|
Name |
Accession |
Description |
Interval |
E-value |
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
190-658 |
1.28e-130 |
|
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: 405.37 E-value: 1.28e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 190 AERPALNIAGTSLSHRQLHAHSRAIQQRLQplldqHQGPL---VVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQR 266
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLR-----ERGVGpgdLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 267 QQYILENAGAVLLLHDGEHPlsetmpgldisgidisdvnldqplmrqrpdldapCMALYTSGTTGHPKGVLLSQANLAHF 346
Cdd:cd05930 76 LAYILEDSGAKLVLTDPDDL----------------------------------AYVIYTSGSTGKPKGVMVEHRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 347 TAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPALLSIL--- 423
Cdd:cd05930 122 LLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLlqe 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 424 -PLDQLQILDHVMTGGDVCEPYVIEQLTRQGN---LYNLYGPTEATVLITARQLRTGD---NNRTLGAPIANSQVLILDE 496
Cdd:cd05930 202 lELAALPSLRLVLVGGEALPPDLVRRWRELLPgarLVNLYGPTEATVDATYYRVPPDDeedGRVPIGRPIPNTRVYVLDE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 497 NFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDlsLPNGQSLRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRV 575
Cdd:cd05930 282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVP--NPFGPGERMYRTGDLVRWLPDGnLEFLGRIDDQVKIRGYRI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 576 EPEEIERCLRDSQRYRQVAVV----IDPHRRILAFLAqpQEEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNG 651
Cdd:cd05930 360 ELGEIEAALLAHPGVREAAVVaredGDGEKRLVAYVV--PDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNG 437
|
....*..
gi 1957676271 652 KVDRKAL 658
Cdd:cd05930 438 KVDRKAL 444
|
|
| Thioester-redct |
TIGR01746 |
thioester reductase domain; This model includes the terminal domain from the fungal alpha ... |
782-1137 |
3.17e-117 |
|
thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.
Pssm-ID: 273787 [Multi-domain] Cd Length: 367 Bit Score: 367.12 E-value: 3.17e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 782 KVIVTGANSFVGVHIVEALLAWGA-SEVACLVRDGGGQSAAQRFAQALRENRLEHLDLS--RVRVYVADITRPQLGLSED 858
Cdd:TIGR01746 1 TVLLTGATGFLGAYLLEELLRRSTrAKVICLVRADSEEHAMERLREALRSYRLWHENLAmeRIEVVAGDLSKPRLGLSDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 859 VYQRLDREFGALVHNAANVNHVLDYESLARDNVEPIFECLRLCEGRSKKIFNFVSTLSASSTISDDGRVLELPAAQTPPI 938
Cdd:TIGR01746 81 EWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDLSTGVTEDDATVTPYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 939 YIKNGYNLSKWVGERILERARVRGVRVNLYRPGNISFNSLTGVCQPhKNRLMLMLKGSIQLGQVPEF-ALNFDLMPVDFL 1017
Cdd:TIGR01746 161 GLAGGYTQSKWVAELLVREASDRGLPVTIVRPGRILGDSYTGAWNS-SDILWRMVKGCLALGAYPQSpELTEDLTPVDFV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 1018 ARFIAFHASRYQAEK--AVFNLHNPEPLSWDCYVASFREAGREFAMVSVADWQQQLGRVDSDN------ALFGVLGFYLN 1089
Cdd:TIGR01746 240 ARAIVALSSRPAASAggIVFHVVNPNPVPLDEFLEWLERAGYNLRLVSFDEWLQRLEDSDTAKrdsrryPLLPLLHFTGD 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1957676271 1090 GFEEDIGDISMIGHDNAQAGVRQMGAHYPEKSSALLRRGCDYLKEINF 1137
Cdd:TIGR01746 320 AFESDETDTRNLDSRSTAEALEGDGIREPSITAPLLHLYLQYLKEIGF 367
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
154-889 |
9.65e-111 |
|
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: 376.12 E-value: 9.65e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 154 ERLAYVHQLNTTAEPWllqlaqiPMIERLEQRFIQSAER----PALNIAGTSLSHRQLHAHSRAIQQRLQpllDQHQGP- 228
Cdd:COG1020 457 ERQQLLAEWNATAAPY-------PADATLHELFEAQAARtpdaVAVVFGDQSLTYAELNARANRLAHHLR---ALGVGPg 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 229 LVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLHDGEhpLSETMPGLDISGIDisdvnLDQ 308
Cdd:COG1020 527 DLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSA--LAARLPELGVPVLA-----LDA 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 309 PLMRQRPDLDAPCMA--------LYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPT 380
Cdd:COG1020 600 LALAAEPATNPPVPVtpddlayvIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGA 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 381 LLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPALLSIL---PLDQLQILDHVMTGGDVCEPYVIEQLTR---QGN 454
Cdd:COG1020 680 LLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEALPPELVRRWRArlpGAR 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 455 LYNLYGPTEATVLITARQLRTGDNNR---TLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERY 531
Cdd:COG1020 760 LVNLYGPTETTVDSTYYEVTPPDADGgsvPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERF 839
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 532 LDLSLPNGQSlRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVI---DPHRRILAFL 607
Cdd:COG1020 840 VADPFGFPGA-RLYRTGDLARWLPDGnLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAredAPGDKRLVAY 918
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 608 AQPQEEQPgAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLELPVNVTENSQRRLPvsadEALLLEIWA 687
Cdd:COG1020 919 VVPEAGAA-AAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPA----EEEEEEAAL 993
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 688 ELLELPASDISTDESFFNLGGHSILLSRMLLRLREEFGRSISINRFIELPTIAKLATLVRGSGTEEVLSEKALADAFREL 767
Cdd:COG1020 994 ALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLP 1073
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 768 DIKSLPVSRMGDVHKVIVTGANSFVGVHIVEALLAWGASEVACLVRDGGGQSAAQRFAQALRENRLEHLDLSRVRVYVAD 847
Cdd:COG1020 1074 PLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAAL 1153
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1957676271 848 ITRPQLGLSEDVYQRLDREFGALVHNAANVNHVLDYESLARD 889
Cdd:COG1020 1154 LALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLL 1195
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
203-595 |
2.46e-107 |
|
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: 342.32 E-value: 2.46e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 203 SHRQLHAHSRAIQQRLQPLLDQHQGPlVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLHD 282
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGD-RVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 283 GEHplSETMPGLDISGIDISDV-------NLDQPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQ 355
Cdd:TIGR01733 80 SAL--ASRLAGLVLPVILLDPLelaalddAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 356 LTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVE-LIRHQRLSHAFLPPALLSILPLDQLQILDH- 433
Cdd:TIGR01733 158 LDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaLIAEHPVTVLNLTPSLLALLAAALPPALASl 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 434 --VMTGGDVCEPYVIEQLTRQG---NLYNLYGPTEATV----LITARQLRTGDNNRTLGAPIANSQVLILDENFQPVAEQ 504
Cdd:TIGR01733 238 rlVILGGEALTPALVDRWRARGpgaRLINLYGPTETTVwstaTLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 505 TVGELYIVGPGVCLGYLNNPLQTAERYLDLSLPNGQSLRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERC 583
Cdd:TIGR01733 318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGARLYRTGDLVRYLPDGnLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
410
....*....|..
gi 1957676271 584 LRDSQRYRQVAV 595
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
186-658 |
2.44e-105 |
|
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: 340.09 E-value: 2.44e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 186 FIQSAER----PALNIAGTSLSHRQLHAHSRAIQQRLQPLldQHQGPLVVGICLPKCSVLYAGILAILGSGAVYLPLEPS 261
Cdd:cd17651 1 FERQAARtpdaPALVAEGRRLTYAELDRRANRLAHRLRAR--GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 262 HPLQRQQYILENAGAVLLL-HDGEHPLSETMPGLDISGIDISDVNLDQPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQ 340
Cdd:cd17651 79 YPAERLAFMLADAGPVLVLtHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 341 ANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPALL 420
Cdd:cd17651 159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 421 SILPLD------QLQILDHVMTGGD--VCEPYVIEQLTRQG--NLYNLYGPTEATVlITARQLRTGDNNR----TLGAPI 486
Cdd:cd17651 239 RALAEHgrplgvRLAALRYLLTGGEqlVLTEDLREFCAGLPglRLHNHYGPTETHV-VTALSLPGDPAAWpappPIGRPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 487 ANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSLPNGQslRAYRTGDMAKWTSDG-IELCGRRD 565
Cdd:cd17651 318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGA--RMYRTGDLARWLPDGeLEFLGRAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 566 NQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHR----RILAFLAQPQEEQPGAAreALKAHAMQFLPDYMQPTAWTE 641
Cdd:cd17651 396 DQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRpgekRLVAYVVGDPEAPVDAA--ELRAALATHLPEYMVPSAFVL 473
|
490
....*....|....*..
gi 1957676271 642 LASMPFASNGKVDRKAL 658
Cdd:cd17651 474 LDALPLTPNGKLDRRAL 490
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
191-658 |
2.55e-104 |
|
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: 336.57 E-value: 2.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSRAIQQRLQpllDQHQGP-LVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQY 269
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLR---ARGVGPgDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 270 ILENAGAVLLLHDGE--HPLSETMPGLDISGIDIsDVNLDQPLMRQRPDLDAPCMalYTSGTTGHPKGVLLSQANLAHFT 347
Cdd:cd12116 79 ILEDAEPALVLTDDAlpDRLPAGLPVLLLALAAA-AAAPAAPRTPVSPDDLAYVI--YTSGSTGRPKGVVVSHRNLVNFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 348 AWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPALLSILPLDQ 427
Cdd:cd12116 156 HSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 428 LQILDHV--MTGGDVCEPYVIEQLT-RQGNLYNLYGPTEATVLITARQLRTGDNNRTLGAPIANSQVLILDENFQPVAEQ 504
Cdd:cd12116 236 WQGRAGLtaLCGGEALPPDLAARLLsRVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 505 TVGELYIVGPGVCLGYLNNPLQTAERYLDLSLPNGQSlRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERC 583
Cdd:cd12116 316 VPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGS-RLYRTGDLVRRRADGrLEYLGRADGQVKIRGHRIELGEIEAA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957676271 584 LRDSQRYRQVAVVIDPH---RRILAFLAQPQEEQPGAAreALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd12116 395 LAAHPGVAQAAVVVREDggdRRLVAYVVLKAGAAPDAA--ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
180-658 |
5.84e-104 |
|
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: 336.10 E-value: 5.84e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 180 ERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQpllDQHQGP-LVVGICLPKCSVLYAGILAILGSGAVYLPL 258
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLR---AAGVGPgDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 259 EPSHPLQRQQYILENAGAVLLLHDGEHPLSETmPGLDISGIDISDVNLDQPLMRQRPDLDAPCMALYTSGTTGHPKGVLL 338
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLTDRSLAGRAG-GLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 339 SQANLAHfTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPA 418
Cdd:cd12117 157 THRGVVR-LVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 419 LLSILPLDQLQILD---HVMTGGDVCEPYVIEQLTRQ---GNLYNLYGPTEATVLITARQLRTGDNNRT---LGAPIANS 489
Cdd:cd12117 236 LFNQLADEDPECFAglrELLTGGEVVSPPHVRRVLAAcpgLRLVNGYGPTENTTFTTSHVVTELDEVAGsipIGRPIANT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 490 QVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSLPNGqsLRAYRTGDMAKWTSDG-IELCGRRDNQV 568
Cdd:cd12117 316 RVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPG--ERLYRTGDLARWLPDGrLEFLGRIDDQV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 569 KIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH----RRILAFLAqpQEEQPGAAreALKAHAMQFLPDYMQPTAWTELAS 644
Cdd:cd12117 394 KIRGFRIELGEIEAALRAHPGVREAVVVVREDaggdKRLVAYVV--AEGALDAA--ELRAFLRERLPAYMVPAAFVVLDE 469
|
490
....*....|....
gi 1957676271 645 MPFASNGKVDRKAL 658
Cdd:cd12117 470 LPLTANGKVDRRAL 483
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
191-658 |
6.69e-104 |
|
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: 334.22 E-value: 6.69e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSRAIQQRLqplLDQHQGP-LVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQY 269
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLL---AARGVGPeRLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 270 ILENAGAVLLLhdgehplseTMPgldisgidisdvnldqplmrqrpdlDAPCMALYTSGTTGHPKGVLLSQANLAHFTAW 349
Cdd:cd17652 79 MLADARPALLL---------TTP-------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 350 YADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPALLSILPLDQLQ 429
Cdd:cd17652 125 QIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 430 ILDHVMTGGDVCEPYVIEQLTRQGNLYNLYGPTEATVLITARQLRTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGEL 509
Cdd:cd17652 205 DLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGEL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 510 YIVGPGVCLGYLNNPLQTAERYL-DLSLPNGQslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDS 587
Cdd:cd17652 285 YIAGAGLARGYLNRPGLTAERFVaDPFGAPGS--RMYRTGDLARWRADGqLEFLGRADDQVKIRGFRIELGEVEAALTEH 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1957676271 588 QRYRQVAVVID----PHRRILAFLAQPQEEQPGAAreALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd17652 363 PGVAEAVVVVRddrpGDKRLVAYVVPAPGAAPTAA--ELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
180-658 |
1.49e-103 |
|
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: 335.01 E-value: 1.49e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 180 ERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLqplLDQHQGP-LVVGICLPKCSVLYAGILAILGSGAVYLPL 258
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLL---RARGVGPeDRVAVLLPRSADLVVALLAVLKAGAAYLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 259 EPSHPLQRQQYILENAGAVLLLHDG--EHPLSETMPGLDISGIDISDVNLDQPLMRQRPDldAPCMALYTSGTTGHPKGV 336
Cdd:cd17646 79 DPGYPADRLAYMLADAGPAVVLTTAdlAARLPAGGDVALLGDEALAAPPATPPLVPPRPD--NLAYVIYTSGSTGRPKGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 337 LLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLP 416
Cdd:cd17646 157 MVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 417 PALLSIL----PLDQLQILDHVMTGGDVCEPYVIEQLTRQGN--LYNLYGPTEATVLITARQLRTGDNNRTL--GAPIAN 488
Cdd:cd17646 237 PSMLRVFlaepAAGSCASLRRVFCSGEALPPELAARFLALPGaeLHNLYGPTEAAIDVTHWPVRGPAETPSVpiGRPVPN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 489 SQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDlsLPNGQSLRAYRTGDMAKWTSDG-IELCGRRDNQ 567
Cdd:cd17646 317 TRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVP--DPFGPGSRMYRTGDLARWRPDGaLEFLGRSDDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 568 VKIRGFRVEPEEIERCLRDSQRYRQVAVVI----DPHRRILAFLaQPQEEQPGAAREALKAHAMQFLPDYMQPTAWTELA 643
Cdd:cd17646 395 VKIRGFRVEPGEIEAALAAHPAVTHAVVVAraapAGAARLVGYV-VPAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLD 473
|
490
....*....|....*
gi 1957676271 644 SMPFASNGKVDRKAL 658
Cdd:cd17646 474 ALPLTANGKLDRAAL 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
188-775 |
2.57e-96 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 339.06 E-value: 2.57e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 188 QSAERPALNIAGTSLSHRQLHAHSRAIQQRLQpllDQHQGPLV-VGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQR 266
Cdd:PRK12467 524 QHPERPALVFGEQVLSYAELNRQANRLAHVLI---AAGVGPDVlVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDR 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 267 QQYILENAGAVLLLHDgehplSETMPGLDI-SGIDISDVNLDQPLMRQRPDLDAP--------CMALYTSGTTGHPKGVL 337
Cdd:PRK12467 601 LAYMLDDSGVRLLLTQ-----SHLLAQLPVpAGLRSLCLDEPADLLCGYSGHNPEvaldpdnlAYVIYTSGSTGQPKGVA 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 338 LSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPP 417
Cdd:PRK12467 676 ISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVP 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 418 ALLSILPLDQLQILD----HVMTGGDVCEPYV---IEQLTRQGNLYNLYGPTEATVLITARQLRTGD---NNRTLGAPIA 487
Cdd:PRK12467 756 SHLQALLQASRVALPrpqrALVCGGEALQVDLlarVRALGPGARLINHYGPTETTVGVSTYELSDEErdfGNVPIGQPLA 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 488 NSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYL-DLSLPNGQslRAYRTGDMAKWTSDG-IELCGRRD 565
Cdd:PRK12467 836 NLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVpDPFGADGG--RLYRTGDLARYRADGvIEYLGRMD 913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 566 NQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDP---HRRILAFL---AQPQEEQPGAAREALKAHAMQFLPDYMQPTAW 639
Cdd:PRK12467 914 HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPgdaGLQLVAYLvpaAVADGAEHQATRDELKAQLRQVLPDYMVPAHL 993
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 640 TELASMPFASNGKVDRKAlLELPVNVTENSQRRLPVSADEALLLEIWAELLELpaSDISTDESFFNLGGHSILLSRMLLR 719
Cdd:PRK12467 994 LLLDSLPLTPNGKLDRKA-LPKPDASAVQATFVAPQTELEKRLAAIWADVLKV--ERVGLTDNFFELGGHSLLATQVISR 1070
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1957676271 720 LREEFGRSISINRFIELPTiakLATLVRGSGTEEVLSEKALADAFREldiKSLPVS 775
Cdd:PRK12467 1071 VRQRLGIQVPLRTLFEHQT---LAGFAQAVAAQQQGAQPALPDVDRD---QPLPLS 1120
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
180-661 |
1.15e-94 |
|
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: 311.01 E-value: 1.15e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 180 ERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDqhqGP-LVVGICLPKCSVLYAGILAILGSGAVYLPL 258
Cdd:cd05918 3 DLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGV---GPgVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 259 EPSHPLQRQQYILENAGAVLLLHDgehplsetmpgldisgidisdvnldqplmrqrpDLDAPCMALYTSGTTGHPKGVLL 338
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKVVLTS---------------------------------SPSDAAYVIFTSGSTGKPKGVVI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 339 SQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDplQLVELIRHQRLSHAFLPPA 418
Cdd:cd05918 127 EHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLTPS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 419 LLSILPLDQLQILDHVMTGGDVCEPYVIEQLTRQGNLYNLYGPTEATVLITARQLRTGDNNRTLGAPIANSQ-VLILDEN 497
Cdd:cd05918 205 VARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCwVVDPDNH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 498 FQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLD-----LSLPNGQSLRAYRTGDMAKWTSDG-IELCGRRDNQVKIR 571
Cdd:cd05918 285 DRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEdpawlKQEGSGRGRRLYRTGDLVRYNPDGsLEYVGRKDTQVKIR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 572 GFRVEPEEIERCLRDS--QRYRQVAVVIDPHR-----RILAFLAQPQEEQPGAARE---------------ALKAHAMQF 629
Cdd:cd05918 365 GQRVELGEIEHHLRQSlpGAKEVVVEVVKPKDgssspQLVAFVVLDGSSSGSGDGDslflepsdefralvaELRSKLRQR 444
|
490 500 510
....*....|....*....|....*....|..
gi 1957676271 630 LPDYMQPTAWTELASMPFASNGKVDRKALLEL 661
Cdd:cd05918 445 LPSYMVPSVFLPLSHLPLTASGKIDRRALREL 476
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
180-660 |
6.32e-94 |
|
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: 309.26 E-value: 6.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 180 ERLEQRFIQSAERPALNIAGTSLSHRQLHAHS----RAIQQR-LQPllDQhqgplVVGICLPKCSVLYAGILAILGSGAV 254
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERAnqlaRTLREKgVGP--DT-----IVGIMAERSLEMIVGILGILKAGGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 255 YLPLEPSHPLQRQQYILENAGAVLLLHDGEHPlsetmPGLDISGiDISDVNLDQPLMRQRPDLDAPCMA------LYTSG 328
Cdd:cd17655 74 YLPIDPDYPEERIQYILEDSGADILLTQSHLQ-----PPIAFIG-LIDLLDEDTIYHEESENLEPVSKSddlayvIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 329 TTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQ 408
Cdd:cd17655 148 STGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 409 RLSHAFLPPALLSILPLDQLQI---LDHVMTGGDVCEPYVIEQLTRQGN----LYNLYGPTEATVLITARQLRTGDNNRT 481
Cdd:cd17655 228 RITIIDLTPAHLKLLDAADDSEglsLKHLIVGGEALSTELAKKIIELFGtnptITNAYGPTETTVDASIYQYEPETDQQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 482 ---LGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYL-DLSLPNGqslRAYRTGDMAKWTSDG 557
Cdd:cd17655 308 svpIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVdDPFVPGE---RMYRTGDLARWLPDG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 558 -IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLAQPQEeqpgAAREALKAHAMQFLPD 632
Cdd:cd17655 385 nIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQgqnyLCAYIVSEKE----LPVAQLREFLARELPD 460
|
490 500
....*....|....*....|....*...
gi 1957676271 633 YMQPTAWTELASMPFASNGKVDRKALLE 660
Cdd:cd17655 461 YMIPSYFIKLDEIPLTPNGKVDRKALPE 488
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
191-658 |
6.74e-94 |
|
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: 307.76 E-value: 6.74e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSRAIQQRLQPLldqHQGPLV-VGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQY 269
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRAL---GVGPEVrVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 270 ILENAGAVLLLhdGEHPlsetmpgldisgidisdvnldqplmrqrpdlDAPCMALYTSGTTGHPKGVLLSQANLAHFTAW 349
Cdd:cd17649 79 MLEDSGAGLLL--THHP-------------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 350 YADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPALLSILPLDQLQ 429
Cdd:cd17649 126 TAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 430 ILDHV-------MTGGDVCEPyviEQLTRQG----NLYNLYGPTEATVLITA----RQLRTGDNNRTLGAPIANSQVLIL 494
Cdd:cd17649 206 TGDGRppslrlyIFGGEALSP---ELLRRWLkapvRLFNAYGPTEATVTPLVwkceAGAARAGASMPIGRPLGGRSAYIL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 495 DENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYL-DLSLPNGQslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRG 572
Cdd:cd17649 283 DADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVpDPFGAPGS--RLYRTGDLARWRDDGvIEYLGRVDHQVKIRG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 573 FRVEPEEIERCLRDSQRYRQVAVVIDP---HRRILAFLAQPQEEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFAS 649
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVALDgagGKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTP 440
|
....*....
gi 1957676271 650 NGKVDRKAL 658
Cdd:cd17649 441 NGKLDRKAL 449
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
99-749 |
1.73e-91 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 320.84 E-value: 1.73e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 99 ELSGNGQalrLRAVADLVDHVALLVSRFSRdadyFSQAEPMASAhfeQVENLLFLERlAYVHQLNTTAEPwllqLAQIPM 178
Cdd:PRK10252 396 EILANPQ---RYDEATLIAHAERLKALIAQ----FAADPALLCG---DVDILLPGEY-AQLAQVNATAVE----IPETTL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 179 IERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQpllDQHQGP-LVVGICLPKCSVLYAGILAILGSGAVYLP 257
Cdd:PRK10252 461 SALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLR---ERGVKPgDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 258 LEPSHPLQRQQYILENAGAVLLLHDGEhpLSETMPGLDISGIDISDVNL----DQPLMRQRPDldAPCMALYTSGTTGHP 333
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITTAD--QLPRFADVPDLTSLCYNAPLapqgAAPLQLSQPH--HTAYIIFTSGSTGRP 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 334 KGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHA 413
Cdd:PRK10252 614 KGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTT 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 414 FLPPALLSI--------LPLDQLQILDHVMTGG-----DVCEPYviEQLTrQGNLYNLYGPTEATVLIT-------ARQL 473
Cdd:PRK10252 694 HFVPSMLAAfvasltpeGARQSCASLRQVFCSGealpaDLCREW--QQLT-GAPLHNLYGPTEAAVDVSwypafgeELAA 770
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 474 RTGdNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDlsLPNGQSLRAYRTGDMAKW 553
Cdd:PRK10252 771 VRG-SSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIA--DPFAPGERMYRTGDVARW 847
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 554 TSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQV---AVVIDPH-------RRILAFLaqPQEEQPGAAREAL 622
Cdd:PRK10252 848 LDDGaVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthACVINQAaatggdaRQLVGYL--VSQSGLPLDTSAL 925
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 623 KAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAlLELPvNVTENSQRRLPVSADEALLLEIWAELLELPASDISTDes 702
Cdd:PRK10252 926 QAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKA-LPLP-ELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADAD-- 1001
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1957676271 703 FFNLGGHSILLSRMLLRLREEFGRSISINRFIELPTIAKLATLVRGS 749
Cdd:PRK10252 1002 FFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAE 1048
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
190-658 |
3.78e-91 |
|
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: 300.32 E-value: 3.78e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 190 AERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPlvVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQY 269
Cdd:cd05945 5 PDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDP--VVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 270 ILENAGAVLLLHDGehplsetmpgldisgidisdvnldqplmrqrpdlDAPCMALYTSGTTGHPKGVLLSQANLAHFTAW 349
Cdd:cd05945 83 ILDAAKPALLIADG----------------------------------DDNAYIIFTSGSTGRPKGVQISHDNLVSFTNW 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 350 YADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPALLSILPLDQ-- 427
Cdd:cd05945 129 MLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPtf 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 428 ----LQILDHVMTGGdvcEPYVIEQLTR------QGNLYNLYGPTEATVLITARQLR---TGDNNR-TLGAPIANSQVLI 493
Cdd:cd05945 209 tpesLPSLRHFLFCG---EVLPHKTARAlqqrfpDARIYNTYGPTEATVAVTYIEVTpevLDGYDRlPIGYAKPGAKLVI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 494 LDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLslpNGQslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRG 572
Cdd:cd05945 286 LDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPD---EGQ--RAYRTGDLVRLEADGlLFYRGRLDFQVKLNG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 573 FRVEPEEIERCLRDSQRYRQVAVVIDPHR----RILAFL-AQPQEEQPGAAreALKAHAMQFLPDYMQPTAWTELASMPF 647
Cdd:cd05945 361 YRIELEEIEAALRQVPGVKEAVVVPKYKGekvtELIAFVvPKPGAEAGLTK--AIKAELAERLPPYMIPRRFVYLDELPL 438
|
490
....*....|.
gi 1957676271 648 ASNGKVDRKAL 658
Cdd:cd05945 439 NANGKIDRKAL 449
|
|
| SDR_e1 |
cd05235 |
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ... |
782-1067 |
3.30e-90 |
|
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187546 [Multi-domain] Cd Length: 290 Bit Score: 291.86 E-value: 3.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 782 KVIVTGANSFVGVHIVEALLA-WGASEVACLVRDGGGQSAAQRFAQALRENRL---EHLDLSRVRVYVADITRPQLGLSE 857
Cdd:cd05235 1 TVLLTGATGFLGAYLLRELLKrKNVSKIYCLVRAKDEEAALERLIDNLKEYGLnlwDELELSRIKVVVGDLSKPNLGLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 858 DVYQRLDREFGALVHNAANVNHVLDYESLARDNVEPIFECLRLCEGRSKKIFNFVSTLSASSTISDDGRVLE-LPAAQTP 936
Cdd:cd05235 81 DDYQELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDDEeSDDMLES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 937 PIYIKNGYNLSKWVGERILERARVRGVRVNLYRPGNISFNSLTGVCQPHkNRLMLMLKGSIQLGQVPEFALNFDLMPVDF 1016
Cdd:cd05235 161 QNGLPNGYIQSKWVAEKLLREAANRGLPVAIIRPGNIFGDSETGIGNTD-DFFWRLLKGCLQLGIYPISGAPLDLSPVDW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1957676271 1017 LARFIAFHASRYQAEKAVFNLHNPEPLSWDCYVASFREAGREFAMVSVADW 1067
Cdd:cd05235 240 VARAIVKLALNESNEFSIYHLLNPPLISLNDLLDALEEKGYSIKEVSYEEW 290
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
153-711 |
1.45e-89 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 318.82 E-value: 1.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 153 LERLAYVHQLNTTAEPWLLQLAQIPMIERLEQRfiqSAERPALNIAGTSLSHRQLHAHSRAIQQRLQpllDQHQGPLV-V 231
Cdd:PRK12316 491 EERGQLVEGWNATAAEYPLQRGVHRLFEEQVER---TPEAPALAFGEETLDYAELNRRANRLAHALI---ERGVGPDVlV 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 232 GICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLHdgEHPLSETMP---GLDISGIDISDVNLD- 307
Cdd:PRK12316 565 GVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS--QSHLGRKLPlaaGVQVLDLDRPAAWLEg 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 308 ----QPLMRQRPDldAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQ 383
Cdd:PRK12316 643 yseeNPGTELNPE--NLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 384 GAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPALLSIL----PLDQLQILDHVMTGGDVCEPYVIEQLTR---QGNLY 456
Cdd:PRK12316 721 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFlqdeDVASCTSLRRIVCSGEALPADAQEQVFAklpQAGLY 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 457 NLYGPTEATVLIT-ARQLRTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYldLS 535
Cdd:PRK12316 801 NLYGPTEAAIDVThWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERF--VP 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 536 LPNGQSLRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRILAFLAqpQEEQ 614
Cdd:PRK12316 879 SPFVAGERMYRTGDLARYRADGvIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVV--LESE 956
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 615 PGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAlleLPVNVTENSQRRL--PVSADEALLLEIWAELLEL 692
Cdd:PRK12316 957 GGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKA---LPAPEASVAQQGYvaPRNALERTLAAIWQDVLGV 1033
|
570
....*....|....*....
gi 1957676271 693 paSDISTDESFFNLGGHSI 711
Cdd:PRK12316 1034 --ERVGLDDNFFELGGDSI 1050
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
189-658 |
1.16e-88 |
|
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: 293.45 E-value: 1.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 189 SAERPALNIAGTSLSHRQLHAHSRAIQQRLQplldqHQGPL---VVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQ 265
Cdd:cd12115 12 TPDAIALVCGDESLTYAELNRRANRLAARLR-----AAGVGpesRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 266 RQQYILENAGAVLLLhdgehplsetmpgldisgidisdvnldqplmrqrPDLDAPCMALYTSGTTGHPKGVLLSQANLAH 345
Cdd:cd12115 87 RLRFILEDAQARLVL----------------------------------TDPDDLAYVIYTSGSTGRPKGVAIEHRNAAA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 346 FTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNedqrrDPLQLVELIRHQRLShafL----PPALLS 421
Cdd:cd12115 133 FLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEVT---LintvPSAAAE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 422 ILPLDQL-QILDHVMTGGDVCEPYVIEQLTRQGN---LYNLYGPTEATVLITARQLRTGDNNR-TLGAPIANSQVLILDE 496
Cdd:cd12115 205 LLRHDALpASVRVVNLAGEPLPRDLVQRLYARLQverVVNLYGPSEDTTYSTVAPVPPGASGEvSIGRPLANTQAYVLDR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 497 NFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYldLSLPNGQSLRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRV 575
Cdd:cd12115 285 ALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERF--LPDPFGPGARLYRTGDLVRWRPDGlLEFLGRADNQVKVRGFRI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 576 EPEEIERCLRDSQRYRQVAVVI----DPHRRILAFLAQPQEEQPgaAREALKAHAMQFLPDYMQPTAWTELASMPFASNG 651
Cdd:cd12115 363 ELGEIEAALRSIPGVREAVVVAigdaAGERRLVAYIVAEPGAAG--LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNG 440
|
....*..
gi 1957676271 652 KVDRKAL 658
Cdd:cd12115 441 KIDRSAL 447
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
191-658 |
3.81e-88 |
|
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: 291.90 E-value: 3.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSRAIQQRLqplLDQHQGPLV-VGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQY 269
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTL---RAEGVGPGDrVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 270 ILENAGAVLLLHDGEHPlsetmpgldisgidisdvnldqplmrqrpdldapCMALYTSGTTGHPKGVLLSQAN----LAH 345
Cdd:cd17643 79 ILADSGPSLLLTDPDDL----------------------------------AYVIYTSGSTGRPKGVVVSHANvlalFAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 346 FTAWYADyvqlTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLS------HAFLPPAL 419
Cdd:cd17643 125 TQRWFGF----NEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTvlnqtpSAFYQLVE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 420 LSILPLDQLQILDHVMTGGDVCEPYVIEQ-----LTRQGNLYNLYGPTEATVLITARQLRTGD----NNRTLGAPIANSQ 490
Cdd:cd17643 201 AADRDGRDPLALRYVIFGGEALEAAMLRPwagrfGLDRPQLVNMYGITETTVHVTFRPLDAADlpaaAASPIGRPLPGLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 491 VLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSlPNGQSLRAYRTGDMAKWTSDG-IELCGRRDNQVK 569
Cdd:cd17643 281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANP-FGGPGSRMYRTGDLARRLPDGeLEYLGRADEQVK 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 570 IRGFRVEPEEIERCLRDSQRYRQVAVVI---DPHR-RILAFLAqPQEEQPgAAREALKAHAMQFLPDYMQPTAWTELASM 645
Cdd:cd17643 360 IRGFRIELGEIEAALATHPSVRDAAVIVredEPGDtRLVAYVV-ADDGAA-ADIAELRALLKELLPDYMVPARYVPLDAL 437
|
490
....*....|...
gi 1957676271 646 PFASNGKVDRKAL 658
Cdd:cd17643 438 PLTVNGKLDRAAL 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
95-767 |
4.06e-88 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 314.41 E-value: 4.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 95 PVAEELS-GNGQALRLRAVADL-VDHVAL---------LVSRFSRDADYFSQAE-PMASAHFEQVENLLFLERLAYVHQL 162
Cdd:PRK12467 2990 PISEALKqGAPSGLRFGAVSSReQTNYPLtlavglgdtLELEFSYDRQHFDAAAiERLAESFDRLLQAMLNNPAARLGEL 3069
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 163 NTTAEPWLLQLAQ-------IPMIERL-----EQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLqplLDQHQGPLV 230
Cdd:PRK12467 3070 PTLAAHERRQVLHawnataaAYPSERLvhqliEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRL---IAIGVGPDV 3146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 231 -VGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLL---HDGEH-PLSETMPGLDISGIDI---S 302
Cdd:PRK12467 3147 lVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLtqaHLLEQlPAPAGDTALTLDRLDLngyS 3226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 303 DVNLDqplmrqrPDLDAPCMA--LYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPT 380
Cdd:PRK12467 3227 ENNPS-------TRVMGENLAyvIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWT 3299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 381 LLQGAELIVPNEDQrRDPLQLVELIRHQRLSHAFLPPALLSILPLD----QLQILDHVMTGGDVCEPYVIEQLTR---QG 453
Cdd:PRK12467 3300 LICGGCLVVRDNDL-WDPEELWQAIHAHRISIACFPPAYLQQFAEDaggaDCASLDIYVFGGEAVPPAAFEQVKRklkPR 3378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 454 NLYNLYGPTEATVLITARqlRTGDNNRTL------GAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQT 527
Cdd:PRK12467 3379 GLTNGYGPTEAVVTVTLW--KCGGDAVCEapyapiGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLT 3456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 528 AERYL-DLSLPNGQslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH---RR 602
Cdd:PRK12467 3457 AERFVaDPFSGSGG--RLYRTGDLARYRADGvIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGaggKQ 3534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 603 ILAFLAqPQEEQpGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLELPVNVTENSQRrlPVSADEALL 682
Cdd:PRK12467 3535 LVAYVV-PADPQ-GDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVA--PRSEVEQQL 3610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 683 LEIWAELLELPasDISTDESFFNLGGHSILLSRMLLRLREEFGRSISINRFIELPTIAKLATLVRGS--GTEEVLSEKAL 760
Cdd:PRK12467 3611 AAIWADVLGVE--QVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSPLGdvPVNLLLDLNRL 3688
|
....*..
gi 1957676271 761 ADAFREL 767
Cdd:PRK12467 3689 ETGFPAL 3695
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
194-660 |
5.79e-88 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 290.75 E-value: 5.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 194 ALNIAGTSLSHRQLHAHSRAIQQRLqplLDQHQGP-LVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILE 272
Cdd:cd17653 15 AVESLGGSLTYGELDAASNALANRL---LQLGVVPgDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 273 NAGAVLLLHDgehplsetmpgldisgidisdvnldqplmrQRPDLDApcMALYTSGTTGHPKGVLLSQANLAHFTAWYAD 352
Cdd:cd17653 92 TSGATLLLTT------------------------------DSPDDLA--YIIFTSGSTGIPKGVMVPHRGVLNYVSQPPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 353 YVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVpnedqrRDPLQ-LVELIRHQRLSHAflPPALLSILPLDQLQIL 431
Cdd:cd17653 140 RLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDpFAHVARTVDALMS--TPSILSTLSPQDFPNL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 432 DHVMTGGDVCEPYVIEQLTRQGNLYNLYGPTEATVLITARQLRTGDNNrTLGAPIANSQVLILDENFQPVAEQTVGELYI 511
Cdd:cd17653 212 KTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQPV-TIGKPIPNSTCYILDADLQPVPEGVVGEICI 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 512 VGPGVCLGYLNNPLQTAERYLDLSLPNGQslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQ-R 589
Cdd:cd17653 291 SGVQVARGYLGNPALTASKFVPDPFWPGS--RMYRTGDYGRWTEDGgLEFLGREDNQVKVRGFRINLEEIEEVVLQSQpE 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957676271 590 YRQVAVVIdpHR-RILAFLAqPQeeqpGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLE 660
Cdd:cd17653 369 VTQAAAIV--VNgRLVAFVT-PE----TVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
182-658 |
4.64e-84 |
|
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: 281.25 E-value: 4.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 182 LEQRFIQSAERPALNIA----GTSLSHRQLHAHSRAIQQRLQPLLDQHQgpLVVGICLPKCSVLYAGILAILGSGAVYLP 257
Cdd:cd17644 2 IHQLFEEQVERTPDAVAvvfeDQQLTYEELNTKANQLAHYLQSLGVKSE--SLVGICVERSLEMIIGLLAILKAGGAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 258 LEPSHPLQRQQYILENAGAVLLLHDGEhplsetmpgldisgidisdvNLdqplmrqrpdldapCMALYTSGTTGHPKGVL 337
Cdd:cd17644 80 LDPNYPQERLTYILEDAQISVLLTQPE--------------------NL--------------AYVIYTSGSTGKPKGVM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 338 LSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPP 417
Cdd:cd17644 126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 418 ALLSILPLDQLQ----ILDH---VMTGGDVCEPYVIEQLTRQG----NLYNLYGPTEATVLITARQL----RTGDNNRTL 482
Cdd:cd17644 206 AYWHLLVLELLLstidLPSSlrlVIVGGEAVQPELVRQWQKNVgnfiQLINVYGPTEATIAATVCRLtqltERNITSVPI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 483 GAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSLPNGQSLRAYRTGDMAKWTSDG-IELC 561
Cdd:cd17644 286 GRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESERLYKTGDLARYLPDGnIEYL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 562 GRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVI--DP--HRRILAFLAQPQEEQPGAA--REALKAHamqfLPDYMQ 635
Cdd:cd17644 366 GRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVreDQpgNKRLVAYIVPHYEESPSTVelRQFLKAK----LPDYMI 441
|
490 500
....*....|....*....|...
gi 1957676271 636 PTAWTELASMPFASNGKVDRKAL 658
Cdd:cd17644 442 PSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
191-658 |
5.68e-84 |
|
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: 281.47 E-value: 5.68e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGplVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYI 270
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGD--LVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 271 LENAGAVLLLHDGEHPLSETMPGLDISGIDISDVNLDQPLMRqRPDLDAPCMALYTSGTTGHPKGVLLSQANLAHFTAWY 350
Cdd:cd12114 80 LADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPV-DVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 351 ADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPALLSIL------P 424
Cdd:cd12114 159 NRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLldvleaA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 425 LDQLQILDHVMTGGD---VCEPYVIEQLTRQGNLYNLYGPTEATVLITARQLRTGDNNRT---LGAPIANSQVLILDENF 498
Cdd:cd12114 239 QALLPSLRLVLLSGDwipLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRsipYGRPLANQRYRVLDPRG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 499 QPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLslpnGQSLRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEP 577
Cdd:cd12114 319 RDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTH----PDGERLYRTGDLGRYRPDGtLEFLGRRDGQVKVRGYRIEL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 578 EEIERCLRDSQRYRQVAVVI--DPHRRILAFLAQPQEEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDR 655
Cdd:cd12114 395 GEIEAALQAHPGVARAVVVVlgDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
|
...
gi 1957676271 656 KAL 658
Cdd:cd12114 475 AAL 477
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
184-658 |
4.12e-82 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 275.20 E-value: 4.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 184 QRFIQSAER----PALNIAGTSLSHRQLHAHSraiQQRLQPLLDQHQGP-LVVGICLPKCSVLYAGILAILGSGAVYLPL 258
Cdd:cd17645 2 QLFEEQVERtpdhVAVVDRGQSLTYKQLNEKA---NQLARHLRGKGVKPdDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 259 EPSHPLQRQQYILENAGAVLLLHDGEhplsetmpgldisgiDISDVnldqplmrqrpdldapcmaLYTSGTTGHPKGVLL 338
Cdd:cd17645 79 DPDYPGERIAYMLADSSAKILLTNPD---------------DLAYV-------------------IYTSGSTGLPKGVMI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 339 SQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLP-P 417
Cdd:cd17645 125 EHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPtG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 418 ALLSILPLDQlQILDHVMTGGDVCEPYVIEQLTrqgnLYNLYGPTEATVLITARQLRTGDNNRTLGAPIANSQVLILDEN 497
Cdd:cd17645 205 AAEQFMQLDN-QSLRVLLTGGDKLKKIERKGYK----LVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 498 FQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSLPNGQslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVE 576
Cdd:cd17645 280 LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGE--RMYRTGDLAKFLPDGnIEFLGRLDQQVKIRGYRIE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 577 PEEIERCLRDSQRYRQVAVVI----DPHRRILAFLAQPQEEQPGAAREALKahamQFLPDYMQPTAWTELASMPFASNGK 652
Cdd:cd17645 358 PGEIEPFLMNHPLIELAAVLAkedaDGRKYLVAYVTAPEEIPHEELREWLK----NDLPDYMIPTYFVHLKALPLTANGK 433
|
....*.
gi 1957676271 653 VDRKAL 658
Cdd:cd17645 434 VDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
167-750 |
4.87e-82 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 295.71 E-value: 4.87e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 167 EPWLLQLAQIPMIERLEQRFIQSAER----PALNIAGTSLSHRQLHAHSRAIQQRLqplLDQHQGPLV-VGICLPKCSVL 241
Cdd:PRK12316 3044 EAWNATAAEYPLERGVHRLFEEQVERtpdaVALAFGEQRLSYAELNRRANRLAHRL---IERGVGPDVlVGVAVERSLEM 3120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 242 YAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLHDgEHPLSETMPGLDISGIDISDVNLDQPLMRQRPDLDAPC 321
Cdd:PRK12316 3121 VVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ-SHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLA 3199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 322 MALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQL 401
Cdd:PRK12316 3200 YVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALL 3279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 402 VELIRHQRLSHAFLPPALLSILPLD----QLQILDHVMTGGDVCEPYVIEQLTRQGNLYNLYGPTEATVLITARQL-RTG 476
Cdd:PRK12316 3280 VELINSEGVDVLHAYPSMLQAFLEEedahRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTHWQCvEEG 3359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 477 DNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSLPNGQslRAYRTGDMAKWTSD 556
Cdd:PRK12316 3360 KDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGE--RLYRTGDLARYRAD 3437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 557 G-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRILAFLAQPQEEqpGAAREALKAHAMQFLPDYMQ 635
Cdd:PRK12316 3438 GvIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEA--GDLREALKAHLKASLPEYMV 3515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 636 PTAWTELASMPFASNGKVDRKAlleLPVNVTENSQRR--LPVSADEALLLEIWAELLELPasDISTDESFFNLGGHSIlL 713
Cdd:PRK12316 3516 PAHLLFLERMPLTPNGKLDRKA---LPRPDAALLQQDyvAPVNELERRLAAIWADVLKLE--QVGLTDNFFELGGDSI-I 3589
|
570 580 590
....*....|....*....|....*....|....*..
gi 1957676271 714 SRMLLRLREEFGRSISINRFIELPTIAKLATLVRGSG 750
Cdd:PRK12316 3590 SLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGG 3626
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
122-768 |
3.55e-81 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 293.02 E-value: 3.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 122 LVSRFSRDADYFSQA-------------EPMASAHFEQVENLLFL---ERLAYVHQLNTTAEPWLLQlaqiPMIERL-EQ 184
Cdd:PRK12316 4484 LSLQFSYDRGHFDAAtierlarhltnllEAMAEDPQRRLGELQLLekaEQQRIVALWNRTDAGYPAT----RCVHQLvAE 4559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 185 RFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLqplLDQHQGPLV-VGICLPKCSVLYAGILAILGSGAVYLPLEPSHP 263
Cdd:PRK12316 4560 RARMTPDAVAVVFDEEKLTYAELNRRANRLAHAL---IARGVGPEVlVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYP 4636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 264 LQRQQYILENAGAVLLLhdGEHPLSETMP---GLDISGIDISDVNLDQPLMRQRPDLDAPCMA--LYTSGTTGHPKGVLL 338
Cdd:PRK12316 4637 RERLAYMMEDSGAALLL--TQSHLLQRLPipdGLASLALDRDEDWEGFPAHDPAVRLHPDNLAyvIYTSGSTGRPKGVAV 4714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 339 SQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPnEDQRRDPLQLVELIRHQRLSHAFLPPA 418
Cdd:PRK12316 4715 SHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIR-DDSLWDPERLYAEIHEHRVTVLVFPPV 4793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 419 LLSILPLD-----QLQILDHVMTGGDVCEPYVIEQLTRQ---GNLYNLYGPTEATVLITARQLRTGDNNRT----LGAPI 486
Cdd:PRK12316 4794 YLQQLAEHaerdgEPPSLRVYCFGGEAVAQASYDLAWRAlkpVYLFNGYGPTETTVTVLLWKARDGDACGAaympIGTPL 4873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 487 ANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYldlsLPN---GQSLRAYRTGDMAKWTSDG-IELCG 562
Cdd:PRK12316 4874 GNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERF----VPDpfgAPGGRLYRTGDLARYRADGvIDYLG 4949
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 563 RRDNQVKIRGFRVEPEEIERCLRDSQRYRQvAVVID---PHRRILAFLAQPQE-------EQPGAAREALKAHAMQFLPD 632
Cdd:PRK12316 4950 RVDHQVKIRGFRIELGEIEARLREHPAVRE-AVVIAqegAVGKQLVGYVVPQDpaladadEAQAELRDELKAALRERLPE 5028
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 633 YMQPTAWTELASMPFASNGKVDRKALLELPVNVTENSQrRLPVSADEALLLEIWAELLELPasDISTDESFFNLGGHSIL 712
Cdd:PRK12316 5029 YMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAY-VAPRSELEQQVAAIWAEVLQLE--RVGLDDNFFELGGHSLL 5105
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1957676271 713 LSRMLLRLREEFGRSISINRFIELPTIAKLATLVRGSGTEEVLSEKALADAFRELD 768
Cdd:PRK12316 5106 AIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEKFDDLEELLSELE 5161
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
154-711 |
3.94e-81 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 292.84 E-value: 3.94e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 154 ERLAYVHQLNTTAEPWLLQLAqipMIERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLqplLDQHQGPLV-VG 232
Cdd:PRK12467 1555 ERRQILEGWNATHTGYPLARL---VHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRL---IALGVGPEVlVG 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 233 ICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLHDG----EHPLSETMPGLDISGIDISDVNLDQ 308
Cdd:PRK12467 1629 IAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQShlqaRLPLPDGLRSLVLDQEDDWLEGYSD 1708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 309 PLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELI 388
Cdd:PRK12467 1709 SNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLV 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 389 VPNEDQRRDPLQLVELIRHQRLSHAFLPPALLSILPLDQLQI-----LDHVMTGGDVCEPYVIEQ-LTRQGN--LYNLYG 460
Cdd:PRK12467 1789 IAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVehplsLRRVVCGGEALEVEALRPwLERLPDtgLFNLYG 1868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 461 PTEATVLITARQLRTGD----NNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSL 536
Cdd:PRK12467 1869 PTETAVDVTHWTCRRKDlegrDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPF 1948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 537 PNGQSlRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVI--DPHRRILAFLAQP--- 610
Cdd:PRK12467 1949 GTVGS-RLYRTGDLARYRADGvIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAqdGANGKQLVAYVVPtdp 2027
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 611 ----QEEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLELpvNVTENSQRRL-PVSADEALLLEI 685
Cdd:PRK12467 2028 glvdDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAP--DASELQQAYVaPQSELEQRLAAI 2105
|
570 580
....*....|....*....|....*.
gi 1957676271 686 WAELLELPasDISTDESFFNLGGHSI 711
Cdd:PRK12467 2106 WQDVLGLE--QVGLHDNFFELGGDSI 2129
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
174-711 |
1.32e-80 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 291.30 E-value: 1.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 174 AQIPMIERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQpllDQHQGPLV-VGICLPKCSVLYAGILAILGSG 252
Cdd:PRK05691 1129 AQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLR---DKGVGPDVcVAIAAERSPQLLVGLLAILKAG 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 253 AVYLPLEPSHPLQRQQYILENAGAVLLLhdGEHPLSETMPGLD-ISGIDISDVNLDQ-PLMRQRPDLDAPCMA--LYTSG 328
Cdd:PRK05691 1206 GAYVPLDPDYPAERLAYMLADSGVELLL--TQSHLLERLPQAEgVSAIALDSLHLDSwPSQAPGLHLHGDNLAyvIYTSG 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 329 TTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQ 408
Cdd:PRK05691 1284 STGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQY 1363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 409 RLSHAFLPPALLSIL---PL-DQLQILDHVMTGGDVCEP----YVIEQLTrQGNLYNLYGPTEATVLITARQLRTGDNNR 480
Cdd:PRK05691 1364 GVTTLHFVPPLLQLFidePLaAACTSLRRLFSGGEALPAelrnRVLQRLP-QVQLHNRYGPTETAINVTHWQCQAEDGER 1442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 481 T-LGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSLPNgQSLRAYRTGDMAKWTSDG-I 558
Cdd:PRK05691 1443 SpIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGE-DGARLYRTGDRARWNADGaL 1521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 559 ELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIdpHRRIlaflAQPQ-------EEQPGAAREALKAHAMQFLP 631
Cdd:PRK05691 1522 EYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLV--REGA----AGAQlvgyytgEAGQEAEAERLKAALAAELP 1595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 632 DYMQPTAWTELASMPFASNGKVDRKAlleLPVNVTENSQRRLPVSADEALLLEIWAELLELPasDISTDESFFNLGGHSI 711
Cdd:PRK05691 1596 EYMVPAQLIRLDQMPLGPSGKLDRRA---LPEPVWQQREHVEPRTELQQQIAAIWREVLGLP--RVGLRDDFFALGGHSL 1670
|
|
| Lys2b |
COG3320 |
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ... |
783-1046 |
1.11e-78 |
|
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 442549 [Multi-domain] Cd Length: 265 Bit Score: 258.98 E-value: 1.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGASEVACLVRDGGGQSAAQRFAQALRENRLEH-LDLSRVRVYVADITRPQLGLSEDVYQ 861
Cdd:COG3320 3 VLLTGATGFLGAHLLRELLRRTDARVYCLVRASDEAAARERLEALLERYGLWLeLDASRVVVVAGDLTQPRLGLSEAEFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 862 RLDREFGALVHNAANVNHVLDYESLARDNVEPIFECLRLCEGRSKKIFNFVSTLSASSTISDDGRVLE--LPAAQTPpiy 939
Cdd:COG3320 83 ELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVAGPADRSGVFEEddLDEGQGF--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 940 iKNGYNLSKWVGERILERARVRGVRVNLYRPGNISFNSLTGVCQPHkNRLMLMLKGSIQLGQVPEFA-LNFDLMPVDFLA 1018
Cdd:COG3320 160 -ANGYEQSKWVAEKLVREARERGLPVTIYRPGIVVGDSRTGETNKD-DGFYRLLKGLLRLGAAPGLGdARLNLVPVDYVA 237
|
250 260
....*....|....*....|....*...
gi 1957676271 1019 RFIAFHASRYQAEKAVFNLHNPEPLSWD 1046
Cdd:COG3320 238 RAIVHLSRQPEAAGRTFHLTNPQPLSLG 265
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
191-658 |
2.71e-78 |
|
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: 264.71 E-value: 2.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGplVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYI 270
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGS--VVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 271 LENAGAVLLLhdgehplseTMPgldisgidisdvnldqplmrqrpdlDAPCMALYTSGTTGHPKGVLLSQANLAH-FTAW 349
Cdd:cd17650 80 LEDSGAKLLL---------TQP-------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHaAHAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 350 YADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPALlsILP----- 424
Cdd:cd17650 126 RREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPAL--IRPvmayv 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 425 ------LDQLQILdhvMTGGDVCEPYVIEQLTRQ----GNLYNLYGPTEATVLITARQLRTGD----NNRTLGAPIANSQ 490
Cdd:cd17650 204 yrngldLSAMRLL---IVGSDGCKAQDFKTLAARfgqgMRIINSYGVTEATIDSTYYEEGRDPlgdsANVPIGRPLPNTA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 491 VLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSLPNGQslRAYRTGDMAKWTSDG-IELCGRRDNQVK 569
Cdd:cd17650 281 MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGE--RMYRTGDLARWRADGnVELLGRVDHQVK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 570 IRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRILAFLAQPQEEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFAS 649
Cdd:cd17650 359 IRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTP 438
|
....*....
gi 1957676271 650 NGKVDRKAL 658
Cdd:cd17650 439 NGKVDRRAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
104-760 |
7.12e-77 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 279.92 E-value: 7.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 104 GQALRLRAVADLVDHVALLVSRFSRDADYFSQAepMASAHFEQVENLLFLERLAYVHQL---NTTAEPWLLQLAqipMIE 180
Cdd:PRK12316 1933 GETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQ--MAEDAQAALGELALLDAGERQRILadwDRTPEAYPRGPG---VHQ 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 181 RLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLqplLDQHQGPLV-VGICLPKCSVLYAGILAILGSGAVYLPLE 259
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRL---RARGVGPEVrVAIAAERSFELVVALLAVLKAGGAYVPLD 2084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 260 PSHPLQRQQYILENAGAVLLLHDGEhpLSETMP---GLDISGIDISDVNLDQPLMRQRPDLDAPCMA--LYTSGTTGHPK 334
Cdd:PRK12316 2085 PNYPAERLAYMLEDSGAALLLTQRH--LLERLPlpaGVARLPLDRDAEWADYPDTAPAVQLAGENLAyvIYTSGSTGLPK 2162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 335 GVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVpNEDQRRDPLQLVELIRHQRLSHAF 414
Cdd:PRK12316 2163 GVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLI-RDDELWDPEQLYDEMERHGVTILD 2241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 415 LPPALLSILpLDQLQILDH------VMTGGDVCEPYVIEQLTRQ---GNLYNLYGPTEATVLITARQLRTGDNNRTLGAP 485
Cdd:PRK12316 2242 FPPVYLQQL-AEHAERDGRppavrvYCFGGEAVPAASLRLAWEAlrpVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVP 2320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 486 I----ANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSLPNGQSlRAYRTGDMAKWTSDG-IEL 560
Cdd:PRK12316 2321 IgralGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGE-RLYRTGDLARYRADGvVEY 2399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 561 CGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQvAVVIDPH----RRILAFLAqPQEEQPGaAREALKAHAMQFLPDYMQP 636
Cdd:PRK12316 2400 LGRIDHQVKIRGFRIELGEIEARLQAHPAVRE-AVVVAQDgasgKQLVAYVV-PDDAAED-LLAELRAWLAARLPAYMVP 2476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 637 TAWTELASMPFASNGKVDRKALLELPVNVTENSQRRlPVSADEALLLEIWAELLELpaSDISTDESFFNLGGHSILLSRM 716
Cdd:PRK12316 2477 AHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVA-PQEGLEQRLAAIWQAVLKV--EQVGLDDHFFELGGHSLLATQV 2553
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1957676271 717 LLRLREEFGRSISINRFIELPTIAKLATLVRGSGTEEVLSEKAL 760
Cdd:PRK12316 2554 VSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKV 2597
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
201-658 |
1.91e-76 |
|
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: 260.48 E-value: 1.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 201 SLSHRQLHAHSRAIQQRLQPLLDQHQGPlvVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLL 280
Cdd:cd17656 13 KLTYRELNERSNQLARFLREKGVKKDSI--VAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 281 HDGEHPLSETMPGL-------DISGIDISDVNLDQplmrqrpDLDAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADY 353
Cdd:cd17656 91 TQRHLKSKLSFNKStilledpSISQEDTSNIDYIN-------NSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 354 VQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPALLS-ILPLDQL---- 428
Cdd:cd17656 164 TNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKfIFSEREFinrf 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 429 -QILDHVMTGGD---VCEPYVIEQLTRQGNLYNLYGPTEATVlITARQLRTGDNNRTL---GAPIANSQVLILDENFQPV 501
Cdd:cd17656 244 pTCVKHIITAGEqlvITNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTINPEAEIPELppiGKPISNTWIYILDQEQQLQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 502 AEQTVGELYIVGPGVCLGYLNNPLQTAERYldLSLPNGQSLRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEI 580
Cdd:cd17656 323 PQGIVGELYISGASVARGYLNRQELTAEKF--FPDPFDPNERMYRTGDLARYLPDGnIEFLGRADHQVKIRGYRIELGEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 581 ERCLRDSQRYRQVAVVI----DPHRRILAFLAQPQEEQPGAAREALKahamQFLPDYMQPTAWTELASMPFASNGKVDRK 656
Cdd:cd17656 401 EAQLLNHPGVSEAVVLDkaddKGEKYLCAYFVMEQELNISQLREYLA----KQLPEYMIPSFFVPLDQLPLTPNGKVDRK 476
|
..
gi 1957676271 657 AL 658
Cdd:cd17656 477 AL 478
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
325-1094 |
2.11e-76 |
|
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: 276.56 E-value: 2.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 325 YTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVEL 404
Cdd:TIGR03443 422 FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEW 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 405 IRHQRLSHAFLPPA---LLSILPLDQLQILDHVMTGGDV-----CepYVIEQLTRQGNLYNLYGPTEatvliTARQL--- 473
Cdd:TIGR03443 502 MAKYGATVTHLTPAmgqLLSAQATTPIPSLHHAFFVGDIltkrdC--LRLQTLAENVCIVNMYGTTE-----TQRAVsyf 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 474 ----RTGDNN--RTL------GAPIANSQVLILDEN--FQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYL------- 532
Cdd:TIGR03443 575 eipsRSSDSTflKNLkdvmpaGKGMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfvdp 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 533 ----DLSLPNGQSL---------RAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCL-------------- 584
Cdd:TIGR03443 655 shwiDLDKENNKPErefwlgprdRLYRTGDLGRYLPDGnVECCGRADDQVKIRGFRIELGEIDTHLsqhplvrenvtlvr 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 585 RDSQRYRQVAVVIDPHRR---ILAFLAQPQEEQPG-----------AAREALKAHAMQFLPDYMQPTAWTELASMPFASN 650
Cdd:TIGR03443 735 RDKDEEPTLVSYIVPQDKsdeLEEFKSEVDDEESSdpvvkglikyrKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPN 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 651 GKVDRKAL-LELPVNVTENSQRRLPVSADEAL------LLEIWAELLELPASDISTDESFFNLGGHSILLSRMLLRLREE 723
Cdd:TIGR03443 815 GKVDKPALpFPDTAQLAAVAKNRSASAADEEFtetereIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKK 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 724 FGRSISINRFIELPTIAKLATLV------------RGSGTEEvlSEKALADAFRElDIKSL--------PVSRMGDVHK- 782
Cdd:TIGR03443 895 LNVELPLGLIFKSPTIKGFAKEVdrlkkgeeladeGDSEIEE--EETVLELDYAK-DAKTLvdslpksyPSRKELDASTp 971
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 --VIVTGANSFVGVHIVEALLAWGAS---EVACLVRDGGGQSAAQRFAQALR------ENRlehldLSRVRVYVADITRP 851
Cdd:TIGR03443 972 itVFLTGATGFLGSFILRDLLTRRSNsnfKVFAHVRAKSEEAGLERLRKTGTtygiwdEEW-----ASRIEVVLGDLSKE 1046
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 852 QLGLSEDVYQRLDREFGALVHNAANVNHVLDYESLARDNVEPIFECLRLC-EGRSkKIFNFVSTLSA---------SSTI 921
Cdd:TIGR03443 1047 KFGLSDEKWSDLTNEVDVIIHNGALVHWVYPYSKLRDANVIGTINVLNLCaEGKA-KQFSFVSSTSAldteyyvnlSDEL 1125
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 922 SDDGR--VLELPAAQTPPIYIKNGYNLSKWVGERILERARVRGVRVNLYRPGNISFNSLTGVCQPhKNRLMLMLKGSIQL 999
Cdd:TIGR03443 1126 VQAGGagIPESDDLMGSSKGLGTGYGQSKWVAEYIIREAGKRGLRGCIVRPGYVTGDSKTGATNT-DDFLLRMLKGCIQL 1204
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 1000 GQVPEFALNFDLMPVDFLARFI---AFHASRyQAEKAVFNLHNPEPLSWDCYVASFREAGREFAMVSVADWQQQLGRV-- 1074
Cdd:TIGR03443 1205 GLIPNINNTVNMVPVDHVARVVvaaALNPPK-ESELAVAHVTGHPRIRFNDFLGTLKTYGYDVEIVDYVHWRKSLERFvi 1283
|
890 900
....*....|....*....|..
gi 1957676271 1075 --DSDNALFGVLGFYLNGFEED 1094
Cdd:TIGR03443 1284 erSEDNALFPLLHFVLDDLPQS 1305
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
178-661 |
6.63e-75 |
|
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: 255.51 E-value: 6.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 178 MIERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGplVVGICLPKCSVLYAGILAILGSGAVYLP 257
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGD--RVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 258 LEPSHPLQRQQYILENAGAVLLLHdgehplsetmpgldisgidisdvnldqplmrqrpdldapCMALYTSGTTGHPKGVL 337
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT---------------------------------------ALILYTSGTTGRPKGVM 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 338 LSQANLAHFTAWYADYVQLTEQSRVL----------QFSSlsfdsslidIFPTLLQGAELIVPNedqRRDPLQLVELIRH 407
Cdd:COG0318 120 LTHRNLLANAAAIAAALGLTPGDVVLvalplfhvfgLTVG---------LLAPLLAGATLVLLP---RFDPERVLELIER 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 408 QRLSHAFLPPALLSILpLDQLQI-------LDHVMTGGDVCEPYVIEQLTRQGN--LYNLYGPTEATVLITARQLRTGDN 478
Cdd:COG0318 188 ERVTVLFGVPTMLARL-LRHPEFarydlssLRLVVSGGAPLPPELLERFEERFGvrIVEGYGLTETSPVVTVNPEDPGER 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 479 NR-TLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDlslpngqslRAYRTGDMAKWTSDG 557
Cdd:COG0318 267 RPgSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD---------GWLRTGDLGRLDEDG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 558 -IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH----RRILAFLAQPQEEQPGAarEALKAHAMQFLPD 632
Cdd:COG0318 338 yLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDekwgERVVAFVVLRPGAELDA--EELRAFLRERLAR 415
|
490 500
....*....|....*....|....*....
gi 1957676271 633 YMQPTAWTELASMPFASNGKVDRKALLEL 661
Cdd:COG0318 416 YKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
188-571 |
6.16e-70 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 240.29 E-value: 6.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 188 QSAERPALNIA-GTSLSHRQLHAHSRAIQQRLQpLLDQHQGPlVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQR 266
Cdd:pfam00501 7 RTPDKTALEVGeGRRLTYRELDERANRLAAGLR-ALGVGKGD-RVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 267 QQYILENAGAVLLLHDGEHPLS---ETMPGLDISGIDI----------------SDVNLDQPLMRQRPDLDAPCMALYTS 327
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALKLEellEALGKLEVVKLVLvldrdpvlkeeplpeeAKPADVPPPPPPPPDPDDLAYIIYTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 328 GTTGHPKGVLLSQANLAHFTAWYADYVQ----LTEQSRVLQFSSLS-FDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLV 402
Cdd:pfam00501 165 GTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFhDFGLSLGLLGPLLAGATVVLPPGFPALDPAALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 403 ELIRHQRLSHAFLPPALLSIL------PLDQLQILDHVMTGGDVCEPYVIEQLTRQ--GNLYNLYGPTEATVLITARQLR 474
Cdd:pfam00501 245 ELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFRELfgGALVNGYGLTETTGVVTTPLPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 475 TGDNNR--TLGAPIANSQVLILDENF-QPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLdlslpngqSLRAYRTGDMA 551
Cdd:pfam00501 325 DEDLRSlgSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD--------EDGWYRTGDLG 396
|
410 420
....*....|....*....|.
gi 1957676271 552 KWTSDG-IELCGRRDNQVKIR 571
Cdd:pfam00501 397 RRDEDGyLEIVGRKKDQIKLG 417
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
178-660 |
7.34e-70 |
|
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: 242.74 E-value: 7.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 178 MIERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPLVV-GICLPkcsVLYAGILAILGSGAVYL 256
Cdd:TIGR01734 2 LIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVyGHMEP---HMLVAFLGSIKSGHAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 257 PLEPSHPLQRQQYILENAGAVLLLHDGEhpLSETMPGLDIsgidISDVNLDQPLMRQRP-DLDAPCMA------LYTSGT 329
Cdd:TIGR01734 79 PVDTSIPSERIEMIIEAAGPELVIHTAE--LSIDAVGTQI----ITLSALEQAETSGGPvSFDHAVKGddnyyiIYTSGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 330 TGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQR 409
Cdd:TIGR01734 153 TGNPKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 410 LSHAFLPPALLSILPLD------QLQILDHVMTGGDVCEPYVIEQL-TR--QGNLYNLYGPTEATVLITARQLRTG--DN 478
Cdd:TIGR01734 233 LNVWVSTPSFVDMCLLDpnfnqeNYPHLTHFLFCGEELPVKTAKALlERfpKATIYNTYGPTEATVAVTSVKITQEilDQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 479 NRTLgaPI----ANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLslpngQSLRAYRTGDMAKWT 554
Cdd:TIGR01734 313 YPRL--PIgfakPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH-----EGQPAYRTGDAGTIT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 555 sDGIELC-GRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV--IDPHRRILAFLAQ--PQEEQPGAARE---ALKAHA 626
Cdd:TIGR01734 386 -DGQLFYqGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVpkYNKDHKVEYLIAAivPETEDFEKEFQltkAIKKEL 464
|
490 500 510
....*....|....*....|....*....|....
gi 1957676271 627 MQFLPDYMQPTAWTELASMPFASNGKVDRKALLE 660
Cdd:TIGR01734 465 KKSLPAYMIPRKFIYRDQLPLTANGKIDRKALAE 498
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
154-711 |
8.46e-68 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 251.63 E-value: 8.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 154 ERLAYVHQLNTTAEPWLL-QLAQIPMIERLEQ----RFIQSAER----PALNIAGTSLSHRQLHAHSraiqQRLQPLLDQ 224
Cdd:PRK05691 2157 QRLAELPLLAAAEQQQLLdSLAGEAGEARLDQtlhgLFAAQAARtpqaPALTFAGQTLSYAELDARA----NRLARALRE 2232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 225 HQ-GPLV-VGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLHDGEhpLSETMPGLDiSGIDIS 302
Cdd:PRK05691 2233 RGvGPQVrVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRA--LFEALGELP-AGVARW 2309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 303 DVNLDQPLMRQRPDLDAPCMAL--------YTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSL 374
Cdd:PRK05691 2310 CLEDDAAALAAYSDAPLPFLSLpqhqayliYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAAS 2389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 375 IDIFPTLLQGAELIVPNEDQRrDPLQLVELIRHQRLSHAFLPPALLSILP---LDQLQILD--HVMTGGDVCEP---YVI 446
Cdd:PRK05691 2390 ERLLVPLLCGARVVLRAQGQW-GAEEICQLIREQQVSILGFTPSYGSQLAqwlAGQGEQLPvrMCITGGEALTGehlQRI 2468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 447 EQLTRQGNLYNLYGPTEATVLITA----RQLRTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLN 522
Cdd:PRK05691 2469 RQAFAPQLFFNAYGPTETVVMPLAclapEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHD 2548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 523 NPLQTAERYL-DLSLPNGQslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV---I 597
Cdd:PRK05691 2549 RPGLTAERFVaDPFAADGG--RLYRTGDLVRLRADGlVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLaldT 2626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 598 DPHRRILAFLAQPQ----EEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAlLELPVNVTENSQRRL 673
Cdd:PRK05691 2627 PSGKQLAGYLVSAVagqdDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRA-LPAPDPELNRQAYQA 2705
|
570 580 590
....*....|....*....|....*....|....*...
gi 1957676271 674 PVSADEALLLEIWAELLELpaSDISTDESFFNLGGHSI 711
Cdd:PRK05691 2706 PRSELEQQLAQIWREVLNV--ERVGLGDNFFELGGDSI 2741
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
178-660 |
7.96e-64 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 225.54 E-value: 7.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 178 MIERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPLVVgiclpkcsvlY--------AGILAIL 249
Cdd:PRK04813 4 IIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIV----------FghmspemlATFLGAV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 250 GSGAVYLPLEPSHPLQRQQYILENAGAVLLLHDGEHPLSETmpglDISGIDISDVNlDQPLMRQRPDLDAPCMA------ 323
Cdd:PRK04813 74 KAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEIL----GIPVITLDELK-DIFATGNPYDFDHAVKGddnyyi 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 324 LYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVE 403
Cdd:PRK04813 149 IFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 404 LIRHQRLS----------HAFLPPALLSilplDQLQILDHVMTGGDVCEPYVIEQL-TR--QGNLYNLYGPTEATVLITA 470
Cdd:PRK04813 229 TLPQLPINvwvstpsfadMCLLDPSFNE----EHLPNLTHFLFCGEELPHKTAKKLlERfpSATIYNTYGPTEATVAVTS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 471 RQLrTGD----NNR-TLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLslpNGQslRAY 545
Cdd:PRK04813 305 IEI-TDEmldqYKRlPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF---DGQ--PAY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 546 RTGDMAKwTSDGIELC-GRRDNQVKIRGFRVEPEEIERCLRDSQRYRQ-VAVVIDPHRRILAFLAQ--PQEEQPGAARE- 620
Cdd:PRK04813 379 HTGDAGY-LEDGLLFYqGRIDFQIKLNGYRIELEEIEQNLRQSSYVESaVVVPYNKDHKVQYLIAYvvPKEEDFEREFEl 457
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1957676271 621 --ALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLE 660
Cdd:PRK04813 458 tkAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
201-658 |
9.19e-63 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 221.12 E-value: 9.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 201 SLSHRQLHAHSRAIQQRLQPLLDQHQGPLVvGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLL 280
Cdd:cd17648 12 RLTYRELNERANRLAHYLLSVAEIRPDDLV-GLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 281 hdgehplsetmpgldisgIDISDVnldqplmrqrpdldapCMALYTSGTTGHPKGVLLSQANLAHF-TAWYADY-VQLTE 358
Cdd:cd17648 91 ------------------TNSTDL----------------AYAIYTSGTTGKPKGVLVEHGSVVNLrTSLSERYfGRDNG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 359 QSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPALLSILPLDQLQILDHVMTGG 438
Cdd:cd17648 137 DEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLARLPHLKRVDAAG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 439 DVCEPYVIEQLTRQ--GNLYNLYGPTEATVLITARQLRTGDN-NRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPG 515
Cdd:cd17648 217 EEFTAPVFEKLRSRfaGLIINAYGPTETTVTNHKRFFPGDQRfDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 516 VCLGYLNNPLQTAERYldlsLPN----------GQSLRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCL 584
Cdd:cd17648 297 VARGYLNRPELTAERF----LPNpfqteqerarGRNARLYKTGDLVRWLPSGeLEYLGRNDFQVKIRGQRIEPGEVEAAL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 585 RDSQRYRQVAVVI-----DPHRRILAFLAQPQEEQPGAAREA-LKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd17648 373 ASYPGVRECAVVAkedasQAQSRIQKYLVGYYLPEPGHVPESdLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| NAD_binding_4 |
pfam07993 |
Male sterility protein; This family represents the C-terminal region of the male sterility ... |
785-1021 |
3.41e-61 |
|
Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.
Pssm-ID: 462334 [Multi-domain] Cd Length: 257 Bit Score: 209.77 E-value: 3.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 785 VTGANSFVGVHIVEALLAW--GASEVACLVRDGGGQSAAQRFAQALRENRLEHLD----LSRVRVYVADITRPQLGLSED 858
Cdd:pfam07993 1 LTGATGFLGKVLLEKLLRStpDVKKIYLLVRAKDGESALERLRQELEKYPLFDALlkeaLERIVPVAGDLSEPNLGLSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 859 VYQRLDREFGALVHNAANVNHVLDYESLARDNVEPIFECLRLCE-GRSKKIFNFVSTlSASSTIS-------------DD 924
Cdd:pfam07993 81 DFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKqGKQLKPFHHVST-AYVNGERgglveekpypegeDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 925 GRVLELPAAQTPPiyIKNGYNLSKWVGERILERARVRGVRVNLYRPGNISFNSLTGVCQPHkNRLMLMLKGSIQLGQVPE 1004
Cdd:pfam07993 160 MLLDEDEPALLGG--LPNGYTQTKWLAEQLVREAARRGLPVVIYRPSIITGEPKTGWINNF-DFGPRGLLGGIGKGVLPS 236
|
250 260
....*....|....*....|.
gi 1957676271 1005 FALN----FDLMPVDFLARFI 1021
Cdd:pfam07993 237 ILGDpdavLDLVPVDYVANAI 257
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
179-768 |
3.74e-57 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 217.73 E-value: 3.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 179 IERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPlvVGICLPKCSVLYAGILAILGSGAVYLPL 258
Cdd:PRK05691 3723 VRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQP--VALLAERGLDLLGMIVGSFKAGAGYLPL 3800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 259 EPSHPLQRQQYILENAGAVLLLHDGE-----HPLSETMPG------LDISGIDISDVNLDQPLMRQRPDLDApcMALYTS 327
Cdd:PRK05691 3801 DPGLPAQRLQRIIELSRTPVLVCSAAcreqaRALLDELGCanrprlLVWEEVQAGEVASHNPGIYSGPDNLA--YVIYTS 3878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 328 GTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAEL-IVPNeDQRRDPLQLVELIR 406
Cdd:PRK05691 3879 GSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVeIVPN-AIAHDPQGLLAHVQ 3957
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 407 HQRLSHAFLPPALLSILPLDQLQILDHV---MTGGDVCEPYVIEQ-LTR--QGNLYNLYGPTEAT---VLITARQLRTGD 477
Cdd:PRK05691 3958 AQGITVLESVPSLIQGMLAEDRQALDGLrwmLPTGEAMPPELARQwLQRypQIGLVNAYGPAECSddvAFFRVDLASTRG 4037
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 478 NNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLdlslPN---GQSLRAYRTGDMAKWT 554
Cdd:PRK05691 4038 SYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFV----PHpfgAPGERLYRTGDLARRR 4113
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 555 SDGI-ELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH---RRILAFLAQPQEEQ-PGAAREALKAHAMQF 629
Cdd:PRK05691 4114 SDGVlEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGvngKHLVGYLVPHQTVLaQGALLERIKQRLRAE 4193
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 630 LPDYMQPTAWTELASMPFASNGKVDRKALLELPVNVTENSQRRLPVSADEALLLEIWAELLElpASDISTDESFFNLGGH 709
Cdd:PRK05691 4194 LPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLATIWADVLK--VERVGVHDNFFELGGH 4271
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1957676271 710 SILLSRMLLRLREEFGRSISINRFIELPTIAKLATLVRGSGTEEVLSEKA--LADAFRELD 768
Cdd:PRK05691 4272 SLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAGSAIDEQKVdrLSDLMAELE 4332
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
320-654 |
6.12e-54 |
|
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: 191.73 E-value: 6.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 320 PCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNedqRRDPL 399
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 400 QLVELIRHQRLSHAFLPPALLSILpLDQLQI-------LDHVMTGGDVCEPYVIEQLTRQGN--LYNLYGPTEATVLITA 470
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARL-LKAPESagydlssLRALVSGGAPLPPELLERFEEAPGikLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 471 rqLRTGDNNR---TLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAEryldlSLPNGqslrAYRT 547
Cdd:cd04433 158 --GPPDDDARkpgSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAA-----VDEDG----WYRT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 548 GDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH----RRILAFLaQPQEEQPgAAREAL 622
Cdd:cd04433 227 GDLGRLDEDGyLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDpewgERVVAVV-VLRPGAD-LDAEEL 304
|
330 340 350
....*....|....*....|....*....|..
gi 1957676271 623 KAHAMQFLPDYMQPTAWTELASMPFASNGKVD 654
Cdd:cd04433 305 RAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
182-655 |
1.20e-42 |
|
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: 162.01 E-value: 1.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 182 LEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGplVVGICLPKCSVLYAGILAILGSGAVYLPLEPS 261
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGD--RVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 262 HPLQRQQYILENAGAVLLLHDgehplsetmpgldisgidisdvnldqplmrqrpdldaPCMALYTSGTTGHPKGVLLSQA 341
Cdd:cd17631 79 LTPPEVAYILADSGAKVLFDD-------------------------------------LALLMYTSGTTGRPKGAMLTHR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 342 NL-AHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPnedQRRDPLQLVELIRHQRLSHAFLPPALL 420
Cdd:cd17631 122 NLlWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVIL---RKFDPETVLDLIERHRVTSFFLVPTMI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 421 SILpLDQ-------LQILDHVMTGGDVCEPYVIEQLTRQG-NLYNLYGPTEATVLITArqLRTGDNNRTLGA---PIANS 489
Cdd:cd17631 199 QAL-LQHprfattdLSSLRAVIYGGAPMPERLLRALQARGvKFVQGYGMTETSPGVTF--LSPEDHRRKLGSagrPVFFV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 490 QVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAEryldlSLPNGQslraYRTGDMAKWTSDG-IELCGRRDNQV 568
Cdd:cd17631 276 EVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAA-----AFRDGW----FHTGDLGRLDEDGyLYIVDRKKDMI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 569 KIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLAqPQEEQPGAArEALKAHAMQFLPDYMQPTAWTELAS 644
Cdd:cd17631 347 ISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwgeaVVAVVV-PRPGAELDE-DELIAHCRERLARYKIPKSVEFVDA 424
|
490
....*....|.
gi 1957676271 645 MPFASNGKVDR 655
Cdd:cd17631 425 LPRNATGKILK 435
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
188-658 |
8.11e-40 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 155.71 E-value: 8.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 188 QSAER----PALNIAGTSLSHRQLHAHSRAIQQRLQPLldqhqGPLV---VGICLPK----CSVLYAGILAilgsGAVYL 256
Cdd:TIGR03098 8 DAAARlpdaTALVHHDRTLTYAALSERVLALASGLRGL-----GLARgerVAIYLDKrletVTAMFGAALA----GGVFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 257 PLEPShpLQRQQ--YILENAGAVLL---------LHDG---------------EHPLSETMPGLDISGIDISDVNLDQPL 310
Cdd:TIGR03098 79 PINPL--LKAEQvaHILADCNVRLLvtsserldlLHPAlpgchdlrtliivgdPAHASEGHPGEEPASWPKLLALGDADP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 311 MRQRPDLDAPCMaLYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVP 390
Cdd:TIGR03098 157 PHPVIDSDMAAI-LYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 391 NEDQRRDPLQLVEliRHQRLSHAFLPP--ALLSIL--PLDQLQILDHVMTGGDVCEPYVIEQLTR---QGNLYNLYGPTE 463
Cdd:TIGR03098 236 DYLLPRDVLKALE--KHGITGLAAVPPlwAQLAQLdwPESAAPSLRYLTNSGGAMPRATLSRLRSflpNARLFLMYGLTE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 464 A---TVLITARQLRTGDnnrTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSLPNGQ 540
Cdd:TIGR03098 314 AfrsTYLPPEEVDRRPD---SIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 541 SLR---AYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAV--VIDPH--RRILAFLAQPQE 612
Cdd:TIGR03098 391 LHLpelAVWSGDTVRRDEEGfLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAfgVPDPTlgQAIVLVVTPPGG 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1957676271 613 EQpgAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:TIGR03098 471 EE--LDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
182-658 |
9.83e-39 |
|
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: 151.18 E-value: 9.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 182 LEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPL----LDQhqgplvVGICLPKCSVLYAGILAILGSGAVYLP 257
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLgvqpGDR------VALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 258 LEPSHPLQRQQYILENAGAVLL--LHDGEHPLSETMPgldisgidisdvnldqPLMRQRPDLDAPCMALYTSGTTGHPKG 335
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALivAVSFTDLLAAGAP----------------LGERVALTPEDVAVLQYTSGTTGVPKG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 336 VLLSQANLAHFT----AWYADyvQLTEQSRVLqfsslsfdsSLIDIFPT----------LLQGAELI-VPnedqRRDPLQ 400
Cdd:cd05936 143 AMLTHRNLVANAlqikAWLED--LLEGDDVVL---------AALPLFHVfgltvalllpLALGATIVlIP----RFRPIG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 401 LVELIRHQRLSHAFLPPALLSIL------PLDQLQILDHVMTGGDVCEPYVIEQLTR--QGNLYNLYGPTEATVLITARQ 472
Cdd:cd05936 208 VLKEIRKHRVTIFPGVPTMYIALlnapefKKRDFSSLRLCISGGAPLPVEVAERFEEltGVPIVEGYGLTETSPVVAVNP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 473 LRTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDlslpnGqslrAYRTGDMAK 552
Cdd:cd05936 288 LDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVD-----G----WLRTGDIGY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 553 WTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLAQPQEEQPGAarEALKAHAM 627
Cdd:cd05936 359 MDEDGyFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYsgeaVKAFVVLKEGASLTE--EEIIAFCR 436
|
490 500 510
....*....|....*....|....*....|.
gi 1957676271 628 QFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd05936 437 EQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
192-658 |
4.47e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 144.36 E-value: 4.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 192 RPALNIAGTSLSHRQLhahSRAIQQRLQPL--LDQHQGPLVVGICLPKCSVLYAGILAILgSGAVYLPLEPSHPLQRQQY 269
Cdd:PRK06188 28 RPALVLGDTRLTYGQL---ADRISRYIQAFeaLGLGTGDAVALLSLNRPEVLMAIGAAQL-AGLRRTALHPLGSLDDHAY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 270 ILENAGA-VLLLHDGEHP-----LSETMPGLD--------ISGIDIS---DVNLDQPLMRQRPDLDAPCMAlYTSGTTGH 332
Cdd:PRK06188 104 VLEDAGIsTLIVDPAPFVeralaLLARVPSLKhvltlgpvPDGVDLLaaaAKFGPAPLVAAALPPDIAGLA-YTGGTTGK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 333 PKGVLLSQANLAHFTAW-YADYvQLTEQSRVLQFSSLSFDSSLIdIFPTLLQGAELIVPnedQRRDPLQLVELIRHQRLS 411
Cdd:PRK06188 183 PKGVMGTHRSIATMAQIqLAEW-EWPADPRFLMCTPLSHAGGAF-FLPTLLRGGTVIVL---AKFDPAEVLRAIEEQRIT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 412 HAFLPPALLSILpLDQ-------LQILDHVMTGGDVCEP-YVIEQLTRQGNLY-NLYGPTEATVLITarQLRTGDNNR-- 480
Cdd:PRK06188 258 ATFLVPTMIYAL-LDHpdlrtrdLSSLETVYYGASPMSPvRLAEAIERFGPIFaQYYGQTEAPMVIT--YLRKRDHDPdd 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 481 -----TLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAEryldlSLPNGQslraYRTGDMAKWTS 555
Cdd:PRK06188 335 pkrltSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAE-----AFRDGW----LHTGDVAREDE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 556 DG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLAQPQEEQPGAA--REALKAHamq 628
Cdd:PRK06188 406 DGfYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwgeaVTAVVVLRPGAAVDAAelQAHVKER--- 482
|
490 500 510
....*....|....*....|....*....|....*
gi 1957676271 629 flpdymQPTAWTE-----LASMPFASNGKVDRKAL 658
Cdd:PRK06188 483 ------KGSVHAPkqvdfVDSLPLTALGKPDKKAL 511
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
191-660 |
2.44e-35 |
|
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: 140.50 E-value: 2.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPLVvGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYI 270
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRV-AFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 271 LENAGAVLLLhdgehplsetmpgldisgidisdvnldqplmrqrpdldAPCMALYTSGTTGHPKGVLLSQANLAHFTAWY 350
Cdd:cd05941 80 ITDSEPSLVL--------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 351 ADYVQLTEQSRVLQfsslsfdsslidIFP-------------TLLQGAELIVpnedQRRDPLQLVELIRHQ--------- 408
Cdd:cd05941 122 VDAWRWTEDDVLLH------------VLPlhhvhglvnallcPLFAGASVEF----LPKFDPKEVAISRLMpsitvfmgv 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 409 -----RL----SHAFLPPALLSILPLDQLQILdhvMTGGDVCEPYVIEQLT-RQGN-LYNLYGPTEaTVLITARQLrtgD 477
Cdd:cd05941 186 ptiytRLlqyyEAHFTDPQFARAAAAERLRLM---VSGSAALPVPTLEEWEaITGHtLLERYGMTE-IGMALSNPL---D 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 478 NNR---TLGAPIANSQVLILDEN-FQPVAEQTVGELYIVGPGVCLGYLNNPLQTAEryldlslpngqSLRA---YRTGDM 550
Cdd:cd05941 259 GERrpgTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKE-----------EFTDdgwFKTGDL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 551 AKWTSDG-IELCGR-RDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH----RRILAFLaQPQEEQPGAAREALKA 624
Cdd:cd05941 328 GVVDEDGyYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDpdwgERVVAVV-VLRAGAAALSLEELKE 406
|
490 500 510
....*....|....*....|....*....|....*....
gi 1957676271 625 HAMQFLPDYMQPTA---WTELasmPFASNGKVDRKALLE 660
Cdd:cd05941 407 WAKQRLAPYKRPRRlilVDEL---PRNAMGKVNKKELRK 442
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
252-659 |
9.33e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 139.11 E-value: 9.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 252 GAVYLPLEPSHPLQRQQYILENAGAVLLLHDgEHPLSETMPGLDISGIDISDVNLD------QPLMRQRPDLDAPCMALY 325
Cdd:cd05922 46 GLVFVPLNPTLKESVLRYLVADAGGRIVLAD-AGAADRLRDALPASPDPGTVLDADgiraarASAPAHEVSHEDLALLLY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 326 TSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVpnEDQRRDPLQLVELI 405
Cdd:cd05922 125 TSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVL--TNDGVLDDAFWEDL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 406 RHQRLSHAFLPPALLSIL--------PLDQLQILDHvmTGGDVCEPYVIE--QLTRQGNLYNLYGPTEATVLITARQL-R 474
Cdd:cd05922 203 REHGATGLAGVPSTYAMLtrlgfdpaKLPSLRYLTQ--AGGRLPQETIARlrELLPGAQVYVMYGQTEATRRMTYLPPeR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 475 TGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAerylDLSLPNGqslrAYRTGDMAKWT 554
Cdd:cd05922 281 ILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRR----KEGRGGG----VLHTGDLARRD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 555 SDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH---RRILAFLAQPQEEQPGAAREALKAHamqfL 630
Cdd:cd05922 353 EDGfLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDplgEKLALFVTAPDKIDPKDVLRSLAER----L 428
|
410 420
....*....|....*....|....*....
gi 1957676271 631 PDYMQPTAWTELASMPFASNGKVDRKALL 659
Cdd:cd05922 429 PPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
231-658 |
1.70e-30 |
|
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: 126.43 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 231 VGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLHDGEhplSETMPGLDISGIDISDVNLDQPL 310
Cdd:cd17654 44 IGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNKE---LDNAPLSFTPEHRHFNIRTDECL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 311 mrqrpdldapCMALYTSGTTGHPKGVLLSQA----NLAHFTAWYadyvQLTeQSRVLQFSSLSFDSSLI-DIFPTLLQGA 385
Cdd:cd17654 121 ----------AYVIHTSGTTGTPKIVAVPHKcilpNIQHFRSLF----NIT-SEDILFLTSPLTFDPSVvEIFLSLSSGA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 386 ELIVPNEDQRRDPLQLVE-LIRHQRLSHAFLPPALLSILPlDQLqILDHVMT----------GGdvcEPY----VIEQLT 450
Cdd:cd17654 186 TLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRFG-SQS-IKSTVLSatsslrvlalGG---EPFpslvILSSWR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 451 RQGN---LYNLYGPTEATVLITARQLRTGDNNRTLGAPIANSQVLILDENFQPVAeqtvGELYIVG-PGVCL--GYLNNP 524
Cdd:cd17654 261 GKGNrtrIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSEGT----GQVFLGGlNRVCIldDEVTVP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 525 LQTAeryldlslpngqslraYRTGDMAKWTSDGIELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRIL 604
Cdd:cd17654 337 KGTM----------------RATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1957676271 605 AFLAQPQ---EEQPGAAREALKAHAmqfLPDYMqptawTELASMPFASNGKVDRKAL 658
Cdd:cd17654 401 AFIVGESsssRIHKELQLTLLSSHA---IPDTF-----VQIDKLPLTSHGKVDKSEL 449
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
199-596 |
5.00e-30 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 125.40 E-value: 5.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 199 GTSLSHRQLHAHSRAIQQRLQPLLDQHQGplVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVL 278
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGD--VVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 279 LLHDGEH--PLSE------------TMPGL---DISGIDISDVNLDQPLMRQRPDL----DAPCMALYTSGTTGHPKGVL 337
Cdd:cd05911 86 IFTDPDGleKVKEaakelgpkdkiiVLDDKpdgVLSIEDLLSPTLGEEDEDLPPPLkdgkDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 338 LSQANL--AHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVpneDQRRDPLQLVELIRHQRLSHAFL 415
Cdd:cd05911 166 LSHRNLiaNLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVII---MPKFDSELFLDLIEKYKITFLYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 416 PPALLSIL------PLDQLQILDHVMTGG-----DVCEpyVIEQLTRQGNLYNLYGPTEATVLITarQLRTGDNNR-TLG 483
Cdd:cd05911 243 VPPIAAALakspllDKYDLSSLRVILSGGaplskELQE--LLAKRFPNATIKQGYGMTETGGILT--VNPDGDDKPgSVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 484 APIANSQVLILDENFQPVAEQ-TVGELYIVGPGVCLGYLNNPLQTAEryldLSLPNGQslraYRTGDMAKWTSDG-IELC 561
Cdd:cd05911 319 RLLPNVEAKIVDDDGKDSLGPnEPGEICVRGPQVMKGYYNNPEATKE----TFDEDGW----LHTGDIGYFDEDGyLYIV 390
|
410 420 430
....*....|....*....|....*....|....*
gi 1957676271 562 GRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV 596
Cdd:cd05911 391 DRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVI 425
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
241-658 |
6.32e-30 |
|
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: 125.71 E-value: 6.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 241 LYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLhdgehplsetmpGLDISGIDISdvnldqplmrqrPDlDAP 320
Cdd:cd17647 58 LMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLI------------VIRAAGVVVG------------PD-SNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 321 CMAlYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQ 400
Cdd:cd17647 113 TLS-FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 401 LVELIRHQRLSHAFLPPALLSILPLD---QLQILDHVMTGGDV-----CepYVIEQLTRQGNLYNLYGPTEATVLITARQ 472
Cdd:cd17647 192 LAEWMAKYGATVTHLTPAMGQLLTAQattPFPKLHHAFFVGDIltkrdC--LRLQTLAENVRIVNMYGTTETQRAVSYFE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 473 LRTGDNNRTL----------GAPIANSQVLILDEN--FQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLD------- 533
Cdd:cd17647 270 VPSRSSDPTFlknlkdvmpaGRGMLNVQLLVVNRNdrTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNnwfvepd 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 534 ----LSLPNGQSL---------RAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCL--------------R 585
Cdd:cd17647 350 hwnyLDKDNNEPWrqfwlgprdRLYRTGDLGRYLPNGdCECCGRADDQVKIRGFRIELGEIDTHIsqhplvrenitlvrR 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 586 DSQRYRQVAVVIDPHRRILAFLAQPQEEQPGAA---------------REALKAHAMQFLPDYMQPTAWTELASMPFASN 650
Cdd:cd17647 430 DKDEEPTLVSYIVPRFDKPDDESFAQEDVPKEVstdpivkgligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPN 509
|
....*...
gi 1957676271 651 GKVDRKAL 658
Cdd:cd17647 510 GKVDKPKL 517
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
203-658 |
6.08e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 121.24 E-value: 6.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 203 SHRQLHAHSRAIQQRLQPLLDQHqGPLVvGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLHD 282
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRP-GDRV-ALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 283 gehplsetmpgldisgidisdvnldqplmrqrpdldaPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRV 362
Cdd:cd05934 83 -------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 363 L-QFSSLSFDSSLIDIFPTLLQGAELIVpnedQRR-DPLQLVELIRHQRLSHAFLPPALLSIL------PLDQLQILdHV 434
Cdd:cd05934 126 LtVLPLFHINAQAVSVLAALSVGATLVL----LPRfSASRFWSDVRRYGATVTNYLGAMLSYLlaqppsPDDRAHRL-RA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 435 MTGGDVCEPYVIEQLTRQG-NLYNLYGPTEATVLItarqLRTGDNNR---TLGAPIANSQVLILDENFQPVAEQTVGELY 510
Cdd:cd05934 201 AYGAPNPPELHEEFEERFGvRLLEGYGMTETIVGV----IGPRDEPRrpgSIGRPAPGYEVRIVDDDGQELPAGEPGELV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 511 I---VGPGVCLGYLNNPLQTAERyldlsLPNGQslraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRD 586
Cdd:cd05934 277 IrglRGWGFFKGYYNMPEATAEA-----MRNGW----FHTGDLGYRDADGfFYFVDRKKDMIRRRGENISSAEVERAILR 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957676271 587 SQRYRQVAVVIDPHR----RILAFLAQPQEEQPGAarEALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd05934 348 HPAVREAAVVAVPDEvgedEVKAVVVLRPGETLDP--EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
230-658 |
8.53e-29 |
|
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: 121.00 E-value: 8.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 230 VVGICL---PKCSVLYagiLAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLHDGEhplsetmpgldisgidisdvnl 306
Cdd:cd05971 33 RVGVFLsqgPECAIAH---IAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDGS---------------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 307 dqplmrqrpdlDAPCMALYTSGTTGHPKGVLLsqanlAH-FTAWYADYVQLTEQsrvLQFSSLSFDSSLID--------- 376
Cdd:cd05971 88 -----------DDPALIIYTSGTTGPPKGALH-----AHrVLLGHLPGVQFPFN---LFPRDGDLYWTPADwawigglld 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 377 -IFPTLLQGAELiVPNEDQRRDPLQLVELIRHQRLSHAFLPPALLSIL-----PLDQLQI-LDHVMTGGdvcEP------ 443
Cdd:cd05971 149 vLLPSLYFGVPV-LAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMrqqgeQLKHAQVkLRAIATGG---ESlgeell 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 444 -YVIEQLTRQGNlyNLYGPTEATVLITARQLRTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPG--VCLGY 520
Cdd:cd05971 225 gWAREQFGVEVN--EFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 521 LNNPLQTAERYldlslpNGQSLRayrTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV--I 597
Cdd:cd05971 303 WNNPSATEKKM------AGDWLL---TGDLGRKDSDGyFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVgiP 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1957676271 598 DPHR--RILAFLA-QPQEEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd05971 374 DPIRgeIVKAFVVlNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
246-658 |
9.93e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 122.22 E-value: 9.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 246 LAILGSGAVYlplepsHP----LQRQQ--YILENAGAVLLLHDGEH-----PLSETMP---------GLDISGIDISDVN 305
Cdd:PRK06187 74 FAVPKIGAVL------HPinirLKPEEiaYILNDAEDRVVLVDSEFvpllaAILPQLPtvrtvivegDGPAAPLAPEVGE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 306 LDQPLMRQRPDLDAP-------CMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQfsslsfdsslidIF 378
Cdd:PRK06187 148 YEELLAAASDTFDFPdidendaAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLV------------IV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 379 P------------TLLQGAELIVPnedqRR-DPLQLVELIRHQRLSHAFLPPALLSILpLDQLQI-------LDHVMTGG 438
Cdd:PRK06187 216 PmfhvhawglpylALMAGAKQVIP----RRfDPENLLDLIETERVTFFFAVPTIWQML-LKAPRAyfvdfssLRLVIYGG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 439 DVCEPYVIEQ-LTRQG-NLYNLYGPTEATVLITARQLRTGDNN-----RTLGAPIANSQVLILDE--NFQPVAEQTVGEL 509
Cdd:PRK06187 291 AALPPALLREfKEKFGiDLVQGYGMTETSPVVSVLPPEDQLPGqwtkrRSAGRPLPGVEARIVDDdgDELPPDGGEVGEI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 510 YIVGPGVCLGYLNNPLQTAEryldlSLPNGQslraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQ 588
Cdd:PRK06187 371 IVRGPWLMQGYWNRPEATAE-----TIDGGW----LHTGDVGYIDEDGyLYITDRIKDVIISGGENIYPRELEDALYGHP 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1957676271 589 RYRQVAVVIDPHR----RILAFLAQPQEEQPGAarEALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PRK06187 442 AVAEVAVIGVPDEkwgeRPVAVVVLKPGATLDA--KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
246-603 |
1.15e-26 |
|
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: 114.40 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 246 LAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLhdgehplsetMPGLDISgidisdvnldqplMRQRPDLDAPCMALY 325
Cdd:cd05903 44 LACLRIGAVTNPILPFFREHELAFILRRAKAKVFV----------VPERFRQ-------------FDPAAMPDAVALLLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 326 TSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIF--PTLLqGAELIVpneDQRRDPLQLVE 403
Cdd:cd05903 101 TSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFtlPLLL-GAPVVL---QDIWDPDKALA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 404 LIRHQRLSHAFLPPALLSilpldqlQILDHVMTGGD--------VC-----EPYVIEQLTRQGNLY--NLYGPTE---AT 465
Cdd:cd05903 177 LMREHGVTFMMGATPFLT-------DLLNAVEEAGEplsrlrtfVCggatvPRSLARRAAELLGAKvcSAYGSTEcpgAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 466 VLIT-ARQLRTGdnnRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLslpngqslrA 544
Cdd:cd05903 250 TSITpAPEDRRL---YTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEG---------W 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1957676271 545 YRTGDMAKWTSDG-IELCGRRDNqVKIR-GFRVEPEEIERCLRDSQRYRQVAVVIDPHRRI 603
Cdd:cd05903 318 FRTGDLARLDEDGyLRITGRSKD-IIIRgGENIPVLEVEDLLLGHPGVIEAAVVALPDERL 377
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
319-661 |
1.27e-26 |
|
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: 112.04 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 319 APCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNedqRRDP 398
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLE---RNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 399 LQLVELirHQRLSHAFL-PPALLSIL----PLDQLQILDHVMTGGDVCEPYVIEQLTRQG-NLYNLYGPTEATVLITARQ 472
Cdd:cd17630 78 LAEDLA--PPGVTHVSLvPTQLQRLLdsgqGPAALKSLRAVLLGGAPIPPELLERAADRGiPLYTTYGMTETASQVATKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 473 LrTGDNNRTLGAPIANSQVLILDEnfqpvaeqtvGELYIVGPGVCLGYLNNPLQtaeryldlSLPNGQSLraYRTGDMAK 552
Cdd:cd17630 156 P-DGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLV--------PEFNEDGW--FTTKDLGE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 553 WTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHR----RILAFLaqpqEEQPGAAREALKAHAM 627
Cdd:cd17630 215 LHADGrLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEelgqRPVAVI----VGRGPADPAELRAWLK 290
|
330 340 350
....*....|....*....|....*....|....
gi 1957676271 628 QFLPDYMQPTAWTELASMPFASNGKVDRKALLEL 661
Cdd:cd17630 291 DKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
182-661 |
1.38e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 115.34 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 182 LEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPLVvGICLPKCSVLYAGILAILGSGAVYLPLEPS 261
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERI-AILSQNSLEYIVLLFAIAKVECIAVPLNIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 262 HPLQRQQYILENAGAVLLLHDGEHP-LSETMPGLDISGIDISDVNLDQPLMRQRPDL-----DAPCMALYTSGTTGHPKG 335
Cdd:PRK06839 87 LTENELIFQLKDSGTTVLFVEKTFQnMALSMQKVSYVQRVISITSLKEIEDRKIDNFvekneSASFIICYTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 336 VLLSQANLAHFTAWYADYVQLTEQSRVLqFSSLSFDSSLIDIF--PTLLQGAELIVPNedqRRDPLQLVELIRHQRLSHA 413
Cdd:PRK06839 167 AVLTQENMFWNALNNTFAIDLTMHDRSI-VLLPLFHIGGIGLFafPTLFAGGVIIVPR---KFEPTKALSMIEKHKVTVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 414 FLPPALLSIL---PLDQLQILDHV---MTGGDVCEPYVIEQLTRQGNLYNL-YGPTEA--TVLITARQlrtgDNNR---T 481
Cdd:PRK06839 243 MGVPTIHQALincSKFETTNLQSVrwfYNGGAPCPEELMREFIDRGFLFGQgFGMTETspTVFMLSEE----DARRkvgS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 482 LGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAEryldlSLPNGQslraYRTGDMAKWTSDG-IEL 560
Cdd:PRK06839 319 IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE-----TIQDGW----LCTGDLARVDEDGfVYI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 561 CGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLAQpqeeQPGAA--REALKAHAMQFLPDYM 634
Cdd:PRK06839 390 VGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKwgeiPIAFIVK----KSSSVliEKDVIEHCRLFLAKYK 465
|
490 500
....*....|....*....|....*..
gi 1957676271 635 QPTAWTELASMPFASNGKVDRKALLEL 661
Cdd:PRK06839 466 IPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
192-658 |
1.98e-26 |
|
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: 113.71 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 192 RPALNIAGTSLSHRQLHAHSRAIQQRLQPLLdQHQGPlVVGICLPKCSVLYAGILAILGSGAVYLPLEP-SHPlQRQQYI 270
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLG-VSSGD-RVLLLMLDSPELVQLFLGCLARGAIAVVINPlLHP-DDYAYI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 271 LENAGAVLLLHDGehplsetmpgldisgidisdvnldqplmrqrpdlDAPCMALYTSGTTGHPKGVLLSQANLAHFT-AW 349
Cdd:cd05919 78 ARDCEARLVVTSA----------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdAM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 350 YADYVQLTEQSRVLQFSSLSFDSSLID--IFPtLLQGAELIVpnEDQRRDPLQLVELIRHQRLSHAFLPPAL------LS 421
Cdd:cd05919 124 AREALGLTPGDRVFSSAKMFFGYGLGNslWFP-LAVGASAVL--NPGWPTAERVLATLARFRPTVLYGVPTFyanlldSC 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 422 ILPLDQLQILDHVMTGGDVCEPYVIEQLTRQ--GNLYNLYGPTEAT-VLITAR--QLRTGdnnrTLGAPIANSQVLILDE 496
Cdd:cd05919 201 AGSPDALRSLRLCVSAGEALPRGLGERWMEHfgGPILDGIGATEVGhIFLSNRpgAWRLG----STGRPVPGYEIRLVDE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 497 NFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDlslpngqslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRV 575
Cdd:cd05919 277 EGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNG---------GWYRTGDKFCRDADGwYTHAGRADDMLKVGGQWV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 576 EPEEIERCLRDSQRYRQVAVVIDPHR----RILAF--LAQPQEEQpGAAREALKAHAMQFLPDYMQPTAWTELASMPFAS 649
Cdd:cd05919 348 SPVEVESLIIQHPAVAEAAVVAVPEStglsRLTAFvvLKSPAAPQ-ESLARDIHRHLLERLSAHKVPRRIAFVDELPRTA 426
|
....*....
gi 1957676271 650 NGKVDRKAL 658
Cdd:cd05919 427 TGKLQRFKL 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
179-660 |
2.32e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 114.62 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 179 IERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPL----LDQhqgplvVGICLPKCSVLYAGILAILGSGAV 254
Cdd:PRK07656 8 PELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALgigkGDR------VAIWAPNSPHWVIAALGALKAGAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 255 YLPLEPSHPLQRQQYILENAGA-VLLLHDGEHPLSETM----PGLD-ISGIDISDVNLDQPLMRQRPDLDAPCMA----- 323
Cdd:PRK07656 82 VVPLNTRYTADEAAYILARGDAkALFVLGLFLGVDYSAttrlPALEhVVICETEEDDPHTEKMKTFTDFLAAGDPaerap 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 324 ----------LYTSGTTGHPKGVLLSQAN-LAHFTAWyADYVQLTEQSRVLQfsslsfdsslidIFP------------- 379
Cdd:PRK07656 162 evdpddvadiLFTSGTTGRPKGAMLTHRQlLSNAADW-AEYLGLTEGDRYLA------------ANPffhvfgykagvna 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 380 TLLQGAE-LIVPnedqRRDPLQLVELIRHQRLSHAFLPPALLSILpldqlqiLDHVM-------------TGGDVCEPYV 445
Cdd:PRK07656 229 PLMRGATiLPLP----VFDPDEVFRLIETERITVLPGPPTMYNSL-------LQHPDrsaedlsslrlavTGAASMPVAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 446 IEQLTRQGNLYNL---YGPTEATVLITARQLRTG--DNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGY 520
Cdd:PRK07656 298 LERFESELGVDIVltgYGLSEASGVTTFNRLDDDrkTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 521 LNNPLQTAEryldlslpngqSLRA---YRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV 596
Cdd:PRK07656 378 YDDPEATAA-----------AIDAdgwLHTGDLGRLDEEGyLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 597 IDPHRRI----LAFLAQpqeeQPGAA--REALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLE 660
Cdd:PRK07656 447 GVPDERLgevgKAYVVL----KPGAEltEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
190-660 |
4.15e-25 |
|
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: 110.48 E-value: 4.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 190 AERPALNIAGT--SLSHRQLHAHSRAIQQRLQPLldqHQGP-LVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQR 266
Cdd:cd05926 1 PDAPALVVPGStpALTYADLAELVDDLARQLAAL---GIKKgDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 267 QQYILENAGAVLLLHDGEhPLSETMPGLDISGIDISDVNLDQPLM---------------------RQRPDLDAPCMALY 325
Cdd:cd05926 78 FEFYLADLGSKLVLTPKG-ELGPASRAASKLGLAILELALDVGVLirapsaeslsnlladkknaksEGVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 326 TSGTTGHPKGVLLSQANLA----HFTAWYadyvQLTEQSRVLqfsslsfdsSLIDIF----------PTLLQGAELIVPN 391
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAasatNITNTY----KLTPDDRTL---------VVMPLFhvhglvasllSTLAAGGSVVLPP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 392 ------------------------------EDQRRDPLQLVELIRHQRLSHAFLPPALLSilpldQLQILDHVmtggdvc 441
Cdd:cd05926 224 rfsastfwpdvrdynatwytavptihqillNRPEPNPESPPPKLRFIRSCSASLPPAVLE-----ALEATFGA------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 442 ePyVIEQltrqgnlynlYGPTEATVLITARQLRTGDNNR-TLGAPiANSQVLILDENFQPVAEQTVGELYIVGPGVCLGY 520
Cdd:cd05926 292 -P-VLEA----------YGMTEAAHQMTSNPLPPGPRKPgSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 521 LNNPLQTAERyldlSLPNGQslraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDP 599
Cdd:cd05926 359 LNNPEANAEA----AFKDGW----FRTGDLGYLDADGyLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVP 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1957676271 600 H----RRILAFLaQPQEEQPgAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLE 660
Cdd:cd05926 431 DekygEEVAAAV-VLREGAS-VTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
190-658 |
6.33e-25 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 110.97 E-value: 6.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 190 AERPALNIAG-----TSLSHRQLHAHSRAIQQRLQplldqHQGplV-----VGICLPKCSVLYAGILAILGSGAVYLPLE 259
Cdd:COG0365 23 GDKVALIWEGedgeeRTLTYAELRREVNRFANALR-----ALG--VkkgdrVAIYLPNIPEAVIAMLACARIGAVHSPVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 260 P---SHPLQrqqYILENAGAVLLL-HDG------EHPLSETM-------PGL------DISGIDIS---DVNLDQPLMRQ 313
Cdd:COG0365 96 PgfgAEALA---DRIEDAEAKVLItADGglrggkVIDLKEKVdealeelPSLehvivvGRTGADVPmegDLDWDELLAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 314 RPDLDA-------PCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQ-LTEQsrvlqfsslsfdssliDIF------- 378
Cdd:COG0365 173 SAEFEPeptdaddPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLdLKPG----------------DVFwctadig 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 379 ----------PTLLQGAELIV----PNedqRRDPLQLVELIRHQRLSHAFLPPALLSIL------PLDQLQI--LDHVMT 436
Cdd:COG0365 237 watghsyivyGPLLNGATVVLyegrPD---FPDPGRLWELIEKYGVTVFFTAPTAIRALmkagdePLKKYDLssLRLLGS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 437 GGDVCEPYVIEQLTRQGN--LYNLYGPTEATVLITA----RQLRTGdnnrTLGAPIANSQVLILDENFQPVAEQTVGELY 510
Cdd:COG0365 314 AGEPLNPEVWEWWYEAVGvpIVDGWGQTETGGIFISnlpgLPVKPG----SMGKPVPGYDVAVVDEDGNPVPPGEEGELV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 511 IVG--PGVCLGYLNNPLQTAERYLDlSLPNgqslrAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLrds 587
Cdd:COG0365 390 IKGpwPGMFRGYWNDPERYRETYFG-RFPG-----WYRTGDGARRDEDGyFWILGRSDDVINVSGHRIGTAEIESAL--- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 588 QRYRQV--AVVI---DPHR--RILAF--LAQPQEEQPGAAREaLKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:COG0365 461 VSHPAVaeAAVVgvpDEIRgqVVKAFvvLKPGVEPSDELAKE-LQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
245-659 |
3.17e-24 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 108.22 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 245 ILAILGS---GAVYLPLEPSHPLQRQQYILENAGAVLLLHDGE-HPLSETMPGLDISG---IDISDVNLDQPLMRQRPDL 317
Cdd:cd05959 68 PTAFLGAiraGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGElAPVLAAALTKSEHTlvvLIVSGGAGPEAGALLLAEL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 318 ---------------DAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYV-QLTEQSRVLQFSSLSFDSSLID--IFP 379
Cdd:cd05959 148 vaaeaeqlkpaathaDDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVlGIREDDVCFSAAKLFFAYGLGNslTFP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 380 TLLQGAELIVPnedQRRDPLQLVELIRHQRLSHAFLPPALLSILPL-------DQLQILDHVMTGgdvcEPYVIEQLTRQ 452
Cdd:cd05959 228 LSVGATTVLMP---ERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAapnlpsrDLSSLRLCVSAG----EALPAEVGERW 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 453 GNLYNL-----YGPTEATVLI---TARQLRTGdnnrTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNP 524
Cdd:cd05959 301 KARFGLdildgIGSTEMLHIFlsnRPGRVRYG----TTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNR 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 525 LQTAERYLdlslpnGQslrAYRTGDMAKWTSDGI-ELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV--IDPHR 601
Cdd:cd05959 377 DKTRDTFQ------GE---WTRTGDKYVRDDDGFyTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVgvEDEDG 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1957676271 602 RI--LAFLA-QPQEEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALL 659
Cdd:cd05959 448 LTkpKAFVVlRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
200-632 |
5.27e-24 |
|
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: 106.53 E-value: 5.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 200 TSLSHRQLHAHSRAIQQRLQPLLDQHQGplVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLL 279
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGD--RVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 280 LhdGEHPlsetmpgldisgidisdvnldqplmrqrpdlDAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQ 359
Cdd:cd05907 82 F--VEDP-------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 360 SRVL----------QFsslsfdsslIDIFPTLLQGAELIVPNED-------QRRDPLQLVELIR-----HQRLSHAFLPP 417
Cdd:cd05907 129 DRHLsflplahvfeRR---------AGLYVPLLAGARIYFASSAetllddlSEVRPTVFLAVPRvwekvYAAIKVKAVPG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 418 ALLSILPLDQLQILDHVMTGGDVCEPYVIEQLTRQG-NLYNLYGPTEATVLITARQLRTGDNNrTLGAPIANSQVLILDE 496
Cdd:cd05907 200 LKRKLFDLAVGGRLRFAASGGAPLPAELLHFFRALGiPVYEGYGLTETSAVVTLNPPGDNRIG-TVGKPLPGVEVRIADD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 497 nfqpvaeqtvGELYIVGPGVCLGYLNNPLQTAERYldlsLPNGqslrAYRTGDMAKWTSDG-IELCGR-RDNQVKIRGFR 574
Cdd:cd05907 279 ----------GEILVRGPNVMLGYYKNPEATAEAL----DADG----WLHTGDLGEIDEDGfLHITGRkKDLIITSGGKN 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1957676271 575 VEPEEIERCLRDSqRYRQVAVVIDPHRRILAFLAQPQEEqpgAAREALKAHAMQFLPD 632
Cdd:cd05907 341 ISPEPIENALKAS-PLISQAVVIGDGRPFLVALIVPDPE---ALEAWAEEHGIAYTDV 394
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
199-658 |
1.38e-23 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 105.88 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 199 GTSLSHRQLHAHSRAIQQRLQPLLDQHQGplvVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGA-- 276
Cdd:cd05909 5 GTSLTYRKLLTGAIALARKLAKMTKEGEN---VGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIkt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 277 -----VLLLHDGEHPL--SETMPGL--------DISGID---------ISDVNLDQPLMRQRPDLDAPCMALYTSGTTGH 332
Cdd:cd05909 82 vltskQFIEKLKLHHLfdVEYDARIvyledlraKISKADkckaflagkFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 333 PKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSL-SFDSSLIDIFPTLLQGAELIV-PNedqrrdPL---QLVELIRH 407
Cdd:cd05909 162 PKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfHSFGLTGCLWLPLLSGIKVVFhPN------PLdykKIPELIYD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 408 QRLSHAFLPPALLSIL-----PlDQLQILDHVMTGGDVCEPYVIEQ-LTRQG-NLYNLYGPTEATVLITARQLRTGDNNR 480
Cdd:cd05909 236 KKATILLGTPTFLRGYaraahP-EDFSSLRLVVAGAEKLKDTLRQEfQEKFGiRILEGYGTTECSPVISVNTPQSPNKEG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 481 TLGAPIANSQVLILD-ENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDlslpngqslRAYRTGDMAKWTSDG-I 558
Cdd:cd05909 315 TVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGD---------GWYDTGDIGKIDGEGfL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 559 ELCGRRDNQVKIRGFRVEPEEIER---CLRDSQryRQVAVVIDPHRR---ILAFLAQPQEEQPGAAREALKAHAmqfLPD 632
Cdd:cd05909 386 TITGRLSRFAKIAGEMVSLEAIEDilsEILPED--NEVAVVSVPDGRkgeKIVLLTTTTDTDPSSLNDILKNAG---ISN 460
|
490 500
....*....|....*....|....*.
gi 1957676271 633 YMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd05909 461 LAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
185-658 |
1.54e-23 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 105.67 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 185 RFIQSAERPALNIA----GTSLSHRQLHAHSRAIQQRLQPLLDQHQGPLVVgiCLPKCSVLYAGILAILGSGAVYLPLEP 260
Cdd:cd05923 8 RRAASRAPDACAIAdparGLRLTYSELRARIEAVAARLHARGLRPGQRVAV--VLPNSVEAVIALLALHRLGAVPALINP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 261 SHPLQRQQYILENAGAVLLLHdgeHPLSETMPGLDISGIDI----SDVNL-----DQPLMRQRP-DLDAPCMALYTSGTT 330
Cdd:cd05923 86 RLKAAELAELIERGEMTAAVI---AVDAQVMDAIFQSGVRVlalsDLVGLgepesAGPLIEDPPrEPEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 331 GHPKGVLLSQANLAHFTAWYADYVQLT--EQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQrrDPLQLVELIRHQ 408
Cdd:cd05923 163 GLPKGAVIPQRAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADALKLIEQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 409 RLSHAFLPPALLSIL-------PLDqLQILDHVMTGGDVCEPYVIEQLTR--QGNLYNLYGPTEATVLITARQLRTGdnn 479
Cdd:cd05923 241 RVTSLFATPTHLDALaaaaefaGLK-LSSLRHVTFAGATMPDAVLERVNQhlPGEKVNIYGTTEAMNSLYMRDARTG--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 480 rTLGAPIANSQVLIL------DENFQPVAEqtvGELYIVGPG--VCLGYLNNPLQTAERYLDlslpngqslRAYRTGDMA 551
Cdd:cd05923 317 -TEMRPGFFSEVRIVriggspDEALANGEE---GELIVAAAAdaAFTGYLNQPEATAKKLQD---------GWYRTGDVG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 552 KWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLAqPQEEQPGAarEALKaha 626
Cdd:cd05923 384 YVDPSGdVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwgqsVTACVV-PREGTLSA--DELD--- 457
|
490 500 510
....*....|....*....|....*....|....*..
gi 1957676271 627 mQF-----LPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd05923 458 -QFcraseLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
246-658 |
2.07e-23 |
|
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: 105.79 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 246 LAILGSGAVYLPLEPSHPLQRQQYILENAGA-VLLLHDGEHPLSETMPG------------LDISGIDISDVNL---DQP 309
Cdd:cd12119 68 YAVPGMGAVLHTINPRLFPEQIAYIINHAEDrVVFVDRDFLPLLEAIAPrlptvehvvvmtDDAAMPEPAGVGVlayEEL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 310 LMRQR-----PDLD--APCMALYTSGTTGHPKGVLLSQANLAH--FTAWYADYVQLTEQSRVLqfsslsfdsSLIDIF-- 378
Cdd:cd12119 148 LAAESpeydwPDFDenTAAAICYTSGTTGNPKGVVYSHRSLVLhaMAALLTDGLGLSESDVVL---------PVVPMFhv 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 379 -----P--TLLQGAELIVPneDQRRDPLQLVELIRHQRLSHAFLPPALLSIL-------PLDqLQILDHVMTGGDVCEPY 444
Cdd:cd12119 219 nawglPyaAAMVGAKLVLP--GPYLDPASLAELIEREGVTFAAGVPTVWQGLldhleanGRD-LSSLRRVVIGGSAVPRS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 445 VIEQLTRQG-NLYNLYGPTEATVLITARQLRTGDNNRTL----------GAPIANSQVLILDE--NFQPVAEQTVGELYI 511
Cdd:cd12119 296 LIEAFEERGvRVIHAWGMTETSPLGTVARPPSEHSNLSEdeqlalrakqGRPVPGVELRIVDDdgRELPWDGKAVGELQV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 512 VGPGVCLGYLNNPLQTAERYLDLSLpngqslrayRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRY 590
Cdd:cd12119 376 RGPWVTKSYYKNDEESEALTEDGWL---------RTGDVATIDEDGyLTITDRSKDVIKSGGEWISSVELENAIMAHPAV 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957676271 591 RQVAVVIDPH----RRILAFLAQPQEEQPGAarEALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd12119 447 AEAAVIGVPHpkwgERPLAVVVLKEGATVTA--EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
202-658 |
4.61e-22 |
|
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: 101.59 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 202 LSHRQLHAHSRAI-----QQRLQP------LLDQHQGPLVVgicLPKCsvLYAGIL-AILGSGAVYLplEPSHPLQRQQY 269
Cdd:cd05906 40 QSYQDLLEDARRLaaglrQLGLRPgdsvilQFDDNEDFIPA---FWAC--VLAGFVpAPLTVPPTYD--EPNARLRKLRH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 270 ILENAGAVLLLHDGE-----HPLSETMPGLDISGIDIS---DVNLDQPLMRQRPDldAPCMALYTSGTTGHPKGVLLSQA 341
Cdd:cd05906 113 IWQLLGSPVVLTDAElvaefAGLETLSGLPGIRVLSIEellDTAADHDLPQSRPD--DLALLMLTSGSTGFPKAVPLTHR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 342 NLAHFTAWYADYVQLTEQSRVLQ--FSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVELIRHQRLSHAFLPPAL 419
Cdd:cd05906 191 NILARSAGKIQHNGLTPQDVFLNwvPLDHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNFA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 420 LSILpLDQLQILDH----------VMTGGDVCEPYVIEQLTRQGNLYNL--------YGPTE-ATVLITARQLRTGDNNR 480
Cdd:cd05906 271 FALL-NDLLEEIEDgtwdlsslryLVNAGEAVVAKTIRRLLRLLEPYGLppdairpaFGMTEtCSGVIYSRSFPTYDHSQ 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 481 T-----LGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDlslpNGQslraYRTGDMAkWTS 555
Cdd:cd05906 350 AlefvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTE----DGW----FRTGDLG-FLD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 556 DG-IELCGRRDNQVKIRGFRVEPEEIERCL----------------RDSQRYR-QVAVVIDPhrrilaflAQPQEEQPGA 617
Cdd:cd05906 421 NGnLTITGRTKDTIIVNGVNYYSHEIEAAVeevpgvepsftaafavRDPGAETeELAIFFVP--------EYDLQDALSE 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1957676271 618 AREALKAHAMQFL---PDYMQPTAWTElasMPFASNGKVDRKAL 658
Cdd:cd05906 493 TLRAIRSVVSREVgvsPAYLIPLPKEE---IPKTSLGKIQRSKL 533
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
190-658 |
6.73e-22 |
|
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: 100.48 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 190 AERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPLVVGicLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQY 269
Cdd:cd05920 29 PDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQ--LPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 270 ILENAGAVLLLHDGEHplsetmpgldiSGIDisdvnlDQPLMRQ-RPDLDAPCMALYTSGTTGHPKGVLLSQANLAHFTA 348
Cdd:cd05920 107 FCAHAEAVAYIVPDRH-----------AGFD------HRALARElAESIPEVALFLLSGGTTGTPKLIPRTHNDYAYNVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 349 WYADYVQLTEQSRVLQFSSLSFDSSLI--DIFPTLLQGAELIVPnedQRRDPLQLVELIRHQRLSHAFLPPALLS----- 421
Cdd:cd05920 170 ASAEVCGLDQDTVYLAVLPAAHNFPLAcpGVLGTLLAGGRVVLA---PDPSPDAAFPLIEREGVTVTALVPALVSlwlda 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 422 -ILPLDQLQILDHVMTGGDVCEPYVIEQL--TRQGNLYNLYGPTEATVLITarqlRTGDNN----RTLGAPI-ANSQVLI 493
Cdd:cd05920 247 aASRRADLSSLRLLQVGGARLSPALARRVppVLGCTLQQVFGMAEGLLNYT----RLDDPDeviiHTQGRPMsPDDEIRV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 494 LDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYldlsLPNGqslrAYRTGDMAKWTSDG-IELCGRRDNQVKIRG 572
Cdd:cd05920 323 VDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF----TPDG----FYRTGDLVRRTPDGyLVVEGRIKDQINRGG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 573 FRVEPEEIERCLRDSQRYRQVAVVIDPH----RRILAFLAqPQEEQPGAAreALKAHAMQF-LPDYMQPTAWTELASMPF 647
Cdd:cd05920 395 EKIAAEEVENLLLRHPAVHDAAVVAMPDellgERSCAFVV-LRDPPPSAA--QLRRFLRERgLAAYKLPDRIEFVDSLPL 471
|
490
....*....|.
gi 1957676271 648 ASNGKVDRKAL 658
Cdd:cd05920 472 TAVGKIDKKAL 482
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
230-658 |
1.87e-21 |
|
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: 98.56 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 230 VVGICLPKCSVLYAGILAILGSGAVYLP----LEPSHPLQRqqyiLENAGAVLLLHDgehplsetmpgldisgidisdvn 305
Cdd:cd05972 27 RVAVLLPRVPELWAVILAVIKLGAVYVPlttlLGPKDIEYR----LEAAGAKAIVTD----------------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 306 ldqplmrqrpdLDAPCMALYTSGTTGHPKGVLLS-QANLAHFTawYADYVQLTEQSRVLQFSSLSFDSSLI--DIFPTLL 382
Cdd:cd05972 80 -----------AEDPALIYFTSGTTGLPKGVLHThSYPLGHIP--TAAYWLGLRPDDIHWNIADPGWAKGAwsSFFGPWL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 383 QGAELIVPNEDqRRDPLQLVELIRHQRLSHAFLPP-ALLSILPLDQLQI----LDHVMTGGDVCEPYVIEQLTRQGNL-- 455
Cdd:cd05972 147 LGATVFVYEGP-RFDAERILELLERYGVTSFCGPPtAYRMLIKQDLSSYkfshLRLVVSAGEPLNPEVIEWWRAATGLpi 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 456 YNLYGPTEATVLIT---ARQLRTGdnnrTLGAPIANSQVLILDENFQPVAEQTVGELYI--VGPGVCLGYLNNPLQTAER 530
Cdd:cd05972 226 RDGYGQTETGLTVGnfpDMPVKPG----SMGRPTPGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEAS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 531 YLDlslpngqslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV--IDPHRR--ILA 605
Cdd:cd05972 302 IRG---------DYYLTGDRAYRDEDGyFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVgsPDPVRGevVKA 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1957676271 606 F--LAQPQEEQPGAAREaLKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd05972 373 FvvLTSGYEPSEELAEE-LQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
191-658 |
2.28e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 99.19 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSRAIQQRLQPLlDQHQGPlVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYI 270
Cdd:PRK06145 17 DRAALVYRDQEISYAEFHQRILQAAGMLHAR-GIGQGD-VVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 271 LENAGAVLLLHDGEHplsETMPGLDISGIdISDVNLDQPLMR-QRPDLDAPCMA----------LYTSGTTGHPKGVLLS 339
Cdd:PRK06145 95 LGDAGAKLLLVDEEF---DAIVALETPKI-VIDAAAQADSRRlAQGGLEIPPQAavaptdlvrlMYTSGTTDRPKGVMHS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 340 QANLAHFTAWYADYVQLTEQSRVLqFSSLSFDSSLIDI--FPTLLQGAELIVPNEdqrRDPLQLVELIRHQRLSHAFLPP 417
Cdd:PRK06145 171 YGNLHWKSIDHVIALGLTASERLL-VVGPLYHVGAFDLpgIAVLWVGGTLRIHRE---FDPEAVLAAIERHRLTCAWMAP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 418 ALLS-ILPLDQ-----LQILDHVMTGGDVCEPYVIEQLTR---QGNLYNLYGPTEA----TVLITARQLrtgDNNRTLGA 484
Cdd:PRK06145 247 VMLSrVLTVPDrdrfdLDSLAWCIGGGEKTPESRIRDFTRvftRARYIDAYGLTETcsgdTLMEAGREI---EKIGSTGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 485 PIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDlslpngqslRAYRTGDMAKWTSDG-IELCGR 563
Cdd:PRK06145 324 ALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYG---------DWFRSGDVGYLDEEGfLYLTDR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 564 RDNQVKIRGFRVEPEEIERCLRDSQRYRQVAV--VIDPH--RRILAFLAQpqeeQPGAA--REALKAHAMQFLPDYMQPT 637
Cdd:PRK06145 395 KKDMIISGGENIASSEVERVIYELPEVAEAAVigVHDDRwgERITAVVVL----NPGATltLEALDRHCRQRLASFKVPR 470
|
490 500
....*....|....*....|.
gi 1957676271 638 AWTELASMPFASNGKVDRKAL 658
Cdd:PRK06145 471 QLKVRDELPRNPSGKVLKRVL 491
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
231-658 |
2.31e-21 |
|
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: 98.34 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 231 VGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGA-VLLLHdgehplsetmpgldisgidisdvnldqP 309
Cdd:cd05969 28 VFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAkVLITT---------------------------E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 310 LMRQRPDLDAPCMALYTSGTTGHPKGVLLSQ-ANLAHF--TAWYADyvqLTEQSRVLQFSSLS-FDSSLIDIFPTLLQGA 385
Cdd:cd05969 81 ELYERTDPEDPTLLHYTSGTTGTPKGVLHVHdAMIFYYftGKYVLD---LHPDDIYWCTADPGwVTGTVYGIWAPWLNGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 386 ELIVpnEDQRRDPLQLVELIRHQRLSHAFLPPALLSIL------PLDQ--LQILDHVMTGGDVCEPYVIeqltRQG-NLY 456
Cdd:cd05969 158 TNVV--YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLmkegdeLARKydLSSLRFIHSVGEPLNPEAI----RWGmEVF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 457 NL-----YGPTEATVLITARQLRTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVG--PGVCLGYLNNPlqtaE 529
Cdd:cd05969 232 GVpihdtWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDE----E 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 530 RYlDLSLPNGQslraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV--IDPHR--RIL 604
Cdd:cd05969 308 RY-KNSFIDGW----YLTGDLAYRDEDGyFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIgkPDPLRgeIIK 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1957676271 605 AFLAQPQEEQPGAA-REALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd05969 383 AFISLKEGFEPSDElKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
319-655 |
5.59e-21 |
|
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: 95.16 E-value: 5.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 319 APCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVpneDQRRDP 398
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 399 LQLVELIRHQRLSHAFLPPALLSIL-----PLDQLQIldhVMTGGDVCEPYVIEQLTRQ---GNLYNLYGPTEATvLITA 470
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALartlePESKIKS---IFSSGQKLFESTKKKLKNIfpkANLIEFYGTSELS-FITY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 471 RQLRTGDNNRTLGAPIANSQVLILDEnfqpvAEQTVGELYIVGPGVCLGYLNNPLQTAERYldlslpngqslraYRTGDM 550
Cdd:cd17633 154 NFNQESRPPNSVGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRGGFSNPDGW-------------MSVGDI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 551 AKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR---ILAFLAqpqeEQPGAAREALKAHA 626
Cdd:cd17633 216 GYVDEEGyLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARfgeIAVALY----SGDKLTYKQLKRFL 291
|
330 340
....*....|....*....|....*....
gi 1957676271 627 MQFLPDYMQPTAWTELASMPFASNGKVDR 655
Cdd:cd17633 292 KQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
319-599 |
5.74e-21 |
|
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: 95.45 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 319 APCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQ-GAELIVPnedqRRD 397
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAgGTNVFVR----RVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 398 PLQLVELIRHQRLSHAFL-PPALLSILPLDQLQILD----HVMTGGDVCEPYVIEQLTRQGNLYNLYGPTEATVLITARQ 472
Cdd:cd17636 77 AEEVLELIEAERCTHAFLlPPTIDQIVELNADGLYDlsslRSSPAAPEWNDMATVDTSPWGRKPGGYGQTEVMGLATFAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 473 LrTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDlslpngqslRAYRTGDMAK 552
Cdd:cd17636 157 L-GGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG---------GWHHTNDLGR 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1957676271 553 WTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAV--VIDP 599
Cdd:cd17636 227 REPDGsLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVigVPDP 276
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
252-667 |
8.17e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 97.18 E-value: 8.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 252 GAVYLPLEPSHPLQRQQYILENAGAVLLLHDgEHPLSETMPGLDISGIdISDVNLDQPLMRQRPDLDAPCMALYTSGTTG 331
Cdd:PRK09088 71 GAIYVPLNWRLSASELDALLQDAEPRLLLGD-DAVAAGRTDVEDLAAF-IASADALEPADTPSIPPERVSLILFTSGTSG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 332 HPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLI-DIFPTLLQGAELIVPN--EDQRR-----DPL---- 399
Cdd:PRK09088 149 QPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLItSVRPVLAVGGSILVSNgfEPKRTlgrlgDPAlgit 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 400 ------QLVELIRHQRlshAFLPPALLSilpldqlqiLDHVMTGGdvcEPYVIEQLT---RQG-NLYNLYGPTEA-TVL- 467
Cdd:PRK09088 229 hyfcvpQMAQAFRAQP---GFDAAALRH---------LTALFTGG---APHAAEDILgwlDDGiPMVDGFGMSEAgTVFg 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 468 ITARQLRTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYldlslpNGQSLraYRT 547
Cdd:PRK09088 294 MSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGW--FRT 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 548 GDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV--IDPHRRILAFLAQPQEEQPGAAREALKA 624
Cdd:PRK09088 366 GDIARRDADGfFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVgmADAQWGEVGYLAIVPADGAPLDLERIRS 445
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1957676271 625 HAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLELPVNVTE 667
Cdd:PRK09088 446 HLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGRK 488
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
246-614 |
8.21e-21 |
|
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: 97.04 E-value: 8.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 246 LAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLhdgehplsetmpgLDISGIDISDVnldqplmrqrpdldapcmaLY 325
Cdd:cd17640 48 QGIMALGAVDVVRGSDSSVEELLYILNHSESVALV-------------VENDSDDLATI-------------------IY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 326 TSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQfsslsfdsslidIFPT------------LLQGAELI----- 388
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLS------------ILPIwhsyersaeyfiFACGCSQAytsir 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 389 -VPNEDQRRDPLQLV--------------ELIRHQRLSHAFLPPALLSIlpldqlQILDHVMTGGDVCEPYVIEQLTRQG 453
Cdd:cd17640 164 tLKDDLKRVKPHYIVsvprlweslysgiqKQVSKSSPIKQFLFLFFLSG------GIFKFGISGGGALPPHVDTFFEAIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 454 -NLYNLYGPTEATVLITARqlRTGDNNR-TLGAPIANSQVLILDEN---FQPVAEQtvGELYIVGPGVCLGYLNNPLQTA 528
Cdd:cd17640 238 iEVLNGYGLTETSPVVSAR--RLKCNVRgSVGRPLPGTEIKIVDPEgnvVLPPGEK--GIVWVRGPQVMKGYYKNPEATS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 529 ErYLDlslPNGQslraYRTGDMAKWTSDG-IELCGR-RDNQVKIRGFRVEPEEIERCLRDSqRYRQVAVVIDPHRRILAF 606
Cdd:cd17640 314 K-VLD---SDGW----FNTGDLGWLTCGGeLVLTGRaKDTIVLSNGENVEPQPIEEALMRS-PFIEQIMVVGQDQKRLGA 384
|
....*...
gi 1957676271 607 LAQPQEEQ 614
Cdd:cd17640 385 LIVPNFEE 392
|
|
| MupV_like_SDR_e |
cd05263 |
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ... |
783-1042 |
1.47e-20 |
|
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187573 [Multi-domain] Cd Length: 293 Bit Score: 93.59 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGAsEVACLVRDGGGQSAAQRFAQALREnrlehldLSRVRVYVADITRPQLGLSEDVYQR 862
Cdd:cd05263 1 VFVTGGTGFLGRHLVKRLLENGF-KVLVLVRSESLGEAHERIEEAGLE-------ADRVRVLEGDLTQPNLGLSAAASRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 863 LDREFGALVHNAANVNHVLDYESLARDNVEPIFECLRLCEGRSKKIFNFVSTLSASSTISDDGRVLELpaaqTPPIYIKN 942
Cdd:cd05263 73 LAGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTAYVAGNREGNIRETEL----NPGQNFKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 943 GYNLSKWVGERILERArvrGVRVNL--YRPGNISFNSLTGvcqpHKNR---LMLMLKGSIQLGQVPEFALN----FDLMP 1013
Cdd:cd05263 149 PYEQSKAEAEQLVRAA---ATQIPLtvYRPSIVVGDSKTG----RIEKidgLYELLNLLAKLGRWLPMPGNkgarLNLVP 221
|
250 260
....*....|....*....|....*....
gi 1957676271 1014 VDFLARFIAFHASRYQAEKAVFNLHNPEP 1042
Cdd:cd05263 222 VDYVADAIVYLSKKPEANGQIFHLTDPTP 250
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
177-670 |
1.47e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 97.03 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 177 PMIERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLlDQHQGPLVvGICLPKCSVLYAGILAILGSGAVYL 256
Cdd:PRK06710 25 PLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKL-GVEKGDRV-AIMLPNCPQAVIGYYGTLLAGGIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 257 PLEPSHPLQRQQYILENAGA-VLLLHDGEHP-LSETMPGLDISGIDISDV--------NLDQPLM-RQRPDL-------- 317
Cdd:PRK06710 103 QTNPLYTERELEYQLHDSGAkVILCLDLVFPrVTNVQSATKIEHVIVTRIadflpfpkNLLYPFVqKKQSNLvvkvsese 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 318 ----------------DAPC-----MAL--YTSGTTGHPKGVLLSQANLAHFT----AWYADYVQLTEQSR-VLQFSSLS 369
Cdd:PRK06710 183 tihlwnsvekevntgvEVPCdpendLALlqYTGGTTGFPKGVMLTHKNLVSNTlmgvQWLYNCKEGEEVVLgVLPFFHVY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 370 FDSSLIDIfpTLLQGAELI-VPNEDQRrdplQLVELIRHQRLSHAFLPP----ALLSILPLDQLQI--LDHVMTGGDVCE 442
Cdd:PRK06710 263 GMTAVMNL--SIMQGYKMVlIPKFDMK----MVFEAIKKHKVTLFPGAPtiyiALLNSPLLKEYDIssIRACISGSAPLP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 443 PYVIEQLTR--QGNLYNLYGPTEATVLITARQLRTGDNNRTLGAPIANSQVLILD-ENFQPVAEQTVGELYIVGPGVCLG 519
Cdd:PRK06710 337 VEVQEKFETvtGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 520 YLNNPLQTAERYLDLSLpngqslrayRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAV--V 596
Cdd:PRK06710 417 YWNKPEETAAVLQDGWL---------HTGDVGYMDEDGfFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTigV 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957676271 597 IDPHR--RILAFLAQPQEEQpgAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLELPVNVTENSQ 670
Cdd:PRK06710 488 PDPYRgeTVKAFVVLKEGTE--CSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNEDEQ 561
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
173-661 |
4.44e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 95.49 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 173 LAQIPMIERLEQRFIQSAERPALNIAGTSLSHRQLHAHSraiqQRLQPLLDQH---QGPLVvGICLPKCSVLYAGILAIL 249
Cdd:PRK06178 30 HGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELS----DRFAALLRQRgvgAGDRV-AVFLPNCPQFHIVFFGIL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 250 GSGAVYLPLEPSHPLQRQQYILENAGA-VLLLHD----------GEHPLSE--------------TMP---GLDISGIDI 301
Cdd:PRK06178 105 KLGAVHVPVSPLFREHELSYELNDAGAeVLLALDqlapvveqvrAETSLRHvivtsladvlpaepTLPlpdSLRAPRLAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 302 SDV--------NLDQPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSS 373
Cdd:PRK06178 185 AGAidllpalrACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 374 LID---IFPtLLQGAELIVPNedqRRDPLQLVELIRHQRLSHAFLPpallsilpLDQ--------------LQILDHVM- 435
Cdd:PRK06178 265 GENfglLFP-LFSGATLVLLA---RWDAVAFMAAVERYRVTRTVML--------VDNavelmdhprfaeydLSSLRQVRv 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 436 ------------------TGGDVCEPYvieqltrqgnlynlYGPTEATvliTARQLRTG--DNNRTL-------GAPIAN 488
Cdd:PRK06178 333 vsfvkklnpdyrqrwralTGSVLAEAA--------------WGMTETH---TCDTFTAGfqDDDFDLlsqpvfvGLPVPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 489 SQVLILDenFQ-----PVAEQtvGELYIVGPGVCLGYLNNPLQTAEryldlSLPNGQslraYRTGDMAKWTSDG-IELCG 562
Cdd:PRK06178 396 TEFKICD--FEtgellPLGAE--GEIVVRTPSLLKGYWNKPEATAE-----ALRDGW----LHTGDIGKIDEQGfLHYLG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 563 RRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLaQPQEEQPGAArEALKAHAMQFLPDYMQPTA 638
Cdd:PRK06178 463 RRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDkgqvPVAFV-QLKPGADLTA-AALQAWCRENMAVYKVPEI 540
|
570 580
....*....|....*....|...
gi 1957676271 639 WTeLASMPFASNGKVDRKALLEL 661
Cdd:PRK06178 541 RI-VDALPMTATGKVRKQDLQAL 562
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
324-653 |
4.73e-20 |
|
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: 92.56 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 324 LYTSGTTGHPKGVLLS-QANLAHFTAWyADYVQLTEQSRVLqfsslsfdssLIDIF-----------PTLLQGAElIVPn 391
Cdd:cd17638 6 MFTSGTTGRSKGVMCAhRQTLRAAAAW-ADCADLTEDDRYL----------IINPFfhtfgykagivACLLTGAT-VVP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 392 eDQRRDPLQLVELIRHQRLSHAFLPPAL-LSIL-----PLDQLQILDHVMTGGDVCEPYVIEQLTRQGNLYNL---YGPT 462
Cdd:cd17638 73 -VAVFDVDAILEAIERERITVLPGPPTLfQSLLdhpgrKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVltaYGLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 463 EAtvlITARQLRTGDN----NRTLGAPIANSQVLILDEnfqpvaeqtvGELYIVGPGVCLGYLNNPLQTAEryldlslpn 538
Cdd:cd17638 152 EA---GVATMCRPGDDaetvATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAE--------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 539 gqSLRA---YRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRI----LAFLAqp 610
Cdd:cd17638 210 --AIDAdgwLHTGDVGELDERGyLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMgevgKAFVV-- 285
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1957676271 611 QEEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKV 653
Cdd:cd17638 286 ARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
201-626 |
1.76e-19 |
|
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: 93.46 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 201 SLSHRQLHAHSRAIQQRLQ--------PLLDQHQGPLVVgICLPKCsvLYAGILAIlgsgAVYLPlEPSHPLQRQQYILE 272
Cdd:cd05931 24 TLTYAELDRRARAIAARLQavgkpgdrVLLLAPPGLDFV-AAFLGC--LYAGAIAV----PLPPP-TPGRHAERLAAILA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 273 NAGAVLLL-----HDGEHPLSETMPGLD---ISGIDISDVNLDQPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQANLA 344
Cdd:cd05931 96 DAGPRVVLttaaaLAAVRAFAASRPAAGtprLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 345 H-----FTAWyadyvQLTEQSRV-----------LQFSslsfdsslidIFPTLLQGAE--LIVPNEDQRRdPLQLVELIR 406
Cdd:cd05931 176 AnvrqiRRAY-----GLDPGDVVvswlplyhdmgLIGG----------LLTPLYSGGPsvLMSPAAFLRR-PLRWLRLIS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 407 HQRLSHAFLPP---ALL-------SILPLDqLQILDHVMTGGDVCEPYVIEQLTRQGNLYNL--------YGPTEATVLI 468
Cdd:cd05931 240 RYRATISAAPNfayDLCvrrvrdeDLEGLD-LSSWRVALNGAEPVRPATLRRFAEAFAPFGFrpeafrpsYGLAEATLFV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 469 TARQLRTG----------------------DNNRTL---GAPIANSQVLILD-ENFQPVAEQTVGELYIVGPGVCLGYLN 522
Cdd:cd05931 319 SGGPPGTGpvvlrvdrdalagravavaaddPAARELvscGRPLPDQEVRIVDpETGRELPDGEVGEIWVRGPSVASGYWG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 523 NPLQTAERYLDLSlpnGQSLRAY-RTGDMAKWTSDGIELCGRRDNQVKIRGFRVEPEEIERCLRDS----QRYRQVAVVI 597
Cdd:cd05931 399 RPEATAETFGALA---ATDEGGWlRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAhpalRPGCVAAFSV 475
|
490 500 510
....*....|....*....|....*....|
gi 1957676271 598 -DPHRRILAFLAqpqEEQPGAAREALKAHA 626
Cdd:cd05931 476 pDDGEERLVVVA---EVERGADPADLAAIA 502
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
189-659 |
1.91e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 92.75 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 189 SAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLldqhqgPLVVGICLPKCSVLYAgILAILGSGAVYLPLEP-SHPLQRQ 267
Cdd:PRK07787 13 ADIADAVRIGGRVLSRSDLAGAATAVAERVAGA------RRVAVLATPTLATVLA-VVGALIAGVPVVPVPPdSGVAERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 268 qYILENAGAVLLLhdGEHPlsetMPGLDISGIDIsDVNLDQPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQ----AN- 342
Cdd:PRK07787 86 -HILADSGAQAWL--GPAP----DDPAGLPHVPV-RLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRraiaADl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 343 --LAHFTAWYADYV-------------------QLTEQSRVLQFSSlsfdsslidifPT-------LLQGAELI--VPNE 392
Cdd:PRK07787 158 daLAEAWQWTADDVlvhglplfhvhglvlgvlgPLRIGNRFVHTGR-----------PTpeayaqaLSEGGTLYfgVPTV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 393 DQR--RDPlQLVELIRHQRL---SHAFLPPALLsilplDQLQILdhvmTGGDVCEpyvieqltRqgnlynlYGPTEATVL 467
Cdd:PRK07787 227 WSRiaADP-EAARALRGARLlvsGSAALPVPVF-----DRLAAL----TGHRPVE--------R-------YGMTETLIT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 468 ITAR---QLRTGdnnrTLGAPIANSQVLILDENFQPVAE--QTVGELYIVGPGVCLGYLNNPLQTAERYLDlslpNGQsl 542
Cdd:PRK07787 282 LSTRadgERRPG----WVGLPLAGVETRLVDEDGGPVPHdgETVGELQVRGPTLFDGYLNRPDATAAAFTA----DGW-- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 543 raYRTGDMAKWTSDG-IELCGRRD-NQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH----RRILAFLAQpqeeQPG 616
Cdd:PRK07787 352 --FRTGDVAVVDPDGmHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDddlgQRIVAYVVG----ADD 425
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1957676271 617 AAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALL 659
Cdd:PRK07787 426 VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
190-656 |
1.51e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 90.83 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 190 AERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPlvVGICLPKCSVLYAGILAILGSGAVYL---PLEPSHPLQR 266
Cdd:PRK05605 46 GDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDR--VAIVLPNCPQHIVAFYAVLRLGAVVVehnPLYTAHELEH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 267 QqyiLENAGA-VLLLHDGEHPLSETMPGlDISGIDISDVNLDQ--PLMRQ------------------------------ 313
Cdd:PRK05605 124 P---FEDHGArVAIVWDKVAPTVERLRR-TTPLETIVSVNMIAamPLLQRlalrlpipalrkaraaltgpapgtvpwetl 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 314 ---------------RPDLDAPCMALYTSGTTGHPKGVLLS----QANLAHFTAWYADyvqLTEQSRVLQFSSLSFDSSL 374
Cdd:PRK05605 200 vdaaiggdgsdvshpRPTPDDVALILYTSGTTGKPKGAQLThrnlFANAAQGKAWVPG---LGDGPERVLAALPMFHAYG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 375 IDIFPTL--LQGAELIV-PnedqRRDPLQLVELIRHQRLShaFLP--PALLS-ILPLDQLQILD-----HVMTGG----- 438
Cdd:PRK05605 277 LTLCLTLavSIGGELVLlP----APDIDLILDAMKKHPPT--WLPgvPPLYEkIAEAAEERGVDlsgvrNAFSGAmalpv 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 439 DVCEPYviEQLTrQGNLYNLYGPTEATVLITARQLrtGDNNR--TLGAPIANSQVLILD-ENF---QPVAEQtvGELYIV 512
Cdd:PRK05605 351 STVELW--EKLT-GGLLVEGYGLTETSPIIVGNPM--SDDRRpgYVGVPFPDTEVRIVDpEDPdetMPDGEE--GELLVR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 513 GPGVCLGYLNNPLQTAERYLDlslpngqslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYR 591
Cdd:PRK05605 424 GPQVFKGYWNRPEETAKSFLD---------GWFRTGDVVVMEEDGfIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVE 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1957676271 592 QVAVVIDPhrrilafLAQPQEE-------QPGAA--REALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRK 656
Cdd:PRK05605 495 DAAVVGLP-------REDGSEEvvaavvlEPGAAldPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
231-658 |
4.87e-18 |
|
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: 88.30 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 231 VGICLPKcSVLYA-GILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLlhdgehplsetmpgldISGIDISDVNLdqp 309
Cdd:cd05935 29 VGICLQN-SPQYViAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVA----------------VVGSELDDLAL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 310 lmrqrpdldapcmALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPT-LLQGAELI 388
Cdd:cd05935 89 -------------IPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTaVYVGGTYV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 389 VPNedqRRDPLQLVELIRHQRLSHAF-LPPALLSIL--PLDQ---LQILDHVMTGGDVCEPYVIEQLTRQGNLYNL--YG 460
Cdd:cd05935 156 LMA---RWDRETALELIEKYKVTFWTnIPTMLVDLLatPEFKtrdLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVegYG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 461 PTEATVLIT----ARQLRTgdnnrTLGAPIANSQVLILD-ENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLs 535
Cdd:cd05935 233 LTETMSQTHtnppLRPKLQ-----CLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEI- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 536 lpNGQslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLAQP 610
Cdd:cd05935 307 --KGR--RFFRTGDLGYMDEEGyFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERvgeeVKAFIVLR 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1957676271 611 QEEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd05935 383 PEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
180-646 |
5.79e-18 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 89.00 E-value: 5.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 180 ERLEQRFIQSAERPALNI----AGTSLSHRQLHAHSRAIQQRLQPL-LDQHQgplVVGICLPKCSVLYAGILAILGSGAV 254
Cdd:COG1022 15 DLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALgVKPGD---RVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 255 YLPLEPSHPLQRQQYILENAGA-VLLLHDGEH-----PLSETMPGLD----ISGIDISD----VNLDQ------------ 308
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAkVLFVEDQEQldkllEVRDELPSLRhivvLDPRGLRDdprlLSLDEllalgrevadpa 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 309 --PLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLqfsslsfdsslidIF-PT----- 380
Cdd:COG1022 172 elEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL-------------SFlPLahvfe 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 381 -------LLQGAELIVPnedqrRDPLQLVELIRH-------------------------------QRLSHAFL------- 415
Cdd:COG1022 239 rtvsyyaLAAGATVAFA-----ESPDTLAEDLREvkptfmlavprvwekvyagiqakaeeagglkRKLFRWALavgrrya 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 416 --------PPALLSIlpldQLQILD----------------HVMTGG-----DVCEPYvieqltrQG---NLYNLYGPTE 463
Cdd:COG1022 314 rarlagksPSLLLRL----KHALADklvfsklrealggrlrFAVSGGaalgpELARFF-------RAlgiPVLEGYGLTE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 464 ATVLITARQLrtgDNNR--TLGAPIANSQVLILDEnfqpvaeqtvGELYIVGPGVCLGYLNNPLQTAEryldlslpngqS 541
Cdd:COG1022 383 TSPVITVNRP---GDNRigTVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAE-----------A 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 542 LRA---YRTGDMAKWTSDGielcgrrdnQVKIRGfR------------VEPEEIERCLRDSQRYRQVAVVIDpHRRILAF 606
Cdd:COG1022 439 FDAdgwLHTGDIGELDEDG---------FLRITG-RkkdlivtsggknVAPQPIENALKASPLIEQAVVVGD-GRPFLAA 507
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1957676271 607 LAQPQEEqpgAAREALKAHAMQFlpdymqpTAWTELASMP 646
Cdd:COG1022 508 LIVPDFE---ALGEWAEENGLPY-------TSYAELAQDP 537
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
168-660 |
1.63e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 87.32 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 168 PWLLQLAQIPMIERLE---QRFiqsAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPLVVgICLPKCSVLYAG 244
Cdd:PRK08314 2 PKSLTLPETSLFHNLEvsaRRY---PDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVL-LYMQNSPQFVIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 245 ILAILGSGAVYLPLEPSHPLQRQQYILENAGAVL-------------------LLH----------------------DG 283
Cdd:PRK08314 78 YYAILRANAVVVPVNPMNREEELAHYVTDSGARVaivgselapkvapavgnlrLRHvivaqysdylpaepeiavpawlRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 284 EHPLSETMPGLDISGIDISDVNLDQPLMRQRPDlDApCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVL 363
Cdd:PRK08314 158 EPPLQALAPGGVVAWKEALAAGLAPPPHTAGPD-DL-AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 364 qfsslsfdsSLIDIF-----------PTLLQGAELIVPnedqRRDPLQLVELIRHQRLSHAFLPPA----LLSILPLDQ- 427
Cdd:PRK08314 236 ---------AVLPLFhvtgmvhsmnaPIYAGATVVLMP----RWDREAAARLIERYRVTHWTNIPTmvvdFLASPGLAEr 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 428 -LQILDHVmTGGDVCEPYVIEQLTRQgnLYNL-----YGPTEatvliTARQLRTGDNNRT----LGAPIANSQVLILD-E 496
Cdd:PRK08314 303 dLSSLRYI-GGGGAAMPEAVAERLKE--LTGLdyvegYGLTE-----TMAQTHSNPPDRPklqcLGIPTFGVDARVIDpE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 497 NFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLslpNGQslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRV 575
Cdd:PRK08314 375 TLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEI---DGK--RFFRTGDLGRMDEEGyFFITDRLKRMINASGFKV 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 576 EPEEIERCLrdsqrYRQVAV----VI---DPHR--RILAFLAQPQEEQPGAAREALKAHAMQFLPDYMQPTAWTELASMP 646
Cdd:PRK08314 450 WPAEVENLL-----YKHPAIqeacVIatpDPRRgeTVKAVVVLRPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLP 524
|
570
....*....|....
gi 1957676271 647 FASNGKVDRKALLE 660
Cdd:PRK08314 525 KSGSGKILWRQLQE 538
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
191-602 |
3.67e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 86.14 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSRAIQQRLQPLldqhqGpLVVG---ICLPKCSVLYA-GILAILGSGAVYLPLEPSHPLQR 266
Cdd:PRK08316 26 DKTALVFGDRSWTYAELDAAVNRVAAALLDL-----G-LKKGdrvAALGHNSDAYAlLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 267 QQYILENAGAVLLLHD-------------GEHPLSETMPGLDISGIDISDVNLDQPLMRQ-------RPDLDAPCMALYT 326
Cdd:PRK08316 100 LAYILDHSGARAFLVDpalaptaeaalalLPVDTLILSLVLGGREAPGGWLDFADWAEAGsvaepdvELADDDLAQILYT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 327 SGTTGHPKGVLLSQANLAHftawyaDYV------QLTEQSRVL---------QfsslsfdsslIDIF--PTLLQGAE-LI 388
Cdd:PRK08316 180 SGTESLPKGAMLTHRALIA------EYVscivagDMSADDIPLhalplyhcaQ----------LDVFlgPYLYVGATnVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 389 VPnedqRRDPLQLVELIRHQRLSHAFLPP----ALLSILPLDQ--LQILDHVMTGGDVCEPYVIEQLTR---QGNLYNLY 459
Cdd:PRK08316 244 LD----APDPELILRTIEAERITSFFAPPtvwiSLLRHPDFDTrdLSSLRKGYYGASIMPVEVLKELRErlpGLRFYNCY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 460 GPTE----ATVLITARQLRTGDnnrTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDls 535
Cdd:PRK08316 320 GQTEiaplATVLGPEEHLRRPG---SAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRG-- 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957676271 536 lpnGQslraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR 602
Cdd:PRK08316 395 ---GW----FHSGDLGVMDEEGyITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPK 455
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
190-581 |
5.18e-17 |
|
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: 85.75 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 190 AERPALNIA--GTSLSHRQLHAHSRAIQQRLQPLLDQhQGPlVVGICLPKCsVLYAGI-LAILGSGAVYLPLEP-SHP-- 263
Cdd:cd05904 19 PSRPALIDAatGRALTYAELERRVRRLAAGLAKRGGR-KGD-VVLLLSPNS-IEFPVAfLAVLSLGAVVTTANPlSTPae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 264 LQRQqyiLENAGAVLLLHDGEhpLSETMPGLDI-----------SGIDISDVNLDQPLMRQRPDL--DAPCMALYTSGTT 330
Cdd:cd05904 96 IAKQ---VKDSGAKLAFTTAE--LAEKLASLALpvvlldsaefdSLSFSDLLFEADEAEPPVVVIkqDDVAALLYSSGTT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 331 GHPKGVLLSQANLahftawyadyVQLTEQSRVLQFSSLSFDSSLIDIFP-------------TLLQGAELIVPnedQRRD 397
Cdd:cd05904 171 GRSKGVMLTHRNL----------IAMVAQFVAGEGSNSDSEDVFLCVLPmfhiyglssfalgLLRLGATVVVM---PRFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 398 PLQLVELIRHQRLSHAFL-PPALLSILPLD-----QLQILDHVMTGGDVCEPYVIEQLTR--------QGnlynlYGPTE 463
Cdd:cd05904 238 LEELLAAIERYKVTHLPVvPPIVLALVKSPivdkyDLSSLRQIMSGAAPLGKELIEAFRAkfpnvdlgQG-----YGMTE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 464 ATVlITARQLRTGDNNRTLGAP---IANSQVLILDEN---FQPVAEQtvGELYIVGPGVCLGYLNNPLQTA-----ERYL 532
Cdd:cd05904 313 STG-VVAMCFAPEKDRAKYGSVgrlVPNVEAKIVDPEtgeSLPPNQT--GELWIRGPSIMKGYLNNPEATAatidkEGWL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1957676271 533 dlslpngqslrayRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIE 581
Cdd:cd05904 390 -------------HTGDLCYIDEDGyLFIVDRLKELIKYKGFQVAPAELE 426
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
202-596 |
9.87e-17 |
|
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: 84.43 E-value: 9.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 202 LSHRQLHAHSRAIQQRLqplldqhqgplvvgiclpkcsvLYAGILAilGSGAVYLpLEPSHPLQRQQYILENAGAVLLLH 281
Cdd:cd05910 3 LSFRELDERSDRIAQGL----------------------TAYGIRR--GMRAVLM-VPPGPDFFALTFALFKAGAVPVLI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 282 DgehplsetmPGLDISgidisdvNLDQPLMRQRPDL-------DAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYV 354
Cdd:cd05910 58 D---------PGMGRK-------NLKQCLQEAEPDAfigipkaDEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 355 QLTEQSRVLqfsslsFDSSLIDIFPTLLqGAELIVPNEDQRR----DPLQLVELIRHQRLSHAFLPPALLSILPLDQLQI 430
Cdd:cd05910 122 GIRPGEVDL------ATFPLFALFGPAL-GLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQH 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 431 ------LDHVMTGGDVCEPYVIEQLTR----QGNLYNLYGPTEA--TVLITARQLRTGDNNRT-------LGAPIANSQV 491
Cdd:cd05910 195 gitlpsLRRVLSAGAPVPIALAARLRKmlsdEAEILTPYGATEAlpVSSIGSRELLATTTAATsggagtcVGRPIPGVRV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 492 LILDENFQPVAEQT---------VGELYIVGPGVCLGYLNNPLQTAeryLDLSLPNGQSLRaYRTGDMAKWTSDG-IELC 561
Cdd:cd05910 275 RIIEIDDEPIAEWDdtlelprgeIGEITVTGPTVTPTYVNRPVATA---LAKIDDNSEGFW-HRMGDLGYLDDEGrLWFC 350
|
410 420 430
....*....|....*....|....*....|....*
gi 1957676271 562 GRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV 596
Cdd:cd05910 351 GRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| carboxyl_red |
NF041592 |
carboxylic acid reductase; |
687-1076 |
1.76e-16 |
|
carboxylic acid reductase;
Pssm-ID: 469476 [Multi-domain] Cd Length: 1161 Bit Score: 85.00 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 687 AELLELPASDISTDESFFNLGGHSILLSRMLLRLREEFG---------------RSISinRFIEL--------PTIAKla 743
Cdd:NF041592 652 AALLGAAAADLRPDAHFTDLGGDSLSALTFSNLLHEIFGvevpvgvivspatdlRALA--DYIEAerasgakrPTFAS-- 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 744 tlVRGSGTEEVLSEKALADAFreLD------IKSLPVSRmGDVHKVIVTGANSFVGVHI-VEAL--LAWGASEVACLVRD 814
Cdd:NF041592 728 --VHGRDATEVRAADLTLDKF--IDaatlaaAPSLPGPS-GEVRTVLLTGATGFLGRYLaLEWLerLALVGGTLICLVRA 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 815 GGGQSAAQRFAQAL-----------RENRLEHLdlsrvRVYVADITRPQLGLSEDVYQRLDREFGALVHNAANVNHVLDY 883
Cdd:NF041592 803 KDDAAARARLDATFdsgdpellahyRELAADHL-----EVLAGDKGEPDLGLDRATWQRLADTVDLIVDPAALVNHVLPY 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 884 ESLARDNVEPIFECLRLCEGRSKKIFNFVSTLSASSTI-----SDDGRVLELPAAQTPPIYIKNGYNLSKWVGERILERA 958
Cdd:NF041592 878 SQLFGPNVVGTAELIRLALTTRLKPFTYLSTIGVGAQIepgafTEDADIREISPVRAIDDSYANGYGNSKWAGEVLLREA 957
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 959 RVR-GVRVNLYRPGNI-SFNSLTGvcqpHKN------RLMLMLkgsIQLGQVPE--FALN---------FDLMPVDFLAR 1019
Cdd:NF041592 958 HDLcGLPVAVFRCDMIlADTRYAG----QLNlpdmftRLMLSL---VATGIAPGsfYELDadgnrqrahYDGLPVDFIAE 1030
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1957676271 1020 FIAFHASRYQAEKAVFNLHNP--EPLSWDCYVASFREAGreFAMVSVADWQQQLGRVDS 1076
Cdd:NF041592 1031 AIATLGARVTDGFETYHVMNPhdDGIGLDEFVDWLIEAG--HPIQRIDDYADWLQRFET 1087
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
246-658 |
1.97e-16 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 84.03 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 246 LAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLL----------HDGEHPLSETMPGLD-ISGID-----ISDVNLDQP 309
Cdd:PRK06087 92 LACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFaptlfkqtrpVDLILPLQNQLPQLQqIVGVDklapaTSSLSLSQI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 310 LMRQRPdLDAPCMA--------LYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLID--IFP 379
Cdd:PRK06087 172 IADYEP-LTTAITThgdelaavLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHgvTAP 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 380 TLLQGAELIVpnedQRRDPLQLVELIRHQRLSHAF-LPPALLSILPLDQ-----LQILDHVMTGGDVCEPYVIEQLTRQG 453
Cdd:PRK06087 251 FLIGARSVLL----DIFTPDACLALLEQQRCTCMLgATPFIYDLLNLLEkqpadLSALRFFLCGGTTIPKKVARECQQRG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 454 -NLYNLYGPTEA---TVLITARQL-RTGDnnrTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTA 528
Cdd:PRK06087 327 iKLLSVYGSTESsphAVVNLDDPLsRFMH---TDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 529 eRYLDlslPNGQslraYRTGDMAKWTSDG-IELCGRRdNQVKIRGFR-VEPEEIERCLRDSQRYRQVAVVIDPHR----R 602
Cdd:PRK06087 404 -RALD---EEGW----YYSGDLCRMDEAGyIKITGRK-KDIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDErlgeR 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1957676271 603 ILAFLAQPQEEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PRK06087 475 SCAYVVLKAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
318-655 |
3.64e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 81.56 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 318 DAPCMALYTSGTTGHPKGVLLSQANL---AHFTawyADYVQLTEQSRV-LQFSSLSFDSSLIDIFPTLLQGAELIVPNED 393
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIvnnGYFI---GERLGLTEQDRLcIPVPLFHCFGSVLGVLACLTHGATMVFPSPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 394 qrRDPLQLVELIRHQRLSHAFLPP----ALLSiLPLDQLQILDHVMTG---GDVCEPYVIEQLTRQGNLYNL---YGPTE 463
Cdd:cd05917 79 --FDPLAVLEAIEKEKCTALHGVPtmfiAELE-HPDFDKFDLSSLRTGimaGAPCPPELMKRVIEVMNMKDVtiaYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 464 ATVLITarQLRTGDNN----RTLGAPIANSQVLILDENFQPVAEQ-TVGELYIVGPGVCLGYLNNPLQTAERYLdlslpn 538
Cdd:cd05917 156 TSPVST--QTRTDDSIekrvNTVGRIMPHTEAKIVDPEGGIVPPVgVPGELCIRGYSVMKGYWNDPEKTAEAID------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 539 gqSLRAYRTGDMAKWTSDG-IELCGRRDNQVkIRGFR-VEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLAQPQE 612
Cdd:cd05917 228 --GDGWLHTGDLAVMDEDGyCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDERygeeVCAWIRLKEG 304
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1957676271 613 EQPGAarEALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDR 655
Cdd:cd05917 305 AELTE--EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
177-661 |
5.82e-16 |
|
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: 82.50 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 177 PMIERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPLVVGicLPKCSVLYAGILAILGSGAVYL 256
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQ--LPNVAEFVIVFFALFRAGAIPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 257 PLEPSHplqRQQ---YILENAGAVLLLHDGEHP----------LSETMPGL-------------DISGIDISDVNLDQPl 310
Cdd:COG1021 104 FALPAH---RRAeisHFAEQSEAVAYIIPDRHRgfdyralareLQAEVPSLrhvlvvgdageftSLDALLAAPADLSEP- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 311 mrqRPDLDAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLqfsslsfdsSLIDI---FP-------- 379
Cdd:COG1021 180 ---RPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYL---------AALPAahnFPlsspgvlg 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 380 TLLQGAELIV---PnedqrrDPLQLVELIRHQRLSHAFLPPALLsILPLD-------QLQILDHVMTGGDVCEPYVIEQL 449
Cdd:COG1021 248 VLYAGGTVVLapdP------SPDTAFPLIERERVTVTALVPPLA-LLWLDaaersryDLSSLRVLQVGGAKLSPELARRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 450 TRQ--GNLYNLYGPTEATVLITarqlRTGDNN----RTLGAPI-ANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLN 522
Cdd:COG1021 321 RPAlgCTLQQVFGMAEGLVNYT----RLDDPEevilTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 523 NPLQTAeRYLDlslPNGqslrAYRTGDMAKWTSDG-IELCGRRDNQVkIR-GFRVEPEEIERCLRDSQRYRQVAVVIDPH 600
Cdd:COG1021 397 APEHNA-RAFT---PDG----FYRTGDLVRRTPDGyLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMPD 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957676271 601 R----RILAFLaQPQEEQPGAAreALKAHAM-QFLPDYMQPTAWTELASMPFASNGKVDRKALLEL 661
Cdd:COG1021 468 EylgeRSCAFV-VPRGEPLTLA--ELRRFLReRGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
314-658 |
8.01e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 81.97 E-value: 8.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 314 RPDLDAPC-MALYTSGTTGHPKGVLLSQANLAHFTAWYA--DYVQLTEQSRV------LQFSSLSFDSSLIDIFPTLLQ- 383
Cdd:PRK13383 169 RPAVAAPGrIVLLTSGTTGKPKGVPRAPQLRSAVGVWVTilDRTRLRTGSRIsvampmFHGLGLGMLMLTIALGGTVLTh 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 384 ---GAELIVPNED-QRRDPLQLVELIRHQRLShafLPPALLSILPLDQLQIldhVMTGGDVCEPYVIEQL--TRQGNLYN 457
Cdd:PRK13383 249 rhfDAEAALAQASlHRADAFTAVPVVLARILE---LPPRVRARNPLPQLRV---VMSSGDRLDPTLGQRFmdTYGDILYN 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 458 LYGPTEATV--LITARQLRtgDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYiVGpgvclGYLNnplqtAERYLD-- 533
Cdd:PRK13383 323 GYGSTEVGIgaLATPADLR--DAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIF-VG-----GELA-----GTRYTDgg 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 534 -LSLPNGQSlrayRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRILAFLAQPQ 611
Cdd:PRK13383 390 gKAVVDGMT----STGDMGYLDNAGrLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFV 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1957676271 612 EEQPG------AAREALKAHAMQFlpdyMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PRK13383 466 VLHPGsgvdaaQLRDYLKDRVSRF----EQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
308-667 |
1.10e-15 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 82.66 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 308 QPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLqfsslsfdsSLIDIF--------- 378
Cdd:PRK08633 772 KRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVIL---------SSLPFFhsfgltvtl 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 379 --PtLLQGAELI-VPNEdqrRDPLQLVELIRHQRLSHAFLPPALLSI-------LPLDqLQILDHVMTGG-----DVCEP 443
Cdd:PRK08633 843 wlP-LLEGIKVVyHPDP---TDALGIAKLVAKHRATILLGTPTFLRLylrnkklHPLM-FASLRLVVAGAeklkpEVADA 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 444 YvieQLTRQGNLYNLYGPTEAT---------VLITARQLRTGDNNRTLGAPIANSQVLILD-ENFQPVAEQTVGELYIVG 513
Cdd:PRK08633 918 F---EEKFGIRILEGYGATETSpvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGG 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 514 PGVCLGYLNNPLQTAEryldlSLPNGQSLRAYRTGDMAKWTSDG-IELCGRRDNQVKIRG-----FRVEPEEIERCLRDS 587
Cdd:PRK08633 995 PQVMKGYLGDPEKTAE-----VIKDIDGIGWYVTGDKGHLDEDGfLTITDRYSRFAKIGGemvplGAVEEELAKALGGEE 1069
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 588 QRYrqVAVVIDPHRR--ILAFLAQPQEEQPGAAREALKAhamQFLPDYMQPTAWTELASMPFASNGKVDRKALLELPVNV 665
Cdd:PRK08633 1070 VVF--AVTAVPDEKKgeKLVVLHTCGAEDVEELKRAIKE---SGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELALAL 1144
|
..
gi 1957676271 666 TE 667
Cdd:PRK08633 1145 LG 1146
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
231-660 |
1.28e-15 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 80.88 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 231 VGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQrqqyilENAGAVLLLHDGEHPLSETMPGldISGIDISDV----NL 306
Cdd:cd05929 45 VYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRA------EACAIIEIKAAALVCGLFTGGG--ALDGLEDYEaaegGS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 307 DQPLMrqrPDLDAPCMALYTSGTTGHPKGVLLS----QANLAHFTAWyADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLL 382
Cdd:cd05929 117 PETPI---EDEAAGWKMLYSGGTTGRPKGIKRGlpggPPDNDTLMAA-ALGFGPGADSVYLSPAPLYHAAPFRWSMTALF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 383 QGAELIVPnedQRRDPLQLVELIRHQRLSHAFLPPALLS-ILPLDQ----------LQILDHVmtgGDVCEPYVIEQLTR 451
Cdd:cd05929 193 MGGTLVLM---EKFDPEEFLRLIERYRVTFAQFVPTMFVrLLKLPEavrnaydlssLKRVIHA---AAPCPPWVKEQWID 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 452 QGN--LYNLYGPTEAT--VLITARQLRTgdNNRTLGAPIAnSQVLILDENFQPVAEQTVGELYIVGPGVCLgYLNNPLQT 527
Cdd:cd05929 267 WGGpiIWEYYGGTEGQglTIINGEEWLT--HPGSVGRAVL-GKVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 528 AERYLDlslpngqslRAYRT-GDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH----R 601
Cdd:cd05929 343 AAARNE---------GGWSTlGDVGYLDEDGyLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDeelgQ 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 602 RILAFLAQPQEEQPGAA-REALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLE 660
Cdd:cd05929 414 RVHAVVQPAPGADAGTAlAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
320-599 |
2.32e-15 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 78.85 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 320 PCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNedqRRDPL 399
Cdd:cd17637 2 PFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVME---KFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 400 QLVELIRHQRLSHAF-LPPALLSIL------PLDqLQILDHVmTGGDVcePYVIEQLTRQ--GNLYNLYGPTEATVLITA 470
Cdd:cd17637 79 EALELIEEEKVTLMGsFPPILSNLLdaaeksGVD-LSSLRHV-LGLDA--PETIQRFEETtgATFWSLYGQTETSGLVTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 471 RQLRtgDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAeryldlslpngQSLRA--YRTG 548
Cdd:cd17637 155 SPYR--ERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTA-----------YTFRNgwHHTG 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1957676271 549 DMAKWTSDG-IELCGRRDNQ--VKIRGFRVEPEEIERCLRDSQRYRQVAV--VIDP 599
Cdd:cd17637 222 DLGRFDEDGyLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVigVPDP 277
|
|
| FAR-N_SDR_e |
cd05236 |
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ... |
781-1037 |
3.71e-15 |
|
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187547 [Multi-domain] Cd Length: 320 Bit Score: 77.72 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 781 HKVIVTGANSFVGVHIVEALL--AWGASEVACLVRDGGGQSAAQRFAQALRENRLEHLD------LSRVRVYVADITRPQ 852
Cdd:cd05236 1 KSVLITGATGFLGKVLLEKLLrsCPDIGKIYLLIRGKSGQSAEERLRELLKDKLFDRGRnlnplfESKIVPIEGDLSEPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 853 LGLSEDVYQRLDREFGALVHNAANVNHVLDYESLARDNVEPIFECLRLC-EGRSKKIFNFVSTLSASSTISD-DGRVLEL 930
Cdd:cd05236 81 LGLSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAkRCKKLKAFVHVSTAYVNGDRQLiEEKVYPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 931 PA-----------------AQTPPIYIK---NGYNLSKWVGERILeRARVRGVRVNLYRP-------------GNISFNS 977
Cdd:cd05236 161 PAdpeklidilelmddlelERATPKLLGghpNTYTFTKALAERLV-LKERGNLPLVIVRPsivgatlkepfpgWIDNFNG 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957676271 978 LTGvcqphknrLMLMLkgsiQLGQVPEFALN----FDLMPVDFLARFI----AFHASRYQAEKAVFNL 1037
Cdd:cd05236 240 PDG--------LFLAY----GKGILRTMNADpnavADIIPVDVVANALlaaaAYSGVRKPRELEVYHC 295
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
202-658 |
4.18e-15 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 79.10 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 202 LSHRQLHAHSRAIQQRLQpllDQHQGP-LVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLL 280
Cdd:cd05973 1 LTFGELRALSARFANALQ---ELGVGPgDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 281 hdgehplsetmpgldisgidisdVNLDQplmRQRPDLDaPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQS 360
Cdd:cd05973 78 -----------------------TDAAN---RHKLDSD-PFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 361 RV-----------LQFSSLSFDSSLIdifPTLLQGAELIVPNEDQrrdplqlvELIRHQRLSHAFLPPALLSIL------ 423
Cdd:cd05973 131 SFwnaadpgwaygLYYAITGPLALGH---PTILLEGGFSVESTWR--------VIERLGVTNLAGSPTAYRLLMaagaev 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 424 PLDQLQILDHVMTGGDVCEPYVIEQL-TRQGNL-YNLYGPTEATVLIT-----ARQLRTGdnnrTLGAPIANSQVLILDE 496
Cdd:cd05973 200 PARPKGRLRRVSSAGEPLTPEVIRWFdAALGVPiHDHYGQTELGMVLAnhhalEHPVHAG----SAGRAMPGWRVAVLDD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 497 NFQPVAEQTVGELYIvgpgvclGYLNNPLQTAERY--LDLSLPNGqslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGF 573
Cdd:cd05973 276 DGDELGPGEPGRLAI-------DIANSPLMWFRGYqlPDTPAIDG---GYYLTGDTVEFDPDGsFSFIGRADDVITMSGY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 574 RVEPEEIERCLRDSQRYRQVAVV--IDPHRR--ILAF--LAQPQEEQPGAAREaLKAHAMQFLPDYMQPTAWTELASMPF 647
Cdd:cd05973 346 RIGPFDVESALIEHPAVAEAAVIgvPDPERTevVKAFvvLRGGHEGTPALADE-LQLHVKKRLSAHAYPRTIHFVDELPK 424
|
490
....*....|.
gi 1957676271 648 ASNGKVDRKAL 658
Cdd:cd05973 425 TPSGKIQRFLL 435
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
230-661 |
5.17e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 79.55 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 230 VVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYILENAGA--VLLLHDGEH----------PLSETMPGLDIS 297
Cdd:PRK05852 70 RVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGArvVLIDADGPHdraepttrwwPLTVNVGGDSGP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 298 GIDISDVNLD---QPLMRQ------RPDlDApcMALYTSGTTGHPKGVLLSQANLA-HFTAWYADYvQLTEQSRVLQFSS 367
Cdd:PRK05852 150 SGGTLSVHLDaatEPTPATstpeglRPD-DA--MIMFTGGTTGLPKMVPWTHANIAsSVRAIITGY-RLSPRDATVAVMP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 368 LSFDSSLI-DIFPTLLQGAELIVPNE---------DQRRD----------PLQLVELIRHQRLSHAFLPPALLSI----L 423
Cdd:PRK05852 226 LYHGHGLIaALLATLASGGAVLLPARgrfsahtfwDDIKAvgatwytavpTIHQILLERAATEPSGRKPAALRFIrscsA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 424 PLDQ--LQILDHVMTGGDVCEpyvieqltrqgnlynlYGPTEATVLITARQLRT---GDNNRTLGAPIANS---QVLILD 495
Cdd:PRK05852 306 PLTAetAQALQTEFAAPVVCA----------------FGMTEATHQVTTTQIEGigqTENPVVSTGLVGRStgaQIRIVG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 496 ENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSLpngqslrayRTGDMAKWTSDG-IELCGRRDNQVKIRGFR 574
Cdd:PRK05852 370 SDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL---------RTGDLGSLSAAGdLSIRGRIKELINRGGEK 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 575 VEPEEIERCLRDSQRYRQVAVVIDPHR---RILAFLAQPQEEQPGAAREaLKAHAMQFLPDYMQPTAWTELASMPFASNG 651
Cdd:PRK05852 441 ISPERVEGVLASHPNVMEAAVFGVPDQlygEAVAAVIVPRESAPPTAEE-LVQFCRERLAAFEIPASFQEASGLPHTAKG 519
|
490
....*....|
gi 1957676271 652 KVDRKALLEL 661
Cdd:PRK05852 520 SLDRRAVAEQ 529
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
191-599 |
5.55e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 79.31 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSRAIQQRLQplldqHQGpLVVGICL----PKCSVLYAGILAILGSGAVYLPLEPSHPLQR 266
Cdd:PRK07470 22 DRIALVWGDRSWTWREIDARVDALAAALA-----ARG-VRKGDRIlvhsRNCNQMFESMFAAFRLGAVWVPTNFRQTPDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 267 QQYILENAGAVLLLHDGEHP-----LSETMPGLDIS--------GIDISDV---NLDQPLMRQRPDLDAPCMALYTSGTT 330
Cdd:PRK07470 96 VAYLAEASGARAMICHADFPehaaaVRAASPDLTHVvaiggaraGLDYEALvarHLGARVANAAVDHDDPCWFFFTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 331 GHPKGVLLSQANLAH-FTAWYADYVQ-LTEQSRVLQfsslsfdsslidIFP--------TLLQ---GAELIVPNEDqRRD 397
Cdd:PRK07470 176 GRPKAAVLTHGQMAFvITNHLADLMPgTTEQDASLV------------VAPlshgagihQLCQvarGAATVLLPSE-RFD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 398 PLQLVELIRHQRLSHAFLPPALLSIL----PLDQLQ--ILDHVMTGGdvcEP-YVIEQ---LTRQGN-LYNLYGPTEATV 466
Cdd:PRK07470 243 PAEVWALVERHRVTNLFTVPTILKMLvehpAVDRYDhsSLRYVIYAG---APmYRADQkraLAKLGKvLVQYFGLGEVTG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 467 LIT-----ARQLRTGDNNR--TLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAEryldlSLPNG 539
Cdd:PRK07470 320 NITvlppaLHDAEDGPDARigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAK-----AFRDG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1957676271 540 QslraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAV--VIDP 599
Cdd:PRK07470 395 W----FRTGDLGHLDARGfLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVlgVPDP 453
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
322-658 |
6.57e-15 |
|
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: 79.05 E-value: 6.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 322 MALY-TSGTTGHPKGVLLSQANLAH-FTAWYADYVQLTEQSRVLQFSSLSFDSSLI-DIFPTLLQGAELIVpNEDQRRDP 398
Cdd:cd05928 177 MAIYfTSGTTGSPKMAEHSHSSLGLgLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACVFV-HHLPRFDP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 399 LQLVELIRHQRLSHAFLPPALLSILPLD-----QLQILDHVMTGGDVCEPYVIEQLTRQGNL--YNLYGPTEaTVLITAR 471
Cdd:cd05928 256 LVILKTLSSYPITTFCGAPTVYRMLVQQdlssyKFPSLQHCVTGGEPLNPEVLEKWKAQTGLdiYEGYGQTE-TGLICAN 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 472 QLRTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYI-VGPG--VCL--GYLNNPLQTAEryldlslpngqSLRA-- 544
Cdd:cd05928 335 FKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrVKPIrpFGLfsGYVDNPEKTAA-----------TIRGdf 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 545 YRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVI--DPHRR--ILAFL---AQPQEEQPG 616
Cdd:cd05928 404 YLTGDRGIMDEDGyFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSspDPIRGevVKAFVvlaPQFLSHDPE 483
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1957676271 617 AAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd05928 484 QLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
306-660 |
8.40e-15 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 78.94 E-value: 8.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 306 LDQPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSqANlahfTAW-----YADYVQLTEQSRVLQFSSLSFDSSLID--IF 378
Cdd:PRK13295 185 APAILARLRPGPDDVTQLIYTSGTTGEPKGVMHT-AN----TLManivpYAERLGLGADDVILMASPMAHQTGFMYglMM 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 379 PTLLqGAELIVpnEDQrRDPLQLVELIRHQRLSHAFLPPALLSIL---------PLDQLQILdhvMTGGDVCEPYVIEQl 449
Cdd:PRK13295 260 PVML-GATAVL--QDI-WDPARAAELIRTEGVTFTMASTPFLTDLtravkesgrPVSSLRTF---LCAGAPIPGALVER- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 450 TRQG---NLYNLYGPTE---ATVLITARQLRTGDNnrTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNN 523
Cdd:PRK13295 332 ARAAlgaKIVSAWGMTEngaVTLTKLDDPDERAST--TDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKR 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 524 PLQT---AERYLDlslpngqslrayrTGDMAKWTSDG-IELCGRRDNqVKIRGFRVEPE-EIERCLRDSQRYRQVAVVID 598
Cdd:PRK13295 410 PQLNgtdADGWFD-------------TGDLARIDADGyIRISGRSKD-VIIRGGENIPVvEIEALLYRHPAIAQVAIVAY 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1957676271 599 PHR----RILAFLAQpqeeQPGAA------REALKAH--AMQFLPDYMqptawTELASMPFASNGKVDRKALLE 660
Cdd:PRK13295 476 PDErlgeRACAFVVP----RPGQSldfeemVEFLKAQkvAKQYIPERL-----VVRDALPRTPSGKIQKFRLRE 540
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
325-662 |
8.58e-15 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 78.77 E-value: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 325 YTSGTTGHPKGVLLSQ----ANLAHFTAWYADYVQLTEQSRVLqfsslSFDSSLIDIFPTL--------LQGAELIVPNE 392
Cdd:PRK08751 215 YTGGTTGVAKGAMLTHrnlvANMQQAHQWLAGTGKLEEGCEVV-----ITALPLYHIFALTanglvfmkIGGCNHLISNP 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 393 dqrRDPLQLVELIRHQRLShAF-----LPPALLSILPLDQLQILDHVMT--GGDVCEPYVIEQLTRQGN--LYNLYGPTE 463
Cdd:PRK08751 290 ---RDMPGFVKELKKTRFT-AFtgvntLFNGLLNTPGFDQIDFSSLKMTlgGGMAVQRSVAERWKQVTGltLVEAYGLTE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 464 ATVLITARQLRTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAErYLDlslPNGQslr 543
Cdd:PRK08751 366 TSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAK-VMD---ADGW--- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 544 aYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLAQpqeEQPGAA 618
Cdd:PRK08751 439 -LHTGDIARMDEQGfVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKsgeiVKVVIVK---KDPALT 514
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1957676271 619 REALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLELP 662
Cdd:PRK08751 515 AEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| WcaG |
COG0451 |
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
782-1086 |
1.62e-14 |
|
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 75.40 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 782 KVIVTGANSFVGVHIVEALLAWGAsEVACLVRDGGGQSAAQrfaqalrenrlehlDLSRVRVYVADITRPqlglsEDVYQ 861
Cdd:COG0451 1 RILVTGGAGFIGSHLARRLLARGH-EVVGLDRSPPGAANLA--------------ALPGVEFVRGDLRDP-----EALAA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 862 RLdREFGALVHNAANVNHVL-DYESLARDNVEPIFECLRLC-EGRSKKIFnFVSTlsaSSTISDDgrvlELPAAQTPPIY 939
Cdd:COG0451 61 AL-AGVDAVVHLAAPAGVGEeDPDETLEVNVEGTLNLLEAArAAGVKRFV-YASS---SSVYGDG----EGPIDEDTPLR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 940 IKNGYNLSKWVGERILER-ARVRGVRVNLYRPGNisfnsltgVCQPHKNRLMLMLKGSIQLGQVPEFALN----FDLMPV 1014
Cdd:COG0451 132 PVSPYGASKLAAELLARAyARRYGLPVTILRPGN--------VYGPGDRGVLPRLIRRALAGEPVPVFGDgdqrRDFIHV 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1957676271 1015 DFLARFIAfHASRYQAEK-AVFNLHNPEPLSWDCYVASFREA-GREFAmVSVADWQQQLGRVDSDNA-LFGVLGF 1086
Cdd:COG0451 204 DDVARAIV-LALEAPAAPgGVYNVGGGEPVTLRELAEAIAEAlGRPPE-IVYPARPGDVRPRRADNSkARRELGW 276
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
318-661 |
1.79e-14 |
|
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: 77.22 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 318 DAPCMALYTSGTTGHPKGVLLSQAN--LAHFTAWYadYVQLTEQSRVLQFSSLSFDSSLID-IFPTLLQGAELIVPNEdQ 394
Cdd:cd05974 85 DDPMLLYFTSGTTSKPKLVEHTHRSypVGHLSTMY--WIGLKPGDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNY-A 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 395 RRDPLQLVELIRHQRLSHAFLPPALLSIL---PLDQLQI-LDHVMTGGDVCEPYVIEQLTRQGNLY--NLYGPTEATVLI 468
Cdd:cd05974 162 RFDAKRVLAALVRYGVTTLCAPPTVWRMLiqqDLASFDVkLREVVGAGEPLNPEVIEQVRRAWGLTirDGYGQTETTALV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 469 T---ARQLRTGdnnrTLGAPIANSQVLILDENFQPVAEqtvGELYIV-----GPGVCLGYLNNPLQTAEryldlSLPNGQ 540
Cdd:cd05974 242 GnspGQPVKAG----SMGRPLPGYRVALLDPDGAPATE---GEVALDlgdtrPVGLMKGYAGDPDKTAH-----AMRGGY 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 541 slraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRILAF------LAQPQEE 613
Cdd:cd05974 310 ----YRTGDIAMRDEDGyLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVpkafivLRAGYEP 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1957676271 614 QPGAAREALKaHAMQFLPDYMQpTAWTELASMPFASNGKVDRKALLEL 661
Cdd:cd05974 386 SPETALEIFR-FSRERLAPYKR-IRRLEFAELPKTISGKIRRVELRRR 431
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
188-658 |
1.82e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 77.22 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 188 QSAERPALNIAGTSLSHRQLHAHSRAIQQRLQplldqHQGplVVgiclPKCSVLYAG---------ILAILGSGAVYLPL 258
Cdd:PRK09029 15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFA-----QQG--VV----EGSGVALRGknspetllaYLALLQCGARVLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 259 EPSHPLQRQQYILENAGAVLLLHDGEHPlsetmpglDISGIDISDVNLDQPLMRQRPDLDAPCMALYTSGTTGHPKGVLL 338
Cdd:PRK09029 84 NPQLPQPLLEELLPSLTLDFALVLEGEN--------TFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 339 S-QANLA---------HFTA---------------------WyadyvqlteqsrvlqfsslsfdsslidifptLLQGAEL 387
Cdd:PRK09029 156 TaQAHLAsaegvlslmPFTAqdswllslplfhvsgqgivwrW-------------------------------LYAGATL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 388 IVPNEDQRRDPLQLVelirhqrlSHAFLPPALLSILpLDQLQ---ILDHVMTGGDVCEPYVIEQLTRQG-NLYNLYGPTE 463
Cdd:PRK09029 205 VVRDKQPLEQALAGC--------THASLVPTQLWRL-LDNRSeplSLKAVLLGGAAIPVELTEQAEQQGiRCWCGYGLTE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 464 ATVLITARQlrtGDNNRTLGAPIANSQVLILDenfqpvaeqtvGELYIVGPGVCLGYlnnplqtaerYLD---LSLPNGQ 540
Cdd:PRK09029 276 MASTVCAKR---ADGLAGVGSPLPGREVKLVD-----------GEIWLRGASLALGY----------WRQgqlVPLVNDE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 541 SLraYRTGDMAKWTSDGIELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVidP-------HRRIlAFLaqpqEE 613
Cdd:PRK09029 332 GW--FATRDRGEWQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVV--PvadaefgQRPV-AVV----ES 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1957676271 614 QPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PRK09029 403 DSEAAVVNLAEWLQDKLARFQQPVAYYLLPPELKNGGIKISRQAL 447
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
268-654 |
2.05e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 77.62 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 268 QYILENAGAVLLLHDGEH-----PLSETMPGL-------DISGIDISD--VNLDQPLMRQRPDLDAP------CMALYTS 327
Cdd:PRK07798 93 RYLLDDSDAVALVYEREFaprvaEVLPRLPKLrtlvvveDGSGNDLLPgaVDYEDALAAGSPERDFGerspddLYLLYTG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 328 GTTGHPKGVLLSQANL--------AHFTAWY-ADYVQLTEQSRvlqfsslsfDSSLIDIFPT--LLQGAEL--------- 387
Cdd:PRK07798 173 GTTGMPKGVMWRQEDIfrvllggrDFATGEPiEDEEELAKRAA---------AGPGMRRFPAppLMHGAGQwaafaalfs 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 388 ---IVPNEDQRRDPLQLVELI-RHQRLS-----HAFLPP---ALLSILPLDqLQILDHVMTGGDVCEPYVIEQLTR---Q 452
Cdd:PRK07798 244 gqtVVLLPDVRFDADEVWRTIeREKVNVitivgDAMARPlldALEARGPYD-LSSLFAIASGGALFSPSVKEALLEllpN 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 453 GNLYNLYGPTEA----TVLITARQLRTGDNNRTLGApiansQVLILDENFQPVA--EQTVGELYIVGPgVCLGYLNNPLQ 526
Cdd:PRK07798 323 VVLTDSIGSSETgfggSGTVAKGAVHTGGPRFTIGP-----RTVVLDEDGNPVEpgSGEIGWIARRGH-IPLGYYKDPEK 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 527 TAE--------RYldlSLPngqslrayrtGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCL------------- 584
Cdd:PRK07798 397 TAEtfptidgvRY---AIP----------GDRARVEADGtITLLGRGSVCINTGGEKVFPEEVEEALkahpdvadalvvg 463
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1957676271 585 RDSQRYRQ--VAVVidphrrilaflaqpqEEQPGAAR--EALKAHAMQFLPDYMQPTAWTELASMPFASNGKVD 654
Cdd:PRK07798 464 VPDERWGQevVAVV---------------QLREGARPdlAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
174-658 |
2.73e-14 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 77.53 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 174 AQIPMIERLEQRFIQSAE-RPALNIAGT-----SLSHRQLHAHSRAIQQRLQPLL----DQhqgplvVGICLPKCSVLYA 243
Cdd:cd05968 58 GRMNIVEQLLDKWLADTRtRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGvgkgDR------VGIYLPMIPEIVP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 244 GILAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLL-HDG------------------------EHPLSETMPGLDIS- 297
Cdd:cd05968 132 AFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALItADGftrrgrevnlkeeadkacaqcptvEKVVVVRHLGNDFTp 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 298 --GIDIS--DVNLDQPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQANL---AHFTAWYAdyVQLTEQSRVLQFSSLSF 370
Cdd:cd05968 212 akGRDLSydEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFplkAAQDMYFQ--FDLKPGDLLTWFTDLGW 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 371 DSSLIDIFPTLLQGAELI----VPNEDqrrDPLQLVELIRHQRLSHAFLPPALL-SILPLDQLQILDH----VMTGGDVC 441
Cdd:cd05968 290 MMGPWLIFGGLILGATMVlydgAPDHP---KADRLWRMVEDHEITHLGLSPTLIrALKPRGDAPVNAHdlssLRVLGSTG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 442 EP-------YVIEQLTRQGN-LYNLYGPTEAT------VLItaRQLRTGDNNrtlgAPIANSQVLILDENFQPVAEQtVG 507
Cdd:cd05968 367 EPwnpepwnWLFETVGKGRNpIINYSGGTEISggilgnVLI--KPIKPSSFN----GPVPGMKADVLDESGKPARPE-VG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 508 ELYIVGP--GVCLGYLNNPlqtaERYLDL---SLPNgqslrAYRTGDMAKWTSDGI-ELCGRRDNQVKIRGFRVEPEEIE 581
Cdd:cd05968 440 ELVLLAPwpGMTRGFWRDE----DRYLETywsRFDN-----VWVHGDFAYYDEEGYfYILGRSDDTINVAGKRVGPAEIE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 582 RCLRDSQRYRQVAVVIDPH----RRILAFLAQPQEEQPGaarEALKAHAMQFLPDYM----QPTAWTELASMPFASNGKV 653
Cdd:cd05968 511 SVLNAHPAVLESAAIGVPHpvkgEAIVCFVVLKPGVTPT---EALAEELMERVADELgkplSPERILFVKDLPKTRNAKV 587
|
....*
gi 1957676271 654 DRKAL 658
Cdd:cd05968 588 MRRVI 592
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
190-659 |
3.19e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 77.09 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 190 AERP---ALNIAGTSLSHRQLhahsRAIQQRLQPLLDQhQGPL---VVGICLPKCSVLYAGILAILGSGAVYLPLEPSHP 263
Cdd:PRK06164 21 RARPdavALIDEDRPLSRAEL----RALVDRLAAWLAA-QGVRrgdRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 264 LQRQQYILENAGAVLL--------------LHDGEHPLSETMPGLDISGIDISD----------VNLDQPLM------RQ 313
Cdd:PRK06164 96 SHEVAHILGRGRARWLvvwpgfkgidfaaiLAAVPPDALPPLRAIAVVDDAADAtpapapgarvQLFALPDPappaaaGE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 314 RPDLDAPCMALYT-SGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVpne 392
Cdd:PRK06164 176 RAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVC--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 393 DQRRDPLQLVELIRHQRLSHAFLPPALLSIL--------PLDQLQILDHVMTGGDVCEpYVIEQLTRQGNLYNLYGPTEA 464
Cdd:PRK06164 253 EPVFDAARTARALRRHRVTHTFGNDEMLRRIldtageraDFPSARLFGFASFAPALGE-LAALARARGVPLTGLYGSSEV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 465 TVLITARQLRTGDNNRTL--GAPI-ANSQVLILDENFQPVAEQTV-GELYIVGPGVCLGYLNNPLQTAERYldlsLPNGQ 540
Cdd:PRK06164 332 QALVALQPATDPVSVRIEggGRPAsPEARVRARDPQDGALLPDGEsGEIEIRAPSLMRGYLDNPDATARAL----TDDGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 541 slraYRTGDMAKWTSDG--IELCgRRDNQVKIRGFRVEPEEIERCL------RDSQryrQVAVVIDPHRRILAFLAQPQE 612
Cdd:PRK06164 408 ----FRTGDLGYTRGDGqfVYQT-RMGDSLRLGGFLVNPAEIEHALealpgvAAAQ---VVGATRDGKTVPVAFVIPTDG 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1957676271 613 EQPGAAreALKAHAMQFLPDYMQPTAWTELASMPFA--SNGKVDRKALL 659
Cdd:PRK06164 480 ASPDEA--GLMAACREALAGFKVPARVQVVEAFPVTesANGAKIQKHRL 526
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
315-658 |
3.20e-14 |
|
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: 76.23 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 315 PDLDAPCMALYTSGTTGHPKGVLLSQANlaHFtaWYADYVQL----TEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVp 390
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGN--HW--WSAIGSALnlglTEDDNWLCALPLFHISGLSILMRSVIYGMTVYL- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 391 neDQRRDPLQLVELIRHQRLSHAFLPPALLSILpldqLQILDH--------VMTGGDVCEPYVIEQLTRQG-NLYNLYGP 461
Cdd:cd05912 149 --VDKFDAEQVLHLINSGKVTIISVVPTMLQRL----LEILGEgypnnlrcILLGGGPAPKPLLEQCKEKGiPVYQSYGM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 462 TE-ATVLITARQLRTGDNNRTLGAPIANSQVLILDENFQPvaeQTVGELYIVGPGVCLGYLNNPLQTAEryldlSLPNGq 540
Cdd:cd05912 223 TEtCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEE-----SFENG- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 541 slrAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR-----ILAFLAqpqeEQ 614
Cdd:cd05912 294 ---WFKTGDIGYLDEEGfLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKwgqvpVAFVVS----ER 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1957676271 615 PGAAREaLKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:cd05912 367 PISEEE-LIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
252-658 |
4.29e-14 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 76.26 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 252 GAVYLPLEPSHPLQRQQYILENAGAVLL-------------LHDGEHPLS------ETMPglDISG-IDISDVNLDQPL- 310
Cdd:PRK08008 86 GAIMVPINARLLREESAWILQNSQASLLvtsaqfypmyrqiQQEDATPLRhicltrVALP--ADDGvSSFTQLKAQQPAt 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 311 MRQRPDL--DAPCMALYTSGTTGHPKGVLLSQANL---AHFTAWyadYVQLTEQSRVLqfssLSFDSSLID-----IFPT 380
Cdd:PRK08008 164 LCYAPPLstDDTAEILFTSGTTSRPKGVVITHYNLrfaGYYSAW---QCALRDDDVYL----TVMPAFHIDcqctaAMAA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 381 LLQGAELIVPNEDQRRDPLQLVELIRhQRLSHAFlpPALLSIL------PLDQLQILDHVMTGGDVCEPYVIEQLTRQG- 453
Cdd:PRK08008 237 FSAGATFVLLEKYSARAFWGQVCKYR-ATITECI--PMMIRTLmvqppsANDRQHCLREVMFYLNLSDQEKDAFEERFGv 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 454 NLYNLYGPTEATV-LITArqlRTGDNNR--TLGAPIANSQVLILDENFQPVAEQTVGELYIVG-PGVCL--GYLNNPLQT 527
Cdd:PRK08008 314 RLLTSYGMTETIVgIIGD---RPGDKRRwpSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGKTIfkEYYLDPKAT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 528 AEryldLSLPNGQslraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAV--VIDPHR--R 602
Cdd:PRK08008 391 AK----VLEADGW----LHTGDTGYVDEEGfFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVvgIKDSIRdeA 462
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1957676271 603 ILAFLAQPQEEQpgAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PRK08008 463 IKAFVVLNEGET--LSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
203-653 |
5.08e-14 |
|
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: 76.46 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 203 SHRQLHAHSraiqQRLQ-PLLDQ--HQGPlVVGICLPKCSVLYAGILAILGSGAVYLPL----EPSHPLQRqqyiLENAG 275
Cdd:cd17634 86 SYRELHREV----CRFAgTLLDLgvKKGD-RVAIYMPMIPEAAVAMLACARIGAVHSVIfggfAPEAVAGR----IIDSS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 276 AVLLL-HDG-------------------------EHPLSETMPGLDISGIDISDVNLDQPLMRQRP-------DLDAPCM 322
Cdd:cd17634 157 SRLLItADGgvragrsvplkknvddalnpnvtsvEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPehqpeamNAEDPLF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 323 ALYTSGTTGHPKGVLLSQANLAHFTA----------------WYADYVQLTEQSRVlqfsslsfdsslidIFPTLLQGAE 386
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGGYLVYAAttmkyvfdygpgdiywCTADVGWVTGHSYL--------------LYGPLACGAT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 387 LI----VPNEDqrrDPLQLVELIRHQRLSHAFLPP-ALLSILPLDQLQILDH----VMTGGDVCEP-------YVIEQLT 450
Cdd:cd17634 303 TLlyegVPNWP---TPARMWQVVDKHGVNILYTAPtAIRALMAAGDDAIEGTdrssLRILGSVGEPinpeayeWYWKKIG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 451 RQGN-LYNLYGPTEA-----TVLITARQLRTGDNNRtlgaPIANSQVLILDENFQPVAEQTVGELYIVG--PGVCLGYLN 522
Cdd:cd17634 380 KEKCpVVDTWWQTETggfmiTPLPGAIELKAGSATR----PVFGVQPAVVDNEGHPQPGGTEGNLVITDpwPGQTRTLFG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 523 NPlqtaERYLDLSLPNGQSLraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH- 600
Cdd:cd17634 456 DH----ERFEQTYFSTFKGM--YFSGDGARRDEDGyYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHa 529
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1957676271 601 ---RRILAFLA-QPQEEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKV 653
Cdd:cd17634 530 ikgQAPYAYVVlNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
269-660 |
6.12e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 75.89 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 269 YILENAGA-VLLLH-DGEHPLSETMP-GLD----------ISGIDISD---------VNLDQPLMRQR----PDLDAPCM 322
Cdd:PRK12406 77 YILEDSGArVLIAHaDLLHGLASALPaGVTvlsvptppeiAAAYRISPalltppagaIDWEGWLAQQEpydgPPVPQPQS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 323 ALYTSGTTGHPKGVLLSQAN---LAHFTAWYADYVQLTEQSRVLQF-SSLSFDSSLIDIFPTLLQGAELIVPnedqRRDP 398
Cdd:PRK12406 157 MIYTSGTTGHPKGVRRAAPTpeqAAAAEQMRALIYGLKPGIRALLTgPLYHSAPNAYGLRAGRLGGVLVLQP----RFDP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 399 LQLVELIRHQRLSHAFLPPALLS-ILPLDQ-------LQILDHVMTGGDVCEPYVIEQLTRQGN--LYNLYGPTEATVLI 468
Cdd:PRK12406 233 EELLQLIERHRITHMHMVPTMFIrLLKLPEevrakydVSSLRHVIHAAAPCPADVKRAMIEWWGpvIYEYYGSTESGAVT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 469 TARQLRTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCL-GYLNNPLQTAEryLDlslpngqslRA--Y 545
Cdd:PRK12406 313 FATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE--ID---------RGgfI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 546 RTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRILAFLAQPQEEQPGAA------ 618
Cdd:PRK12406 382 TSGDVGYLDADGyLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATldeadi 461
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1957676271 619 REALKAHamqfLPDYMQPTAWTELASMPFASNGKVDRKALLE 660
Cdd:PRK12406 462 RAQLKAR----LAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
191-659 |
6.40e-14 |
|
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: 75.80 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGplVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQRQQYI 270
Cdd:cd12118 19 DRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGD--TVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 271 LENAGAVLLLHDGEHPLSEtmpgLDISGidisdvNLDQPLmrQRPDLDAPCMAL-YTSGTTGHPKGVLLSQ-----ANLA 344
Cdd:cd12118 97 LRHSEAKVLFVDREFEYED----LLAEG------DPDFEW--IPPADEWDPIALnYTSGTTGRPKGVVYHHrgaylNALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 345 HFTAWYADY--VQLTeqsrvlqfsslsfdssLIDIF----------PTLLQGAELIVPNedqrRDPLQLVELIRHQRLSH 412
Cdd:cd12118 165 NILEWEMKQhpVYLW----------------TLPMFhcngwcfpwtVAAVGGTNVCLRK----VDAKAIYDLIEKHKVTH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 413 AFLPPALLSIL----PLDQLQILD--HVMTGGDVCEPYVIEQLTRQG-NLYNLYGPTEATVLITAR-----------QLR 474
Cdd:cd12118 225 FCGAPTVLNMLanapPSDARPLPHrvHVMTAGAPPPAAVLAKMEELGfDVTHVYGLTETYGPATVCawkpewdelptEER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 475 TGDNNRTLGAPIANSQVLILD-ENFQPVAE--QTVGELYIVGPGVCLGYLNNPLQTAEryldlSLPNGQslraYRTGDMA 551
Cdd:cd12118 305 ARLKARQGVRYVGLEEVDVLDpETMKPVPRdgKTIGEIVFRGNIVMKGYLKNPEATAE-----AFRGGW----FHSGDLA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 552 KWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLaqpqEEQPGA-AREA-LKA 624
Cdd:cd12118 376 VIHPDGyIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKwgevPCAFV----ELKEGAkVTEEeIIA 451
|
490 500 510
....*....|....*....|....*....|....*
gi 1957676271 625 HAMQFLPDYMQPTAwTELASMPFASNGKVdRKALL 659
Cdd:cd12118 452 FCREHLAGFMVPKT-VVFGELPKTSTGKI-QKFVL 484
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
199-652 |
7.93e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 75.33 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 199 GTSLSHRQLHAHSRAIQQRLQPLLDQHQGplVVGICLPKCSVLYAGILAILGSGAVYLPLepSHPLQRQQ--YILENAGA 276
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGD--VVAILLENNPEFFEVYWAARRSGLYYTPI--NWHLTAAEiaYIVDDSGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 277 -VLLLH----DGEHPLSETMP-GLDISGIDISDVNLDQP---LMRQRPDLDAP-----CMALYTSGTTGHPKGVL----- 337
Cdd:PRK08276 85 kVLIVSaalaDTAAELAAELPaGVPLLLVVAGPVPGFRSyeeALAAQPDTPIAdetagADMLYSSGTTGRPKGIKrplpg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 338 -----LSQANLAHFTAWY---ADYVQLTE----QSRVLQFSSlsfdsslidifpTLLQGAELIVPNEdqRRDPLQLVELI 405
Cdd:PRK08276 165 ldpdeAPGMMLALLGFGMyggPDSVYLSPaplyHTAPLRFGM------------SALALGGTVVVME--KFDAEEALALI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 406 RHQRLSHAFLPPA----LLSiLPLDQ-----LQILDHVMTGGDVCEPYVIEQ-LTRQGN-LYNLYGPTEA--TVLITARQ 472
Cdd:PRK08276 231 ERYRVTHSQLVPTmfvrMLK-LPEEVrarydVSSLRVAIHAAAPCPVEVKRAmIDWWGPiIHEYYASSEGggVTVITSED 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 473 LRT--GdnnrTLGAPIAnSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSLpngqslraYRTGDM 550
Cdd:PRK08276 310 WLAhpG----SVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGW--------VTVGDV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 551 AKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH----RRILAfLAQPqeEQPGAAREALKAH 625
Cdd:PRK08276 377 GYLDEDGyLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDeemgERVKA-VVQP--ADGADAGDALAAE 453
|
490 500 510
....*....|....*....|....*....|.
gi 1957676271 626 AMQFLPD----YMQPTAWTELASMPFASNGK 652
Cdd:PRK08276 454 LIAWLRGrlahYKCPRSIDFEDELPRTPTGK 484
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
164-661 |
1.26e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 74.61 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 164 TTAEPWLLQLAQIpmierleqrfiqSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPL-LDQHQgplVVGICLPKCSVLY 242
Cdd:PRK03640 2 ETMPNWLKQRAFL------------TPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALgVKKGD---RVALLMKNGMEMI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 243 AGILAI--LGSGAVYLPLEPSHplQRQQYILENAGAVLLLHDGEHPlSETMPGLDISGIDISDVNLDQPLMRQRPDLDAP 320
Cdd:PRK03640 67 LVIHALqqLGAVAVLLNTRLSR--EELLWQLDDAEVKCLITDDDFE-AKLIPGISVKFAELMNGPKEEAEIQEEFDLDEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 321 CMALYTSGTTGHPKGVLLSQANlaHFtaWYADYVQL----TEQSRVLqfsslsfdsSLIDIF----------------PT 380
Cdd:PRK03640 144 ATIMYTSGTTGKPKGVIQTYGN--HW--WSAVGSALnlglTEDDCWL---------AAVPIFhisglsilmrsviygmRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 381 LLQgaelivpnedQRRDPLQLVELIRHQRLSHAFLPPALLSIL--PLDQLQILDHVMT---GGDVCEPYVIEQLTRQG-N 454
Cdd:PRK03640 211 VLV----------EKFDAEKINKLLQTGGVTIISVVSTMLQRLleRLGEGTYPSSFRCmllGGGPAPKPLLEQCKEKGiP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 455 LYNLYGPTEatvliTARQLRTGDNNRTL------GAPIANSQVLILDeNFQPVAEQTVGELYIVGPGVCLGYLNNPLQTA 528
Cdd:PRK03640 281 VYQSYGMTE-----TASQIVTLSPEDALtklgsaGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 529 EryldlSLPNGQslraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV-ID-------P 599
Cdd:PRK03640 355 E-----TFQDGW----FKTGDIGYLDEEGfLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVgVPddkwgqvP 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957676271 600 HrrilAFLAQPQEeqpgAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLEL 661
Cdd:PRK03640 426 V----AFVVKSGE----VTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
324-654 |
1.80e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 73.19 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 324 LYTSGTTGHPKGVLLSQAN--LAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFP------------TLLQGAELIV 389
Cdd:cd05924 9 LYTGGTTGMPKGVMWRQEDifRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPlmhgtgswtafgGLLGGQTVVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 390 PneDQRRDPLQLVELI-RHQRLS-----HAFLPP---ALLSILPLDqLQILDHVMTGGDVCEPYVIEQLTR---QGNLYN 457
Cdd:cd05924 89 P--DDRFDPEEVWRTIeKHKVTSmtivgDAMARPlidALRDAGPYD-LSSLFAISSGGALLSPEVKQGLLElvpNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 458 LYGPTEATVLITARQLRTGDNNRTlgAPIANSQVLILDENFQPVAEQTVGELYIVGPG-VCLGYLNNPLQTAERYLDLsl 536
Cdd:cd05924 166 AFGSSETGFTGSGHSAGSGPETGP--FTRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTAETFPEV-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 537 pNGQslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR---ILAFLAQpQE 612
Cdd:cd05924 242 -DGV--RYAVPGDRATVEADGtVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERwgqEVVAVVQ-LR 317
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1957676271 613 EQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVD 654
Cdd:cd05924 318 EGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
192-658 |
6.13e-13 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 72.87 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 192 RPALNIAGTSLSHRQLHAHSRAIQQRLQPLldQHQGPLVVGIClpkCSVLYAGILAILGS---GAVYLPLEPSHPLQRQQ 268
Cdd:PRK13382 59 RPGLIDELGTLTWRELDERSDALAAALQAL--PIGEPRVVGIM---CRNHRGFVEALLAAnriGADILLLNTSFAGPALA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 269 YILENAGAVLLLHDGEhpLSETMPG--------------LDISGIDISDVNLDQPLMRQRPDLDAPC-MALYTSGTTGHP 333
Cdd:PRK13382 134 EVVTREGVDTVIYDEE--FSATVDRaladcpqatrivawTDEDHDLTVEVLIAAHAGQRPEPTGRKGrVILLTSGTTGTP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 334 KGVLLSQA-------NLAHFTAWYAdyvqltEQSRVLQFSSLSFDSslidiFPTLLQGAELIVPNEDQRR-DPLQLVELI 405
Cdd:PRK13382 212 KGARRSGPggigtlkAILDRTPWRA------EEPTVIVAPMFHAWG-----FSQLVLAASLACTIVTRRRfDPEATLDLI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 406 -RHQRLSHAFLPPALLSILPLDQlQILDH--------VMTGGDVCEP-YVIEQLTRQGN-LYNLYGPTEATVLITA--RQ 472
Cdd:PRK13382 281 dRHRATGLAVVPVMFDRIMDLPA-EVRNRysgrslrfAAASGSRMRPdVVIAFMDQFGDvIYNNYNATEAGMIATAtpAD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 473 LRTGDNnrTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNplqTAERYLDLSLPngqslrayrTGDMAK 552
Cdd:PRK13382 360 LRAAPD--TAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDFHDGFMA---------SGDVGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 553 WTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAV--VIDPH--RRILAFLAqpQEEQPGAAREALKAHAM 627
Cdd:PRK13382 426 LDENGrLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVigVDDEQygQRLAAFVV--LKPGASATPETLKQHVR 503
|
490 500 510
....*....|....*....|....*....|.
gi 1957676271 628 QFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PRK13382 504 DNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
191-653 |
1.13e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 72.12 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSraiqQRLQPLLDQHQ---GPLVVGICLPKCSVLYAgILAILGSGAVYLPLEPSHPLQRQ 267
Cdd:PRK07786 32 DAPALRFLGNTTTWRELDDRV----AALAGALSRRGvgfGDRVLILMLNRTEFVES-VLAANMLGAIAVPVNFRLTPPEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 268 QYILENAGA-VLLLHDGEHPLS----ETMPGLDISGI-----DISDVNLDQPLMRQRPDL-------DAPCMALYTSGTT 330
Cdd:PRK07786 107 AFLVSDCGAhVVVTEAALAPVAtavrDIVPLLSTVVVaggssDDSVLGYEDLLAEAGPAHapvdipnDSPALIMYTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 331 GHPKGVLLSQANLA-----HFTAWYADyvqlTEQSRVLQFSSLSFDSSLIDIFPTLLQGAElIVPNEDQRRDPLQLVELI 405
Cdd:PRK07786 187 GRPKGAVLTHANLTgqamtCLRTNGAD----INSDVGFVGVPLFHIAGIGSMLPGLLLGAP-TVIYPLGAFDPGQLLDVL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 406 RHQRLSHAFLPPALLSILPLDQ--------LQILDHvmtGGDVCEPYVIEQLTR---QGNLYNLYGPTEATVlITArQLR 474
Cdd:PRK07786 262 EAEKVTGIFLVPAQWQAVCAEQqarprdlaLRVLSW---GAAPASDTLLRQMAAtfpEAQILAAFGQTEMSP-VTC-MLL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 475 TGDNNRTLGA---PIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAEryldlSLPNGQslraYRTGDMA 551
Cdd:PRK07786 337 GEDAIRKLGSvgkVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAE-----AFAGGW----FHSGDLV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 552 KWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR---ILAFLAQPQEEQPGAAREALKAHAM 627
Cdd:PRK07786 408 RQDEEGyVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwgeVPVAVAAVRNDDAALTLEDLAEFLT 487
|
490 500
....*....|....*....|....*.
gi 1957676271 628 QFLPDYMQPTAWTELASMPFASNGKV 653
Cdd:PRK07786 488 DRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
447-658 |
1.40e-12 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 71.62 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 447 EQLTRQgNLYNLYGPTEATVLITARQLRTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQ 526
Cdd:PRK08974 346 VKLTGQ-YLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 527 TAERYLDLSLpngqslrayRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH----R 601
Cdd:PRK08974 425 TDEVIKDGWL---------ATGDIAVMDEEGfLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSevsgE 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1957676271 602 RILAFLAQpqeEQPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PRK08974 496 AVKIFVVK---KDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
274-582 |
1.48e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 71.57 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 274 AGAVLLlhdGE--HPLSETMPGLDISGIDISDVNLDQPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYA 351
Cdd:PRK07768 109 AKAVVV---GEpfLAAAPVLEEKGIRVLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 352 DYVQLTEQSRVLqfsslsfdsslIDIFPT-------------LLQGAELI-VPNEDQRRDPLQLVELIRHQRLSHAFLPP 417
Cdd:PRK07768 186 VAAEFDVETDVM-----------VSWLPLfhdmgmvgfltvpMYFGAELVkVTPMDFLRDPLLWAELISKYRGTMTAAPN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 418 ALLSIL-----------PLDqLQILDHVMTGGDVCEPYVIEQLTRQGNLYNL--------YGPTEATV------------ 466
Cdd:PRK07768 255 FAYALLarrlrrqakpgAFD-LSSLRFALNGAEPIDPADVEDLLDAGARFGLrpeailpaYGMAEATLavsfspcgaglv 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 467 -------LITARQL---RTGDNNR---TLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLN----NPLQTAE 529
Cdd:PRK07768 334 vdevdadLLAALRRavpATKGNTRrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLTmdgfIPAQDAD 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1957676271 530 RYLDlslpngqslrayrTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIER 582
Cdd:PRK07768 414 GWLD-------------TGDLGYLTEEGeVVVCGRVKDVIIMAGRNIYPTDIER 454
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
246-632 |
7.20e-12 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 69.42 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 246 LAILGSGAVYLPLEPSHPLQRQQYILENAGAVLL----LHD--------GEHPLSETMPGLDISGID--ISDVNLDQPLM 311
Cdd:cd05932 49 LAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALfvgkLDDwkamapgvPEGLISISLPPPSAANCQyqWDDLIAQHPPL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 312 RQRPDLDAPCMA--LYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIV 389
Cdd:cd05932 129 EERPTRFPEQLAtlIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 390 --------PNEDQRRDPLQLVELIR----HQRLSHAFLPPA----LLSI--------------LPLDQLQILdhvMTGGD 439
Cdd:cd05932 209 faesldtfVEDVQRARPTLFFSVPRlwtkFQQGVQDKIPQQklnlLLKIpvvnslvkrkvlkgLGLDQCRLA---GCGSA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 440 VCEPYVIEQLTRQG-NLYNLYGPTE----ATVLITARQlRTGdnnrTLGAPIANSQVLILDEnfqpvaeqtvGELYIVGP 514
Cdd:cd05932 286 PVPPALLEWYRSLGlNILEAYGMTEnfaySHLNYPGRD-KIG----TVGNAGPGVEVRISED----------GEILVRSP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 515 GVCLGYLNNPLQTAERYLDLSLpngqslraYRTGDMAKWTSDG-IELCGR-RDNQVKIRGFRVEPEEIERCLRDSQRYRQ 592
Cdd:cd05932 351 ALMMGYYKDPEATAEAFTADGF--------LRTGDKGELDADGnLTITGRvKDIFKTSKGKYVAPAPIENKLAEHDRVEM 422
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1957676271 593 VAVVID--PHRRILAFL-AQPQEEQPGAAREALKAHAMQFLPD 632
Cdd:cd05932 423 VCVIGSglPAPLALVVLsEEARLRADAFARAELEASLRAHLAR 465
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
178-746 |
1.09e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.81 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 178 MIERLEQRFIQSAERPALNI------AGTSLSHRQLHAHSR----AIQQRLQP----LLDQHQGPLVVGICLpkcSVLYA 243
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARtiaaALQARASFgdraVLLFPSGPDYVAAFF---GCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 244 GILAIlgsgAVYLPlEPS--HPLQRQQYILENAGAVLLLHDGEhpLSETMPGLD-ISGIDISDV----NLDQPLMR--QR 314
Cdd:PRK05691 88 GVIAV----PAYPP-ESArrHHQERLLSIIADAEPRLLLTVAD--LRDSLLQMEeLAAANAPELlcvdTLDPALAEawQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 315 PDLDAPCMAL--YTSGTTGHPKGVLLSQANLAH------------------FTAWYADYVQLTEQSRVLQFsslsfdssl 374
Cdd:PRK05691 161 PALQPDDIAFlqYTSGSTALPKGVQVSHGNLVAneqlirhgfgidlnpddvIVSWLPLYHDMGLIGGLLQP--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 375 idIF---PTLLqgaelIVPNEDQRRdPLQLVELIRHQ------------RLSHAFLPPALLSILPLDQLQIldhVMTGGd 439
Cdd:PRK05691 232 --IFsgvPCVL-----MSPAYFLER-PLRWLEAISEYggtisggpdfayRLCSERVSESALERLDLSRWRV---AYSGS- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 440 vcEPYVIEQLTR-----------QGNLYNLYGPTEATVLITARQ-------LRTGDN----NR----------TLGAPIA 487
Cdd:PRK05691 300 --EPIRQDSLERfaekfaacgfdPDSFFASYGLAEATLFVSGGRrgqgipaLELDAEalarNRaepgtgsvlmSCGRSQP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 488 NSQVLILD-ENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLslpNGQSLraYRTGDMAKWTSDGIELCGRRDN 566
Cdd:PRK05691 378 GHAVLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEH---DGRTW--LRTGDLGFLRDGELFVTGRLKD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 567 QVKIRGFRVEPEEIERCLRdsqryRQVAVVidPHRRILAFLAQPQ-EEQPGAARE-------ALKAHAM-----QFLPDY 633
Cdd:PRK05691 453 MLIVRGHNLYPQDIEKTVE-----REVEVV--RKGRVAAFAVNHQgEEGIGIAAEisrsvqkILPPQALiksirQAVAEA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 634 MQPT----AWTELASMPFASNGKVDRKAL-------------LELPVNVTENSQRRLPVSADEALLLEIWAELLELPAsd 696
Cdd:PRK05691 526 CQEApsvvLLLNPGALPKTSSGKLQRSACrlrladgsldsyaLFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQ-- 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1957676271 697 ISTDESFFNLGGHSILLSRMLLRLREEFGRSISINRFIELPTIAKLATLV 746
Cdd:PRK05691 604 VAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAV 653
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
198-658 |
1.51e-11 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 68.33 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 198 AGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPlVVGICLPKCSVLYAGILAILGSGAVYLPLEPSHPLQ--RQQYILENAG 275
Cdd:PLN02574 63 TGFSISYSELQPLVKSMAAGLYHVMGVRQGD-VVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGeiKKRVVDCSVG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 276 AVLLLHDGehplSETMPGLDISGIDISD-VNLDQ---------PLMRQRPDldaPCMA-----------LYTSGTTGHPK 334
Cdd:PLN02574 142 LAFTSPEN----VEKLSPLGVPVIGVPEnYDFDSkriefpkfyELIKEDFD---FVPKpvikqddvaaiMYSSGTTGASK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 335 GVLLSQANLAH----FTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPT--LLQGAELIVPnedQRRDPLQLVELIRHQ 408
Cdd:PLN02574 215 GVVLTHRNLIAmvelFVRFEASQYEYPGSDNVYLAALPMFHIYGLSLFVVglLSLGSTIVVM---RRFDASDMVKVIDRF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 409 RLSH-AFLPPALLSILPLDQ------LQILDHVMTGGDVCEPYVIEQLTR---QGNLYNLYGPTEATVLITaRQLRTGDN 478
Cdd:PLN02574 292 KVTHfPVVPPILMALTKKAKgvcgevLKSLKQVSCGAAPLSGKFIQDFVQtlpHVDFIQGYGMTESTAVGT-RGFNTEKL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 479 NR--TLGAPIANSQVLILD-ENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTaerylDLSLPNGQSLrayRTGDMAKWTS 555
Cdd:PLN02574 371 SKysSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKAT-----QSTIDKDGWL---RTGDIAYFDE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 556 DG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRI----LAFLAQPQEEqpGAAREALKAHAMQFL 630
Cdd:PLN02574 443 DGyLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECgeipVAFVVRRQGS--TLSQEAVINYVAKQV 520
|
490 500
....*....|....*....|....*...
gi 1957676271 631 PDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PLN02574 521 APYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
318-582 |
2.02e-11 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 68.00 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 318 DAPCMALYTSGTTGHPKGVLLSQANL-AHFTAWYADYvqlteqsrvlqfsslSFDSSLIDI--FP-----TLLQGAELIV 389
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFeAQIEALREDY---------------GIEPGEIDLptFPlfalfGPALGMTSVI 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 390 PNEDQRR----DPLQLVELIRHQRLSHAFLPPALLSIL---------PLDQLQildHVMTGGDVCEPYVIEQLTR----Q 452
Cdd:PRK09274 239 PDMDPTRpatvDPAKLFAAIERYGVTNLFGSPALLERLgrygeangiKLPSLR---RVISAGAPVPIAVIERFRAmlppD 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 453 GNLYNLYGPTEATVL--ITARQLRTGDNNRT-------LGAPIANSQVLILD---------ENFQPVAEQTVGELYIVGP 514
Cdd:PRK09274 316 AEILTPYGATEALPIssIESREILFATRAATdngagicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGP 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1957676271 515 GVCLGYLNNPLQTAERyldlSLPNGQSLRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIER 582
Cdd:PRK09274 396 MVTRSYYNRPEATRLA----KIPDGQGDVWHRMGDLGYLDAQGrLWFCGRKAHRVETAGGTLYTIPCER 460
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
192-658 |
2.20e-11 |
|
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: 67.50 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 192 RPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPLVvGICLPKCSVLYAGILAILGSGAVYLPLEPShpLQRQQ--Y 269
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRV-LLRGSNSPELVACWFGIQKAGAIAVATMPL--LRPKElaY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 270 ILENAGAVLLLHDGEHPLSEtmpgldisgiDIsdvnldqplmrqrpdldapCMALYTSGTTGHPKGVLLSQAN-LAHFTA 348
Cdd:cd05958 78 ILDKARITVALCAHALTASD----------DI-------------------CILAFTSGTTGAPKATMHFHRDpLASADR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 349 WYADYVQLTEQSRVLQFSSLSFD--SSLIDIFPTLLQGAELIVPnedqRRDPLQLVELIRHQRLSHAFLPP----ALLSI 422
Cdd:cd05958 129 YAVNVLRLREDDRFVGSPPLAFTfgLGGVLLFPFGVGASGVLLE----EATPDLLLSAIARYKPTVLFTAPtayrAMLAH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 423 LPLDQ--LQILDHVMTGGDVCEPYVIEQLTRQG--NLYNLYGPTEAT-VLITAR--QLRTGdnnrTLGAPIANSQVLILD 495
Cdd:cd05958 205 PDAAGpdLSSLRKCVSAGEALPAALHRAWKEATgiPIIDGIGSTEMFhIFISARpgDARPG----ATGKPVPGYEAKVVD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 496 ENFQPVAEQTVGELYIVGPGVCLgYLNNPLQtaERYLDlslpNGQSLrayrTGDMAKWTSDG-IELCGRRDNQVKIRGFR 574
Cdd:cd05958 281 DEGNPVPDGTIGRLAVRGPTGCR-YLADKRQ--RTYVQ----GGWNI----TGDTYSRDPDGyFRHQGRSDDMIVSGGYN 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 575 VEPEEIERCLRDSQRYRQVAVV--IDPHRRIL--AFLAQPQEEQPGAA-REALKAHAMQFLPDYMQPTAWTELASMPFAS 649
Cdd:cd05958 350 IAPPEVEDVLLQHPAVAECAVVghPDESRGVVvkAFVVLRPGVIPGPVlARELQDHAKAHIAPYKYPRAIEFVTELPRTA 429
|
....*....
gi 1957676271 650 NGKVDRKAL 658
Cdd:cd05958 430 TGKLQRFAL 438
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
246-635 |
3.22e-11 |
|
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: 67.08 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 246 LAILGSGAVYLPLEPSHPLQRQQYILENAGAVLLLhdgehplsetmpgldisgidISDvNLDQPLMrqrpdldapcmaLY 325
Cdd:cd05914 50 FAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF--------------------VSD-EDDVALI------------NY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 326 TSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFdsslidIFPTLLQG------------------AEL 387
Cdd:cd05914 97 TSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHH------IYPLTFTLllpllngahvvfldkipsAKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 388 IVPNEDQRRDPLQL-VELIRHQRLSHAFLPPALLSIL------PLDQLQI---------------LDHVMTGGDVCEPYV 445
Cdd:cd05914 171 IALAFAQVTPTLGVpVPLVIEKIFKMDIIPKLTLKKFkfklakKINNRKIrklafkkvheafggnIKEFVIGGAKINPDV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 446 IEQLTRQGNLYNL-YGPTEATVLITArqlrTGDNNRTL---GAPIANSQVLILDENfqPVAEQtvGELYIVGPGVCLGYL 521
Cdd:cd05914 251 EEFLRTIGFPYTIgYGMTETAPIISY----SPPNRIRLgsaGKVIDGVEVRIDSPD--PATGE--GEIIVRGPNVMKGYY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 522 NNPLQTAERYldlsLPNGQslraYRTGDMAKWTSDG-IELCGRRDNQ-VKIRGFRVEPEEIERCLRDS----------QR 589
Cdd:cd05914 323 KNPEATAEAF----DKDGW----FHTGDLGKIDAEGyLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMpfvleslvvvQE 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1957676271 590 YRQVA-VVIDPHRRILAFLAQPQEEQpgAAREALKAHAMQFLPDYMQ 635
Cdd:cd05914 395 KKLVAlAYIDPDFLDVKALKQRNIID--AIKWEVRDKVNQKVPNYKK 439
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
459-661 |
3.43e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 67.15 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 459 YGPTEATVLITARQLRTGDNNRTLGAPIANSQVLILDE--NFQPVAEQtvGELYIVGPGVCLGYLNNPLQTAEryldlsl 536
Cdd:PRK12492 365 YGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDdgNELPLGER--GELCIKGPQVMKGYWQQPEATAE------- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 537 pngqSLRA---YRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR---ILAFLAQ 609
Cdd:PRK12492 436 ----ALDAegwFKTGDIAVIDPDGfVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERsgeAVKLFVV 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1957676271 610 PQEeqPGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLEL 661
Cdd:PRK12492 512 ARD--PGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
177-600 |
6.38e-11 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 66.05 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 177 PMIERLEQRFiQSAERPALNI-AGTSLSHRQLHAHSRAIQQRLQPLldqhqgPLVVGICL-------PKCSVLYagiLAI 248
Cdd:PRK07514 4 NLFDALRAAF-ADRDAPFIETpDGLRYTYGDLDAASARLANLLVAL------GVKPGDRVavqveksPEALALY---LAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 249 LGSGAVYLPLEPSHPLQRQQYILENAGAVLLLHDG--EHPLSETMPGLDISGIDISDVNLDQPLM---RQRPDL--DAPC 321
Cdd:PRK07514 74 LRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPanFAWLSKIAAAAGAPHVETLDADGTGSLLeaaAAAPDDfeTVPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 322 MA------LYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQfsslsfdssLIDIFPT----------LLQGA 385
Cdd:PRK07514 154 GAddlaaiLYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIH---------ALPIFHThglfvatnvaLLAGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 386 ELI----------------------VPN------EDQRRDPlqlvELIRHQRLSHAFLPPALLSIlpldqlqildHV--- 434
Cdd:PRK07514 225 SMIflpkfdpdavlalmpratvmmgVPTfytrllQEPRLTR----EAAAHMRLFISGSAPLLAET----------HRefq 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 435 -MTGGDVCEpyvieqltRqgnlynlYGPTEaTVLITARQLrtgDNNR---TLGAPIANSQVLILD-ENFQPVAEQTVGEL 509
Cdd:PRK07514 291 eRTGHAILE--------R-------YGMTE-TNMNTSNPY---DGERragTVGFPLPGVSLRVTDpETGAELPPGEIGMI 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 510 YIVGPGVCLGYLNNPLQTAEryldlslpngqSLRA---YRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLR 585
Cdd:PRK07514 352 EVKGPNVFKGYWRMPEKTAE-----------EFRAdgfFITGDLGKIDERGyVHIVGRGKDLIISGGYNVYPKEVEGEID 420
|
490
....*....|....*
gi 1957676271 586 DSQRYRQVAVVIDPH 600
Cdd:PRK07514 421 ELPGVVESAVIGVPH 435
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
320-655 |
1.31e-10 |
|
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: 64.20 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 320 PCMALYTSGTTGHPKGVLLSqanlaHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFP-----TLLQGAELIVPNEDq 394
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLA-----NKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGlwwilTCLIHGGLCVTGGE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 395 RRDPLQLVELIRHQRLSHAFLPPALLSILPL---DQLQI---LDHVMTGGDvcepYVIE------QLTRQGNLYNLYGPT 462
Cdd:cd17635 77 NTTYKSLFKILTTNAVTTTCLVPTLLSKLVSelkSANATvpsLRLIGYGGS----RAIAadvrfiEATGLTNTAQVYGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 463 EATvliTARQLRTGDNNRTLGA---PIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDlslpng 539
Cdd:cd17635 153 ETG---TALCLPTDDDSIEINAvgrPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLID------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 540 qslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLAQPQEEQ 614
Cdd:cd17635 224 ---GWVNTGDLGERREDGfLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEfgelVGLAVVASAELD 300
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1957676271 615 PGAAReALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDR 655
Cdd:cd17635 301 ENAIR-ALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
165-658 |
1.72e-10 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 65.04 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 165 TAEPWLLQL-----AQIP------MIERLEQRFIQSAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQhQGPLVvGI 233
Cdd:PRK07059 1 MEKIWLKSYppgvpAEIDasqypsLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLA-KGARV-AI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 234 CLPkcSVLY--AGILAILGSGAV-------YLPLEPSHPLQ----RQQYILEN----AGAVLLLHDGEHPLSETMPglDI 296
Cdd:PRK07059 79 MMP--NVLQypVAIAAVLRAGYVvvnvnplYTPRELEHQLKdsgaEAIVVLENfattVQQVLAKTAVKHVVVASMG--DL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 297 SGIDISDVNL--------------------------DQPLMRQRPDLDAPCMAL--YTSGTTGHPKGVLLSQANLAhfta 348
Cdd:PRK07059 155 LGFKGHIVNFvvrrvkkmvpawslpghvrfndalaeGARQTFKPVKLGPDDVAFlqYTGGTTGVSKGATLLHRNIV---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 349 wyadyvqlteqSRVLQFSS----LSFDSSLIDIFPTL--------------------LQGAELIVPNEdqrRD-PLQLVE 403
Cdd:PRK07059 231 -----------ANVLQMEAwlqpAFEKKPRPDQLNFVcalplyhifaltvcgllgmrTGGRNILIPNP---RDiPGFIKE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 404 LIRHQrlSHAF-----LPPALLSILPLDQLQILDHVMTGGD---VCEPyVIEQ-LTRQG-NLYNLYGPTEATVLITARQL 473
Cdd:PRK07059 297 LKKYQ--VHIFpavntLYNALLNNPDFDKLDFSKLIVANGGgmaVQRP-VAERwLEMTGcPITEGYGLSETSPVATCNPV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 474 RTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAEryldLSLPNGqslrAYRTGDMAKW 553
Cdd:PRK07059 374 DATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAK----VMTADG----FFRTGDVGVM 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 554 TSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAV--VIDPH--RRILAFLAQpqeEQPGAAREALKAHAMQ 628
Cdd:PRK07059 446 DERGyTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAvgVPDEHsgEAVKLFVVK---KDPALTEEDVKAFCKE 522
|
570 580 590
....*....|....*....|....*....|
gi 1957676271 629 FLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PRK07059 523 RLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
316-663 |
2.21e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 64.79 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 316 DLDAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSR-VLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDq 394
Cdd:PRK12583 199 DRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRlCVPVPLYHCFGMVLANLGCMTVGACLVYPNEA- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 395 rRDPLQLVELIRHQRLSHAFLPPALLsILPLDQLQI----LDHVMTG---GDVCEPYVIEQLTRQGNLYNL---YGPTEA 464
Cdd:PRK12583 278 -FDPLATLQAVEEERCTALYGVPTMF-IAELDHPQRgnfdLSSLRTGimaGAPCPIEVMRRVMDEMHMAEVqiaYGMTET 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 465 T--VLITAR----QLRTGDNNRTLgaPIANSQVLILDENFQPVAEqtVGELYIVGPGVCLGYLNNPLQTAERyLDlslPN 538
Cdd:PRK12583 356 SpvSLQTTAaddlERRVETVGRTQ--PHLEVKVVDPDGATVPRGE--IGELCTRGYSVMKGYWNNPEATAES-ID---ED 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 539 GQslraYRTGDMAKWTSDG-IELCGRRDNQVkIRGFR-VEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLaqpqE 612
Cdd:PRK12583 428 GW----MHTGDLATMDEQGyVRIVGRSKDMI-IRGGEnIYPREIEEFLFTHPAVADVQVFGVPDEKygeeIVAWV----R 498
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1957676271 613 EQPG--AAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLELPV 663
Cdd:PRK12583 499 LHPGhaASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISI 551
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
679-748 |
2.59e-10 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 57.56 E-value: 2.59e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1957676271 679 EALLLEIWAELLELPASDISTDESFFN-LGGHSILLSRMLLRLREEFGRSISINRFIELPTIAKLATLVRG 748
Cdd:COG0236 7 EERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
325-658 |
2.60e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 64.42 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 325 YTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVpnedQRR-DPLQLVE 403
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHL----MRKfIPNQVLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 404 LIRHQRLSHAFLPPALLSILpLDQLQILDHVMT----GGDVCEPYViEQLTRQ---GNLYNLYGPTEATvLITArqLRTG 476
Cdd:PRK07638 226 KLETENISVMYTVPTMLESL-YKENRVIENKMKiissGAKWEAEAK-EKIKNIfpyAKLYEFYGASELS-FVTA--LVDE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 477 DNNR---TLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNnplqtaerylDLSLPNGQSLRAYRT-GDMAK 552
Cdd:PRK07638 301 ESERrpnSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYII----------GGVLARELNADGWMTvRDVGY 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 553 WTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH----RRILAFLAQpqeeqpGAAREALKAHAM 627
Cdd:PRK07638 371 EDEEGfIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDsywgEKPVAIIKG------SATKQQLKSFCL 444
|
330 340 350
....*....|....*....|....*....|.
gi 1957676271 628 QFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PRK07638 445 QRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
304-660 |
2.84e-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: 64.44 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 304 VNLDQPLMRQRPDL-----------DAPCMALYTSGTTGHPKGVLLSQA-NLAHF-TAWYadYVQLTEQSRVLQFSSLSF 370
Cdd:cd05970 160 IDFRKLIKNASPDFerptansypcgEDILLVYFSSGTTGMPKMVEHDFTyPLGHIvTAKY--WQNVREGGLHLTVADTGW 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 371 DSSLI-DIFPTLLQGAELIVPNEDqRRDPLQLVELIRHQRLSHAFLPPALLSILPLDQLQ-----ILDHVMTGGDVCEPY 444
Cdd:cd05970 238 GKAVWgKIYGQWIAGAAVFVYDYD-KFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSrydlsSLRYCTTAGEALNPE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 445 VIEQLTRQG--NLYNLYGPTEATVLITA---RQLRTGdnnrTLGAPIANSQVLILDENFQPVAEQTVGELYI-----VGP 514
Cdd:cd05970 317 VFNTFKEKTgiKLMEGFGQTETTLTIATfpwMEPKPG----SMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskgKPV 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 515 GVCLGYLNNPLQTAERYLDlslpngqslRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQV 593
Cdd:cd05970 393 GLFGGYYKDAEKTAEVWHD---------GYYHTGDAAWMDEDGyLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLEC 463
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957676271 594 AV--VIDPHR--RILAFLAQPQEEQPGAA-REALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLE 660
Cdd:cd05970 464 AVtgVPDPIRgqVVKATIVLAKGYEPSEElKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
324-661 |
7.56e-10 |
|
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: 62.93 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 324 LYTSGTTGHPKGVLLSQANL-AHFTAWYADYV--QLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQ 400
Cdd:cd17642 190 MNSSGSTGLPKGVQLTHKNIvARFSHARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFLR 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 401 LVElirHQRLSHAFLPPALLSILP----LDQ--LQILDHVMTGGDVCEPYVIEQLTRQGNLYNL---YGPTEATVLItar 471
Cdd:cd17642 270 SLQ---DYKVQSALLVPTLFAFFAkstlVDKydLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIrqgYGLTETTSAI--- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 472 qLRTGDNNRTLGA-----PIANSQVLILDENFQPVAEQTvGELYIVGPGVCLGYLNNPLQTAEryldLSLPNGQslraYR 546
Cdd:cd17642 344 -LITPEGDDKPGAvgkvvPFFYAKVVDLDTGKTLGPNER-GELCVKGPMIMKGYVNNPEATKA----LIDKDGW----LH 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 547 TGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVidphrrilaflAQPQE---EQPGA----- 617
Cdd:cd17642 414 SGDIAYYDEDGhFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVA-----------GIPDEdagELPAAvvvle 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1957676271 618 -AREALKAHAMQFLPDYMQPTAWTE-----LASMPFASNGKVDRKALLEL 661
Cdd:cd17642 483 aGKTMTEKEVMDYVASQVSTAKRLRggvkfVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
191-658 |
1.00e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 62.39 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQhQGPLVVGICL---PKCSVLYAGilAILgSGAVYLPLEPSH---PL 264
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLDP-TRPPHVGVLLdntPEFSLLLGA--AAL-SGIVPVGLNPTRrgaAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 265 QRQqyiLENAGAVLLLHDGEHplSETMPGLDiSGIDISDV-----------NLDQPLMRQRPDLDAPCMALYTSGTTGHP 333
Cdd:PRK07867 94 ARD---IAHADCQLVLTESAH--AELLDGLD-PGVRVINVdspawadelaaHRDAEPPFRVADPDDLFMLIFTSGTSGDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 334 KGVLLSQANLA--------HFTAWYADYVQLT----EQSRVLQfsslsfdssliDIFPTLLQGAELIVPnedQRRDPLQL 401
Cdd:PRK07867 168 KAVRCTHRKVAsagvmlaqRFGLGPDDVCYVSmplfHSNAVMA-----------GWAVALAAGASIALR---RKFSASGF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 402 VELIRHQRLSHA-FLPPALLSIL-----PLDQLQILdHVMTGGDVCEPYVIEQLTRQG-NLYNLYGPTEATVLITarqlR 474
Cdd:PRK07867 234 LPDVRRYGATYAnYVGKPLSYVLatperPDDADNPL-RIVYGNEGAPGDIARFARRFGcVVVDGFGSTEGGVAIT----R 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 475 TGDN-NRTLGAPIANSQVL-----------ILDENFQPVAEQTVGELY-IVGPGVCLGYLNNPLQTAERyldlsLPNGQs 541
Cdd:PRK07867 309 TPDTpPGALGPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAER-----MRGGV- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 542 lraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAV--VIDPH--RRILAFLAQpqeeQPG 616
Cdd:PRK07867 383 ---YWSGDLAYRDADGyAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVyaVPDPVvgDQVMAALVL----APG 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1957676271 617 AAREALKAHAmqFL---PDyMQPTAWTEL----ASMPFASNGKVDRKAL 658
Cdd:PRK07867 456 AKFDPDAFAE--FLaaqPD-LGPKQWPSYvrvcAELPRTATFKVLKRQL 501
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
325-658 |
1.06e-09 |
|
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: 61.73 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 325 YTSGTTGHPKGVLLSQANLAhFTAWYADYVQLTEQSRVLQFSSLSFDSSLIdiFPTLL----QGAELIVPNEDQRRDPL- 399
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEV-YNAWMLALNSLFDPDDVLLCGLPLFHVNGS--VVTLLtplaSGAHVVLAGPAGYRNPGl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 400 --QLVELIRHQRLSHAFLPPALLSIL---PLD-QLQILDHVMTGGDVCEPYVIEQLTRQGNLYNL--YGPTEATVLIT-- 469
Cdd:cd05944 86 fdNFWKLVERYRITSLSTVPTVYAALlqvPVNaDISSLRFAMSGAAPLPVELRARFEDATGLPVVegYGLTEATCLVAvn 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 470 --ARQLRTGdnnrTLGAPIANSQVLILDEN-----FQPVAEQTVGELYIVGPGVCLGYLNNplqtaERYLDLSLPNGQsl 542
Cdd:cd05944 166 ppDGPKRPG----SVGLRLPYARVRIKVLDgvgrlLRDCAPDEVGEICVAGPGVFGGYLYT-----EGNKNAFVADGW-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 543 raYRTGDMAKWTSDG-IELCGRRDNQVkIR-GFRVEPEEIERCLrdsQRYRQVAVVI-----DPHRRIL--AFLaqpqEE 613
Cdd:cd05944 235 --LNTGDLGRLDADGyLFITGRAKDLI-IRgGHNIDPALIEEAL---LRHPAVAFAGavgqpDAHAGELpvAYV----QL 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1957676271 614 QPGA--AREALKAHAMQFLPDYMQ-PTAWTELASMPFASNGKVDRKAL 658
Cdd:cd05944 305 KPGAvvEEEELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
680-740 |
1.14e-09 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 55.26 E-value: 1.14e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1957676271 680 ALLLEIWAELLELPASDISTDESFFNLGGHSILLSRMLLRLREEFGRSISINRFIELPTIA 740
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
184-658 |
2.15e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 61.32 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 184 QRFiqsAERPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDQHQGPLVvGICLPKC--------SVLYAGiLAILGSGAVY 255
Cdd:PRK05677 35 QRF---ADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRI-AVQLPNVlqypvavfGAMRAG-LIVVNTNPLY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 256 LPLEPSHplqrqQYILENAGAVLLLHDGEHPLSETMPGLDISGIDISDV--------------------------NL--- 306
Cdd:PRK05677 110 TAREMEH-----QFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIVTEVadmlpplkrllinavvkhvkkmvpayHLpqa 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 307 -----------DQPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQANLAhftawyADYVQLTEqsrVLQFSSLSFDSSLI 375
Cdd:PRK05677 185 vkfndalakgaGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLV------ANMLQCRA---LMGSNLNEGCEILI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 376 DIFP-------------TLLQGAE-LIVPNEdqrRDPLQLVELIRHQRLShAF--LPPALLSILPLDQLQILD------- 432
Cdd:PRK05677 256 APLPlyhiyaftfhcmaMMLIGNHnILISNP---RDLPAMVKELGKWKFS-GFvgLNTLFVALCNNEAFRKLDfsalklt 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 433 ---------------HVMTGGDVCEPYvieqltrqgnlynlyGPTEATVLIT---ARQLRTGdnnrTLGAPIANSQVLIL 494
Cdd:PRK05677 332 lsggmalqlataerwKEVTGCAICEGY---------------GMTETSPVVSvnpSQAIQVG----TIGIPVPSTLCKVI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 495 DENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAErYLDlslpngqSLRAYRTGDMAKWTSDG-IELCGRRDNQVKIRGF 573
Cdd:PRK05677 393 DDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDE-ILD-------SDGWLKTGDIALIQEDGyMRIVDRKKDMILVSGF 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 574 RVEPEEIERCLRDSQRYRQVAVVIDPHRR----ILAFLAQPqeeqPGAA--REALKAHAMQFLPDYMQPTAWTELASMPF 647
Cdd:PRK05677 465 NVYPNELEDVLAALPGVLQCAAIGVPDEKsgeaIKVFVVVK----PGETltKEQVMEHMRANLTGYKVPKAVEFRDELPT 540
|
570
....*....|.
gi 1957676271 648 ASNGKVDRKAL 658
Cdd:PRK05677 541 TNVGKILRREL 551
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
297-658 |
4.51e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 60.41 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 297 SGIDISDVNLDQPLMRQRPDL--DAPCMALYTSGTTGHPKGVLLsqANLAHFT----------AWYADYVQLTEQSRVlq 364
Cdd:PRK05857 146 AVTRESEHSLDAASLAGNADQgsEDPLAMIFTSGTTGEPKAVLL--ANRTFFAvpdilqkeglNWVTWVVGETTYSPL-- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 365 fsslsfDSSLID----IFPTLLQGAELIVPNEDQrrdpLQLVELIRHQRLSHAFLPPALLSILpLDQLQILDHVMT---- 436
Cdd:PRK05857 222 ------PATHIGglwwILTCLMHGGLCVTGGENT----TSLLEILTTNAVATTCLVPTLLSKL-VSELKSANATVPslrl 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 437 ---GGDVCEPYVIEQLTRQG-NLYNLYGPTEATVliTARQLRTGDNNRT------LGAPIANSQVLILDEN-FQPVAEQT 505
Cdd:PRK05857 291 vgyGGSRAIAADVRFIEATGvRTAQVYGLSETGC--TALCLPTDDGSIVkieagaVGRPYPGVDVYLAATDgIGPTAPGA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 506 V-----GELYIVGPGVCLGYLNNPLQTAERYLDLSLpngqslrayRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEE 579
Cdd:PRK05857 369 GpsasfGTLWIKSPANMLGYWNNPERTAEVLIDGWV---------NTGDLLERREDGfFYIKGRSSEMIICGGVNIAPDE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 580 IERCLRDSQRYRQVAV--VIDPHRRILAFLAQ-PQEEQPGAAREALK----AHAMQFLPDYMQPTAWTELASMPFASNGK 652
Cdd:PRK05857 440 VDRIAEGVSGVREAACyeIPDEEFGALVGLAVvASAELDESAARALKhtiaARFRRESEPMARPSTIVIVTDIPRTQSGK 519
|
....*.
gi 1957676271 653 VDRKAL 658
Cdd:PRK05857 520 VMRASL 525
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
405-661 |
6.31e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 59.62 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 405 IRHQRLSHAFLPPALLSILPlDQLQIL-----------DHVMTGGDVCEPYVIEQlTRQGNLyNL---YGPTEatvliTA 470
Cdd:PRK07445 196 LKSGQELPPNPSDFFLSLVP-TQLQRLlqlrpqwlaqfRTILLGGAPAWPSLLEQ-ARQLQL-RLaptYGMTE-----TA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 471 RQ---LRTGD---NNRTLGAPIANSQVLIldenfqpvAEQTVGELYIVGPGVCLGYLNNPLQTAeryldlslpngqslRA 544
Cdd:PRK07445 268 SQiatLKPDDflaGNNSSGQVLPHAQITI--------PANQTGNITIQAQSLALGYYPQILDSQ--------------GI 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 545 YRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAV--VIDPH--RRILAFLAqPQEEQPgaAR 619
Cdd:PRK07445 326 FETDDLGYLDAQGyLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVlgLPDPHwgEVVTAIYV-PKDPSI--SL 402
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1957676271 620 EALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLEL 661
Cdd:PRK07445 403 EELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
269-604 |
8.91e-09 |
|
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: 59.54 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 269 YILENAGAVLLLHDgehplsetmPGLDI-SGIDISDVNLDQPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQAN----- 342
Cdd:cd05927 73 YILNHAEISIVFCD---------AGVKVySLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNivsnv 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 343 ------------------------LAH----FTAWYADYV------------QLTEQSRVLQfsslsfdsslidifPTLL 382
Cdd:cd05927 144 agvfkileilnkinptdvyisylpLAHiferVVEALFLYHgakigfysgdirLLLDDIKALK--------------PTVF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 383 QGaeliVP-----------NEDQRRDPLQ-----------LVELIRHQRLSHAFLPPALLSILpldQLQILDHV---MTG 437
Cdd:cd05927 210 PG----VPrvlnriydkifNKVQAKGPLKrklfnfalnykLAELRSGVVRASPFWDKLVFNKI---KQALGGNVrlmLTG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 438 GDVCEPYVIEQL-------TRQGnlynlYGPTEATVLITARqlRTGDNNR-TLGAPIANSQVLILD--E-NFQPVAEQTV 506
Cdd:cd05927 283 SAPLSPEVLEFLrvalgcpVLEG-----YGQTECTAGATLT--LPGDTSVgHVGGPLPCAEVKLVDvpEmNYDAKDPNPR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 507 GELYIVGPGVCLGYLNNPLQTAERyLDLslpNGQslraYRTGDMAKWTSDG-IELCGRRDNQVKI-RGFRVEPEEIERCL 584
Cdd:cd05927 356 GEVCIRGPNVFSGYYKDPEKTAEA-LDE---DGW----LHTGDIGEWLPNGtLKIIDRKKNIFKLsQGEYVAPEKIENIY 427
|
410 420
....*....|....*....|
gi 1957676271 585 RDSQRYRQVAVVIDPHRRIL 604
Cdd:cd05927 428 ARSPFVAQIFVYGDSLKSFL 447
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
459-665 |
1.61e-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: 58.38 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 459 YGPTE----ATVLITArQLRTGdnnrTLGAPIANSQVLILD---ENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERY 531
Cdd:cd17639 281 YGLTEtcagGTVQDPG-DLETG----RVGPPLPCCEIKLVDweeGGYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAF 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 532 ldlslpNGQslRAYRTGDMAKWTSDG-IELCGRRDNQVKIR-GFRVEPEEIERCLRDSQRYRQVAVVIDPHRRILAFLAQ 609
Cdd:cd17639 356 ------DGD--GWFHTGDIGEFHPDGtLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAIVV 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957676271 610 PQEeqpgaarealkAHAMQFLPDYMQPTA-WTELASMP---------FASNGKVDRKALLELPVNV 665
Cdd:cd17639 428 PNE-----------KHLTKLAEKHGVINSeWEELCEDKklqkavlksLAETARAAGLEKFEIPQGV 482
|
|
| PRK07201 |
PRK07201 |
SDR family oxidoreductase; |
784-1042 |
2.29e-08 |
|
SDR family oxidoreductase;
Pssm-ID: 235962 [Multi-domain] Cd Length: 657 Bit Score: 58.42 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 784 IVTGANSFVGVHIVEALLAW-GASEVACLVRdgggQSAAQRFAqALRENrlehLDLSRVRVYVADITRPQLGLSEDVYQR 862
Cdd:PRK07201 4 FVTGGTGFIGRRLVSRLLDRrREATVHVLVR----RQSLSRLE-ALAAY----WGADRVVPLVGDLTEPGLGLSEADIAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 863 LDrEFGALVHNAANVNHVLDYESLARDNVEPIFECLRLCEGRSKKIFNFVSTLSA--------SSTISDDGRVLELPaaq 934
Cdd:PRK07201 75 LG-DIDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAERLQAATFHHVSSIAVagdyegvfREDDFDEGQGLPTP--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 935 tppiyikngYNLSKWVGERIlerarVR---GVRVNLYRPGNISFNSLTGVcqphknrlmlMLK--------GSIQ-LGQV 1002
Cdd:PRK07201 151 ---------YHRTKFEAEKL-----VReecGLPWRVYRPAVVVGDSRTGE----------MDKidgpyyffKVLAkLAKL 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1957676271 1003 PEF---------ALNfdLMPVDFLARFIAFHASRYQAEKAVFNLHNPEP 1042
Cdd:PRK07201 207 PSWlpmvgpdggRTN--IVPVDYVADALDHLMHKDGRDGQTFHLTDPKP 253
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
322-582 |
2.58e-08 |
|
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: 57.88 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 322 MALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLI--DIFPTLLQGAELIVPNEDQRRDPL 399
Cdd:cd05908 110 FIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIafHLAPLIAGMNQYLMPTRLFIRRPI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 400 QLVELIRHQRLShAFLPPALLSILPLDQLQI-------LDHV---MTGGDVCEPYVIEQLTRQGNLYNL--------YGP 461
Cdd:cd05908 190 LWLKKASEHKAT-IVSSPNFGYKYFLKTLKPekandwdLSSIrmiLNGAEPIDYELCHEFLDHMSKYGLkrnailpvYGL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 462 TEATV----------LITARQLRTGDNNR-----------------TLGAPIANSQVLILDENFQPVAEQTVGELYIVGP 514
Cdd:cd05908 269 AEASVgaslpkaqspFKTITLGRRHVTHGepepevdkkdsecltfvEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGK 348
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957676271 515 GVCLGYLNNPLQTAEryldLSLPNGQslraYRTGDMAKWTSDGIELCGRRDNQVKIRGFRVEPEEIER 582
Cdd:cd05908 349 NVTPGYYNNPEATAK----VFTDDGW----LKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIER 408
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
176-669 |
2.90e-08 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 57.68 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 176 IPMIERLEQRFIQSAERPALNIA------GTSLSHRQLHAHSRAIQQRLQPL-LDQHQgplVVGICLPKCSVLYAGILAI 248
Cdd:PLN02330 24 VPDKLTLPDFVLQDAELYADKVAfveavtGKAVTYGEVVRDTRRFAKALRSLgLRKGQ---VVVVVLPNVAEYGIVALGI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 249 LGSGAVYLPLEPSHPLQRQQYILENAGAVLLLHDGEHplSETMPGLDISGIDISDVNLDQPlMRQRPDLDAP-------- 320
Cdd:PLN02330 101 MAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTN--YGKVKGLGLPVIVLGEEKIEGA-VNWKELLEAAdragdtsd 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 321 ---------CMALYTSGTTGHPKGVLLSQANL-AHF-TAWYADYVQLTEQSRVLQFSSLSFDSSLIDI-FPTLLQGAELI 388
Cdd:PLN02330 178 neeilqtdlCALPFSSGTTGISKGVMLTHRNLvANLcSSLFSVGPEMIGQVVTLGLIPFFHIYGITGIcCATLRNKGKVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 389 VPNEDQRRDPLQlvELIRHQRLSHAFLPPALLSILP--------LDQLQiLDHVMTGGdvcEPYVIEQLTRQGNLY---- 456
Cdd:PLN02330 258 VMSRFELRTFLN--ALITQEVSFAPIVPPIILNLVKnpiveefdLSKLK-LQAIMTAA---APLAPELLTAFEAKFpgvq 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 457 --NLYGPTEATVLitarQLRTGDNNRTLGAPIANSQVLILD---------ENFQPVAEQTVGELYIVGPGVCLGYLNNPL 525
Cdd:PLN02330 332 vqEAYGLTEHSCI----TLTHGDPEKGHGIAKKNSVGFILPnlevkfidpDTGRSLPKNTPGELCVRSQCVMQGYYNNKE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 526 QTAeRYLDlslPNGQslraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHrril 604
Cdd:PLN02330 408 ETD-RTID---EDGW----LHTGDIGYIDDDGdIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPD---- 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1957676271 605 aflaQPQEEQPGA-------AREAlKAHAMQFLPD----YMQPTAWTELASMPFASNGKVDRKALLELPVNVTENS 669
Cdd:PLN02330 476 ----EEAGEIPAAcvvinpkAKES-EEDILNFVAAnvahYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSINKAN 546
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
463-753 |
4.51e-08 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 55.91 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 463 EATVLITARQLRTGDNNRTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGvclgYLNNPLQTAERYLDLSLPNGQSL 542
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAG----LLLRIRLLAAAARAPFIPVPYPA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 543 RAYRTGDMAKWTSDGIELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRILA----FLAQPQEEQPGAA 618
Cdd:COG3433 77 QPGRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAgvglLLIVGAVAALDGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 619 REALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLELPVN----VTENSQRRLPVSADEALLLEIWAELLELPA 694
Cdd:COG3433 157 AAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAeallAAASPAPALETALTEEELRADVAELLGVDP 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1957676271 695 SDISTDESFFNLGGHSIlLSRMLLRLREEFGRSISINRFIELPTIAKLATLVRGSGTEE 753
Cdd:COG3433 237 EEIDPDDNLFDLGLDSI-RLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAA 294
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
269-660 |
4.71e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 57.26 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 269 YILENAGAVLLLHDGE-----HPLSETMPGLDISGID-----------ISDVNLDQPLMRQRPDLDAP-------CMAL- 324
Cdd:PRK08162 109 FMLRHGEAKVLIVDTEfaevaREALALLPGPKPLVIDvddpeypggrfIGALDYEAFLASGDPDFAWTlpadewdAIALn 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 325 YTSGTTGHPKGV--------LLSQANLA-----------------HFTAWyadyvqlteqsrvlqfsslsfdsslidIFP 379
Cdd:PRK08162 189 YTSGTTGNPKGVvyhhrgayLNALSNILawgmpkhpvylwtlpmfHCNGW---------------------------CFP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 380 ---TLLQGAELIVpnedQRRDPLQLVELIRHQRLSHAFLPPALLSIL---PLDQLQILDH---VMTGGDVCEPYVIEQLT 450
Cdd:PRK08162 242 wtvAARAGTNVCL----RKVDPKLIFDLIREHGVTHYCGAPIVLSALinaPAEWRAGIDHpvhAMVAGAAPPAAVIAKME 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 451 RQG-NLYNLYGPTE----ATVL----------------ITARQlrtgdnnrtlGAPI-ANSQVLILD-ENFQPVAE--QT 505
Cdd:PRK08162 318 EIGfDLTHVYGLTEtygpATVCawqpewdalplderaqLKARQ----------GVRYpLQEGVTVLDpDTMQPVPAdgET 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 506 VGELYIVGPGVCLGYLNNPLQTAEryldlSLPNGQslraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCL 584
Cdd:PRK08162 388 IGEIMFRGNIVMKGYLKNPKATEE-----AFAGGW----FHTGDLAVLHPDGyIKIKDRSKDIIISGGENISSIEVEDVL 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 585 rdsqrYRQVAVVidphrrILAFLAQPQE---EQPGA---------AREA-LKAHAMQFLPDYMQPTAwTELASMPFASNG 651
Cdd:PRK08162 459 -----YRHPAVL------VAAVVAKPDPkwgEVPCAfvelkdgasATEEeIIAHCREHLAGFKVPKA-VVFGELPKTSTG 526
|
....*....
gi 1957676271 652 KVDRKALLE 660
Cdd:PRK08162 527 KIQKFVLRE 535
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
271-351 |
5.26e-08 |
|
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: 56.98 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 271 LENAGAVLLLHDgehPLSETMPGLdIS-------GIDISDVNLDQPLMRQRPDldAPCMALYTSGTTGHPKGVLLSQANL 343
Cdd:cd05933 102 LPHLKAIIQYKE---PLKEKEPNL-YSwdefmelGRSIPDEQLDAIISSQKPN--QCCTLIYTSGTTGMPKGVMLSHDNI 175
|
....*...
gi 1957676271 344 AhFTAWYA 351
Cdd:cd05933 176 T-WTAKAA 182
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
321-605 |
7.43e-08 |
|
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: 56.66 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 321 CMALYTSGTTGHPKGVLLSQANLAHFTA------------WYADYVQLT---EQsrVLQFSSLSFDSSLIDiFP----TL 381
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAaylaadplgpgdEYVSVLPLPwigEQ--MYSVGQALVCGFIVN-FPeepeTM 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 382 LQGAELIVPN-----------------------------------------EDQRRDPLQLVELIRHQR-LSHAFLPPAL 419
Cdd:cd17641 238 MEDLREIGPTfvllpprvwegiaadvrarmmdatpfkrfmfelgmklglraLDRGKRGRPVSLWLRLASwLADALLFRPL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 420 LSILPLDQLQIldhVMTGGDVCEPYVIEQLTRQG-NLYNLYGPTEATVLITARqlRTGD-NNRTLGAPIANSQVLIlDEn 497
Cdd:cd17641 318 RDRLGFSRLRS---AATGGAALGPDTFRFFHAIGvPLKQLYGQTELAGAYTVH--RDGDvDPDTVGVPFPGTEVRI-DE- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 498 fqpvaeqtVGELYIVGPGVCLGYLNNPLQTAERYLDlslpNGQslraYRTGDMAKWTSDG-IELCGR-RDNQVKIRGFRV 575
Cdd:cd17641 391 --------VGEILVRSPGVFVGYYKNPEATAEDFDE----DGW----LHTGDAGYFKENGhLVVIDRaKDVGTTSDGTRF 454
|
330 340 350
....*....|....*....|....*....|
gi 1957676271 576 EPEEIERCLRDSQRYRQvAVVIDPHRRILA 605
Cdd:cd17641 455 SPQFIENKLKFSPYIAE-AVVLGAGRPYLT 483
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
252-663 |
8.96e-08 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 56.31 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 252 GAVYLPLEPSHPLQRQQYILENAGAVLLLHDGEH-PLSETMPGLDISGIDI------SDVNLDQPL-MRQRPDLDAPCMA 323
Cdd:PRK06155 95 GAIAVPINTALRGPQLEHILRNSGARLLVVEAALlAALEAADPGDLPLPAVwlldapASVSVPAGWsTAPLPPLDAPAPA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 324 -----------LYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVpne 392
Cdd:PRK06155 175 aavqpgdtaaiLYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVL--- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 393 DQRRDPLQLVELIRHQRLSHAFLPPALLSIL------PLDQLQILdHVMTGGDVCEPYVIEQLTRQG-NLYNLYGPTEAT 465
Cdd:PRK06155 252 EPRFSASGFWPAVRRHGATVTYLLGAMVSILlsqparESDRAHRV-RVALGPGVPAALHAAFRERFGvDLLDGYGSTETN 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 466 VLI--TARQLRTGdnnrTLGAPIANSQVLILDENFQPVAEQTVGELYIVG--PGV-CLGYLNNPLQTAERYLDLslpngq 540
Cdd:PRK06155 331 FVIavTHGSQRPG----SMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdePFAfATGYFGMPEKTVEAWRNL------ 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 541 slrAYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVidPHRRILAflaqpQEE------ 613
Cdd:PRK06155 401 ---WFHTGDRVVRDADGwFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVF--PVPSELG-----EDEvmaavv 470
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1957676271 614 -QPGAARE--ALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLELPV 663
Cdd:PRK06155 471 lRDGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGV 523
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
326-661 |
1.21e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 55.05 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 326 TSGTTGHPKGVLLSQANL-AHFTAWYAdyvQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNEDQRRDPLQLVEL 404
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALtASADATHD---RLGGPGQWLLALPAHHIAGLQVLVRSVIAGSEPVELDVSAGFDPTALPRA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 405 I-------RHQRLSHAFLPPALLSILPLDQLQILDHVMTGGdvcepyvieqltrqgnlynlyGPTEATVLITARQL---- 473
Cdd:PRK07824 120 VaelgggrRYTSLVPMQLAKALDDPAATAALAELDAVLVGG---------------------GPAPAPVLDAAAAAginv 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 474 -RTGDNNRTLGA------PIANSQVLILDenfqpvaeqtvGELYIVGPGVCLGYLNNPlqtaeRYLDLSLPNGqslraYR 546
Cdd:PRK07824 179 vRTYGMSETSGGcvydgvPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV-----DPDPFAEPGW-----FR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 547 TGDMAKWTSDGIELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRILAFLAQPQEEQPGAAR--EALKA 624
Cdd:PRK07824 238 TDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPtlEALRA 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 1957676271 625 HAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLEL 661
Cdd:PRK07824 318 HVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
191-658 |
2.24e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 54.70 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 191 ERPALNIA--GTSLSHRQLHAHSRAI-----QQRLQPLldQHqgplvVGICLPKCSVLYAGILAILGSGAVYLPLEPSHP 263
Cdd:PRK13391 12 DKPAVIMAstGEVVTYRELDERSNRLahlfrSLGLKRG--DH-----VAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 264 LQRQQYILENAGAVLLLHDGEH-----PLSETMPG----LDISGIDISD--VNLDQPLMRQ----RPDLDAPCMALYTSG 328
Cdd:PRK13391 85 PAEAAYIVDDSGARALITSAAKldvarALLKQCPGvrhrLVLDGDGELEgfVGYAEAVAGLpatpIADESLGTDMLYSSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 329 TTGHPKGVL--LSQANLAH---FTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPnedQRRDPLQLVE 403
Cdd:PRK13391 165 TTGRPKGIKrpLPEQPPDTplpLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVM---EHFDAEQYLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 404 LIRHQRLSHAFLPPALLS---ILPLDQLQILDH-----VMTGGDVCEPYVIEQLTRQGN--LYNLYGPTE---ATVLITA 470
Cdd:PRK13391 242 LIEEYGVTHTQLVPTMFSrmlKLPEEVRDKYDLsslevAIHAAAPCPPQVKEQMIDWWGpiIHEYYAATEglgFTACDSE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 471 RQLrtgDNNRTLGAPIAnSQVLILDENFQPVAEQTVGELYIVGpGVCLGYLNNPLQTAE-RYLDLSLPNgqslrayrTGD 549
Cdd:PRK13391 322 EWL---AHPGTVGRAMF-GDLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEaRHPDGTWST--------VGD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 550 MAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHR------RILAFLAQPQEEQPGAAREaL 622
Cdd:PRK13391 389 IGYVDEDGyLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEdlgeevKAVVQPVDGVDPGPALAAE-L 467
|
490 500 510
....*....|....*....|....*....|....*.
gi 1957676271 623 KAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PRK13391 468 IAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
231-702 |
2.32e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 54.90 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 231 VGICLPKCSVLYAGILAILGSGAVYLPL------EPSHplQRqqyiLENAGAVLLLHDG---EHPLSETMPGL------- 294
Cdd:PRK04319 101 VFIFMPRIPELYFALLGALKNGAIVGPLfeafmeEAVR--DR----LEDSEAKVLITTPallERKPADDLPSLkhvllvg 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 295 DISGIDISDVNLDQpLMRQRPD------LDAPCMAL--YTSGTTGHPKGVL-LSQANLAHF-TAWY-------------A 351
Cdd:PRK04319 175 EDVEEGPGTLDFNA-LMEQASDefdiewTDREDGAIlhYTSGSTGKPKGVLhVHNAMLQHYqTGKYvldlheddvywctA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 352 DYVQLTEQSrvlqfsslsfdsslIDIFPTLLQGAELIVPNEdqRRDPLQLVELIRHQRLSHAFLPPALLSIL------PL 425
Cdd:PRK04319 254 DPGWVTGTS--------------YGIFAPWLNGATNVIDGG--RFSPERWYRILEDYKVTVWYTAPTAIRMLmgagddLV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 426 DQ--LQILDHVMTGGDVCEPYVIeqltRQG-NLYNL-----YGPTE-ATVLIT---ARQLRTGdnnrTLGAPIANSQVLI 493
Cdd:PRK04319 318 KKydLSSLRHILSVGEPLNPEVV----RWGmKVFGLpihdnWWMTEtGGIMIAnypAMDIKPG----SMGKPLPGIEAAI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 494 LDENFQPVAEQTVGELYI-VG-PGVCLGYLNNPlqtaERYLDLSLPNgqslrAYRTGDMAKWTSDG-IELCGRRDNQVKI 570
Cdd:PRK04319 390 VDDQGNELPPNRMGNLAIkKGwPSMMRGIWNNP----EKYESYFAGD-----WYVSGDSAYMDEDGyFWFQGRVDDVIKT 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 571 RGFRVEPEEIERCLRDSQryrqvAV----VI---DPHR--RILAFLA-----QP----QEEQPGAAREALKAHA----MQ 628
Cdd:PRK04319 461 SGERVGPFEVESKLMEHP-----AVaeagVIgkpDPVRgeIIKAFVAlrpgyEPseelKEEIRGFVKKGLGAHAapreIE 535
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1957676271 629 FLPdymqptawtelaSMPFASNGKVDRKallelpvnvtensqrrlpvsadealLLEIWAelLELPASDISTDES 702
Cdd:PRK04319 536 FKD------------KLPKTRSGKIMRR-------------------------VLKAWE--LGLPEGDLSTMED 570
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
231-658 |
3.08e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.65 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 231 VGICLPKCSVLYAGILAILGSGAVYLPLEPShpLQRQQYILE--NAGAVLLLHDGehPLSETM-PGLDISGIDI-SDVNL 306
Cdd:PRK06060 58 VLLCLPDSPDLVQLLLACLARGVMAFLANPE--LHRDDHALAarNTEPALVVTSD--ALRDRFqPSRVAEAAELmSEAAR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 307 DQPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQANLAHFT-AWYADYVQLTEQSRVLQFSSLSFDSSLIDI--FPTLLQ 383
Cdd:PRK06060 134 VAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVdAMCRKALRLTPEDTGLCSARMYFAYGLGNSvwFPLATG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 384 GAELIVPNEdqrrdplqlVELIRHQRLSHAFLPPALLSILPL----------DQLQILDHVMTGGDVCEPYVIEQLTR-Q 452
Cdd:PRK06060 214 GSAVINSAP---------VTPEAAAILSARFGPSVLYGVPNFfarvidscspDSFRSLRCVVSAGEALELGLAERLMEfF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 453 GNLYNL--YGPTEAT---VLITARQLRTGdnnrTLGAPIANSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLN--NPL 525
Cdd:PRK06060 285 GGIPILdgIGSTEVGqtfVSNRVDEWRLG----TLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNrpDSP 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 526 QTAERYLDlslpngqslrayrTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV----IDPH 600
Cdd:PRK06060 361 VANEGWLD-------------TRDRVCIDSDGwVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVavreSTGA 427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1957676271 601 RRILAFLAQPQEEQ-PGAAREALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PRK06060 428 STLQAFLVATSGATiDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
455-662 |
3.74e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 54.16 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 455 LYNLYGPTEATVLITAR--QLRTgdNNRTLGAPIANSQVLILDENFQPVAEQTVGELYiVGPGVCL-GYLN-NPLQTAER 530
Cdd:PRK07788 351 LYNLYGSTEVAFATIATpeDLAE--APGTVGRPPKGVTVKILDENGNEVPRGVVGRIF-VGNGFPFeGYTDgRDKQIIDG 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 531 YLDlslpngqslrayrTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAV--VIDPH--RRILA 605
Cdd:PRK07788 428 LLS-------------SGDVGYFDEDGlLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVigVDDEEfgQRLRA 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1957676271 606 FLAQpqeeQPGAAR--EALKAHAMQFLPDYMQPTAWTELASMPFASNGKVDRKALLELP 662
Cdd:PRK07788 495 FVVK----APGAALdeDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| AR_FR_like_1_SDR_e |
cd05228 |
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ... |
783-971 |
3.94e-07 |
|
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187539 [Multi-domain] Cd Length: 318 Bit Score: 53.44 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGASeVACLVRDGGgqsaaqrfaqalrenRLEHLDLSRVRVYVADITRPQLgLSEDVyqr 862
Cdd:cd05228 1 ILVTGATGFLGSNLVRALLAQGYR-VRALVRSGS---------------DAVLLDGLPVEVVEGDLTDAAS-LAAAM--- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 863 ldREFGALVHNAANVNHVL-DYESLARDNVEPIFECLRLCEGRSKKIFNFVSTLSAsSTISDDGRVLElpAAQTPPIYIK 941
Cdd:cd05228 61 --KGCDRVFHLAAFTSLWAkDRKELYRTNVEGTRNVLDAALEAGVRRVVHTSSIAA-LGGPPDGRIDE--TTPWNERPFP 135
|
170 180 190
....*....|....*....|....*....|
gi 1957676271 942 NGYNLSKWVGERILERARVRGVRVNLYRPG 971
Cdd:cd05228 136 NDYYRSKLLAELEVLEAAAEGLDVVIVNPS 165
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
277-581 |
6.19e-07 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 53.66 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 277 VLLLHDGEHPLSETMPGLDISGIDISDVNLDQPLMRQRPDlDAPCMAlYTSGTTGHPKGVLLSQANLAHFTAWYADYVQL 356
Cdd:PRK08315 160 VIFLGDEKHPGMLNFDELLALGRAVDDAELAARQATLDPD-DPINIQ-YTSGTTGFPKGATLTHRNILNNGYFIGEAMKL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 357 TEQSRVLqfsslsfdsslidiFPTLL---------------QGAELIVPNEdqRRDPLQLVELIRHQRLShaflppALLS 421
Cdd:PRK08315 238 TEEDRLC--------------IPVPLyhcfgmvlgnlacvtHGATMVYPGE--GFDPLATLAAVEEERCT------ALYG 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 422 IlPLDQLQILDHVM----------TG---GDVCEPYVIEQLTRQGNLYNL---YGPTEATVLITarQLRTGDN--NR--T 481
Cdd:PRK08315 296 V-PTMFIAELDHPDfarfdlsslrTGimaGSPCPIEVMKRVIDKMHMSEVtiaYGMTETSPVST--QTRTDDPleKRvtT 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 482 LGAPIANSQVLILD-ENFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAE-----RYLdlslpngqslrayRTGDMAKWTS 555
Cdd:PRK08315 373 VGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEaidadGWM-------------HTGDLAVMDE 439
|
330 340
....*....|....*....|....*...
gi 1957676271 556 DG-IELCGRRDNQVkIRGFR-VEPEEIE 581
Cdd:PRK08315 440 EGyVNIVGRIKDMI-IRGGEnIYPREIE 466
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
178-660 |
6.57e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 53.49 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 178 MIERLEQRFIQSAE--RPALNIAGTSLSHRQLHAHSRAIQQRLQPLLDqHQGPLVVGICL---PKCSVLYAGilAILGsG 252
Cdd:PRK13388 1 MRDTIAQLLRDRAGddTIAVRYGDRTWTWREVLAEAAARAAALIALAD-PDRPLHVGVLLgntPEMLFWLAA--AALG-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 253 AVYLPLEPShplQRQQYILEN---AGAVLLLHDGEH-PLsetMPGLDISGIDISDVnlDQPLMRQR------------PD 316
Cdd:PRK13388 77 YVLVGLNTT---RRGAALAADirrADCQLLVTDAEHrPL---LDGLDLPGVRVLDV--DTPAYAELvaaagaltphreVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 317 LDAPCMALYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQsrvlqfsslsfdssliDIF-----------------P 379
Cdd:PRK13388 149 AMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRD----------------DVCyvsmplfhsnavmagwaP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 380 TLLQGAELIVPNEDQRRDPLQLVEliRHQRLSHAFLPPALLSIL-----PLDQLQILDHVMtgGDVCEPYVIEQLTRQ-- 452
Cdd:PRK13388 213 AVASGAAVALPAKFSASGFLDDVR--RYGATYFNYVGKPLAYILatperPDDADNPLRVAF--GNEASPRDIAEFSRRfg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 453 GNLYNLYGPTEATVLITarqLRTGDNNRTLGAP-----IANSQVL------ILDENFQPV-AEQTVGELYIV-GPGVCLG 519
Cdd:PRK13388 289 CQVEDGYGSSEGAVIVV---REPGTPPGSIGRGapgvaIYNPETLtecavaRFDAHGALLnADEAIGELVNTaGAGFFEG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 520 YLNNPLQTAERyldlsLPNGQslraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAV--V 596
Cdd:PRK13388 366 YYNNPEATAER-----MRHGM----YWSGDLAYRDADGwIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVyaV 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1957676271 597 IDPHR--RILA--FLAQPQEEQPGAAREALKAHamqflPDyMQPTAWTEL----ASMPFASNGKVDRKALLE 660
Cdd:PRK13388 437 PDERVgdQVMAalVLRDGATFDPDAFAAFLAAQ-----PD-LGTKAWPRYvriaADLPSTATNKVLKRELIA 502
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
433-661 |
9.30e-07 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 53.10 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 433 HVMTGGDVCEPYVIEQLTRQG-NLYNLYGPTEAT--VLITARQ---------------LRTGDNNRTLG-APIANSQVLi 493
Cdd:PLN03102 304 HVLTGGSPPPAALVKKVQRLGfQVMHAYGLTEATgpVLFCEWQdewnrlpenqqmelkARQGVSILGLAdVDVKNKETQ- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 494 ldeNFQPVAEQTVGELYIVGPGVCLGYLNNPLQTAERYLDLSLpngqslrayRTGDMAKWTSDG-IELCGRRDNQVKIRG 572
Cdd:PLN03102 383 ---ESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAFKHGWL---------NTGDVGVIHPDGhVEIKDRSKDIIISGG 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 573 FRVEPEEIERCLRDSQRYRQVAVVIDPH----RRILAFLAQPQEEQPGAAREA--------LKAHAMQFLPDYMQPTAWT 640
Cdd:PLN03102 451 ENISSVEVENVLYKYPKVLETAVVAMPHptwgETPCAFVVLEKGETTKEDRVDklvtrerdLIEYCRENLPHFMCPRKVV 530
|
250 260
....*....|....*....|.
gi 1957676271 641 ELASMPFASNGKVDRKALLEL 661
Cdd:PLN03102 531 FLQELPKNGNGKILKPKLRDI 551
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
325-658 |
1.07e-06 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 52.92 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 325 YTSGTTGHPKGVLLSqanlaHFTAwyadYVQLTEQSRVLQFSSLSFDSSLIDIFP--------TLlqgAELIVPNEDQRR 396
Cdd:PLN02479 202 YTSGTTASPKGVVLH-----HRGA----YLMALSNALIWGMNEGAVYLWTLPMFHcngwcftwTL---AALCGTNICLRQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 397 DPLQLV-ELIRHQRLSHAFLPPALL----------SILPLDQLQildHVMTGGDVCEPYVIEQLTRQG----NLYNL--- 458
Cdd:PLN02479 270 VTAKAIySAIANYGVTHFCAAPVVLntivnapkseTILPLPRVV---HVMTAGAAPPPSVLFAMSEKGfrvtHTYGLset 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 459 YGPT-------EATVLITARQLRTgdNNRTLGAPIANSQVLILD-ENFQPVAE--QTVGELYIVGPGVCLGYLNNPLQTA 528
Cdd:PLN02479 347 YGPStvcawkpEWDSLPPEEQARL--NARQGVRYIGLEGLDVVDtKTMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 529 EryldlSLPNGQslraYRTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRI---- 603
Cdd:PLN02479 425 E-----AFANGW----FHSGDLGVKHPDGyIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWgesp 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1957676271 604 LAFLAqPQEEQPGAAREALKAHAMQF----LPDYMQPTAwTELASMPFASNGKVDRKAL 658
Cdd:PLN02479 496 CAFVT-LKPGVDKSDEAALAEDIMKFcrerLPAYWVPKS-VVFGPLPKTATGKIQKHVL 552
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
481-658 |
1.47e-06 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 52.30 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 481 TLGAPIA-NSQVLILDENFQPVAEQTVGELYIVGPGVCLGYLNNPLQtaeryldlslpNGQSLRA---YRTGDMAKWTSD 556
Cdd:PRK10946 354 TQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQH-----------NASAFDAngfYCSGDLVSIDPD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 557 G-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPHRRI----LAFLAQPQEEQPGAAREALKAhamQFLP 631
Cdd:PRK10946 423 GyITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMgeksCAFLVVKEPLKAVQLRRFLRE---QGIA 499
|
170 180
....*....|....*....|....*..
gi 1957676271 632 DYMQPTAWTELASMPFASNGKVDRKAL 658
Cdd:PRK10946 500 EFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
324-584 |
2.24e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 51.74 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 324 LYTSGTTGHPKGVLLSQANLAHFTAWYADYVQLTEQSRVLQFSSLSFDS--SLIDIFPtLLQGAELIVPNedqrrDPLQ- 400
Cdd:PRK06334 189 LFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYgfNSCTLFP-LLSGVPVVFAY-----NPLYp 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 401 --LVELIRHQRLSHAFLPPALLS-ILPLDQ-----LQILDHVMTGGDVCEPYVIEQLTR---QGNLYNLYGPTEATVLIT 469
Cdd:PRK06334 263 kkIVEMIDEAKVTFLGSTPVFFDyILKTAKkqescLPSLRFVVIGGDAFKDSLYQEALKtfpHIQLRQGYGTTECSPVIT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 470 ARQLRTGDNNRTLGAPIANSQVLIL-DENFQPVAEQTVGELYIVGPGVCLGYL-NNPLQTaerYLDLSlpnGQSLraYRT 547
Cdd:PRK06334 343 INTVNSPKHESCVGMPIRGMDVLIVsEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQG---FVELG---GETW--YVT 414
|
250 260 270
....*....|....*....|....*....|....*...
gi 1957676271 548 GDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCL 584
Cdd:PRK06334 415 GDLGYVDRHGeLFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
459-655 |
7.14e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 50.15 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 459 YGPTEATVLITA-----------RQLRTGDNNRT---LGAPIANSQVLIL-DENFQPVAEQTVGELYIVGPGVCLGYLNn 523
Cdd:PRK05851 310 YGLAESTCAVTVpvpgiglrvdeVTTDDGSGARRhavLGNPIPGMEVRISpGDGAAGVAGREIGEIEIRGASMMSGYLG- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 524 plqtaeryldlslpnGQSLRA---YRTGDMAKWTSDGIELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVV---- 596
Cdd:PRK05851 389 ---------------QAPIDPddwFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVavgt 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1957676271 597 ----IDPHRRILAFLAQPQEeqPGAAREALKAHAMQ--FLPD---YMQPtawtelASMPFASNGKVDR 655
Cdd:PRK05851 454 gegsARPGLVIAAEFRGPDE--AGARSEVVQRVASEcgVVPSdvvFVAP------GSLPRTSSGKLRR 513
|
|
| UDP_AE_SDR_e |
cd05256 |
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ... |
782-953 |
8.92e-06 |
|
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187566 [Multi-domain] Cd Length: 304 Bit Score: 49.14 E-value: 8.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 782 KVIVTGANSFVGVHIVEALLAWGAsEVACLvrdgggqsaaQRFAQALRENRLEHLDlsRVRVYVADITrpQLGLSEDVYQ 861
Cdd:cd05256 1 RVLVTGGAGFIGSHLVERLLERGH-EVIVL----------DNLSTGKKENLPEVKP--NVKFIEGDIR--DDELVEFAFE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 862 RLDREFgalvHNAA---NVNHVLDYESLARDNVEPIFECLRLC-EGRSKKifnFVSTlSASSTIsddGRVLELPAAQTPP 937
Cdd:cd05256 66 GVDYVF----HQAAqasVPRSIEDPIKDHEVNVLGTLNLLEAArKAGVKR---FVYA-SSSSVY---GDPPYLPKDEDHP 134
|
170
....*....|....*.
gi 1957676271 938 IYIKNGYNLSKWVGER 953
Cdd:cd05256 135 PNPLSPYAVSKYAGEL 150
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
326-584 |
1.38e-05 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 49.18 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 326 TSGTTGHPKGVLLSQANLAhFTAWYADYVQLTEQSRVLqfsslsfdsslidIFP---------------TLLQGAELIVP 390
Cdd:PRK07529 221 TGGTTGMPKLAQHTHGNEV-ANAWLGALLLGLGPGDTV-------------FCGlplfhvnallvtglaPLARGAHVVLA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 391 NEDQRRDPlQLV----ELIRHQRLSHAFLPPALLSIL---PLDQLQI--LDHVMTGGDVCEPYVIEQLTRQGN--LYNLY 459
Cdd:PRK07529 287 TPQGYRGP-GVIanfwKIVERYRINFLSGVPTVYAALlqvPVDGHDIssLRYALCGAAPLPVEVFRRFEAATGvrIVEGY 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 460 GPTEATVLITA----RQLRTGdnnrTLGAPIANSQV--LILDEN---FQPVAEQTVGELYIVGPGVCLGYL----NNPLQ 526
Cdd:PRK07529 366 GLTEATCVSSVnppdGERRIG----SVGLRLPYQRVrvVILDDAgryLRDCAVDEVGVLCIAGPNVFSGYLeaahNKGLW 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 527 TAERYLDlslpngqslrayrTGDMAKWTSDG-IELCGRRDNQVkIR-GFRVEPEEIERCL 584
Cdd:PRK07529 442 LEDGWLN-------------TGDLGRIDADGyFWLTGRAKDLI-IRgGHNIDPAAIEEAL 487
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
171-346 |
4.40e-05 |
|
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: 47.45 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 171 LQLAQIpmIERLEQRFiqsAERPAL---------NIAGTSLSHRQL----HAHSRAIQQRLQPLLDQHQGPLVVG----I 233
Cdd:cd17632 22 LRLAQI--IATVMTGY---ADRPALgqratelvtDPATGRTTLRLLprfeTITYAELWERVGAVAAAHDPEQPVRpgdfV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 234 C-LPKCSVLYAGI-LAILGSGAVYLPLEPSHPLQRQQYILENAG----AV--------------------LLLHDGEHPL 287
Cdd:cd17632 97 AvLGFTSPDYATVdLALTRLGAVSVPLQAGASAAQLAPILAETEprllAVsaehldlaveavleggtpprLVVFDHRPEV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1957676271 288 SETMPGLDIS----------------GIDISDVNLDQPLMRQRPDLDAPCMALYTSGTTGHPKGVLLSQANLAHF 346
Cdd:cd17632 177 DAHRAALESArerlaavgipvttltlIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATF 251
|
|
| 3beta-17beta-HSD_like_SDR_c |
cd05341 |
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ... |
783-974 |
5.69e-05 |
|
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187600 [Multi-domain] Cd Length: 247 Bit Score: 45.84 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGASEVACLVRDGGGQSAAQRFAqalRENRLEHLDLSRVRVY--VADITRPQLGlsedvy 860
Cdd:cd05341 8 AIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELG---DAARFFHLDVTDEDGWtaVVDTAREAFG------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 861 qRLDrefgALVHNA-----ANVNHVL--DYESLARDNVEPIFECLRLCEGRSKK-----IFNFVSTLSAsstisddgrvl 928
Cdd:cd05341 79 -RLD----VLVNNAgiltgGTVETTTleEWRRLLDINLTGVFLGTRAVIPPMKEagggsIINMSSIEGL----------- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1957676271 929 eLPAAQTPpiyiknGYNLSKWvGERILERA-------RVRGVRVNLYRPGNIS 974
Cdd:cd05341 143 -VGDPALA------AYNASKG-AVRGLTKSaalecatQGYGIRVNSVHPGYIY 187
|
|
| SDR_c8 |
cd08930 |
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ... |
783-973 |
6.53e-05 |
|
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187635 [Multi-domain] Cd Length: 250 Bit Score: 45.79 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGASeVACLVRDGGGQSAAQrfaqalreNRLEHLDLSRVRVYVADITRP----QLGLS-E 857
Cdd:cd08930 5 ILITGAAGLIGKAFCKALLSAGAR-LILADINAPALEQLK--------EELTNLYKNRVIALELDITSKesikELIESyL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 858 DVYQRLDrefgALVHNAANVNHV-------LDYESLARD---NVEPIFEC----LRLCEGRSK-KIFNFVSTLsasSTIS 922
Cdd:cd08930 76 EKFGRID----ILINNAYPSPKVwgsrfeeFPYEQWNEVlnvNLGGAFLCsqafIKLFKKQGKgSIINIASIY---GVIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1957676271 923 DDGRVLELPAAQTPPIY--IKNGYN-LSKWVgerilerARV---RGVRVNLYRPGNI 973
Cdd:cd08930 149 PDFRIYENTQMYSPVEYsvIKAGIIhLTKYL-------AKYyadTGIRVNAISPGGI 198
|
|
| Epimerase |
pfam01370 |
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
783-973 |
7.57e-05 |
|
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.
Pssm-ID: 396097 [Multi-domain] Cd Length: 238 Bit Score: 45.37 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGAsEVACLVRDGGGQSAAQRFAQALREnrLEHLDLSRVRVYVADitrpqlglsedvyQR 862
Cdd:pfam01370 1 ILVTGATGFIGSHLVRRLLEKGY-EVIGLDRLTSASNTARLADLRFVE--GDLTDRDALEKLLAD-------------VR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 863 LDrefgALVHNAAnVNHVLDYES----LARDNVE---PIFECLRLCeGRSKKIFnfvstLSASSTISDDGRVLELPAAQT 935
Cdd:pfam01370 65 PD----AVIHLAA-VGGVGASIEdpedFIEANVLgtlNLLEAARKA-GVKRFLF-----ASSSEVYGDGAEIPQEETTLT 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 1957676271 936 PPIYIKNGYNLSKWVGERILERARVR-GVRVNLYRPGNI 973
Cdd:pfam01370 134 GPLAPNSPYAAAKLAGEWLVLAYAAAyGLRAVILRLFNV 172
|
|
| YqjQ |
COG0300 |
Short-chain dehydrogenase [General function prediction only]; |
783-874 |
8.24e-05 |
|
Short-chain dehydrogenase [General function prediction only];
Pssm-ID: 440069 [Multi-domain] Cd Length: 252 Bit Score: 45.63 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGAsEVACLVRDgggQSAAQRFAQALRENRlehldlSRVRVYVADITRPQlGLsEDVYQR 862
Cdd:COG0300 8 VLITGASSGIGRALARALAARGA-RVVLVARD---AERLEALAAELRAAG------ARVEVVALDVTDPD-AV-AALAEA 75
|
90
....*....|....*
gi 1957676271 863 LDREFG---ALVHNA 874
Cdd:COG0300 76 VLARFGpidVLVNNA 90
|
|
| FabG |
COG1028 |
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ... |
783-875 |
1.67e-04 |
|
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440651 [Multi-domain] Cd Length: 249 Bit Score: 44.39 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGASeVACLVRDgggQSAAQRFAQALRENRlehldlSRVRVYVADITRPqlglsEDV--- 859
Cdd:COG1028 9 ALVTGGSSGIGRAIARALAAEGAR-VVITDRD---AEALEAAAAELRAAG------GRALAVAADVTDE-----AAVeal 73
|
90
....*....|....*....
gi 1957676271 860 YQRLDREFGA---LVHNAA 875
Cdd:COG1028 74 VAAAVAAFGRldiLVNNAG 92
|
|
| YbjT |
COG0702 |
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ... |
782-851 |
3.22e-04 |
|
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];
Pssm-ID: 440466 [Multi-domain] Cd Length: 215 Bit Score: 43.30 E-value: 3.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 782 KVIVTGANSFVGVHIVEALLAWGAsEVACLVRDgggqsaaqrfaqalrENRLEHLDLSRVRVYVADITRP 851
Cdd:COG0702 1 KILVTGATGFIGRRVVRALLARGH-PVRALVRD---------------PEKAAALAAAGVEVVQGDLDDP 54
|
|
| SDR_e |
cd08946 |
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ... |
783-973 |
4.49e-04 |
|
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 212494 [Multi-domain] Cd Length: 200 Bit Score: 42.67 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGAsevaclvrdgggqsaaqrfaqalrenrlehldlsrvRVYVADitrpqlglsedvyqR 862
Cdd:cd08946 1 ILVTGGAGFIGSHLVRRLLERGH------------------------------------EVVVID--------------R 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 863 LDrefgALVHNAANVNHVLDYESLARD---NVEPIFECLRLCegRSKKIFNFVstlsASSTISDDGRVLELPAAQTPPIY 939
Cdd:cd08946 31 LD----VVVHLAALVGVPASWDNPDEDfetNVVGTLNLLEAA--RKAGVKRFV----YASSASVYGSPEGLPEEEETPPR 100
|
170 180 190
....*....|....*....|....*....|....*
gi 1957676271 940 IKNGYNLSKWVGERILERARVR-GVRVNLYRPGNI 973
Cdd:cd08946 101 PLSPYGVSKLAAEHLLRSYGESyGLPVVILRLANV 135
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
283-356 |
5.08e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 44.32 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 283 GEHPLSETMPGLDISGIDISDVnLDQPLMRQRP-------DLDAPCmalYTSGTTGHPKGVLLSQANLAHFTAWYADYVQ 355
Cdd:PLN02736 183 ADEPLPSLPSGTGVEIVTYSKL-LAQGRSSPQPfrppkpeDVATIC---YTSGTTGTPKGVVLTHGNLIANVAGSSLSTK 258
|
.
gi 1957676271 356 L 356
Cdd:PLN02736 259 F 259
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
313-581 |
5.32e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 44.23 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 313 QRPDLDAPCMALYTSGTTGHPKGVLLSQ-ANLAHFTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLqGAELIV-- 389
Cdd:PRK09192 171 PRPTPDDIAYLQYSSGSTRFPRGVIITHrALMANLRAISHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPV-ATQLSVdy 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 390 -PNEDQRRDPLQLVELIRHQRLSHAFLPP------------ALLSILPLDQLQILDhvmTGGDVCEPYVIEQLT------ 450
Cdd:PRK09192 250 lPTRDFARRPLQWLDLISRNRGTISYSPPfgyelcarrvnsKDLAELDLSCWRVAG---IGADMIRPDVLHQFAeafapa 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 451 --RQGNLYNLYGPTEATVLIT---------------------ARQLRTGDNNRTL------GAPIANSQVLILDENFQPV 501
Cdd:PRK09192 327 gfDDKAFMPSYGLAEATLAVSfsplgsgivveevdrdrleyqGKAVAPGAETRRVrtfvncGKALPGHEIEIRNEAGMPL 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 502 AEQTVGELYIVGPGVCLGYLNNPLQT----AERYLDlslpngqslrayrTGDMAkWTSDG-IELCGRRDNQVKIRGFRVE 576
Cdd:PRK09192 407 PERVVGHICVRGPSLMSGYFRDEESQdvlaADGWLD-------------TGDLG-YLLDGyLYITGRAKDLIIINGRNIW 472
|
....*
gi 1957676271 577 PEEIE 581
Cdd:PRK09192 473 PQDIE 477
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
316-660 |
6.65e-04 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 43.59 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 316 DLDAPCMALYTSGTTGHPKGVLLS-QANLAH-FTAWYADYVQLTEQSRVLQFSSLSFDSSLIDIFPTLLQGAELIVPNed 393
Cdd:PRK06018 175 DENTAAGMCYTSGTTGDPKGVLYShRSNVLHaLMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPG-- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 394 QRRDPLQLVELIRHQRLSHAFLPPA----LLSILPLDQLQI--LDHVMTGGDVCEPYVIEQLTRQG-NLYNLYGPTEATV 466
Cdd:PRK06018 253 AKLDGASVYELLDTEKVTFTAGVPTvwlmLLQYMEKEGLKLphLKMVVCGGSAMPRSMIKAFEDMGvEVRHAWGMTEMSP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 467 LITARQLRTG----------DNNRTLGAPIANSQVLILDE--NFQPVAEQTVGELYIVGPGVCLGYL--NNPLQTAERYL 532
Cdd:PRK06018 333 LGTLAALKPPfsklpgdarlDVLQKQGYPPFGVEMKITDDagKELPWDGKTFGRLKVRGPAVAAAYYrvDGEILDDDGFF 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 533 DlslpngqslrayrTGDMAKWTSDG-IELCGRRDNQVKIRGFRVEPEEIERCLRDSQRYRQVAVVIDPH-----RRILaf 606
Cdd:PRK06018 413 D-------------TGDVATIDAYGyMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHpkwdeRPLL-- 477
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1957676271 607 LAQPQEEQPGAAREALKAH----AMQFLPDymqPTAWTElaSMPFASNGKVDRKALLE 660
Cdd:PRK06018 478 IVQLKPGETATREEILKYMdgkiAKWWMPD---DVAFVD--AIPHTATGKILKTALRE 530
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
324-357 |
9.64e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 43.21 E-value: 9.64e-04
10 20 30
....*....|....*....|....*....|....
gi 1957676271 324 LYTSGTTGHPKGVLlsqanlaHFTAWYADYVQLT 357
Cdd:PRK00174 251 LYTSGSTGKPKGVL-------HTTGGYLVYAAMT 277
|
|
| fabG |
PRK05653 |
3-oxoacyl-ACP reductase FabG; |
783-874 |
1.32e-03 |
|
3-oxoacyl-ACP reductase FabG;
Pssm-ID: 235546 [Multi-domain] Cd Length: 246 Bit Score: 41.68 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGAsEVACLVRDgggQSAAQRFAQALRENrlehldLSRVRVYVADITRP-QLglsEDVYQ 861
Cdd:PRK05653 8 ALVTGASRGIGRAIALRLAADGA-KVVIYDSN---EEAAEALAAELRAA------GGEARVLVFDVSDEaAV---RALIE 74
|
90
....*....|....*.
gi 1957676271 862 RLDREFGA---LVHNA 874
Cdd:PRK05653 75 AAVEAFGAldiLVNNA 90
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
310-357 |
1.47e-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: 42.55 E-value: 1.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1957676271 310 LMRQRPD------LDA--PCMALYTSGTTGHPKGVLlsqanlaHFTAWYADYVQLT 357
Cdd:cd05966 215 LMAKQSPecepewMDSedPLFILYTSGSTGKPKGVV-------HTTGGYLLYAATT 263
|
|
| SPR-like_SDR_c |
cd05367 |
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ... |
783-918 |
1.48e-03 |
|
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187625 [Multi-domain] Cd Length: 241 Bit Score: 41.50 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWG-ASEVACLVRDgggQSAAQRFAQALRENrlehldlSRVRVYVADITRPQlGLSEdVYQ 861
Cdd:cd05367 2 IILTGASRGIGRALAEELLKRGsPSVVVLLARS---EEPLQELKEELRPG-------LRVTTVKADLSDAA-GVEQ-LLE 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1957676271 862 RLDREFG---ALVHNAANVNHVLDYESLARDNVEPIF------------ECLRLCEGRS-KKIFNFVSTLSAS 918
Cdd:cd05367 70 AIRKLDGerdLLINNAGSLGPVSKIEFIDLDELQKYFdlnltspvcltsTLLRAFKKRGlKKTVVNVSSGAAV 142
|
|
| SDR_c7 |
cd05354 |
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ... |
783-851 |
1.56e-03 |
|
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
Pssm-ID: 187612 [Multi-domain] Cd Length: 235 Bit Score: 41.62 E-value: 1.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGASEVACLVRDGGgqSAAQrfaqalrenrLEHLDLSRVRVYVADITRP 851
Cdd:cd05354 6 VLVTGANRGIGKAFVESLLAHGAKKVYAAVRDPG--SAAH----------LVAKYGDKVVPLRLDVTDP 62
|
|
| adh_short |
pfam00106 |
short chain dehydrogenase; This family contains a wide variety of dehydrogenases. |
783-974 |
2.15e-03 |
|
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
Pssm-ID: 395056 [Multi-domain] Cd Length: 195 Bit Score: 40.67 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGASEVACLVRDGGGQSAaqrfAQALRENRlehldlSRVRVYVADIT-RPQLglsEDVYQ 861
Cdd:pfam00106 3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAV----AKELGALG------GKALFIQGDVTdRAQV---KALVE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 862 RLDREFG---ALVHNAAnVNHVLDYESLARDNVEPIFEClrlcegrskkifNFVSTLSASSTISDD------GRVL---- 928
Cdd:pfam00106 70 QAVERLGrldILVNNAG-ITGLGPFSELSDEDWERVIDV------------NLTGVFNLTRAVLPAmikgsgGRIVniss 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1957676271 929 ---ELPAAQTPPiyikngYNLSKWvGERILERA-----RVRGVRVNLYRPGNIS 974
Cdd:pfam00106 137 vagLVPYPGGSA------YSASKA-AVIGFTRSlalelAPHGIRVNAVAPGGVD 183
|
|
| UDP_G4E_5_SDR_e |
cd05264 |
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ... |
782-973 |
2.17e-03 |
|
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187574 [Multi-domain] Cd Length: 300 Bit Score: 41.53 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 782 KVIVTGANSFVGVHIVEALLAWGasevaCLVRdgggqsAAQRFAQALRenrlehLDLSRVRVYVADITRPqlglsEDVYQ 861
Cdd:cd05264 1 RVLIVGGNGFIGSHLVDALLEEG-----PQVR------VFDRSIPPYE------LPLGGVDYIKGDYENR-----ADLES 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 862 RLdREFGALVHNA-------ANVNHVLDYESlardNVEPIFECLRLCEGRSKKIFNFVSTlsaSSTISddGRVLELPAAQ 934
Cdd:cd05264 59 AL-VGIDTVIHLAsttnpatSNKNPILDIQT----NVAPTVQLLEACAAAGIGKIIFASS---GGTVY--GVPEQLPISE 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1957676271 935 TPPIYIKNGYNLSKWVGERILERARVR-GVRVNLYRPGNI 973
Cdd:cd05264 129 SDPTLPISSYGISKLAIEKYLRLYQYLyGLDYTVLRISNP 168
|
|
| UDP_G4E_2_SDR_e |
cd05234 |
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ... |
783-973 |
2.84e-03 |
|
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of archaeal and bacterial proteins, and has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187545 [Multi-domain] Cd Length: 305 Bit Score: 41.13 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 783 VIVTGANSFVGVHIVEALLAWGaSEVACLVRDGGGQsaaqrfaqalRENRLEHLDLSRVRVYVADITRPqlglSEDVYqr 862
Cdd:cd05234 2 ILVTGGAGFIGSHLVDRLLEEG-NEVVVVDNLSSGR----------RENIEPEFENKAFRFVKRDLLDT----ADKVA-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 863 lDREFGALVHNAANV---NHVLDYESLARDNVEPIFeclRLCEG-RSKKIFNFVstLSASSTISDDGRVLELPaAQTPPI 938
Cdd:cd05234 65 -KKDGDTVFHLAANPdvrLGATDPDIDLEENVLATY---NVLEAmRANGVKRIV--FASSSTVYGEAKVIPTP-EDYPPL 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 1957676271 939 YIkNGYNLSKWVGERILER-ARVRGVRVNLYRPGNI 973
Cdd:cd05234 138 PI-SVYGASKLAAEALISAyAHLFGFQAWIFRFANI 172
|
|
| AR_SDR_e |
cd05227 |
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ... |
782-834 |
3.20e-03 |
|
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187538 [Multi-domain] Cd Length: 301 Bit Score: 41.10 E-value: 3.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1957676271 782 KVIVTGANSFVGVHIVEALLAWGasevaCLVRdGGGQSAAQR------FAQALRENRLE 834
Cdd:cd05227 1 LVLVTGATGFIASHIVEQLLKAG-----YKVR-GTVRSLSKSaklkalLKAAGYNDRLE 53
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
324-359 |
3.24e-03 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 41.46 E-value: 3.24e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1957676271 324 LYTSGTTGHPKGVLlsqanlaHFTAWYADYVQLTEQ 359
Cdd:TIGR02188 243 LYTSGSTGKPKGVL-------HTTGGYLLYAAMTMK 271
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
314-343 |
5.55e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 41.10 E-value: 5.55e-03
10 20 30
....*....|....*....|....*....|
gi 1957676271 314 RPDLDAPCMALYTSGTTGHPKGVLLSQANL 343
Cdd:PRK06814 789 NRDPDDPAVILFTSGSEGTPKGVVLSHRNL 818
|
|
| SDR_a1 |
cd05265 |
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ... |
782-1055 |
6.90e-03 |
|
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187575 [Multi-domain] Cd Length: 250 Bit Score: 39.58 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 782 KVIVTGANSFVGVHIVEALLAWGAsEVACLVRdggGQSAAQRFAqalrenrlehldlsRVRVYVADITrpqlglSEDVYQ 861
Cdd:cd05265 2 KILIIGGTRFIGKALVEELLAAGH-DVTVFNR---GRTKPDLPE--------------GVEHIVGDRN------DRDALE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 862 RL--DREFGALVHNAAnvnhvldYEslARDnVEPIfecLRLCEGRSKKiFNFVSTLSA---SSTISDDGRVLELPAAQTP 936
Cdd:cd05265 58 ELlgGEDFDVVVDTIA-------YT--PRQ-VERA---LDAFKGRVKQ-YIFISSASVylkPGRVITESTPLREPDAVGL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 937 PIYIKNGYNlsKWVGERILERA---RVRGVRVNL-YRPGNIsfnslTGVCQPHKNRlmlMLKG-----------SIQLGQ 1001
Cdd:cd05265 124 SDPWDYGRG--KRAAEDVLIEAaafPYTIVRPPYiYGPGDY-----TGRLAYFFDR---LARGrpilvpgdghsLVQFIH 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1957676271 1002 VPEfalnfdlmpvdfLARFIAFHASRYQAEKAVFNLHNPEPLSWDCYVASFREA 1055
Cdd:cd05265 194 VKD------------LARALLGAAGNPKAIGGIFNITGDEAVTWDELLEACAKA 235
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
316-339 |
8.57e-03 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 40.11 E-value: 8.57e-03
10 20
....*....|....*....|....
gi 1957676271 316 DLDAPCMALYTSGTTGHPKGVLLS 339
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAIS 108
|
|
| YdfG |
COG4221 |
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ... |
777-874 |
9.46e-03 |
|
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation
Pssm-ID: 443365 [Multi-domain] Cd Length: 240 Bit Score: 39.01 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1957676271 777 MGDVHKVI-VTGANSFVGVHIVEALLAWGAsEVACLVRDgggQSAAQRFAQALREnrlehldlsRVRVYVADITRPQlgl 855
Cdd:COG4221 1 MSDKGKVAlITGASSGIGAATARALAAAGA-RVVLAARR---AERLEALAAELGG---------RALAVPLDVTDEA--- 64
|
90 100
....*....|....*....|...
gi 1957676271 856 S-EDVYQRLDREFG---ALVHNA 874
Cdd:COG4221 65 AvEAAVAAAVAEFGrldVLVNNA 87
|
|
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