVGVMmpeskmeistdGELIIWG---KNVMRGY 337
Cdd:PRK08008 319 YGMTE----TIVGIIGDRpgdkrrwpsigrpgfcyeaeIRDDHNRPLPAGEI-----------GEICIKGvpgKTIFKEY 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 338 LGLPQENAaKLLRREdeafrGY-RTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKS 414
Cdd:PRK08008 384 YLDPKATA-KVLEAD-----GWlHTGDTGYvdEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDS 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658547412 415 cgsvLR---IAAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK08008 458 ----IRdeaIKAFVVlnegETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
133-472 |
5.30e-14 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 74.25 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGVQIGRESVwhfMKWVSQ-------DFSLPEKPVL-----MNHaVFSfdLSLIpLLANLAMGGH 200
Cdd:PLN02246 180 DVVALPYSSGTTGLPKGVMLTHKGL---VTSVAQqvdgenpNLYFHSDDVIlcvlpMFH-IYS--LNSV-LLCGLRVGAA 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 201 IVLNAKEDIQKenWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINS 280
Cdd:PLN02246 253 ILIMPKFEIGA--LLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 281 YGPTEA--TIAT-----------------TVVEITDA-ILNSDSavlpvGVMMPESKmeistDGELIIWGKNVMRGYLGL 340
Cdd:PLN02246 331 YGMTEAgpVLAMclafakepfpvksgscgTVVRNAELkIVDPET-----GASLPRNQ-----PGEICIRGPQIMKGYLND 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 341 PQENAAKLlrrEDEAFrgYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPlMK--SCG 416
Cdd:PLN02246 401 PEATANTI---DKDGW--LHTGDIGYidDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVP-MKdeVAG 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 417 SVlrIAAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLLDA 472
Cdd:PLN02246 475 EV--PVAFVVrsngSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
60-394 |
6.85e-14 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 73.68 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 60 GTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQE---RLREICHLASAPYyydvatrqFIATGEPGKVLEEQdLAY 136
Cdd:cd05908 40 GQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEhklKLNKVWNTLKNPY--------LITEEEVLCELADE-LAF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 137 IMFTSGSTGKPKGVQIGRESVWHFM-------KWVSQDFSLPEKPVLMNHAVFSFDLSliPLLANLamgGHIVLNAKEDI 209
Cdd:cd05908 111 IQFSSGSTGDPKGVMLTHENLVHNMfailnstEWKTKDRILSWMPLTHDMGLIAFHLA--PLIAGM---NQYLMPTRLFI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 210 QKE-NWLERLKSNAVSAwVSTPSFAYQQLLSpQFNSEY-----LPALNVFIFIGEVLNKALVKQLRRRFPQAK-----II 278
Cdd:cd05908 186 RRPiLWLKKASEHKATI-VSSPNFGYKYFLK-TLKPEKandwdLSSIRMILNGAEPIDYELCHEFLDHMSKYGlkrnaIL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 279 NSYGPTEATIATTVVEI-------------------TDAILNSDS---AVLPVGVMMPESKMEISTD----------GEL 326
Cdd:cd05908 264 PVYGLAEASVGASLPKAqspfktitlgrrhvthgepEPEVDKKDSeclTFVEVGKPIDETDIRICDEdnkilpdgyiGHI 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 327 IIWGKNVMRGYLGLPQENAAKLlrREDeafrGY-RTGDLGY-EAGLIYCQGRNDSQVKLNGYRIEINEIE 394
Cdd:cd05908 344 QIRGKNVTPGYYNNPEATAKVF--TDD----GWlKTGDLGFiRNGRLVITGREKDIIFVNGQNVYPHDIE 407
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
24-470 |
1.02e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 73.11 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLREI- 102
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAl 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 103 -CHLASAPYYYDVATRQFIATGE------PGKVLEEQDLA---------YIMFTSGSTGKPKGVQIGRESVWHFMKWVSq 166
Cdd:PRK13383 129 rAHHISTVVADNEFAERIAGADDavavidPATAGAEESGGrpavaapgrIVLLTSGTTGKPKGVPRAPQLRSAVGVWVT- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 167 dfsLPEKPVL-----MNHAVFSFD-LSLIPLLANLAMGGHIVLNAKEDiqKENWLERLKSNAVSAWVSTPSFAYQQL-LS 239
Cdd:PRK13383 208 ---ILDRTRLrtgsrISVAMPMFHgLGLGMLMLTIALGGTVLTHRHFD--AEAALAQASLHRADAFTAVPVVLARILeLP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 240 PQFNSEY-LPALNVFIFIGEVLNKALVkqlrRRFPQAK---IINSYGPTEATIAT--TVVEITDA--------------I 299
Cdd:PRK13383 283 PRVRARNpLPQLRVVMSSGDRLDPTLG----QRFMDTYgdiLYNGYGSTEVGIGAlaTPADLRDApetvgkpvagcpvrI 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 300 LNSDSAvlPVGvmmPESKMEISTDGELII------WGKNVMRGYLGlpqenaakllrredeafrgyrTGDLGY--EAGLI 371
Cdd:PRK13383 359 LDRNNR--PVG---PRVTGRIFVGGELAGtrytdgGGKAVVDGMTS---------------------TGDMGYldNAGRL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 372 YCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLM-KSCGSvlRIAAFCV----TDMAPDTIKTSLSKVVPHYM 446
Cdd:PRK13383 413 FIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPdERFGH--RLAAFVVlhpgSGVDAAQLRDYLKDRVSRFE 490
|
490 500
....*....|....*....|....
gi 658547412 447 VPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK13383 491 QPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
129-409 |
1.36e-13 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 72.83 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 129 LEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLmnhavfsfdLSLIPL---------LANLAMGG 199
Cdd:COG1022 180 VKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRT---------LSFLPLahvfertvsYYALAAGA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 200 HIVL-----NAKEDIQ--KENWL-------ERLKsNAVSAWVSTPSFAYQQLlspqFNSeylpALNV------FIFIGE- 258
Cdd:COG1022 251 TVAFaespdTLAEDLRevKPTFMlavprvwEKVY-AGIQAKAEEAGGLKRKL----FRW----ALAVgrryarARLAGKs 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 259 ----------VLNKALVKQLRRRF-PQAKIINS-----------------------YGPTEATIATTVveitdailNSDS 304
Cdd:COG1022 322 pslllrlkhaLADKLVFSKLREALgGRLRFAVSggaalgpelarffralgipvlegYGLTETSPVITV--------NRPG 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 305 AVLP--VGVMMPESKMEISTDGELIIWGKNVMRGYLGLPQENAakllrredEAFR--GY-RTGDLGY--EAGLIYCQGRN 377
Cdd:COG1022 394 DNRIgtVGPPLPGVEVKIAEDGEILVRGPNVMKGYYKNPEATA--------EAFDadGWlHTGDIGEldEDGFLRITGRK 465
|
330 340 350
....*....|....*....|....*....|...
gi 658547412 378 DSQVKL-NGYRIEINEIENRLLAMSGINEAVVL 409
Cdd:COG1022 466 KDLIVTsGGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
131-470 |
2.01e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 72.37 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 131 EQDLAYIMFTSGSTGKPKGVQIGRES-VWHFMKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAM--GGHIVLNAKE 207
Cdd:PRK06710 205 ENDLALLQYTGGTTGFPKGVMLTHKNlVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNLSImqGYKMVLIPKF 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 208 DIQKEnwLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIfIGEVLNKALVKQLRRRFPQAKIINSYGPTEAT 287
Cdd:PRK06710 285 DMKMV--FEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACI-SGSAPLPVEVQEKFETVTGGKLVEGYGLTESS 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 288 IATtvveiTDAILNSDSAVLPVGVMMPESKMEIST-----------DGELIIWGKNVMRGYLGLPQENAAKLlrrEDeaf 356
Cdd:PRK06710 362 PVT-----HSNFLWEKRVPGSIGVPWPDTEAMIMSletgealppgeIGEIVVKGPQIMKGYWNKPEETAAVL---QD--- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 357 rGY-RTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSC-GSVLRiaAFCV----TD 428
Cdd:PRK06710 431 -GWlHTGDVGYmdEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYrGETVK--AFVVlkegTE 507
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 658547412 429 MAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK06710 508 CSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
324-470 |
3.56e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 71.61 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 324 GELIIWGKNVMRGYLGLPQENAakllrredEAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLA 399
Cdd:PRK07470 367 GEICVIGPAVFAGYYNNPEANA--------KAFRDgwFRTGDLGHldARGFLYITGRASDMYISGGSNVYPREIEEKLLT 438
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658547412 400 MSGINEAVVL----PLMKSCGsvlriAAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK07470 439 HPAVSEVAVLgvpdPVWGEVG-----VAVCVardgAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
130-470 |
7.94e-13 |
|
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: 70.15 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 130 EEQDLAYIMFTSGSTGKPKG------VQIGRESVWHFmkwvSQDFSLPEKPVLMNHAVFS-----FDLslipLLANLAMG 198
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGalhahrVLLGHLPGVQF----PFNLFPRDGDLYWTPADWAwigglLDV----LLPSLYFG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 199 GHIVLNAKEDIQKENWLERLKSNAVSAWVSTPS------FAYQQLLSPQFNseyLPALNVFifiGEVLNKALVKQLRRRF 272
Cdd:cd05971 158 VPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTalkmmrQQGEQLKHAQVK---LRAIATG---GESLGEELLGWAREQF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 273 pQAKIINSYGPTEAtiattvveitDAILNSDSAVLPV--GVM---MPESKMEISTD-GELIIWGKnvmRGYLGLPQENAA 346
Cdd:cd05971 232 -GVEVNEFYGQTEC----------NLVIGNCSALFPIkpGSMgkpIPGHRVAIVDDnGTPLPPGE---VGEIAVELPDPV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 347 KLLR--REDEAFRG------YRTGDLGYEA--GLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSC- 415
Cdd:cd05971 298 AFLGywNNPSATEKkmagdwLLTGDLGRKDsdGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIr 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658547412 416 GSVLRiaAFCVtdMAP-----DTIKTSLSKVVP----HYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05971 378 GEIVK--AFVV--LNPgetpsDALAREIQELVKtrlaAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
127-470 |
8.56e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 70.39 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 127 KVLEEQDLAYIMFTSGSTGKPKGVQIGRESVwhFMKWVSQDFSLpeKPVLMNHAVfsfDLSLIPLL----------ANLA 196
Cdd:PLN02330 179 EEILQTDLCALPFSSGTTGISKGVMLTHRNL--VANLCSSLFSV--GPEMIGQVV---TLGLIPFFhiygitgiccATLR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 197 MGGHIVLNAKEDIQkeNWLERLKSNAVSAWVSTPSFAYQQLLSP---QFNSEYLpALNVFIFIGEVLNKALVKQLRRRFP 273
Cdd:PLN02330 252 NKGKVVVMSRFELR--TFLNALITQEVSFAPIVPPIILNLVKNPiveEFDLSKL-KLQAIMTAAAPLAPELLTAFEAKFP 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 274 QAKIINSYGPTEATIATTVVEITD-----AILNSDSAVLP---VGVMMPESKMEI--STDGELIIWGKNVMRGYLGLPQE 343
Cdd:PLN02330 329 GVQVQEAYGLTEHSCITLTHGDPEkghgiAKKNSVGFILPnleVKFIDPDTGRSLpkNTPGELCVRSQCVMQGYYNNKEE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 344 NAakllRREDEafRGY-RTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLR 420
Cdd:PLN02330 409 TD----RTIDE--DGWlHTGDIGYidDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIP 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 658547412 421 IAAFCVTDMAPDTIKTSLSKV---VPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PLN02330 483 AACVVINPKAKESEEDILNFVaanVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
117-472 |
1.00e-12 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 70.29 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 117 RQFIATGE----PGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMK----WVSQDFSLPEKPVLMNHAVFSFdlSL 188
Cdd:PRK08751 189 REALALGRkhsmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQqahqWLAGTGKLEEGCEVVITALPLY--HI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 189 IPLLAN----LAMGG--HIVLNAKEdiqKENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNK 262
Cdd:PRK08751 267 FALTANglvfMKIGGcnHLISNPRD---MPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQR 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 263 ALVKQLrRRFPQAKIINSYGPTEATIATTV---------------VEITDAILNSDSA-VLPVGVMmpeskmeistdGEL 326
Cdd:PRK08751 344 SVAERW-KQVTGLTLVEAYGLTETSPAACInpltlkeyngsiglpIPSTDACIKDDAGtVLAIGEI-----------GEL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 327 IIWGKNVMRGYLGLPQENAAKLlrredEAFRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGIN 404
Cdd:PRK08751 412 CIKGPQVMKGYWKRPEETAKVM-----DADGWLHTGDIARmdEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL 486
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658547412 405 E--AVVLPLMKSCGSVLRIAAFCVTDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKI-DRKLLDA 472
Cdd:PRK08751 487 EvaAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKIlRRELRDA 557
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
137-470 |
1.16e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 69.84 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 137 IMFTSGSTGKPKGVQIGRESVWHfmkwVSQDFSLPEKpvLMNHAVFSFD---LSLIPLLAN----LAMGGHI-VLNAKED 208
Cdd:PRK09088 140 ILFTSGTSGQPKGVMLSERNLQQ----TAHNFGVLGR--VDAHSSFLCDapmFHIIGLITSvrpvLAVGGSIlVSNGFEP 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 209 IQKENWLERLkSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVfIFIGEVLNKA--LVKQLRRRFPqakIINSYGPTEA 286
Cdd:PRK09088 214 KRTLGRLGDP-ALGITHYFCVPQMAQAFRAQPGFDAAALRHLTA-LFTGGAPHAAedILGWLDDGIP---MVDGFGMSEA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 287 -TIATTVVEiTDAILNSDSAvlpVGVMMPESKMEISTD----------GELIIWGKNVMRGYLGLPQENAakllrredEA 355
Cdd:PRK09088 289 gTVFGMSVD-CDVIRAKAGA---AGIPTPTVQTRVVDDqgndcpagvpGELLLRGPNLSPGYWRRPQATA--------RA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 356 FRG---YRTGDLGYE--AGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKS-CGSVLRIAAFCVTDM 429
Cdd:PRK09088 357 FTGdgwFRTGDIARRdaDGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAqWGEVGYLAIVPADGA 436
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 658547412 430 APDT--IKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK09088 437 PLDLerIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
132-468 |
1.77e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 69.26 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 132 QDLAYIMFTSGSTGKPKGVQI-----------GREsvwhfmkWVSqdfSLPEKP-----VL-MNHAvfsFDLSLIPLLAn 194
Cdd:PRK05605 219 DDVALILYTSGTTGKPKGAQLthrnlfanaaqGKA-------WVP---GLGDGPervlaALpMFHA---YGLTLCLTLA- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 195 LAMGGHIVLNAKEDI---------QKENWL-------ERLKSNAVSAWVSTPSFAYQqlLSPQFNseyLPALNVFIFigE 258
Cdd:PRK05605 285 VSIGGELVLLPAPDIdlildamkkHPPTWLpgvpplyEKIAEAAEERGVDLSGVRNA--FSGAMA---LPVSTVELW--E 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 259 VLNKALvkqlrrrfpqakIINSYGPTEatiaTTVVeITDAILNSDSAVLPVGVMMPESKMEIS------------TDGEL 326
Cdd:PRK05605 358 KLTGGL------------LVEGYGLTE----TSPI-IVGNPMSDDRRPGYVGVPFPDTEVRIVdpedpdetmpdgEEGEL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 327 IIWGKNVMRGYLGLPQENAAKLLrreDEAFRgyrTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGIN 404
Cdd:PRK05605 421 LVRGPQVFKGYWNRPEETAKSFL---DGWFR---TGDVVVmeEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVE 494
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658547412 405 EAVVLPLMKSCGSVLRIAAFCVTDMA---PDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRK 468
Cdd:PRK05605 495 DAAVVGLPREDGSEEVVAAVVLEPGAaldPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
129-376 |
2.86e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 68.77 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 129 LEEQDLAYIMFTSGSTGKPKGV---------QIGResvwhfmkwVSQDFslPEKPVlmnhavfSFDLSLIPLLA--NLAM 197
Cdd:PRK09274 171 LAPDDMAAILFTSGSTGTPKGVvythgmfeaQIEA---------LREDY--GIEPG-------EIDLPTFPLFAlfGPAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 198 GGHIVLN-------AKEDIQKenwlerLKSnAVSAWVSTPSFAYQQLLSP-----QFNSEYLPALNVFIFIGEVLNKALV 265
Cdd:PRK09274 233 GMTSVIPdmdptrpATVDPAK------LFA-AIERYGVTNLFGSPALLERlgrygEANGIKLPSLRRVISAGAPVPIAVI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 266 KQLRRRFPQ-AKIINSYGPTEA----TI-------ATT---------------------VVEITDAILN--SDSAVLPVG 310
Cdd:PRK09274 306 ERFRAMLPPdAEILTPYGATEAlpisSIesreilfATRaatdngagicvgrpvdgvevrIIAISDAPIPewDDALRLATG 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658547412 311 vmmpeskmEIstdGELIIWGKNVMRGYLGLPQENAAKLLRREDEAFRgYRTGDLGY--EAGLIYCQGR 376
Cdd:PRK09274 386 --------EI---GEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVW-HRMGDLGYldAQGRLWFCGR 441
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
133-470 |
3.09e-12 |
|
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: 68.31 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFSFDLSLI-PLLANLAMGGHIVLNAKEDIQK 211
Cdd:cd05973 89 DPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYyAITGPLALGHPTILLEGGFSVE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 212 ENW--LERLksnAVSAWVSTPSfAYQQLLSPQFNSEYLPA--LNVFIFIGEVLNKALVKQLRRRFpQAKIINSYGPTE-- 285
Cdd:cd05973 169 STWrvIERL---GVTNLAGSPT-AYRLLMAAGAEVPARPKgrLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTElg 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 286 ---------------ATIATTVVEITDAILNSDSAVLPVGVMmpeSKMEISTDGELIIWgknvMRGYLGLPQENAAKllr 350
Cdd:cd05973 244 mvlanhhalehpvhaGSAGRAMPGWRVAVLDDDGDELGPGEP---GRLAIDIANSPLMW----FRGYQLPDTPAIDG--- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 351 redeafRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVL----PLMkscGSVLRiaAF 424
Cdd:cd05973 314 ------GYYLTGDTVEfdPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIgvpdPER---TEVVK--AF 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 658547412 425 CV--------TDMApDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05973 383 VVlrgghegtPALA-DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
133-474 |
3.19e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 68.62 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFT-SGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQK 211
Cdd:PRK06164 181 DAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAAR 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 212 EnwLERLKSNAVsawvsTPSFA----YQQLLSPQFNSEYLPALNVFIF------IGEVLNKALVkqlrRRFPQAKIinsY 281
Cdd:PRK06164 261 T--ARALRRHRV-----THTFGndemLRRILDTAGERADFPSARLFGFasfapaLGELAALARA----RGVPLTGL---Y 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 282 GPTEaTIAttVVEITDAILNSDSAVLPVGVMM-PESKMEI-----------STDGELIIWGKNVMRGYLGLPqENAAKLL 349
Cdd:PRK06164 327 GSSE-VQA--LVALQPATDPVSVRIEGGGRPAsPEARVRArdpqdgallpdGESGEIEIRAPSLMRGYLDNP-DATARAL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 350 RREdeafrGY-RTGDLGY---EAGLIYcQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKscGSVLRIAAFC 425
Cdd:PRK06164 403 TDD-----GYfRTGDLGYtrgDGQFVY-QTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATR--DGKTVPVAFV 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 658547412 426 V----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALP--LNPNG-KIDRKLLDAYA 474
Cdd:PRK06164 475 IptdgASPDEAGLMAACREALAGFKVPARVQVVEAFPvtESANGaKIQKHRLREMA 530
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
125-470 |
4.74e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 67.94 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 125 PGKVLEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMK-WVSQDFSLPEKP--------VLMNHAVFSFDLSLIPLLAnl 195
Cdd:PLN02574 191 PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElFVRFEASQYEYPgsdnvylaALPMFHIYGLSLFVVGLLS-- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 196 aMGGHIVLNAKEDIQKE-NWLERLKsnaVSAWVSTPSfayqqLLSPQFNSEYLPALNVFIFIGEV------LNKALVKQL 268
Cdd:PLN02574 269 -LGSTIVVMRRFDASDMvKVIDRFK---VTHFPVVPP-----ILMALTKKAKGVCGEVLKSLKQVscgaapLSGKFIQDF 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 269 RRRFPQAKIINSYGPTEATIATTVVEITDAILNSDSavlpVGVMMPESKMEI-----------STDGELIIWGKNVMRGY 337
Cdd:PLN02574 340 VQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYSS----VGLLAPNMQAKVvdwstgcllppGNCGELWIQGPGVMKGY 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 338 LGLPQenaAKLLRREDEAFrgYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLM-KS 414
Cdd:PLN02574 416 LNNPK---ATQSTIDKDGW--LRTGDIAYfdEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPdKE 490
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 415 CGSVlrIAAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PLN02574 491 CGEI--PVAFVVrrqgSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
10-470 |
1.02e-11 |
|
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: 67.09 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 10 LQDFLRAALcdPASPQQLAISGSDEALSWLQLSAAVTDWAQRYQRCQPVAGTPVVLYGHQQAEFAVAIYSCLlhNIPYIP 89
Cdd:COG1021 27 LGDLLRRRA--ERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALF--RAGAIP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 90 VDCiYPQERLREICHLAS------------------APYYYDVAT-----RQFIATGEPGKV--LEE------------- 131
Cdd:COG1021 103 VFA-LPAHRRAEISHFAEqseavayiipdrhrgfdyRALARELQAevpslRHVLVVGDAGEFtsLDAllaapadlseprp 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 132 --QDLAYIMFTSGSTGKPKG--------VQIGRESV--WHFmkwvSQD----FSLPekpvlmnhAVFSFDLSLIPLLANL 195
Cdd:COG1021 182 dpDDVAFFQLSGGTTGLPKLiprthddyLYSVRASAeiCGL----DADtvylAALP--------AAHNFPLSSPGVLGVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 196 AMGGHIVL--NAKED-----IQKEnwlerlKSNAVSAwvsTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQL 268
Cdd:COG1021 250 YAGGTVVLapDPSPDtafplIERE------RVTVTAL---VPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 269 RRRFPqAKIINSYG-------------PTEaTIATTV---------VEITDAilnsDSAVLPVGvmmpeskmeisTDGEL 326
Cdd:COG1021 321 RPALG-CTLQQVFGmaeglvnytrlddPEE-VILTTQgrpispddeVRIVDE----DGNPVPPG-----------EVGEL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 327 IIWGKNVMRGYLGLPQENAAkllrredeAF--RG-YRTGDL------GYeaglIYCQGRNDSQVKLNGYRIEINEIENRL 397
Cdd:COG1021 384 LTRGPYTIRGYYRAPEHNAR--------AFtpDGfYRTGDLvrrtpdGY----LVVEGRAKDQINRGGEKIAAEEVENLL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 398 LAMSGINEAVVL----PLM--KSCgsvlriaAFCVTDMAP---DTIKTSL-SKVVPHYMVPSQIIVKDALPLNPNGKIDR 467
Cdd:COG1021 452 LAHPAVHDAAVVampdEYLgeRSC-------AFVVPRGEPltlAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDK 524
|
...
gi 658547412 468 KLL 470
Cdd:COG1021 525 KAL 527
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
118-470 |
1.50e-11 |
|
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: 66.50 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 118 QFIATGEPG---KVLEEQDLAYIMFTSGSTGKPKGVQIGRESVW-HFMKWVSQD-FSLPEK----PVL-MNHaVFSFDLs 187
Cdd:cd12119 146 ELLAAESPEydwPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVlHAMAALLTDgLGLSESdvvlPVVpMFH-VNAWGL- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 188 liPLLANLAmGGHIVLNAKEDiQKENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQ 267
Cdd:cd12119 224 --PYAAAMV-GAKLVLPGPYL-DPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 268 LRRRFpqAKIINSYGPTE----ATIATTVVEITDAILNSDSAVLPV-GVMMPESKMEISTD------------GELIIWG 330
Cdd:cd12119 300 FEERG--VRVIHAWGMTEtsplGTVARPPSEHSNLSEDEQLALRAKqGRPVPGVELRIVDDdgrelpwdgkavGELQVRG 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 331 KNVMRGYLGLPQENAAKLlrrEDEAFrgyRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVV 408
Cdd:cd12119 378 PWVTKSYYKNDEESEALT---EDGWL---RTGDVATidEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAV 451
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658547412 409 L----------PLmkscgsvlriaAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd12119 452 IgvphpkwgerPL-----------AVVVlkegATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
128-408 |
1.70e-11 |
|
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: 66.23 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 128 VLE--EQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMN-----HAvFSFDLSLIPLLANLAMGGH 200
Cdd:cd17640 82 VVEndSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSilpiwHS-YERSAEYFIFACGCSQAYT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 201 IVLNAKEDIQKEN----------WlERLKSNaVSAWVSTPSFAYQQLLspQFnseylpalnvFIFIGEVL-----NKALV 265
Cdd:cd17640 161 SIRTLKDDLKRVKphyivsvprlW-ESLYSG-IQKQVSKSSPIKQFLF--LF----------FLSGGIFKfgisgGGALP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 266 KQLRRRFPQA--KIINSYGPTEATIATTVVEITDAILNSDSAVLP---VGVMMPESKMEISTDGELIIW--GKNVMRGYL 338
Cdd:cd17640 227 PHVDTFFEAIgiEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPgteIKIVDPEGNVVLPPGEKGIVWvrGPQVMKGYY 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658547412 339 GLPqENAAKLLrREDEAFrgyRTGDLGY--EAGLIYCQGR-NDSQVKLNGYRIEINEIENRLLAMSGINEAVV 408
Cdd:cd17640 307 KNP-EATSKVL-DSDGWF---NTGDLGWltCGGELVLTGRaKDTIVLSNGENVEPQPIEEALMRSPFIEQIMV 374
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
115-472 |
2.47e-11 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 65.55 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 115 ATRQFIATGEPGKVleeqdlayIMFTSGSTGKPKGVQ------IGR-ESVWHFMKWVSQDFSLPEKPvlMNHAV-FSfdl 186
Cdd:PRK13382 187 AGQRPEPTGRKGRV--------ILLTSGTTGTPKGARrsgpggIGTlKAILDRTPWRAEEPTVIVAP--MFHAWgFS--- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 187 sliPLLANLAMGGHIVLNAKEDiqKENWLERLKSNAVSAWVSTPSFAYQQLLSPQ--FNSEYLPALNVFIFIGEVLNKAL 264
Cdd:PRK13382 254 ---QLVLAASLACTIVTRRRFD--PEATLDLIDRHRATGLAVVPVMFDRIMDLPAevRNRYSGRSLRFAAASGSRMRPDV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 265 VKQLRRRFPQAkIINSYGPTEATIATTVveiTDAILNS--DSAVLPVgvMMPESKMeisTDGEliiwGKNVMRGYLGlpq 342
Cdd:PRK13382 329 VIAFMDQFGDV-IYNNYNATEAGMIATA---TPADLRAapDTAGRPA--EGTEIRI---LDQD----FREVPTGEVG--- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 343 enaaKLLRREDEAFRGYR-------------TGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAV 407
Cdd:PRK13382 393 ----TIFVRNDTQFDGYTsgstkdfhdgfmaSGDVGYldENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAA 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 408 VLPLMKS-CGSvlRIAAFCVTD----MAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLLDA 472
Cdd:PRK13382 469 VIGVDDEqYGQ--RLAAFVVLKpgasATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
113-474 |
5.41e-11 |
|
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: 64.40 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 113 DVATRQFIatGEPgkvlEEQDLAYIMFTSGSTGKPKGVqigresVWHFMKWVSQDFSLPEkpvLMNHAVFSFDLSLIPLL 192
Cdd:cd05910 72 EAEPDAFI--GIP----KADEPAAILFTSGSTGTPKGV------VYRHGTFAAQIDALRQ---LYGIRPGEVDLATFPLF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 193 A--NLAMGGHIVLNAKEDIQKENWLERLKSNAVSAWVSTPSFAYQQLLSP-----QFNSEYLPALNVFIFIGEVLNKALV 265
Cdd:cd05910 137 AlfGPALGLTSVIPDMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERvarycAQHGITLPSLRRVLSAGAPVPIALA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 266 KQLRRRF-PQAKIINSYGPTEA----TIATTVVEITDAILNSDSAVLPVGVMMPESKMEI--STD--------------- 323
Cdd:cd05910 217 ARLRKMLsDEAEILTPYGATEAlpvsSIGSRELLATTTAATSGGAGTCVGRPIPGVRVRIieIDDepiaewddtlelprg 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 324 --GELIIWGKNVMRGYLGLPQENAAKLLRREDEAFRgYRTGDLGY---EAGLIYCqGRNDSQVKLNG---YRIEINEIEN 395
Cdd:cd05910 297 eiGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFW-HRMGDLGYlddEGRLWFC-GRKAHRVITTGgtlYTEPVERVFN 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 396 -----RLLAMSGINEAVV-LPLMkscgsvlriaafCVTDMaPDTIKTS---------LSKVVPHYMVPSQIIVKDALPLN 460
Cdd:cd05910 375 thpgvRRSALVGVGKPGCqLPVL------------CVEPL-PGTITPRarleqelraLAKDYPHTQRIGRFLIHPSFPVD 441
|
410
....*....|....*.
gi 658547412 461 P--NGKIDRKLLDAYA 474
Cdd:cd05910 442 IrhNAKIFREKLAVWA 457
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
263-470 |
5.64e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 64.84 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 263 ALVKQLRRRFPQ---AKIINSYGPTEAT-IATTVVEITDAILNSdsavlpVGVMMPESKMEISTD----------GELII 328
Cdd:PRK12492 344 ALVKATAERWEQltgCTIVEGYGLTETSpVASTNPYGELARLGT------VGIPVPGTALKVIDDdgnelplgerGELCI 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 329 WGKNVMRGYLGLPQENAAKLlrredEAFRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGI--- 403
Cdd:PRK12492 418 KGPQVMKGYWQQPEATAEAL-----DAEGWFKTGDIAVidPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVanc 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658547412 404 ----------NEAVVLPLMKSCG--SVLRIAAFCvtdmapdtiKTSLSKvvphYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK12492 493 aaigvpdersGEAVKLFVVARDPglSVEELKAYC---------KENFTG----YKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
135-465 |
6.06e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 64.41 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 135 AYIMFTSGSTGKPKGvqigreSVWHFMKWVSQDFSLpekpVLMNHAVFSFDLSLI--PL---------LANLAMGGHIVL 203
Cdd:PRK07786 177 ALIMYTSGTTGRPKG------AVLTHANLTGQAMTC----LRTNGADINSDVGFVgvPLfhiagigsmLPGLLLGAPTVI 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 204 NAKEDIQKENWLERLKSNAVSAWVSTPSfAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGP 283
Cdd:PRK07786 247 YPLGAFDPGQLLDVLEAEKVTGIFLVPA-QWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 284 TEATIATTVVEITDAI--LNSDSAVLP-VGVMMPESKME---ISTDGELIIWGKNVMRGYLGLPQENAakllrredEAFR 357
Cdd:PRK07786 326 TEMSPVTCMLLGEDAIrkLGSVGKVIPtVAARVVDENMNdvpVGEVGEIVYRAPTLMSGYWNNPEATA--------EAFA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 358 G--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLRIAAFCVT----DM 429
Cdd:PRK07786 398 GgwFHSGDLVRqdEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRnddaAL 477
|
330 340 350
....*....|....*....|....*....|....*.
gi 658547412 430 APDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKI 465
Cdd:PRK07786 478 TLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
132-467 |
1.67e-10 |
|
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: 63.28 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 132 QDLAYIMFTSGSTGKPKGVQ---------IGRESVWHFMKWVSQDFSLPE----KPV--------LMNHAVFSFDLslip 190
Cdd:cd05970 185 EDILLVYFSSGTTGMPKMVEhdftyplghIVTAKYWQNVREGGLHLTVADtgwgKAVwgkiygqwIAGAAVFVYDY---- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 191 llanlamgghivlnakEDIQKENWLERLKSNAVSAWVSTPSFaYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRR 270
Cdd:cd05970 261 ----------------DKFDPKALLEKLSKYGVTTFCAPPTI-YRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 271 rFPQAKIINSYGPTEATIATTV---VEITDAILNSDSAVLPVGVMMPESK-MEISTDGELIIwgkNVMRGY-LGLPQENA 345
Cdd:cd05970 324 -KTGIKLMEGFGQTETTLTIATfpwMEPKPGSMGKPAPGYEIDLIDREGRsCEAGEEGEIVI---RTSKGKpVGLFGGYY 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 346 AKLLRREDEAFRG-YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVL----PLMkscGSV 418
Cdd:cd05970 400 KDAEKTAEVWHDGyYHTGDAAWmdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTgvpdPIR---GQV 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 658547412 419 LRIAAFCVTDMAP-DTIKTSL----SKVVPHYMVPSQIIVKDALPLNPNGKIDR 467
Cdd:cd05970 477 VKATIVLAKGYEPsEELKKELqdhvKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
129-472 |
1.96e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 62.99 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 129 LEEQDLAYIMFTSGSTGKPKGV-QIGRESVWHFM--KWVsQDfsLPEKPVL-----------MNHAVFSfdlsliPLLAN 194
Cdd:PRK04319 202 TDREDGAILHYTSGSTGKPKGVlHVHNAMLQHYQtgKYV-LD--LHEDDVYwctadpgwvtgTSYGIFA------PWLNG 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 195 LAMgghIVLNAKEDiqKENWLERLKSNAVSAWVSTPSfAYQQLLS--PQFNSEY-LPALNVFIFIGEVLNKALVKQLRRR 271
Cdd:PRK04319 273 ATN---VIDGGRFS--PERWYRILEDYKVTVWYTAPT-AIRMLMGagDDLVKKYdLSSLRHILSVGEPLNPEVVRWGMKV 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 272 FPQaKIINSYGPTEA---TIATTVVE-------------ITDAILNSDSAVLPVGVMmpeskmeistdGELII---WgKN 332
Cdd:PRK04319 347 FGL-PIHDNWWMTETggiMIANYPAMdikpgsmgkplpgIEAAIVDDQGNELPPNRM-----------GNLAIkkgW-PS 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 333 VMRGYLGLPQenaakllrREDEAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVV 408
Cdd:PRK04319 414 MMRGIWNNPE--------KYESYFAGdwYVSGDSAYmdEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658547412 409 L----PLMkscGSVlrIAAFCV--TDMAP-DTIKTSLSKVV-----PHyMVPSQIIVKDALPLNPNGKIDRKLLDA 472
Cdd:PRK04319 486 IgkpdPVR---GEI--IKAFVAlrPGYEPsEELKEEIRGFVkkglgAH-AAPREIEFKDKLPKTRSGKIMRRVLKA 555
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
360-472 |
2.34e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 62.36 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 360 RTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVL----PLMKScgsvlRIAAFCVTD--MAP 431
Cdd:PRK08308 294 FTKDLGYksERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgkdPVAGE-----RVKAKVISHeeIDP 368
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 658547412 432 DTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLLDA 472
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
133-474 |
2.41e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 62.75 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKG-VQIGRESVWHFMKWVSQDFSLPEKPVLMNH-AVFSF---DLSLI-PLLAnlamGGHIVLNAK 206
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGcEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFlPEFWIageNFGLLfPLFS----GATLVLLAR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 207 EDIQ---------KENWLERLKSNAVSAwVSTPSFAyqqllspQFNSEYLPALNVFIFIgevlnKALVKQLRRRFPQAK- 276
Cdd:PRK06178 286 WDAVafmaaveryRVTRTVMLVDNAVEL-MDHPRFA-------EYDLSSLRQVRVVSFV-----KKLNPDYRQRWRALTg 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 277 -II--NSYGPTEATIA---TTVVEITDAILNSDSAV--LPV------------GVMMPeskmeISTDGELIIWGKNVMRG 336
Cdd:PRK06178 353 sVLaeAAWGMTETHTCdtfTAGFQDDDFDLLSQPVFvgLPVpgtefkicdfetGELLP-----LGAEGEIVVRTPSLLKG 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 337 YLGLPQENAakllrredEAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIEnrllAMSGINEAVVlplm 412
Cdd:PRK06178 428 YWNKPEATA--------EALRDgwLHTGDIGKidEQGFLHYLGRRKEMLKVNGMSVFPSEVE----ALLGQHPAVL---- 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 413 kSCGSVLR-------------------------IAAFCVTDMAPdtiktslskvvphYMVPsQIIVKDALPLNPNGKIDR 467
Cdd:PRK06178 492 -GSAVVGRpdpdkgqvpvafvqlkpgadltaaaLQAWCRENMAV-------------YKVP-EIRIVDALPMTATGKVRK 556
|
....*..
gi 658547412 468 KLLDAYA 474
Cdd:PRK06178 557 QDLQALA 563
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
235-474 |
5.20e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 61.16 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 235 QQLLspQFNSEYLPALNVfIFIG------EVLNKAlvkqlrrRFPQAKIINSYGPTEaTIATTVVEITDAILNSDSAVlp 308
Cdd:PRK07445 219 QRLL--QLRPQWLAQFRT-ILLGgapawpSLLEQA-------RQLQLRLAPTYGMTE-TASQIATLKPDDFLAGNNSS-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 309 vGVMMPESKMEI--STDGELIIWGKNVMRGYLglPQ-ENAAKLLRredeafrgyrTGDLGY--EAGLIYCQGRNDSQVKL 383
Cdd:PRK07445 286 -GQVLPHAQITIpaNQTGNITIQAQSLALGYY--PQiLDSQGIFE----------TDDLGYldAQGYLHILGRNSQKIIT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 384 NGYRIEINEIENRLLAMSGINEAVVLPLM-KSCGSVlrIAAFCV---TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPL 459
Cdd:PRK07445 353 GGENVYPAEVEAAILATGLVQDVCVLGLPdPHWGEV--VTAIYVpkdPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPR 430
|
250
....*....|....*
gi 658547412 460 NPNGKIDRKLLDAYA 474
Cdd:PRK07445 431 NPQGKINRQQLQQIA 445
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
324-470 |
5.28e-10 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 61.54 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 324 GELIIWGKNVMRGYLGLPQENAAKLlrrEDEAFrgYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMS 401
Cdd:PRK10946 381 GRLMTRGPYTFRGYYKSPQHNASAF---DANGF--YCSGDLVSidPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHP 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658547412 402 GINEA--VVLP--LM--KSCgsvlriaAFCVT--DMAPDTIKTSL-SKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK10946 456 AVIHAalVSMEdeLMgeKSC-------AFLVVkePLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
133-475 |
7.00e-10 |
|
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: 60.57 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGVQiGRESVWHFMKWVSQDFSL--PEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNA----- 205
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQ-HTHSNEVYNAWMLALNSLfdPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 206 KEDIQKENW--LERLKSNAVSAwVSTpsfAYQQLLSPQFNSEyLPALNvFIFIGevlNKALVKQLRRRFPQA---KIINS 280
Cdd:cd05944 82 NPGLFDNFWklVERYRITSLST-VPT---VYAALLQVPVNAD-ISSLR-FAMSG---AAPLPVELRARFEDAtglPVVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 281 YGPTEATIATTVveitdAILNSDSAVLPVGVMMPESKMEI---------------STDGELIIWGKNVMRGYLGlpQENA 345
Cdd:cd05944 153 YGLTEATCLVAV-----NPPDGPKRPGSVGLRLPYARVRIkvldgvgrllrdcapDEVGEICVAGPGVFGGYLY--TEGN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 346 akllRREDEAFRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMsgineavvlPLMKSCGSVLRIAA 423
Cdd:cd05944 226 ----KNAFVADGWLNTGDLGRldADGYLFITGRAKDLIIRGGHNIDPALIEEALLRH---------PAVAFAGAVGQPDA 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658547412 424 FC------VTDMAPDTIKTS------LSKVVPHY-MVPSQIIVKDALPLNPNGKIDRKLL--DAYAR 475
Cdd:cd05944 293 HAgelpvaYVQLKPGAVVEEeellawARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALraDAIHR 359
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
126-470 |
9.95e-10 |
|
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: 60.57 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 126 GKVLEEQDLAYIMFTSGSTGKPKG-VQIGRESVWHFMKWVSQDFSLPEKPVLMNHA--VFSFDLSLIpLLANLAMGGHIV 202
Cdd:cd05958 91 HALTASDDICILAFTSGTTGAPKAtMHFHRDPLASADRYAVNVLRLREDDRFVGSPplAFTFGLGGV-LLFPFGVGASGV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 203 LnaKEDIQKENWLERLKSNAVSAWVSTPSfAYQQLL-SPQFNSEYLPALNVFIFIGEVLNKAlvkqLRRRFPQA---KII 278
Cdd:cd05958 170 L--LEEATPDLLLSAIARYKPTVLFTAPT-AYRAMLaHPDAAGPDLSSLRKCVSAGEALPAA----LHRAWKEAtgiPII 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 279 NSYGPTEA---------------TIATTVVEITDAILNSDSAVLPVGVMmpeskmeistdGELIIWGKNvmrGYLGLPQE 343
Cdd:cd05958 243 DGIGSTEMfhifisarpgdarpgATGKPVPGYEAKVVDDEGNPVPDGTI-----------GRLAVRGPT---GCRYLADK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 344 NAAKLLRREDEAfrgyrTGDLGYEA--GLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINE-AVVLPLMKSCGSVLR 420
Cdd:cd05958 309 RQRTYVQGGWNI-----TGDTYSRDpdGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAEcAVVGHPDESRGVVVK 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 658547412 421 iaAFCVT--DMAPD-----TIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05958 384 --AFVVLrpGVIPGpvlarELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
136-473 |
1.09e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 60.53 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 136 YIMFTSGSTGKPKGVQigRESVWHFMKWVSQDFSLPEKP----VLMNHAV--FSFDLSLIPLLAN---LAMG-GHIVLNA 205
Cdd:PTZ00237 258 YILYTSGTTGNSKAVV--RSNGPHLVGLKYYWRSIIEKDiptvVFSHSSIgwVSFHGFLYGSLSLgntFVMFeGGIIKNK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 206 KEDIQKENWLERLKSNAVSAWVSTpsFAYQQLLSP---QFNSEY-LPALNVFIFIGEVLNKALVKQLRRRFpQAKIINSY 281
Cdd:PTZ00237 336 HIEDDLWNTIEKHKVTHTLTLPKT--IRYLIKTDPeatIIRSKYdLSNLKEIWCGGEVIEESIPEYIENKL-KIKSSRGY 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 282 GPTEATIA-------------TTVVE---ITDAILNSDSAVLPVGvmmpeskmEIstdGELIIwgknvmrgYLGLPQENA 345
Cdd:PTZ00237 413 GQTEIGITylycyghinipynATGVPsifIKPSILSEDGKELNVN--------EI---GEVAF--------KLPMPPSFA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 346 AKLLRREDE------AFRG-YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMK-SC 415
Cdd:PTZ00237 474 TTFYKNDEKfkqlfsKFPGyYNSGDLGFkdENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDpDC 553
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658547412 416 GSVLriAAFCVTDMAPDTIKTSLSKV-----------VPHYMVPSQIIVKDALPLNPNGKIDRKLLDAY 473
Cdd:PTZ00237 554 YNVP--IGLLVLKQDQSNQSIDLNKLkneinniitqdIESLAVLRKIIIVNQLPKTKTGKIPRQIISKF 620
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
24-470 |
1.36e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 60.26 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 24 PQQLAISGSDEALSWLQLSAAVTDWAQRYQ-RCQPVAGTPVVLYGHQQAE-----FAVAIYSCLL--HNIPYIPVDCIYP 95
Cdd:PRK06839 16 PDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEyivllFAIAKVECIAvpLNIRLTENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 96 QER--LREIChlASAPYYYDVATRQFIATGEPGKVLE-----------------EQDLAYIMFTSGSTGKPKGVQIGRES 156
Cdd:PRK06839 96 LKDsgTTVLF--VEKTFQNMALSMQKVSYVQRVISITslkeiedrkidnfveknESASFIICYTSGTTGKPKGAVLTQEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 157 vwhfMKWVSQdfslpekpvlmnHAVFSFDLS-------LIPL----------LANLAMGGHIVLNAKEDIQKEnwLERLK 219
Cdd:PRK06839 174 ----MFWNAL------------NNTFAIDLTmhdrsivLLPLfhiggiglfaFPTLFAGGVIIVPRKFEPTKA--LSMIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 220 SNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRR---FPQAkiinsYGPTEATIATTVVEIT 296
Cdd:PRK06839 236 KHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRgflFGQG-----FGMTETSPTVFMLSEE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 297 DAILNSDSAVLP-----VGVMMPES-KMEISTDGELIIWGKNVMRGYLGLPQENAakllrredEAFRG--YRTGDLGY-- 366
Cdd:PRK06839 311 DARRKVGSIGKPvlfcdYELIDENKnKVEVGEVGELLIRGPNVMKEYWNRPDATE--------ETIQDgwLCTGDLARvd 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 367 EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVLRIAAFCVTDMAPDT---IKTSLSKVVP 443
Cdd:PRK06839 383 EDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIekdVIEHCRLFLA 462
|
490 500
....*....|....*....|....*..
gi 658547412 444 HYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK06839 463 KYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
130-474 |
1.48e-09 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 59.89 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 130 EEQDLAYIMFTSGSTGKPKGVQIGRE----------SVWHfmkWVSQDFSLPEKPVLMNHAVFsfdlslipllanlaMGG 199
Cdd:PRK07514 154 GADDLAAILYTSGTTGRSKGAMLSHGnllsnaltlvDYWR---FTPDDVLIHALPIFHTHGLF--------------VAT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 200 HIVLNAKediQKENWLERLKSNAVSAWV--ST-----PSFaYQQLL-SPQFNSEylPALNVFIFI-GevlNKALVKQLRR 270
Cdd:PRK07514 217 NVALLAG---ASMIFLPKFDPDAVLALMprATvmmgvPTF-YTRLLqEPRLTRE--AAAHMRLFIsG---SAPLLAETHR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 271 RFpQAK----IINSYGPTEAT-----------IATTV--------VEITDAilnSDSAVLPVGvmmpeskmEIstdGELI 327
Cdd:PRK07514 288 EF-QERtghaILERYGMTETNmntsnpydgerRAGTVgfplpgvsLRVTDP---ETGAELPPG--------EI---GMIE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 328 IWGKNVMRGYLGLPQENAAKLlrREDEAFRgyrTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINE 405
Cdd:PRK07514 353 VKGPNVFKGYWRMPEKTAEEF--RADGFFI---TGDLGKidERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVE 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 406 ----------------AVVlplmkscgsVLRIAAfcvtDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKL 469
Cdd:PRK07514 428 savigvphpdfgegvtAVV---------VPKPGA----ALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNL 494
|
....*.
gi 658547412 470 L-DAYA 474
Cdd:PRK07514 495 LrEQYA 500
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
140-467 |
1.86e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.78 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 140 TSGSTGKPKGVQIGRESVWHFMKWVSQDFSL-PEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDIQKE--NWLE 216
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLdAATDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTAFSASpfRWLS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 217 RLkSNAVSAWVSTPSFAYQQL--LSPQFNSEYLPALNVFIFIGEVLN-----KALVKQLRRRFPQAKIINSYGPTEATIA 289
Cdd:PRK05851 240 WL-SDSRATLTAAPNFAYNLIgkYARRVSDVDLGALRVALNGGEPVDcdgfeRFATAMAPFGFDAGAAAPSYGLAESTCA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 290 TTVVE-----ITDAILNSDS------AVLpvGVMMPESKMEIS-TD----------GELIIWGKNVMRGYLGlpqenAAK 347
Cdd:PRK05851 319 VTVPVpgiglRVDEVTTDDGsgarrhAVL--GNPIPGMEVRISpGDgaagvagreiGEIEIRGASMMSGYLG-----QAP 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 348 LlrREDEAFrgyRTGDLGY--EAGLIYCqGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSV---LRIA 422
Cdd:PRK05851 392 I--DPDDWF---PTGDLGYlvDGGLVVC-GRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSArpgLVIA 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 658547412 423 A-FCVTDMApdtikTSLSKVVPHY-----MVPSQIIV--KDALPLNPNGKIDR 467
Cdd:PRK05851 466 AeFRGPDEA-----GARSEVVQRVasecgVVPSDVVFvaPGSLPRTSSGKLRR 513
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
124-475 |
1.86e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 59.97 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 124 EPGKVLEEQDLAYIMFTSGSTGKPKgvqIGRESVWH--FMKWVSQDFSL--PEKPVLMNHAVFSFDLSLIPLLANLAMGG 199
Cdd:PRK07529 205 FSGRPIGPDDVAAYFHTGGTTGMPK---LAQHTHGNevANAWLGALLLGlgPGDTVFCGLPLFHVNALLVTGLAPLARGA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 200 HIVLNA-----KEDIQKENW--LERLKSNAVSAwVSTpsfAYQQLLSPQFNSEYLPALNVFIfigeVLNKALVKQLRRRF 272
Cdd:PRK07529 282 HVVLATpqgyrGPGVIANFWkiVERYRINFLSG-VPT---VYAALLQVPVDGHDISSLRYAL----CGAAPLPVEVFRRF 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 273 PQA---KIINSYGPTEATIATTVveitdAILNSDSAVLPVGVMMPESKMEI-------------STD--GELIIWGKNVM 334
Cdd:PRK07529 354 EAAtgvRIVEGYGLTEATCVSSV-----NPPDGERRIGSVGLRLPYQRVRVvilddagrylrdcAVDevGVLCIAGPNVF 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 335 RGYLGLPQENAaklLRREDeafRGYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVV---- 408
Cdd:PRK07529 429 SGYLEAAHNKG---LWLED---GWLNTGDLGRidADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAvgrp 502
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658547412 409 ------LPlmksCGSVLRIAAFCVTdmaPDTIKTSLSKVVPH-YMVPSQIIVKDALPLNPNGKIDRKLL--DAYAR 475
Cdd:PRK07529 503 dahageLP----VAYVQLKPGASAT---EAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPALrrDAIRR 571
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
129-385 |
3.29e-09 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 58.98 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 129 LEEQDLAYIMFTSGSTGKPKGVQIGRESVwhfMKWVSQdfslpekpvlmnhAVFSFDL--------SLIPLLAN--LAM- 197
Cdd:PRK12476 190 LDTDDVSHLQYTSGSTRPPVGVEITHRAV---GTNLVQ-------------MILSIDLldrnthgvSWLPLYHDmgLSMi 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 198 ------GGHIVLNAKEDI--QKENWLERLKSNAVSAWVST--PSFAY----QQLLSPQfnSEYLPALNVFIFIG-EVLNK 262
Cdd:PRK12476 254 gfpavyGGHSTLMSPTAFvrRPQRWIKALSEGSRTGRVVTaaPNFAYewaaQRGLPAE--GDDIDLSNVVLIIGsEPVSI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 263 ALVKQLRRRF-----PQAKIINSYGPTEAT--IAT-------TVVEITDAILNSDSAVlPVGVMMPESKMEIS------- 321
Cdd:PRK12476 332 DAVTTFNKAFapyglPRTAFKPSYGIAEATlfVATiapdaepSVVYLDREQLGAGRAV-RVAADAPNAVAHVScgqvars 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 322 ---------TDGELI------IW--GKNVMRGYLGLPQEN----AAKLLRREDEAF---------RGYRTGDLG-YEAGL 370
Cdd:PRK12476 411 qwavivdpdTGAELPdgevgeIWlhGDNIGRGYWGRPEETertfGAKLQSRLAEGShadgaaddgTWLRTGDLGvYLDGE 490
|
330
....*....|....*
gi 658547412 371 IYCQGRNDSQVKLNG 385
Cdd:PRK12476 491 LYITGRIADLIVIDG 505
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
308-470 |
4.41e-09 |
|
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: 58.46 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 308 PVGVMMPESKMEISTD----GELIIWGKNVMRGYLGLPQENAakllrredEAFRG--YRTGDLG--YEAG---------- 369
Cdd:cd12118 320 EVDVLDPETMKPVPRDgktiGEIVFRGNIVMKGYLKNPEATA--------EAFRGgwFHSGDLAviHPDGyieikdrskd 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 370 LIYCQGRNDSQVklngyrieinEIENRLLAMSGINEAVVLPLMKSC-GSVLriAAFcVT-----DMAPDTIKTSLSKVVP 443
Cdd:cd12118 392 IIISGGENISSV----------EVEGVLYKHPAVLEAAVVARPDEKwGEVP--CAF-VElkegaKVTEEEIIAFCREHLA 458
|
170 180
....*....|....*....|....*..
gi 658547412 444 HYMVPSQIIVKDaLPLNPNGKIDRKLL 470
Cdd:cd12118 459 GFMVPKTVVFGE-LPKTSTGKIQKFVL 484
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
132-470 |
5.09e-09 |
|
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: 58.25 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 132 QDLAYIMFTSGSTGKPKGVQIGRESVWHFMK-----WVSqdfsLPEKPVLMNHAVFSFDLSLI-PLLANLAMGGHIVLNA 205
Cdd:cd05928 174 QEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKvngryWLD----LTASDIMWNTSDTGWIKSAWsSLFEPWIQGACVFVHH 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 206 KEDIQKENWLERLKSNAVSAWVSTPSfAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRfPQAKIINSYGPTE 285
Cdd:cd05928 250 LPRFDPLVILKTLSSYPITTFCGAPT-VYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQ-TGLDIYEGYGQTE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 286 ATIATTV---VEITDA------------ILNSDSAVLPVGvmmpeskmeisTDGELIIWGKNV-----MRGYLGLPQENA 345
Cdd:cd05928 328 TGLICANfkgMKIKPGsmgkasppydvqIIDDNGNVLPPG-----------TEGDIGIRVKPIrpfglFSGYVDNPEKTA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 346 AkllrredeAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVL----PLMkscGS 417
Cdd:cd05928 397 A--------TIRGdfYLTGDRGImdEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVsspdPIR---GE 465
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658547412 418 VLRiaAFCVtdMAPD-----------TIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05928 466 VVK--AFVV--LAPQflshdpeqltkELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
129-467 |
8.83e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 57.86 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 129 LEEQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEK-----PVLMNHAvFSFDLSlipLLANLAMGGHIVL 203
Cdd:PRK12583 198 LDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHdrlcvPVPLYHC-FGMVLA---NLGCMTVGACLVY 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 204 NAkEDIQKENWLERLKSNAVSAWVSTPSFAYQQLLSPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRFPQAKIINSYGP 283
Cdd:PRK12583 274 PN-EAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGM 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 284 TEATIATTVVEITDAIlnsDSAVLPVGVMMPESKMEI----------STDGELIIWGKNVMRGYLGLPqENAAKLLRREd 353
Cdd:PRK12583 353 TETSPVSLQTTAADDL---ERRVETVGRTQPHLEVKVvdpdgatvprGEIGELCTRGYSVMKGYWNNP-EATAESIDED- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 354 eafrGY-RTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVV--LPLMKScGSvlRIAAFCVTD 428
Cdd:PRK12583 428 ----GWmHTGDLATmdEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVfgVPDEKY-GE--EIVAWVRLH 500
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 658547412 429 ----MAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDR 467
Cdd:PRK12583 501 pghaASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
276-475 |
1.66e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 56.78 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 276 KIINSYGPTEATIATTVVE----------ITDAILNSDSAVLPVG-----VMMPESKMEISTDG----ELIIWGKNVMRG 336
Cdd:PLN02479 336 RVTHTYGLSETYGPSTVCAwkpewdslppEEQARLNARQGVRYIGlegldVVDTKTMKPVPADGktmgEIVMRGNMVMKG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 337 YLGLPQENAakllrredEAFRG--YRTGDLG--YEAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLM 412
Cdd:PLN02479 416 YLKNPKANE--------EAFANgwFHSGDLGvkHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARP 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658547412 413 KS------CGSVLRIAAFCVTD---MAPDTIKTSLSKvVPHYMVPSQIIVkDALPLNPNGKIDRKLLDAYAR 475
Cdd:PLN02479 488 DErwgespCAFVTLKPGVDKSDeaaLAEDIMKFCRER-LPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKAK 557
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
139-410 |
3.02e-08 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 55.65 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 139 FTSGSTGKPKGVQIGRES--VWHF--MKWVS---QDFSLP-EKPVLMNHAVFSFdlsliplLANLAMGGHIVLNAKEDIQ 210
Cdd:cd05974 92 FTSGTTSKPKLVEHTHRSypVGHLstMYWIGlkpGDVHWNiSSPGWAKHAWSCF-------FAPWNAGATVFLFNYARFD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 211 KENWLERLKSNAVSAWVSTPSfAYQQLLSPQFNSEYLPALNVfIFIGEVLNKALVKQLRRRFPQAkIINSYGPTEATIAt 290
Cdd:cd05974 165 AKRVLAALVRYGVTTLCAPPT-VWRMLIQQDLASFDVKLREV-VGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETTAL- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 291 tvveitdaILNSDSAVLPVGVM---MPESKMEIS-------TDGEL-IIWGKN----VMRGYLGLPQENAakllrredEA 355
Cdd:cd05974 241 --------VGNSPGQPVKAGSMgrpLPGYRVALLdpdgapaTEGEVaLDLGDTrpvgLMKGYAGDPDKTA--------HA 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 658547412 356 FRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLP 410
Cdd:cd05974 305 MRGgyYRTGDIAMrdEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVP 363
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
133-365 |
6.86e-08 |
|
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: 54.91 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGVQIGRES----VWHFMKWVSqDFSLPEKPVL----MNHaVFSFDLSLIPLLANLAMG-GH--- 200
Cdd:cd17639 89 DLACIMYTSGSTGNPKGVMLTHGNlvagIAGLGDRVP-ELLGPDDRYLaylpLAH-IFELAAENVCLYRGGTIGyGSprt 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 201 ----IVLNAKEDIQKEN----------WlERLKsNAVSAWVSTPSFAYQQL--LSPQFNSEYL------PALNVFIFige 258
Cdd:cd17639 167 ltdkSKRGCKGDLTEFKptlmvgvpaiW-DTIR-KGVLAKLNPMGGLKRTLfwTAYQSKLKALkegpgtPLLDELVF--- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 259 vlnkALVKQL---RRRF---------PQAK---------IINSYGPTEATIATTVVEITDAILNSDSAVLPVG----VMM 313
Cdd:cd17639 242 ----KKVRAAlggRLRYmlsggaplsADTQeflnivlcpVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCeiklVDW 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 314 PESKMeiSTD-----GELIIWGKNVMRGYLGLPQENAakllrredEAFRG---YRTGDLG 365
Cdd:cd17639 318 EEGGY--STDkppprGEILIRGPNVFKGYYKNPEKTK--------EAFDGdgwFHTGDIG 367
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
322-471 |
8.44e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 54.64 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 322 TDGELIIWGKNVMRGYLGLPQENAakllrredEAFR-GY-RTGDLG--YEAGLIYCQGRNDSQVKLNGYRIEINEIENRL 397
Cdd:PLN03102 391 TMGEIVIKGSSIMKGYLKNPKATS--------EAFKhGWlNTGDVGviHPDGHVEIKDRSKDIIISGGENISSVEVENVL 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 398 LAMSGINEAVVL----PLMKSCGsvlriAAFCVTDMAPDTIKTSLSKVV--------------PHYMVPSQIIVKDALPL 459
Cdd:PLN03102 463 YKYPKVLETAVVamphPTWGETP-----CAFVVLEKGETTKEDRVDKLVtrerdlieycrenlPHFMCPRKVVFLQELPK 537
|
170
....*....|...
gi 658547412 460 NPNGKIDR-KLLD 471
Cdd:PLN03102 538 NGNGKILKpKLRD 550
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
392-464 |
1.02e-07 |
|
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: 49.08 E-value: 1.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658547412 392 EIENRLLAMSGINEAVVLPLM-KSCGSVlrIAAFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGK 464
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPdELKGEA--PVAFVVlkpgVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
132-465 |
1.38e-07 |
|
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: 54.12 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 132 QDLAYIMFTSGSTGKPKGV-------------------QIGRESVWhfmkWVSQDFSLpekpvLMNHAVFsfdlslipLL 192
Cdd:cd17634 232 EDPLFILYTSGTTGKPKGVlhttggylvyaattmkyvfDYGPGDIY----WCTADVGW-----VTGHSYL--------LY 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 193 ANLAMGGHIVL-NAKEDIQKENWLERLKS-NAVSAWVSTPSfAYQQLLS--PQFNSEY-LPALNVFIFIGEVLNKALVKQ 267
Cdd:cd17634 295 GPLACGATTLLyEGVPNWPTPARMWQVVDkHGVNILYTAPT-AIRALMAagDDAIEGTdRSSLRILGSVGEPINPEAYEW 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 268 LRRRFPQAK--IINSYGPTEATIATTVVEITDAILNSDSAVLPVGVMMPE------SKMEISTDGELII---WgKNVMRG 336
Cdd:cd17634 374 YWKKIGKEKcpVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAvvdnegHPQPGGTEGNLVItdpW-PGQTRT 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 337 YLGLPQENAAKLLRRedeaFRG-YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPL-- 411
Cdd:cd17634 453 LFGDHERFEQTYFST----FKGmYFSGDGARrdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIph 528
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658547412 412 -----MKSCGSVLRIAafcVTDmaPDTIKTSLSKVVPHYM----VPSQIIVKDALPLNPNGKI 465
Cdd:cd17634 529 aikgqAPYAYVVLNHG---VEP--SPELYAELRNWVRKEIgplaTPDVVHWVDSLPKTRSGKI 586
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
281-467 |
3.74e-07 |
|
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: 51.89 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 281 YGPTEATIATTVVEITD--------------AILNSDSAVLPVGvmmpeskmeisTDGELIIWGKNVMRGYLGLPQENAA 346
Cdd:cd17637 143 YGQTETSGLVTLSPYRErpgsagrpgplvrvRIVDDNDRPVPAG-----------ETGEIVVRGPLVFQGYWNLPELTAY 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 347 kllrredeAFRG--YRTGDLGY--EAGLIYCQGRNDSQ--VKLNGYRIEINEIENRLLAMSGINEAVVL----PLMKSCg 416
Cdd:cd17637 212 --------TFRNgwHHTGDLGRfdEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIgvpdPKWGEG- 282
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 658547412 417 svlrIAAFCVtdMAPDTIKTS--LSKVV----PHYMVPSQIIVKDALPLNPNGKIDR 467
Cdd:cd17637 283 ----IKAVCV--LKPGATLTAdeLIEFVgsriARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
137-385 |
3.87e-07 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 52.36 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 137 IMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHAVFSFDLS-----LIPLLANLAMGGHIVLnAKEDIQK 211
Cdd:cd05933 155 LIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLShiaaqILDIWLPIKVGGQVYF-AQPDALK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 212 ----------------------ENWLERLKSNA---------VSAWVSTPSFAYQQLL----SPQFNSEYLPALNVFifi 256
Cdd:cd05933 234 gtlvktlrevrptafmgvprvwEKIQEKMKAVGaksgtlkrkIASWAKGVGLETNLKLmggeSPSPLFYRLAKKLVF--- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 257 gEVLNKAL-VKQLRRRFPQA----------------KIINSYGPTEATIATTVveitdailNSDSAV--LPVGVMMPESK 317
Cdd:cd05933 311 -KKVRKALgLDRCQKFFTGAapisretlefflslniPIMELYGMSETSGPHTI--------SNPQAYrlLSCGKALPGCK 381
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658547412 318 MEIST-----DGELIIWGKNVMRGYLGLPQENAAKLlrreDEafRGY-RTGDLGY--EAGLIYCQGRNDSQVKLNG 385
Cdd:cd05933 382 TKIHNpdadgIGEICFWGRHVFMGYLNMEDKTEEAI----DE--DGWlHSGDLGKldEDGFLYITGRIKELIITAG 451
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
122-376 |
6.03e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 51.92 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 122 TGEPGKVLE--EQDLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSL-PEKPVLMNHAVFSFDLSLIPLLA-NLAM 197
Cdd:PRK07768 140 AADPIDPVEtgEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFdVETDVMVSWLPLFHDMGMVGFLTvPMYF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 198 GGHIVLNAKEDIQKEN--WLE---RLKSNAVSAwvstPSFAY----QQLLSPQFNSEY-LPALNVFIFIGEVLNKALVKQ 267
Cdd:PRK07768 220 GAELVKVTPMDFLRDPllWAElisKYRGTMTAA----PNFAYallaRRLRRQAKPGAFdLSSLRFALNGAEPIDPADVED 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 268 L-----RRRFPQAKIINSYGPTEATIATT--------VVEITDA-ILNSDSAVLPV-----------GVMMPESKMEIST 322
Cdd:PRK07768 296 LldagaRFGLRPEAILPAYGMAEATLAVSfspcgaglVVDEVDAdLLAALRRAVPAtkgntrrlatlGPPLPGLEVRVVD 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658547412 323 D----------GELIIWGKNVMRGYLGLPQENAAkllrREDEAFrgYRTGDLGY--EAGLIYCQGR 376
Cdd:PRK07768 376 EdgqvlpprgvGVIELRGESVTPGYLTMDGFIPA----QDADGW--LDTGDLGYltEEGEVVVCGR 435
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
276-470 |
7.06e-07 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 51.59 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 276 KIINSYGPTEAT--IATTVVEITDailNSDSAVLPVgvmmPESKMEISTD----------GELIIWGKNVMRGYLGLPQE 343
Cdd:PRK08974 352 YLLEGYGLTECSplVSVNPYDLDY---YSGSIGLPV----PSTEIKLVDDdgnevppgepGELWVKGPQVMLGYWQRPEA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 344 NAAKLlrrEDeafrGY-RTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINE--AVVLPlMKSCGSV 418
Cdd:PRK08974 425 TDEVI---KD----GWlATGDIAVmdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEvaAVGVP-SEVSGEA 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658547412 419 LRIaaFCV---TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK08974 497 VKI--FVVkkdPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
281-409 |
1.52e-06 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 50.50 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 281 YGPTEATIATTVVEITDAilNSDSavlpVGVMMPESKMEISTDGELIIWGKNVMRGYLGLPQENAAKLLrrEDEAFrgyR 360
Cdd:cd17641 355 YGQTELAGAYTVHRDGDV--DPDT----VGVPFPGTEVRIDEVGEILVRSPGVFVGYYKNPEATAEDFD--EDGWL---H 423
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 658547412 361 TGDLGY--EAGLIYCQGR-NDSQVKLNGYRIEINEIENRLLAMSGINEAVVL 409
Cdd:cd17641 424 TGDAGYfkENGHLVVIDRaKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVL 475
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
277-470 |
2.66e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 49.76 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 277 IINSYGPTEATIATTVVEITDAILNSdsavlpVGVMMPESKMEISTD----------GELIIWGKNVMRGYLGLPQENAA 346
Cdd:PRK05677 354 ICEGYGMTETSPVVSVNPSQAIQVGT------IGIPVPSTLCKVIDDdgnelplgevGELCVKGPQVMKGYWQRPEATDE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 347 KLlrrEDEAFrgYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINE--AVVLPLMKScGSVLRIa 422
Cdd:PRK05677 428 IL---DSDGW--LKTGDIALiqEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQcaAIGVPDEKS-GEAIKV- 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 658547412 423 aFCVTDMAP----DTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK05677 501 -FVVVKPGEtltkEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
132-470 |
1.47e-05 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 47.32 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 132 QDLAYIMFTSGSTGKPKG-VQIGRESVWHFMK---WVSQDFSLPEKPVLMN--------HAvfsFDLSLIPLLAnLAMGG 199
Cdd:PRK07059 204 DDVAFLQYTGGTTGVSKGaTLLHRNIVANVLQmeaWLQPAFEKKPRPDQLNfvcalplyHI---FALTVCGLLG-MRTGG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 200 HIVLNAK-EDIQ---KEnwLERLKSNAVSAwVSTpsfAYQQLL-SPQFNSEYLPALNVFIFIGEVLNKALVKQLRRRfPQ 274
Cdd:PRK07059 280 RNILIPNpRDIPgfiKE--LKKYQVHIFPA-VNT---LYNALLnNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEM-TG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 275 AKIINSYGPTE-ATIAT----TVVEITDAIlnsdsavlpvGVMMPESKMEISTD----------GELIIWGKNVMRGYLG 339
Cdd:PRK07059 353 CPITEGYGLSEtSPVATcnpvDATEFSGTI----------GLPLPSTEVSIRDDdgndlplgepGEICIRGPQVMAGYWN 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 340 LPQENAAKLLrrEDEAFrgyRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINE--AVVLPLMKSc 415
Cdd:PRK07059 423 RPDETAKVMT--ADGFF---RTGDVGVmdERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEvaAVGVPDEHS- 496
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658547412 416 GSVLR--------------IAAFCvtdmapdtiKTSLSkvvpHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK07059 497 GEAVKlfvvkkdpalteedVKAFC---------KERLT----NYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
61-376 |
2.59e-05 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 46.80 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 61 TPVVLYGHQQAEFAVAIYSCLLhniPYIPVDCIYPQERLREICHLASapyyydvatrqFIATGEPGKVLE------EQDL 134
Cdd:PRK08180 146 TPGLVFADDGAAFARALAAVVP---ADVEVVAVRGAVPGRAATPFAA-----------LLATPPTAAVDAahaavgPDTI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 135 AYIMFTSGSTGKPKGV----------QIGRESVWHFMKwvsqdfslPEKPVLM-----NHaVF--SFDLSLIpllanLAM 197
Cdd:PRK08180 212 AKFLFTSGSTGLPKAVinthrmlcanQQMLAQTFPFLA--------EEPPVLVdwlpwNH-TFggNHNLGIV-----LYN 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 198 GG--HIvlnakeDIQK------ENWLERLKSNAVSAWVSTPSfAYQQLLS-----PQFNSEYLPALNVFIFIGEVLNKAL 264
Cdd:PRK08180 278 GGtlYI------DDGKptpggfDETLRNLREISPTVYFNVPK-GWEMLVPalerdAALRRRFFSRLKLLFYAGAALSQDV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 265 VKQLRR--------RFPqakIINSYGPTEATIATTVVeitdAILNSDSAVlpVGVMMP--ESKMeISTDG--ELIIWGKN 332
Cdd:PRK08180 351 WDRLDRvaeatcgeRIR---MMTGLGMTETAPSATFT----TGPLSRAGN--IGLPAPgcEVKL-VPVGGklEVRVKGPN 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 658547412 333 VMRGYLGLPQENAAKLlrrEDEAFrgYRTGDLGY-------EAGLIYcQGR 376
Cdd:PRK08180 421 VTPGYWRAPELTAEAF---DEEGY--YRSGDAVRfvdpadpERGLMF-DGR 465
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
129-475 |
2.65e-05 |
|
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: 46.54 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 129 LEEQDLAYIMFTSGSTGKPKGVQ-------------------IGRESVWhfmkWVSQDFSLpekpvLMNHavfsfdlSLI 189
Cdd:cd05967 227 VAATDPLYILYTSGTTGKPKGVVrdngghavalnwsmrniygIKPGDVW----WAASDVGW-----VVGH-------SYI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 190 ---PLLANLAMgghIVLNAKEDIQKE--NWLERLKSNAVSAWVSTPSfAYQQLLSPQFNSEY-----LPALNVFIFIGEV 259
Cdd:cd05967 291 vygPLLHGATT---VLYEGKPVGTPDpgAFWRVIEKYQVNALFTAPT-AIRAIRKEDPDGKYikkydLSSLRTLFLAGER 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 260 LNKALVKQLRRRFPQAkIINSYGPTEA--TIATTVVEITDAILNSDSAVLP-----VGVMMPE-SKMEISTDGELIIwgk 331
Cdd:cd05967 367 LDPPTLEWAENTLGVP-VIDHWWQTETgwPITANPVGLEPLPIKAGSPGKPvpgyqVQVLDEDgEPVGPNELGNIVI--- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 332 nvmrgYLGLPQENAAKLLRrEDEAFRG---------YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAM 400
Cdd:cd05967 443 -----KLPLPPGCLLTLWK-NDERFKKlylskfpgyYDTGDAGYkdEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSH 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 401 SGINEAVVLPLMKSC-GSVlrIAAFCV----TDMAPDTIKTSLSKVVPHYMVP----SQIIVKDALPLNPNGKIDRKLLD 471
Cdd:cd05967 517 PAVAECAVVGVRDELkGQV--PLGLVVlkegVKITAEELEKELVALVREQIGPvaafRLVIFVKRLPKTRSGKILRRTLR 594
|
....
gi 658547412 472 AYAR 475
Cdd:cd05967 595 KIAD 598
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
132-365 |
3.79e-05 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 46.05 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 132 QDLAYIMFTSGSTGKPKGVQIGRESVwhfMKWVSQDFSLPEKPVLMNHavFSFDLSLIPL---------LANLAMGGHI- 201
Cdd:cd05927 114 EDLATICYTSGTTGNPKGVMLTHGNI---VSNVAGVFKILEILNKINP--TDVYISYLPLahifervveALFLYHGAKIg 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 202 --------------------------VLNAKED-----IQKENWLERL--------KSNAVSAWVSTPSFAYQQLLspqF 242
Cdd:cd05927 189 fysgdirlllddikalkptvfpgvprVLNRIYDkifnkVQAKGPLKRKlfnfalnyKLAELRSGVVRASPFWDKLV---F 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 243 N--SEYLPALNVFIFIGEV-LNKALVKQLRRRFpQAKIINSYGPTEATIATTVVEITDAILNSDSAVLP------VGVmm 313
Cdd:cd05927 266 NkiKQALGGNVRLMLTGSApLSPEVLEFLRVAL-GCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPcaevklVDV-- 342
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 314 PEskMEISTD-----GELIIWGKNVMRGYLGLPQENAakllrredEAFR--GY-RTGDLG 365
Cdd:cd05927 343 PE--MNYDAKdpnprGEVCIRGPNVFSGYYKDPEKTA--------EALDedGWlHTGDIG 392
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
23-150 |
5.08e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 45.63 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 23 SPQQLAISGSDEALSWLQLSAAVTDWAQRYQRcQPV-AGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLRE 101
Cdd:PRK09029 16 RPQAIALRLNDEVLTWQQLCARIDQLAAGFAQ-QGVvEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 658547412 102 IC-HLASAPYYYDVATRQFIAT---------GEPGKVLEEQDLAYIMFTSGSTGKPKGV 150
Cdd:PRK09029 95 LLpSLTLDFALVLEGENTFSALtslhlqlveGAHAVAWQPQRLATMTLTSGSTGLPKAA 153
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
281-465 |
8.41e-05 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 45.19 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 281 YGPTEATIATTVVEITDAIlnsDSAVLPVGVMMP--ESK---------MEISTDGELIIWGKNVMRGYLGLPQENAAKLl 349
Cdd:PRK08315 348 YGMTETSPVSTQTRTDDPL---EKRVTTVGRALPhlEVKivdpetgetVPRGEQGELCTRGYSVMKGYWNDPEKTAEAI- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 350 rreDEAfrGY-RTGDLGY--EAGliYCQ--GRNDSQVKLNGYRIEINEIENRLLAMSGINEAVV--LPLMKScGSVLriA 422
Cdd:PRK08315 424 ---DAD--GWmHTGDLAVmdEEG--YVNivGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVvgVPDEKY-GEEV--C 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 658547412 423 AFCV----TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKI 465
Cdd:PRK08315 494 AWIIlrpgATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
133-470 |
1.54e-04 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 43.98 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 133 DLAYIMFTSGSTGKPKGVQIGRESVWHFMKWVSQDFSLPEKPVLMNHavfsfdlslIPLLanlamggHIvlnakediqke 212
Cdd:PRK06155 181 DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTT---------LPLF-------HT----------- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 213 nwlerlksNAVSAWVSTPSFAYQQLLSPQFN-SEYLPAL-----NVFIFIGEVLN------------------------- 261
Cdd:PRK06155 234 --------NALNAFFQALLAGATYVLEPRFSaSGFWPAVrrhgaTVTYLLGAMVSillsqparesdrahrvrvalgpgvp 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 262 KALVKQLRRRFPQAkIINSYGPTEAT--IATTVVE------------ITDAILNSDSAVLPVGVMmpeskmeistdGELI 327
Cdd:PRK06155 306 AALHAAFRERFGVD-LLDGYGSTETNfvIAVTHGSqrpgsmgrlapgFEARVVDEHDQELPDGEP-----------GELL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 328 IWGKN---VMRGYLGLPQENAakllrredEAFRG--YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAM 400
Cdd:PRK06155 374 LRADEpfaFATGYFGMPEKTV--------EAWRNlwFHTGDRVVrdADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSH 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658547412 401 SGINEAVVLPLMKSCGSVLRIAAFCVTD---MAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK06155 446 PAVAAAAVFPVPSELGEDEVMAAVVLRDgtaLEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
310-472 |
1.89e-04 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 43.50 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 310 GVMMPESKMEIStDGELIIWGKNVMRGYLGLPqenaakllrrEDEAFRG---YRTGDLG-YEAGLIYCQGRNDSQVKLNG 385
Cdd:PRK07824 195 GVPLDGVRVRVE-DGRIALGGPTLAKGYRNPV----------DPDPFAEpgwFRTDDLGaLDDGVLTVLGRADDAISTGG 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 386 YRIEINEIENRLLAMSGINEAVVLPLM-KSCGSvlRIAAFCVTDMAPDTIKTSLSKVV----PHYMVPSQIIVKDALPLN 460
Cdd:PRK07824 264 LTVLPQVVEAALATHPAVADCAVFGLPdDRLGQ--RVVAAVVGDGGPAPTLEALRAHVartlDRTAAPRELHVVDELPRR 341
|
170
....*....|..
gi 658547412 461 PNGKIDRKLLDA 472
Cdd:PRK07824 342 GIGKVDRRALVR 353
|
|
| HicDH_like |
cd05291 |
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; ... |
276-341 |
2.07e-04 |
|
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; L-2-hydroxyisocapronate dehydrogenase (HicDH) catalyzes the conversion of a variety of 2-oxo carboxylic acids with medium-sized aliphatic or aromatic side chains. This subfamily is composed of HicDHs and some bacterial L-lactate dehydrogenases (LDH). LDHs catalyze the last step of glycolysis in which pyruvate is converted to L-lactate. Bacterial LDHs can be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. Members of this subfamily with known structures such as the HicDH of Lactobacillus confusus, the non-allosteric LDH of Lactobacillus pentosus, and the allosteric LDH of Bacillus stearothermophilus, show that they exist as homotetramers. The HicDH-like subfamily is part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.
Pssm-ID: 133427 [Multi-domain] Cd Length: 306 Bit Score: 43.22 E-value: 2.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658547412 276 KIINSYGPTEATIATTVVEITDAILNSDSAVLPVGVMMpeskmeistDGELIIwgKNVmrgYLGLP 341
Cdd:cd05291 218 EIINGKGATYYGIATALARIVKAILNDENAILPVSAYL---------DGEYGE--KDV---YIGVP 269
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
113-473 |
2.52e-04 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 43.53 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 113 DVATRQFIATGEPGKVLEEQDLAYIMFTSGSTGKPKGVQigR-----ESVWHFMKWVSQDFSLPEKPVL-----MNH-AV 181
Cdd:PRK12406 133 AIDWEGWLAQQEPYDGPPVPQPQSMIYTSGTTGHPKGVR--RaaptpEQAAAAEQMRALIYGLKPGIRAlltgpLYHsAP 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 182 FSFDLSLIPLlanlamGGHIVLNAKEDiqKENWLERLKSNAVSAWVSTPSFaYQQLLSpqfnseyLPAlnvfifigEVLN 261
Cdd:PRK12406 211 NAYGLRAGRL------GGVLVLQPRFD--PEELLQLIERHRITHMHMVPTM-FIRLLK-------LPE--------EVRA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 262 KALVKQLR----------RRFPQAKI------INS-YGPTEATIATTVveitdailNSDSAVL---PVGVMMPESKMEIS 321
Cdd:PRK12406 267 KYDVSSLRhvihaaapcpADVKRAMIewwgpvIYEyYGSTESGAVTFA--------TSEDALShpgTVGKAAPGAELRFV 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 322 TD-------GELiiwGKNVMR-------GYLGLPQENAAklLRREdeafrGYRT-GDLGY--EAGLIYCQGRNDSQVKLN 384
Cdd:PRK12406 339 DEdgrplpqGEI---GEIYSRiagnpdfTYHNKPEKRAE--IDRG-----GFITsGDVGYldADGYLFLCDRKRDMVISG 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 385 GYRIEINEIENRLLAMSGIN-------------EAVVLPLMKSCGSVLriaafcvtdmAPDTIKTSLSKVVPHYMVPSQI 451
Cdd:PRK12406 409 GVNIYPAEIEAVLHAVPGVHdcavfgipdaefgEALMAVVEPQPGATL----------DEADIRAQLKARLAGYKVPKHI 478
|
410 420
....*....|....*....|...
gi 658547412 452 IVKDALPLNPNGKI-DRKLLDAY 473
Cdd:PRK12406 479 EIMAELPREDSGKIfKRRLRDPY 501
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
118-179 |
3.38e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 43.09 E-value: 3.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658547412 118 QFIATGEpGK-----VLEEQDLAYIMFTSGSTGKPKGVQIGRES-------VWHFMKWVSQdfSLPEKPVLMNH 179
Cdd:PLN02614 205 EFLKLGE-GKqydlpIKKKSDICTIMYTSGTTGDPKGVMISNESivtliagVIRLLKSANA--ALTVKDVYLSY 275
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
324-365 |
4.89e-04 |
|
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: 42.29 E-value: 4.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 658547412 324 GELIIWGKNVMRGYLGLPQENAAKLlrredeAFRGYRTGDLG 365
Cdd:cd17636 190 GEIVARGPTVMAGYWNRPEVNARRT------RGGWHHTNDLG 225
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
129-151 |
5.56e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 42.63 E-value: 5.56e-04
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
125-151 |
7.34e-04 |
|
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: 42.16 E-value: 7.34e-04
10 20
....*....|....*....|....*..
gi 658547412 125 PGKVLEEQDLAYIMFTSGSTGKPKGVQ 151
Cdd:cd05966 224 EPEWMDSEDPLFILYTSGSTGKPKGVV 250
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
37-209 |
8.75e-04 |
|
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: 41.67 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 37 SWLQLSAAVTDWAQRYQRCQPvaGTPVVLYGHQQAEFAVAIYSCLLHNIPYIPVDCIYPQERLREICH------LASAPY 110
Cdd:cd17632 72 ELWERVGAVAAAHDPEQPVRP--GDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAeteprlLAVSAE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 111 YYDVATRQFIATGEPGKVL-------------------------------------------------EEQD---LAYIM 138
Cdd:cd17632 150 HLDLAVEAVLEGGTPPRLVvfdhrpevdahraalesarerlaavgipvttltliavrgrdlppaplfrPEPDddpLALLI 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658547412 139 FTSGSTGKPKGVQIGRESVWHFMKWVS--QDFSlPEKPVLMNHAVFSFDLSLIPLLANLAMGGHIVLNAKEDI 209
Cdd:cd17632 230 YTSGSTGTPKGAMYTERLVATFWLKVSsiQDIR-PPASITLNFMPMSHIAGRISLYGTLARGGTAYFAAASDM 301
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
359-470 |
1.04e-03 |
|
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: 41.39 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 359 YRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPL---MKscGSVlrIAAFCV------- 426
Cdd:cd05966 471 YFTGDGARrdEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRphdIK--GEA--IYAFVTlkdgeep 546
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 658547412 427 TDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:cd05966 547 SDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
133-152 |
1.10e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 41.64 E-value: 1.10e-03
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
127-470 |
1.10e-03 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 41.28 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 127 KVLEEQDLAYIMFTSGSTGKPKGVQIG-RESVWH--------FMKWVSQDFSLPEKPvlMNHA-VFSFDLSLIPLLANLA 196
Cdd:PRK06018 172 KTFDENTAAGMCYTSGTTGDPKGVLYShRSNVLHalmanngdALGTSAADTMLPVVP--LFHAnSWGIAFSAPSMGTKLV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 197 MGGhivlnAKEDIQkeNWLERLKSNAVSAWVSTPSfAYQQLLSP-QFNSEYLPALNVFIFIGEVLNKALVKQLRRRfpQA 275
Cdd:PRK06018 250 MPG-----AKLDGA--SVYELLDTEKVTFTAGVPT-VWLMLLQYmEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM--GV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 276 KIINSYGPTEATIATTVVEITDAILN-SDSAVL---------PVGVMM----PESKmEISTDGE----LIIWGKNVMRGY 337
Cdd:PRK06018 320 EVRHAWGMTEMSPLGTLAALKPPFSKlPGDARLdvlqkqgypPFGVEMkitdDAGK-ELPWDGKtfgrLKVRGPAVAAAY 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 338 LGLpqenAAKLLrrEDEAFrgYRTGDLGY--EAGLIYCQGRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVL------ 409
Cdd:PRK06018 399 YRV----DGEIL--DDDGF--FDTGDVATidAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIgvyhpk 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658547412 410 ----PLMkscgsVLRIAAfcVTDMAPDTIKTSLSKVVPHYMVPSQIIVKDALPLNPNGKIDRKLL 470
Cdd:PRK06018 471 wderPLL-----IVQLKP--GETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
136-151 |
1.28e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 41.28 E-value: 1.28e-03
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
133-150 |
4.46e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 39.57 E-value: 4.46e-03
|
| Mdh |
COG0039 |
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ... |
275-341 |
6.92e-03 |
|
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439809 [Multi-domain] Cd Length: 302 Bit Score: 38.46 E-value: 6.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658547412 275 AKIINSYGPTEATIATTVVEITDAILNSDSAVLPVGVMMpeskmeistDGELIIwgKNVmrgYLGLP 341
Cdd:COG0039 214 AEIIEGKGSTYYAIAAAAARIVEAILRDEKRVLPVSVYL---------DGEYGI--EDV---YLGVP 266
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
375-465 |
7.47e-03 |
|
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: 38.79 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658547412 375 GRNDSQVKLNGYRIEINEIENRLLAMSGINEAVVLPLMKSCGSVlRIAAFCVtdMAP-------------DTIKTSLSkv 441
Cdd:cd05943 504 GRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDE-RVILFVK--LREgvelddelrkrirSTIRSALS-- 578
|
90 100
....*....|....*....|....
gi 658547412 442 vPHYmVPSQIIVKDALPLNPNGKI 465
Cdd:cd05943 579 -PRH-VPAKIIAVPDIPRTLSGKK 600
|
|
| |
