|
Name |
Accession |
Description |
Interval |
E-value |
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
146-675 |
0e+00 |
|
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: 591.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 146 DLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPD 225
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 226 WPDARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPFDatptaateprsgerttgpldaaapeaaepqpgpvlgdhalpp 305
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVID------------------------------------------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 306 lDANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHEPDWLDAGPDDVFLQAAPIAFDASTLEIWAS 385
Cdd:cd12117 119 -EALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 386 LSAGARLVLLPPGRV-DPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLV 464
Cdd:cd12117 198 LLNGARLVLAPKGTLlDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 465 FTNGYGPTENTTFTTCATFGGPAArpgEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTA 544
Cdd:cd12117 278 LVNGYGPTENTTFTTSHVVTELDE---VAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 545 AVFT--PAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAA 622
Cdd:cd12117 355 ERFVadPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVA 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 502993053 623 YVVFadgdRPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd12117 435 YVVA----EGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
156-675 |
4.98e-160 |
|
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: 471.24 E-value: 4.98e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 156 PDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLL 235
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 236 DDAGVRIVLADaqvagrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhalppldanrraate 315
Cdd:cd05930 81 EDSGAKLVLTD--------------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 316 plpgdlsPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHepdW----LDAGPDDVFLQAAPIAFDASTLEIWASLSAGAR 391
Cdd:cd05930 92 -------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL---WmqeaYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGAT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 392 LVLLPPG-RVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH-HLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGY 469
Cdd:cd05930 162 LVVLPEEvRKDPEALADLLAEEGITVLHLTPSLLRLLLQElELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLY 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 470 GPTENTTfttCATFGGPAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFT- 548
Cdd:cd05930 242 GPTEATV---DATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVp 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 549 -PAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFA 627
Cdd:cd05930 319 nPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPD 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 502993053 628 DGDrpGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05930 399 EGG--ELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
75-775 |
9.85e-154 |
|
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: 482.05 E-value: 9.85e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 75 GDVRLSVTGDAAEVHGAEPAQVAGQVDRALADGTRAPSPRVSELDLASDADRA-LVATFEGGTAPAPA-RLVHDLVDERA 152
Cdd:COG1020 407 DGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQqLLAEWNATAAPYPAdATLHELFEAQA 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 153 RLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLT 232
Cdd:COG1020 487 ARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLA 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 233 GLLDDAGVRIVLADAQVAGRVRGDRTAVPFDATPTAATEPrsgerttgpldaaapeaaepqpgpvlgdhalppldanrra 312
Cdd:COG1020 567 YMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEP---------------------------------------- 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 313 aTEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHE-PDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGAR 391
Cdd:COG1020 607 -ATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWmQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGAT 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 392 LVLLPP-GRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYG 470
Cdd:COG1020 686 LVLAPPeARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYG 765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 471 PTENTTFTTCATfggPAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTP- 549
Cdd:COG1020 766 PTETTVDSTYYE---VTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVAd 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 550 --AGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFA 627
Cdd:COG1020 843 pfGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPE 922
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 628 DGDRPgvPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAEEGALDENGAPEDALERFLCELWAKVL 707
Cdd:COG1020 923 AGAAA--AAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLV 1000
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 708 MVDSVGVDDDFFELGGHSLVAADLLGQLQQDFGVELPARTFYLSPTIAELAELKELRPLRERFEAPLP 775
Cdd:COG1020 1001 VVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAA 1068
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
145-675 |
1.00e-142 |
|
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: 428.62 E-value: 1.00e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 145 HDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPP 224
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 225 DWPDARLTGLLDDAGVRIVLADAQVAGRvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpGPVLGDHALP 304
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAAR------------------------------------------LPAGGDVALL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 305 PLDANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRA-VSRLVHEPDWLDAGPDDVFLQAAPIAFDASTLEIW 383
Cdd:cd17646 119 GDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGiVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 384 ASLSAGARLVLLPP-GRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH-HLDRLAGVRHLIAGGDVISPDAVRRLLAAhP 461
Cdd:cd17646 199 WPLVAGARLVVARPgGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEpAAGSCASLRRVFCSGEALPPELAARFLAL-P 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 462 DLVFTNGYGPTEnttfTTCATFGGPAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPA 541
Cdd:cd17646 278 GAELHNLYGPTE----AAIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 542 VTAAVFT--PAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTR 619
Cdd:cd17646 354 LTAERFVpdPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAAR 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502993053 620 LAAYVVfADGDRPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd17646 434 LVGYVV-PAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
94-759 |
1.60e-134 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 441.14 E-value: 1.60e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 94 AQVAGQVDRALADGTRAPSPRVSELDLASDADRA-LVATFEGGTAPAPARLVHDLVDERARLAPDAPALTAAGKTVPYRW 172
Cdd:PRK12467 463 ERLATHWRNLLEAIVAEPRRRLGELPLLDAEERArELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 173 LAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAgr 252
Cdd:PRK12467 543 LNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLL-- 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 253 vrgDRTAVPFDAtptaateprsgerttgpldaaapeaaepqpgPVLGDHALPPLDANRRAATEPLPgdLSPGTLAYVSYT 332
Cdd:PRK12467 621 ---AQLPVPAGL-------------------------------RSLCLDEPADLLCGYSGHNPEVA--LDPDNLAYVIYT 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 333 SGSTGTPKGVCVPHRAVSRLVHE-PDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPGRV-DPAELGAVVA 410
Cdd:PRK12467 665 SGSTGQPKGVAISHGALANYVCViAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCArDAEAFAALMA 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 411 AEGVTVLWLTAGLFHQLVDHHL-DRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTTFTTCATFGGPAAr 489
Cdd:PRK12467 745 DQGVTVLKIVPSHLQALLQASRvALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEER- 823
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 490 pgEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTP---AGGGERQYRTGDLARWR 566
Cdd:PRK12467 824 --DFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPdpfGADGGRLYRTGDLARYR 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 567 TDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGStRLAAYVV---FADGDRPGVPAPALRDWL 643
Cdd:PRK12467 902 ADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGL-QLVAYLVpaaVADGAEHQATRDELKAQL 980
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 644 RERLPEFLVPARIVALDAFPLTPNGKLDREALPG--SAAEEGALDengAPEDALERFLCELWAKVLMVDSVGVDDDFFEL 721
Cdd:PRK12467 981 RQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKpdASAVQATFV---APQTELEKRLAAIWADVLKVERVGLTDNFFEL 1057
|
650 660 670
....*....|....*....|....*....|....*...
gi 502993053 722 GGHSLVAADLLGQLQQDFGVELPARTFYLSPTIAELAE 759
Cdd:PRK12467 1058 GGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQ 1095
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
150-676 |
5.28e-134 |
|
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: 406.34 E-value: 5.28e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 150 ERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDA 229
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 230 RLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPFDATPTAATEPrsgerttgpldaaapeaaepqpgpvlgdhalpplDAN 309
Cdd:cd17651 83 RLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGA----------------------------------DAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 310 RRAAteplpgdLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVhepDWLD----AGPDDVFLQAAPIAFDASTLEIWAS 385
Cdd:cd17651 129 PDPA-------LDADDLAYVIYTSGSTGRPKGVVMPHRSLANLV---AWQArassLGPGARTLQFAGLGFDVSVQEIFST 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 386 LSAGARLVLLPPG-RVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH---HLDRLAGVRHLIAGGD-VISPDAVRRLLAAH 460
Cdd:cd17651 199 LCAGATLVLPPEEvRTDPPALAAWLDEQRISRVFLPTVALRALAEHgrpLGVRLAALRYLLTGGEqLVLTEDLREFCAGL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 461 PDLVFTNGYGPTEnTTFTTCATFGGPAARPGEagPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRP 540
Cdd:cd17651 279 PGLRLHNHYGPTE-THVVTALSLPGDPAAWPA--PPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 541 AVTAAVFT--PAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGST 618
Cdd:cd17651 356 ELTAERFVpdPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEK 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 619 RLAAYVVFADGDRPgvPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALP 676
Cdd:cd17651 436 RLVAYVVGDPEAPV--DAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
92-760 |
1.36e-131 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 422.53 E-value: 1.36e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 92 EPAQVAGQVDRA---LADGTRAPSPRVSELDLASDADRALVATFEGGTAPAPARLVHDLVDERARLAPDAPALTAAGKTV 168
Cdd:PRK10252 405 DEATLIAHAERLkalIAQFAADPALLCGDVDILLPGEYAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQF 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 169 PYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQ 248
Cdd:PRK10252 485 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTAD 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 249 VAGRVRGdrtaVPFDATPTAATeprsgerttgpldaaapeaaepqpgpvlgdhalPPLDANRRAATEPLPGDLspgtlAY 328
Cdd:PRK10252 565 QLPRFAD----VPDLTSLCYNA---------------------------------PLAPQGAAPLQLSQPHHT-----AY 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 329 VSYTSGSTGTPKGVCVPHRA-VSRLVHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPP-GRVDPAELG 406
Cdd:PRK10252 603 IIFTSGSTGRPKGVMVGQTAiVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPeAHRDPLAMQ 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 407 AVVAAEGVTVL-----WLTAGLFHQLVDHHLDRLAGVRHLIAGGDVIsPDAVRRLLAAHPDLVFTNGYGPTENTTFTTCA 481
Cdd:PRK10252 683 QFFAEYGVTTThfvpsMLAAFVASLTPEGARQSCASLRQVFCSGEAL-PADLCREWQQLTGAPLHNLYGPTEAAVDVSWY 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 482 TFGGPAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFT--PAGGGERQYRT 559
Cdd:PRK10252 762 PAFGEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIadPFAPGERMYRT 841
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 560 GDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALP------EPGAGGSTRLAAYVVFADGDRPG 633
Cdd:PRK10252 842 GDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHAcvinqaAATGGDARQLVGYLVSQSGLPLD 921
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 634 vpAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPgsAAEEGALDENGAPEDALERFLCELWAKVLMVDSVG 713
Cdd:PRK10252 922 --TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALP--LPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVD 997
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 502993053 714 VDDDFFELGGHSLVAADLLGQLQQDFGVELPARTFYLSPTIAELAEL 760
Cdd:PRK10252 998 ADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATL 1044
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
186-608 |
1.31e-129 |
|
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: 392.01 E-value: 1.31e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 186 RAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRG-DRTAVPFDA 264
Cdd:TIGR01733 19 AGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGlVLPVILLDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 265 TPTAATEPRsgerttgpldaaapeaaepqpgpvlgdhalppldanrrAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCV 344
Cdd:TIGR01733 99 LELAALDDA--------------------------------------PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 345 PHRAVSRLV-HEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPG--RVDPAELGAVVAAEGVTVLWLTA 421
Cdd:TIGR01733 141 THRSLVNLLaWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDeeRDDAALLAALIAEHPVTVLNLTP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 422 GLFHQLVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTTFTTCATFggPAARPGEAGPLPIGRP 501
Cdd:TIGR01733 221 SLLALLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLV--DPDDAPRESPVPIGRP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 502 IRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTP----AGGGERQYRTGDLARWRTDGSLDFLGRA 577
Cdd:TIGR01733 299 LANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRI 378
|
410 420 430
....*....|....*....|....*....|.
gi 502993053 578 DDQVKIKGYRVEPAEVAAALGAHPAVTAAVA 608
Cdd:TIGR01733 379 DDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
90-758 |
2.53e-126 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 417.25 E-value: 2.53e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 90 GAEPAQVAGQVDRALADGTRAPSPRVSELDLASDADRALVATFEGGTAPAPA--RLVHDLVDERARLAPDAPALTAAGKT 167
Cdd:PRK12467 3041 AAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPseRLVHQLIEAQVARTPEAPALVFGDQQ 3120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 168 VPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADA 247
Cdd:PRK12467 3121 LSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQA 3200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 248 QVA---GRVRGDRTAVpfdatptaateprsgerttgpLDAAAPEaaepqpgpvlgdhalPPLDANRRAATEPlpgdlspG 324
Cdd:PRK12467 3201 HLLeqlPAPAGDTALT---------------------LDRLDLN---------------GYSENNPSTRVMG-------E 3237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 325 TLAYVSYTSGSTGTPKGVCVPHRAVSRLVHepdWLDA----GPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPGRV 400
Cdd:PRK12467 3238 NLAYVIYTSGSTGKPKGVGVRHGALANHLC---WIAEayelDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLW 3314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 401 DPAELGAVVAAEGVTVLWLTAGLFHQLV-DHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTTFTT 479
Cdd:PRK12467 3315 DPEELWQAIHAHRISIACFPPAYLQQFAeDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVT 3394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 480 CATFGGPAArpGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTP---AGGGERQ 556
Cdd:PRK12467 3395 LWKCGGDAV--CEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVAdpfSGSGGRL 3472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 557 YRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGsTRLAAYVVFADGDrpGVPA 636
Cdd:PRK12467 3473 YRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGG-KQLVAYVVPADPQ--GDWR 3549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 637 PALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAEegALDENGAPEDALERFLCELWAKVLMVDSVGVDD 716
Cdd:PRK12467 3550 ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAK--GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTD 3627
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 502993053 717 DFFELGGHSLVAADLLGQLQQDFGVELPARTFYLSPTIAELA 758
Cdd:PRK12467 3628 NFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA 3669
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
111-758 |
4.66e-125 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 413.40 E-value: 4.66e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 111 PSPRVSELDLASDADRALVatFEGGTAPA----PARLVHDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVR 186
Cdd:PRK12467 1541 PERRLGELDLLDEAERRQI--LEGWNATHtgypLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIA 1618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 187 AGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVrgdrtavpfdatp 266
Cdd:PRK12467 1619 LGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARL------------- 1685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 267 taateprsgerttgPLDAAAPEAAEPQPGPVLGDHAlpplDANRRAAteplpgdLSPGTLAYVSYTSGSTGTPKGVCVPH 346
Cdd:PRK12467 1686 --------------PLPDGLRSLVLDQEDDWLEGYS----DSNPAVN-------LAPQNLAYVIYTSGSTGRPKGAGNRH 1740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 347 RAVSRLVH-EPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPG-RVDPAELGAVVAAEGVTVLWLTAGLF 424
Cdd:PRK12467 1741 GALVNRLCaTQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGaHRDPEQLIQLIERQQVTTLHFVPSML 1820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 425 HQLVDH--HLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENT---TFTTCATfggpaARPGEAGPLPIG 499
Cdd:PRK12467 1821 QQLLQMdeQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAvdvTHWTCRR-----KDLEGRDSVPIG 1895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 500 RPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTP---AGGGERQYRTGDLARWRTDGSLDFLGR 576
Cdd:PRK12467 1896 QPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVAdpfGTVGSRLYRTGDLARYRADGVIEYLGR 1975
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 577 ADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGsTRLAAYVV------FADGDRPGVPAPALRDWLRERLPEF 650
Cdd:PRK12467 1976 IDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANG-KQLVAYVVptdpglVDDDEAQVALRAILKNHLKASLPEY 2054
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 651 LVPARIVALDAFPLTPNGKLDREALPGSAAEEGALDENgAPEDALERFLCELWAKVLMVDSVGVDDDFFELGGHSLVAAD 730
Cdd:PRK12467 2055 MVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYV-APQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQ 2133
|
650 660
....*....|....*....|....*...
gi 502993053 731 LLGQLQQDfGVELPARTFYLSPTIAELA 758
Cdd:PRK12467 2134 VVSRARQA-GIRFTPKDLFQHQTVQSLA 2160
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
156-675 |
2.29e-124 |
|
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: 379.73 E-value: 2.29e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 156 PDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLL 235
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 236 DDAGVRIVLADaqvagrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhalppldanrraate 315
Cdd:cd17643 81 ADSGPSLLLTD--------------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 316 plpgdlsPGTLAYVSYTSGSTGTPKGVCVPHRAVSRL-VHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVL 394
Cdd:cd17643 92 -------PDDLAYVIYTSGSTGRPKGVVVSHANVLALfAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 395 LPPG-RVDPAELGAVVAAEGVTVLWLTAGLFHQLV---DHHLDRLAGVRHLIAGGDVISPDAVRRLLAAH----PDLVft 466
Cdd:cd17643 165 VPYEvARSPEDFARLLRDEGVTVLNQTPSAFYQLVeaaDRDGRDPLALRYVIFGGEALEAAMLRPWAGRFgldrPQLV-- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 467 NGYGPTENTTFTTCATFGGPAARPGEAGPlpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAV 546
Cdd:cd17643 243 NMYGITETTVHVTFRPLDAADLPAAAASP--IGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAER 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 547 FTPA---GGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAY 623
Cdd:cd17643 321 FVANpfgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAY 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502993053 624 VVFADGDRPgvPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd17643 401 VVADDGAAA--DIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
156-675 |
7.43e-123 |
|
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: 376.63 E-value: 7.43e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 156 PDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLL 235
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 236 DDAGVRIVLADaqvagrvrgdrtavpfDATPtaateprsgerttgpldaaapeaaepQPGPVLGDHALPPLDANRRAATE 315
Cdd:cd12116 81 EDAEPALVLTD----------------DALP--------------------------DRLPAGLPVLLLALAAAAAAPAA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 316 PLPGDlSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHE-PDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVL 394
Cdd:cd12116 119 PRTPV-SPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSmRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 395 LPPG-RVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAGVRhLIAGGDVISPDAVRRLLAAHPDLvfTNGYGPTE 473
Cdd:cd12116 198 APREtQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGLT-ALCGGEALPPDLAARLLSRVGSL--WNLYGPTE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 474 NTTFTTCATFGgpaarpGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTP---A 550
Cdd:cd12116 275 TTIWSTAARVT------AAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPdpfA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 551 GGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGaGGSTRLAAYVVFADGD 630
Cdd:cd12116 349 GPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAGA 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 502993053 631 RPGvpAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd12116 428 APD--AAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
94-758 |
1.62e-122 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 406.27 E-value: 1.62e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 94 AQVAGQVDRALADGTRAPSPRVSELDLASDADRA-LVATFEGGTAPAP-ARLVHDLVDERARLAPDAPALTAAGKTVPYR 171
Cdd:PRK12316 461 ERMARHWQNLLRGMVENPQARVDELPMLDAEERGqLVEGWNATAAEYPlQRGVHRLFEEQVERTPEAPALAFGEETLDYA 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 172 WLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAG 251
Cdd:PRK12316 541 ELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGR 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 252 RVrgdrtavpfdatptaateprsgerttgPLDAAAPEAAEPQPGPVLGDHAlppldanrraaTEPLPGDLSPGTLAYVSY 331
Cdd:PRK12316 621 KL---------------------------PLAAGVQVLDLDRPAAWLEGYS-----------EENPGTELNPENLAYVIY 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 332 TSGSTGTPKGVCVPHRAVSRLVhepDW------LDAGpdDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPG-RVDPAE 404
Cdd:PRK12316 663 TSGSTGKPKGAGNRHRALSNRL---CWmqqaygLGVG--DTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGdHRDPAK 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 405 LGAVVAAEGVTVLWLTAGLFHQLV-DHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTTFTTCATf 483
Cdd:PRK12316 738 LVELINREGVDTLHFVPSMLQAFLqDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWT- 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 484 ggpaARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPA--GGGERQYRTGD 561
Cdd:PRK12316 817 ----CVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSpfVAGERMYRTGD 892
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 562 LARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALpepgAGGSTRLAAYVVFAdgDRPGVPAPALRD 641
Cdd:PRK12316 893 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVGYVVLE--SEGGDWREALKA 966
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 642 WLRERLPEFLVPARIVALDAFPLTPNGKLDREALPgsaAEEGALDENG--APEDALERFLCELWAKVLMVDSVGVDDDFF 719
Cdd:PRK12316 967 HLAASLPEYMVPAQWLALERLPLTPNGKLDRKALP---APEASVAQQGyvAPRNALERTLAAIWQDVLGVERVGLDDNFF 1043
|
650 660 670
....*....|....*....|....*....|....*....
gi 502993053 720 ELGGHSLVAADLLGQLQQDfGVELPARTFYLSPTIAELA 758
Cdd:PRK12316 1044 ELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIRSLA 1081
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
156-676 |
5.52e-122 |
|
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: 373.13 E-value: 5.52e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 156 PDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLL 235
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 236 DDAGVRIVLAdaqvagrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhalppldanrraate 315
Cdd:cd17652 81 ADARPALLLT---------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 316 plpgdlSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVH-EPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVL 394
Cdd:cd17652 91 ------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAaQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 395 LPPGRVDP-AELGAVVAAEGVTVLWLTAGLFHQLVDhhlDRLAGVRHLIAGGDVISPDAVRRLlaaHPDLVFTNGYGPTE 473
Cdd:cd17652 165 APAEELLPgEPLADLLREHRITHVTLPPAALAALPP---DDLPDLRTLVVAGEACPAELVDRW---APGRRMINAYGPTE 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 474 NTTfttCATFGGPaarPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTP---A 550
Cdd:cd17652 239 TTV---CATMAGP---LPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVAdpfG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 551 GGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGD 630
Cdd:cd17652 313 APGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGA 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 502993053 631 RPgvPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALP 676
Cdd:cd17652 393 AP--TAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
147-676 |
1.20e-120 |
|
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: 371.66 E-value: 1.20e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 147 LVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDW 226
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 227 PDARLTGLLDDAGVRIVLADAQVAgrvrgdrtavpfdatptaatEPRSGERTTGPLDAaapeaaepqpgpvlgdhalppl 306
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQ--------------------PPIAFIGLIDLLDE---------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 307 DANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHepdWLD----AGPDDVFLQAAPIAFDASTLEI 382
Cdd:cd17655 120 DTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVE---WANkviyQGEHLRVALFASISFDASVTEI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 383 WASLSAGARLVLLPPGRV-DPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHP 461
Cdd:cd17655 197 FASLLSGNTLYIVRKETVlDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 462 DLV-FTNGYGPTENTTfttCATFGGPAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRP 540
Cdd:cd17655 277 TNPtITNAYGPTETTV---DASIYQYEPETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 541 AVTAAVFT--PAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGST 618
Cdd:cd17655 354 ELTAEKFVddPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQN 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 619 RLAAYVVFadgDRPgVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALP 676
Cdd:cd17655 434 YLCAYIVS---EKE-LPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALP 487
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-762 |
1.83e-120 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 400.10 E-value: 1.83e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 72 VTVGD-VRLSVTGDAAEVHGAEPAQVAGQVDRALADGTRAPSPRVSELD-LASDADRALVATFEGGTAPAPA-RLVHDLV 148
Cdd:PRK12316 4478 VGLGEtLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQlLEKAEQQRIVALWNRTDAGYPAtRCVHQLV 4557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 149 DERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPD 228
Cdd:PRK12316 4558 AERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPR 4637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 229 ARLTGLLDDAGVRIVLADAQVAGRVrgdrtavpfdatPTAAteprsgerttgpldaaapeaaepqpgpvlGDHAL---PP 305
Cdd:PRK12316 4638 ERLAYMMEDSGAALLLTQSHLLQRL------------PIPD-----------------------------GLASLaldRD 4676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 306 LDANRRAATEPLpGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVH-EPDWLDAGPDDVFLQAAPIAFDASTLEIWA 384
Cdd:PRK12316 4677 EDWEGFPAHDPA-VRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHaTGERYELTPDDRVLQFMSFSFDGSHEGLYH 4755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 385 SLSAGARLVLLPPGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDR--LAGVRHLIAGGDVISPDAVRRLLAAHPD 462
Cdd:PRK12316 4756 PLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDgePPSLRVYCFGGEAVAQASYDLAWRALKP 4835
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 463 LVFTNGYGPTENTTFTTCATfgGPAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAV 542
Cdd:PRK12316 4836 VYLFNGYGPTETTVTVLLWK--ARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPAL 4913
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 543 TAAVFTP---AGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGStR 619
Cdd:PRK12316 4914 TAERFVPdpfGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGK-Q 4992
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 620 LAAYVVFAD---GDRPGVPAP---ALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAeeGALDEN-GAPE 692
Cdd:PRK12316 4993 LVGYVVPQDpalADADEAQAElrdELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDA--SLLQQAyVAPR 5070
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 693 DALERFLCELWAKVLMVDSVGVDDDFFELGGHSLVAADLLGQLQQDFGVELPARTFYLSPTIAELAELKE 762
Cdd:PRK12316 5071 SELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAA 5140
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
156-676 |
5.52e-119 |
|
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: 365.92 E-value: 5.52e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 156 PDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLL 235
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 236 DDAGVRIVLADAqvagrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhalppldanrraate 315
Cdd:cd17649 81 EDSGAGLLLTHH-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 316 plpgdlsPGTLAYVSYTSGSTGTPKGVCVPHRAVSR-LVHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVL 394
Cdd:cd17649 93 -------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAhCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 395 LPPGR-VDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAG----VRHLIAGGDVISPDAVRRLLAAHPDLVftNGY 469
Cdd:cd17649 166 RPDELwASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGrppsLRLYIFGGEALSPELLRRWLKAPVRLF--NAY 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 470 GPTEnTTFTtcATFGGPAARPGEAGP-LPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFT 548
Cdd:cd17649 244 GPTE-ATVT--PLVWKCEAGAARAGAsMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFV 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 549 P---AGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGsTRLAAYVV 625
Cdd:cd17649 321 PdpfGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGG-KQLVAYVV 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 502993053 626 FADGDRPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALP 676
Cdd:cd17649 400 LRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
95-759 |
1.06e-117 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 392.22 E-value: 1.06e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 95 QVAGQVDRALADgtrapsprvseLDLASDADRALVATFEGGTAPAPARLVHDLVDERARLAPDAPALTAAGKTVPYRWLA 174
Cdd:PRK05691 1095 QVCEDPQRALGD-----------VQLLDAAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELH 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 175 EHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVr 254
Cdd:PRK05691 1164 AQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERL- 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 255 gdrtavpfdatptaatePRSGERTTGPLDAAAPEAAEPQPgPVLgdhalppldanrraateplpgDLSPGTLAYVSYTSG 334
Cdd:PRK05691 1243 -----------------PQAEGVSAIALDSLHLDSWPSQA-PGL---------------------HLHGDNLAYVIYTSG 1283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 335 STGTPKGVCVPHRAVSRLVHepdWLDA----GPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPG-RVDPAELGAVV 409
Cdd:PRK05691 1284 STGQPKGVGNTHAALAERLQ---WMQAtyalDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGeHRDPQRIAELV 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 410 AAEGVTVLWLTAGLFHQLVDHHL-DRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTE---NTTFTTCAtfgg 485
Cdd:PRK05691 1361 QQYGVTTLHFVPPLLQLFIDEPLaAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTEtaiNVTHWQCQ---- 1436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 486 paARPGEAGPlpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTP---AGGGERQYRTGDL 562
Cdd:PRK05691 1437 --AEDGERSP--IGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPdplGEDGARLYRTGDR 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 563 ARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGStRLAAYvvFADGDRPGVPAPALRDW 642
Cdd:PRK05691 1513 ARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGA-QLVGY--YTGEAGQEAEAERLKAA 1589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 643 LRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAEEGaldENGAPEDALERFLCELWAKVLMVDSVGVDDDFFELG 722
Cdd:PRK05691 1590 LAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQR---EHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALG 1666
|
650 660 670
....*....|....*....|....*....|....*..
gi 502993053 723 GHSLVAADLLGQLQQDFGVELPARTFYLSPTIAELAE 759
Cdd:PRK05691 1667 GHSLLATQIVSRTRQACDVELPLRALFEASELGAFAE 1703
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-758 |
9.58e-117 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 389.32 E-value: 9.58e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 72 VTVGD-VRLSVTGDAAEVHGAEPAQVAGQVDRALADGTRAPSPRVSELDLASDADRALV-ATFEGGTAPAPARL-VHDLV 148
Cdd:PRK12316 1930 VTLGEtLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRIlADWDRTPEAYPRGPgVHQRI 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 149 DERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPD 228
Cdd:PRK12316 2010 AEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPA 2089
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 229 ARLTGLLDDAGVRIVLADAQVAGRVrgdrtavpfdatptaatePRSGERTTGPLDaaapeaaepqpgpvlgdhalPPLDA 308
Cdd:PRK12316 2090 ERLAYMLEDSGAALLLTQRHLLERL------------------PLPAGVARLPLD--------------------RDAEW 2131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 309 NRRAATEPLPgDLSPGTLAYVSYTSGSTGTPKGVCVPHRA-VSRLVHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLS 387
Cdd:PRK12316 2132 ADYPDTAPAV-QLAGENLAYVIYTSGSTGLPKGVAVSHGAlVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLL 2210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 388 AGARLVLLPPGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH--HLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVF 465
Cdd:PRK12316 2211 NGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHaeRDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYL 2290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 466 TNGYGPTEnTTFTTCATFGGPAARPGEAGPlPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAA 545
Cdd:PRK12316 2291 FNGYGPTE-AVVTPLLWKCRPQDPCGAAYV-PIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAE 2368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 546 VFTP---AGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGsTRLAA 622
Cdd:PRK12316 2369 RFVPdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASG-KQLVA 2447
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 623 YVVFADGdRPGVPApALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAEEgALDENGAPEDALERFLCEL 702
Cdd:PRK12316 2448 YVVPDDA-AEDLLA-ELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQ-LRQAYVAPQEGLEQRLAAI 2524
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 502993053 703 WAKVLMVDSVGVDDDFFELGGHSLVAADLLGQLQQDFGVELPARTFYLSPTIAELA 758
Cdd:PRK12316 2525 WQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFA 2580
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
144-675 |
1.16e-110 |
|
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: 344.30 E-value: 1.16e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 144 VHDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALP 223
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 224 PDWPDARLTGLLDDAGVRIVLADAQvagrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhal 303
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLTDPD------------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 304 ppldanrraateplpgdlspgTLAYVSYTSGSTGTPKGVCVPHRAVSRLVhepDW--LDAGPDDV--FLQAAPIAFDAST 379
Cdd:cd12115 106 ---------------------DLAYVIYTSGSTGRPKGVAIEHRNAAAFL---QWaaAAFSAEELagVLASTSICFDLSV 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 380 LEIWASLSAGARLVLlppgrVDPA-ELGAVVAAEGVTVLWLTAGLFHQLVDHhlDRL-AGVRHLIAGGDVISPDAVRRLL 457
Cdd:cd12115 162 FELFGPLATGGKVVL-----ADNVlALPDLPAAAEVTLINTVPSAAAELLRH--DALpASVRVVNLAGEPLPRDLVQRLY 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 458 AAHPDLVFTNGYGPTENTTFTTCAtfggpAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYL 537
Cdd:cd12115 235 ARLQVERVVNLYGPSEDTTYSTVA-----PVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 538 GRPAVTAAVFTPA--GGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAG 615
Cdd:cd12115 310 GRPGLTAERFLPDpfGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAA 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 616 GSTRLAAYVVfADGDRPGVPApALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd12115 390 GERRLVAYIV-AEPGAAGLVE-DLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
156-675 |
6.95e-104 |
|
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: 327.69 E-value: 6.95e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 156 PDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLL 235
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 236 DDAGVRIVLADaqvagrvrgdrtavpfdatptaateprsgerttGPLDAAAPEAAEPQPGPVLGDHALPPldanrraate 315
Cdd:cd12114 81 ADAGARLVLTD---------------------------------GPDAQLDVAVFDVLILDLDALAAPAP---------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 316 PLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHE-PDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVL 394
Cdd:cd12114 118 PPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDiNRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 395 LPPGRV-DPAELGAVVAAEGVTVLWLTAGLFHQLVDH---HLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYG 470
Cdd:cd12114 198 PDEARRrDPAHWAELIERHGVTLWNSVPALLEMLLDVleaAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 471 PTENTTFTTCATFGGPaarPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPA 550
Cdd:cd12114 278 ATEASIWSIYHPIDEV---PPDWRSIPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 551 GGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGsTRLAAYVVfADGD 630
Cdd:cd12114 355 PDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGG-KRLAAFVV-PDND 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 502993053 631 RPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd12114 433 GTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
92-758 |
3.77e-100 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 340.99 E-value: 3.77e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 92 EP--AQVAGQVDRALADGTRAPSPRVSELDLASDADRALVATFEGGTA--PAPARLVHDLVDERARLAPDAPALTAAGKT 167
Cdd:PRK05691 2134 EPriARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAgeARLDQTLHGLFAAQAARTPQAPALTFAGQT 2213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 168 VPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADA 247
Cdd:PRK05691 2214 LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDR 2293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 248 QVagrvrgdrtavpFDATptaateprsgerttGPLDAAAPEAAEPQPGPVLGDHAlppldanrraaTEPLPGDLSPGTLA 327
Cdd:PRK05691 2294 AL------------FEAL--------------GELPAGVARWCLEDDAAALAAYS-----------DAPLPFLSLPQHQA 2336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 328 YVSYTSGSTGTPKGVCVPH-------RAVSRLvhepdwLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPGRV 400
Cdd:PRK05691 2337 YLIYTSGSTGKPKGVVVSHgeiamhcQAVIER------FGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQW 2410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 401 DPAELGAVVAAEGVTVLWLTAGLFHQLVDHHL--DRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTTFT 478
Cdd:PRK05691 2411 GAEEICQLIREQQVSILGFTPSYGSQLAQWLAgqGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMP 2490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 479 TCATfgGPAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTP---AGGGER 555
Cdd:PRK05691 2491 LACL--APEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVAdpfAADGGR 2568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 556 QYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGStRLAAYVVFA----DGDR 631
Cdd:PRK05691 2569 LYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGK-QLAGYLVSAvagqDDEA 2647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 632 PGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAEEgALDENGAPEDALERFLCELWAKVLMVDS 711
Cdd:PRK05691 2648 QAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPEL-NRQAYQAPRSELEQQLAQIWREVLNVER 2726
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 502993053 712 VGVDDDFFELGGHSLVAADLLGQLQQdFGVELPARTFYLSPTIAELA 758
Cdd:PRK05691 2727 VGLGDNFFELGGDSILSIQVVSRARQ-LGIHFSPRDLFQHQTVQTLA 2772
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
146-675 |
1.04e-99 |
|
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: 315.02 E-value: 1.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 146 DLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPD 225
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 226 WPDARLTGLLDDAGVRIVLADAqvagrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhalpp 305
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTTD---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 306 ldanrraateplpgdlSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLV-HEPDWLDAGPDDVFLQAAPIAFDASTLEIWA 384
Cdd:cd17653 103 ----------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVsQPPARLDVGPGSRVAQVLSIAFDACIGEIFS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 385 SLSAGARLVLlppgrVDPAELGAVVAAEgVTVLWLTAGLFHQLVDHHLDRLAGVrhlIAGGDVISPDAVRRLLaahPDLV 464
Cdd:cd17653 167 TLCNGGTLVL-----ADPSDPFAHVART-VDALMSTPSILSTLSPQDFPNLKTI---FLGGEAVPPSLLDRWS---PGRR 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 465 FTNGYGPTEnttfTTCATFGgPAARPGEagPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTA 544
Cdd:cd17653 235 LYNAYGPTE----CTISSTM-TELLPGQ--PVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 545 A--VFTPAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVE-PAEVAAALGAHPAVTAAVALPEPGaggstRLA 621
Cdd:cd17653 308 SkfVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINlEEIEEVVLQSQPEVTQAAAIVVNG-----RLV 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502993053 622 AYVVFADGDRPGvpapaLRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd17653 383 AFVTPETVDVDG-----LRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
144-676 |
3.13e-99 |
|
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: 315.14 E-value: 3.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 144 VHDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALP 223
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 224 PDWPDARLTGLLDDAGVRIVLadaqvagrvrgdrtavpfdatptaaTEPRSgerttgpldaaapeaaepqpgpvlgdhal 303
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLL-------------------------TQPEN----------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 304 ppldanrraateplpgdlspgtLAYVSYTSGSTGTPKGVCVPHRAV---SRLVHEPdwLDAGPDDVFLQAAPIAFDASTL 380
Cdd:cd17644 108 ----------------------LAYVIYTSGSTGKPKGVMIEHQSLvnlSHGLIKE--YGITSSDRVLQFASIAFDVAAE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 381 EIWASLSAGARLVLLPPG-RVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH-HLDRLAGVRHL---IAGGDVISPDAVRR 455
Cdd:cd17644 164 EIYVTLLSGATLVLRPEEmRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLElLLSTIDLPSSLrlvIVGGEAVQPELVRQ 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 456 LLAAHPDLV-FTNGYGPTENTTFTTCATFGGPAARPGEAgpLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLAL 534
Cdd:cd17644 244 WQKNVGNFIqLINVYGPTEATIAATVCRLTQLTERNITS--VPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLAR 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 535 GYLGRPAVTAAVFTP----AGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALP 610
Cdd:cd17644 322 GYLNRPELTAEKFIShpfnSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIV 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993053 611 EPGAGGSTRLAAYVVfadGDRPGVPAPA-LRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALP 676
Cdd:cd17644 402 REDQPGNKRLVAYIV---PHYEESPSTVeLRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
95-763 |
3.48e-99 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 338.08 E-value: 3.48e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 95 QVAGQVDRALADGTRAPSPRVSELDLASDADRALVATFEGGTAP--APARLVHDLVDERARLAPDAPALTAAGKTVPYRW 172
Cdd:PRK12316 3008 RLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAeyPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAE 3087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 173 LAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGR 252
Cdd:PRK12316 3088 LNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLP 3167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 253 VRGDRTAVPFDATPTAATEprsgerttgpldaaapeaaepqpgpvlgdhalppldanrraatEPLPGDLSPGTLAYVSYT 332
Cdd:PRK12316 3168 LAQGVQVLDLDRGDENYAE-------------------------------------------ANPAIRTMPENLAYVIYT 3204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 333 SGSTGTPKGVCVPHRAVS-RLVHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPGR-VDPAELGAVVA 410
Cdd:PRK12316 3205 SGSTGKPKGVGIRHSALSnHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDwRDPALLVELIN 3284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 411 AEGVTVLWLTAGLFHQ-LVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLvftNGYGPTENTTFTTCATFGGPAAr 489
Cdd:PRK12316 3285 SEGVDVLHAYPSMLQAfLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLY---NLYGPTEATITVTHWQCVEEGK- 3360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 490 pgeaGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVF--TPAGGGERQYRTGDLARWRT 567
Cdd:PRK12316 3361 ----DAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFvpDPFVPGERLYRTGDLARYRA 3436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 568 DGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGaggsTRLAAYVVfadgdrPGVPAPALRDWLR--- 644
Cdd:PRK12316 3437 DGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDG----RQLVAYVV------PEDEAGDLREALKahl 3506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 645 -ERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAEEGALDENgAPEDALERFLCELWAKVLMVDSVGVDDDFFELGG 723
Cdd:PRK12316 3507 kASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYV-APVNELERRLAAIWADVLKLEQVGLTDNFFELGG 3585
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 502993053 724 HSLVAADLLGQLQQdFGVELPARTFYLSPTIAELAELKEL 763
Cdd:PRK12316 3586 DSIISLQVVSRARQ-AGIRFTPKDLFQHQTIQGLARVARV 3624
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
144-675 |
5.11e-97 |
|
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: 308.66 E-value: 5.11e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 144 VHDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALP 223
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 224 PDWPDARLTGLLDDAGVRIVLAdaqvagrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhal 303
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 304 ppldanrraateplpgdlspgtlAYVSYTSGSTGTPKGVCVPHRA-VSRLVHEPDWLDAGPDDVFLQAAPIAFDAS-TLE 381
Cdd:COG0318 103 -----------------------ALILYTSGTTGRPKGVMLTHRNlLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 382 IWASLSAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH---HLDRLAGVRHLIAGGDVISPDAVRRLLA 458
Cdd:COG0318 160 LLAPLLAGATLVLLP--RFDPERVLELIERERVTVLFGVPTMLARLLRHpefARYDLSSLRLVVSGGAPLPPELLERFEE 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 459 AHpDLVFTNGYGPTENTTFTTCATFGGPAARPGeagplPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLG 538
Cdd:COG0318 238 RF-GVRIVEGYGLTETSPVVTVNPEDPGERRPG-----SVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWN 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 539 RPAVTAAVFtpAGGGerqYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGST 618
Cdd:COG0318 312 DPEATAEAF--RDGW---LRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGE 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 502993053 619 RLAAYVVFADGdrPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:COG0318 387 RVVAFVVLRPG--AELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
145-676 |
6.21e-95 |
|
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: 302.94 E-value: 6.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 145 HDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPP 224
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 225 DWPDARLTGLLDDAGVRIVLADaqvagrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhalp 304
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTN---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 305 pldanrraateplpgdlsPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLV--HEPdWLDAGPDDVFLQAAPIAFDASTLEI 382
Cdd:cd17645 103 ------------------PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCewHRP-YFGVTPADKSLVYASFSFDASAWEI 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 383 WASLSAGARLVLLPPG-RVDPAELGAVVAAEGVTVLWLTAGL---FHQLVDHHLdrlagvRHLIAGGDVISpdavrrlLA 458
Cdd:cd17645 164 FPHLTAGAALHVVPSErRLDLDALNDYFNQEGITISFLPTGAaeqFMQLDNQSL------RVLLTGGDKLK-------KI 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 459 AHPDLVFTNGYGPTENTTFTTCATFGGPAARpgeagpLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLG 538
Cdd:cd17645 231 ERKGYKLVNNYGPTENTVVATSFEIDKPYAN------IPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLN 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 539 RPAVTAAVFT--PAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGG 616
Cdd:cd17645 305 RPELTAEKFIvhPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADG 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 617 STRLAAYVVfadgDRPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALP 676
Cdd:cd17645 385 RKYLVAYVT----APEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
156-675 |
2.62e-94 |
|
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: 301.31 E-value: 2.62e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 156 PDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLL 235
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 236 DDAGVRIVLADaqvagrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhalppldanrraate 315
Cdd:cd17650 81 EDSGAKLLLTQ--------------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 316 plpgdlsPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHEpdW-----LDAGPDDVfLQAAPIAFDASTLEIWASLSAGA 390
Cdd:cd17650 92 -------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHA--WrreyeLDSFPVRL-LQMASFSFDVFAGDFARSLLNGG 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 391 RLVLLPPG-RVDPAELGAVVAAEGVTVLWLTAGLFHQL---VDHHLDRLAGVRHLIAGGDVISP----DAVRRLLAAhpd 462
Cdd:cd17650 162 TLVICPDEvKLDPAALYDLILKSRITLMESTPALIRPVmayVYRNGLDLSAMRLLIVGSDGCKAqdfkTLAARFGQG--- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 463 LVFTNGYGPTENTTFTTcaTFGGPAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAV 542
Cdd:cd17650 239 MRIINSYGVTEATIDST--YYEEGRDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPEL 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 543 TAAVFT--PAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRL 620
Cdd:cd17650 317 TAERFVenPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARL 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502993053 621 AAYVVFADgdrpGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd17650 397 CAYVVAAA----TLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
156-676 |
6.18e-93 |
|
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: 299.00 E-value: 6.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 156 PDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLL 235
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 236 DDAGVRIVLADAQVAgrvrgdrtaVPFDATptaateprsgerttgpldaaapeaaepqpgpvlGDHALPPLDANRRAATE 315
Cdd:cd17656 82 LDSGVRVVLTQRHLK---------SKLSFN---------------------------------KSTILLEDPSISQEDTS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 316 PLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLV-HEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVL 394
Cdd:cd17656 120 NIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLhFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 395 LPPG-RVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHH--LDRLA-GVRHLIAGGD-VISPDAVRRLLAAHpDLVFTNGY 469
Cdd:cd17656 200 IREEtKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSERefINRFPtCVKHIITAGEqLVITNEFKEMLHEH-NVHLHNHY 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 470 GPTENTTFTTCaTFggpaaRPGEAGPL--PIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVF 547
Cdd:cd17656 279 GPSETHVVTTY-TI-----NPEAEIPElpPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 548 T--PAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVV 625
Cdd:cd17656 353 FpdPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 502993053 626 FADgdrpGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALP 676
Cdd:cd17656 433 MEQ----ELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
144-675 |
1.11e-91 |
|
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: 295.61 E-value: 1.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 144 VHDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALP 223
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 224 PDWPDARLTGLLDDAGVRIVLADaqvagrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhal 303
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTS--------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 304 ppldanrraateplpgdlSPGTLAYVSYTSGSTGTPKGVCVPHRAV-SRLVHEPDWLDAGPDDVFLQAAPIAFDASTLEI 382
Cdd:cd05918 104 ------------------SPSDAAYVIFTSGSTGKPKGVVIEHRALsTSALAHGRALGLTSESRVLQFASYTFDVSILEI 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 383 WASLSAGArLVLLPP--GRVDpaELGAVVAAEGVTVLWLTAGLFHQLvdhHLDRLAGVRHLIAGGDVISPDAVRRLlAAH 460
Cdd:cd05918 166 FTTLAAGG-CLCIPSeeDRLN--DLAGFINRLRVTWAFLTPSVARLL---DPEDVPSLRTLVLGGEALTQSDVDTW-ADR 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 461 PDLVftNGYGPTENTTFTTCAtfggpaARPGEAGPLPIGRPIrGTRVRVLDRL--GRPVPPGVVGDLYALGEGLALGYLG 538
Cdd:cd05918 239 VRLI--NAYGPAECTIAATVS------PVVPSTDPRNIGRPL-GATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLN 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 539 RPAVTAAVF--TPA-------GGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPA----VTA 605
Cdd:cd05918 310 DPEKTAAAFieDPAwlkqegsGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPgakeVVV 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 606 AVALPePGAGGSTRLAAYVVFAD--------GDRPGVPAP-------ALRDWLRERLPEFLVPARIVALDAFPLTPNGKL 670
Cdd:cd05918 390 EVVKP-KDGSSSPQLVAFVVLDGsssgsgdgDSLFLEPSDefralvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKI 468
|
....*
gi 502993053 671 DREAL 675
Cdd:cd05918 469 DRRAL 473
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
152-675 |
3.23e-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: 293.38 E-value: 3.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 152 ARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARL 231
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 232 TGLLDDAGVRIVLADaqvagrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhalppldanrr 311
Cdd:cd05945 81 REILDAAKPALLIAD----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 312 aateplpgdlsPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVhepDWLDA----GPDDVFLQAAPIAFDASTLEIWASLS 387
Cdd:cd05945 96 -----------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFT---NWMLSdfplGPGDVFLNQAPFSFDLSVMDLYPALA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 388 AGARLVLLPPGRV-DPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLD---RLAGVRHLIAGGDVISPDAVRRLLAAHPDL 463
Cdd:cd05945 162 SGATLVPVPRDATaDPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFtpeSLPSLRHFLFCGEVLPHKTARALQQRFPDA 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 464 VFTNGYGPTENTTftTCATFGGPAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVT 543
Cdd:cd05945 242 RIYNTYGPTEATV--AVTYIEVTPEVLDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKT 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 544 AAVFTPaGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAY 623
Cdd:cd05945 320 AAAFFP-DEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAF 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502993053 624 VVFADGDRPGVPApALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05945 399 VVPKPGAEAGLTK-AIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
148-584 |
8.38e-86 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 278.04 E-value: 8.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 148 VDERARLAPDAPAL-TAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDW 226
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 227 PDARLTGLLDDAGVRIVLAD-AQVAGRVRGDRTAVPFDATPTAateprsgerttgpLDAAAPEAAEPQPGPVLGDHALPp 305
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDdALKLEELLEALGKLEVVKLVLV-------------LDRDPVLKEEPLPEEAKPADVPP- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 306 ldanrraatePLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLV-----HEPDWLDAGPDDVFLQAAPIAFDAS-T 379
Cdd:pfam00501 147 ----------PPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVlsikrVRPRGFGLGPDDRVLSTLPLFHDFGlS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 380 LEIWASLSAGARLVLLPPG-RVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH---HLDRLAGVRHLIAGGDVISPDAVRR 455
Cdd:pfam00501 217 LGLLGPLLAGATVVLPPGFpALDPAALLELIERYKVTVLYGVPTLLNMLLEAgapKRALLSSLRLVLSGGAPLPPELARR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 456 LLAAHPDLVFtNGYGPTENTTFTTC-ATFGGPAARPGeagplPIGRPIRGTRVRVLD-RLGRPVPPGVVGDLYALGEGLA 533
Cdd:pfam00501 297 FRELFGGALV-NGYGLTETTGVVTTpLPLDEDLRSLG-----SVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVM 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 502993053 534 LGYLGRPAVTAAVFTPagggERQYRTGDLARWRTDGSLDFLGRADDQVKIK 584
Cdd:pfam00501 371 KGYLNDPELTAEAFDE----DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
183-759 |
4.37e-84 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 293.61 E-value: 4.37e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 183 RLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAgrvrgdrtavpf 262
Cdd:PRK05691 3761 ALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACR------------ 3828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 263 datptaateprsgERTTGPLDAaapeaaepqpgpvLGDHALPPL----DANRRAATEPLPGDLS-PGTLAYVSYTSGSTG 337
Cdd:PRK05691 3829 -------------EQARALLDE-------------LGCANRPRLlvweEVQAGEVASHNPGIYSgPDNLAYVIYTSGSTG 3882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 338 TPKGVCVPHRAV--SRLVHEPdWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPGRV-DPAELGAVVAAEGV 414
Cdd:PRK05691 3883 LPKGVMVEQRGMlnNQLSKVP-YLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAhDPQGLLAHVQAQGI 3961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 415 TVLWLTAGLFHQLVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTTftTCATFGGPAARPgEAG 494
Cdd:PRK05691 3962 TVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSD--DVAFFRVDLAST-RGS 4038
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 495 PLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTP---AGGGERQYRTGDLARWRTDGSL 571
Cdd:PRK05691 4039 YLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPhpfGAPGERLYRTGDLARRRSDGVL 4118
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 572 DFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGStRLAAYVVFADGDR-PGVPAPALRDWLRERLPEF 650
Cdd:PRK05691 4119 EYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGK-HLVGYLVPHQTVLaQGALLERIKQRLRAELPDY 4197
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 651 LVPARIVALDAFPLTPNGKLDREALPgsAAEEGALDENG--APEDALERFLCELWAKVLMVDSVGVDDDFFELGGHSLVA 728
Cdd:PRK05691 4198 MVPLHWLWLDRLPLNANGKLDRKALP--ALDIGQLQSQAylAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLA 4275
|
570 580 590
....*....|....*....|....*....|.
gi 502993053 729 ADLLGQLQQDFGVELPARTFYLSPTIAELAE 759
Cdd:PRK05691 4276 TQIASRVQKALQRNVPLRAMFECSTVEELAE 4306
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
186-676 |
1.04e-78 |
|
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: 260.41 E-value: 1.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 186 RAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADaqvagrvrgdrtavpfdat 265
Cdd:cd17648 32 VAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVITN------------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 266 ptaateprsgerttgpldaaapeaaepqpgpvlgdhalppldanrraateplpgdlsPGTLAYVSYTSGSTGTPKGVCVP 345
Cdd:cd17648 93 ---------------------------------------------------------STDLAYAIYTSGTTGKPKGVLVE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 346 HRAVSRL---VHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPP-GRVDPAELGAVVAAEGVTVLWLTA 421
Cdd:cd17648 116 HGSVVNLrtsLSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDeMRFDPDRFYAYINREKVTYLSGTP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 422 GLFhQLVDhhLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFtNGYGPTEnTTFTTCATFGGPAARPGEAgplpIGRP 501
Cdd:cd17648 196 SVL-QQYD--LARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLII-NAYGPTE-TTVTNHKRFFPGDQRFDKS----LGRP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 502 IRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTP----------AGGGERQYRTGDLARWRTDGSL 571
Cdd:cd17648 267 VRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPnpfqteqeraRGRNARLYKTGDLVRWLPSGEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 572 DFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALP--EPGAGGSTRLAAYVVFADGDRPGVPAPALRDWLRERLPE 649
Cdd:cd17648 347 EYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAkeDASQAQSRIQKYLVGYYLPEPGHVPESDLLSFLRAKLPR 426
|
490 500
....*....|....*....|....*..
gi 502993053 650 FLVPARIVALDAFPLTPNGKLDREALP 676
Cdd:cd17648 427 YMVPARLVRLEGIPVTINGKLDVRALP 453
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
325-671 |
2.99e-71 |
|
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: 236.41 E-value: 2.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 325 TLAYVSYTSGSTGTPKGVCVPHRAVSRLVHEP-DWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPpgRVDPA 403
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALaASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP--KFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 404 ELGAVVAAEGVTVLWLTAGLFHQLVDHHLDR---LAGVRHLIAGGDVISPDAVRRLLAAhPDLVFTNGYGPTENTTFTTC 480
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAgydLSSLRALVSGGAPLPPELLERFEEA-PGIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 481 ATFGGPAARPGeagplPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFtpaggGERQYRTG 560
Cdd:cd04433 158 GPPDDDARKPG-----SVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-----EDGWYRTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 561 DLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGstRLAAYVVFADGDRPgvPAPA 638
Cdd:cd04433 228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVaeAAVVGVPDPEWGE--RVVAVVVLRPGADL--DAEE 303
|
330 340 350
....*....|....*....|....*....|...
gi 502993053 639 LRDWLRERLPEFLVPARIVALDAFPLTPNGKLD 671
Cdd:cd04433 304 LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
139-675 |
2.17e-57 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 205.73 E-value: 2.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 139 APARL--VHDLVDERARLAPDAPALTAAG-----KTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLA 211
Cdd:COG0365 4 VGGRLniAYNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 212 VLKAGGAYLALPPDW-PDArLTGLLDDAGVRIVLADAqvAGRVRGDRTAVP--FDATPTAATEPRS---GERTTGPLDAA 285
Cdd:COG0365 84 CARIGAVHSPVFPGFgAEA-LADRIEDAEAKVLITAD--GGLRGGKVIDLKekVDEALEELPSLEHvivVGRTGADVPME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 286 apeaaepqpgpvlGDHALPPLDANRRAATEPLPgdLSPGTLAYVSYTSGSTGTPKGVCVPHRAVsrLVHEPD----WLDA 361
Cdd:COG0365 161 -------------GDLDWDELLAAASAEFEPEP--TDADDPLFILYTSGTTGKPKGVVHTHGGY--LVHAATtakyVLDL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 362 GPDDVFLQAAPIAF--DASTLeIWASLSAGARLVLLP--PGRVDPAELGAVVAAEGVTVLWLTAGLFHQLV---DHHLDR 434
Cdd:COG0365 224 KPGDVFWCTADIGWatGHSYI-VYGPLLNGATVVLYEgrPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMkagDEPLKK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 435 --LAGVRHLIAGGDVISPDAVRRLlAAHPDLVFTNGYGPTEnttftTCATFGGPA----ARPGEagplpIGRPIRGTRVR 508
Cdd:COG0365 303 ydLSSLRLLGSAGEPLNPEVWEWW-YEAVGVPIVDGWGQTE-----TGGIFISNLpglpVKPGS-----MGKPVPGYDVA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 509 VLDRLGRPVPPGVVGDLYALGE--GLALGYLGRPAVTAAVFTPAGGGerQYRTGDLARWRTDGSLDFLGRADDQVKIKGY 586
Cdd:COG0365 372 VVDEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPERYRETYFGRFPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGH 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 587 RVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDRPGVP-APALRDWLRERLPEFLVPARIVALDAFPLT 665
Cdd:COG0365 450 RIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDElAKELQAHVREELGPYAYPREIEFVDELPKT 529
|
570
....*....|
gi 502993053 666 PNGKLDREAL 675
Cdd:COG0365 530 RSGKIMRRLL 539
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
184-758 |
4.13e-57 |
|
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: 212.23 E-value: 4.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 184 LVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVR--IVLADA-QVAGRVRgD---- 256
Cdd:TIGR03443 287 LLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRalIVIEKAgTLDQLVR-Dyidk 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 257 ----RTAVPfdatptAATEPRSGERTTGPLDAAApeaaepqpgpvlgDHALPPLDANRRAATEPLPGDLSPGTLayvSYT 332
Cdd:TIGR03443 366 elelRTEIP------ALALQDDGSLVGGSLEGGE-------------TDVLAPYQALKDTPTGVVVGPDSNPTL---SFT 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 333 SGSTGTPKGVCVPHRAvsrLVHEPDWL----DAGPDDVFLQAAPIAFDASTLEIWASLSAGARLvlLPPGRVD---PAEL 405
Cdd:TIGR03443 424 SGSEGIPKGVLGRHFS---LAYYFPWMakrfGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQL--LVPTADDigtPGRL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 406 GAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTEntTFTTCATFGG 485
Cdd:TIGR03443 499 AEWMAKYGATVTHLTPAMGQLLSAQATTPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTE--TQRAVSYFEI 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 486 PAaRPGEAGPL-------PIGRPIRGTRVRVLDRLGRPVPPGV--VGDLYALGEGLALGYLGRPAVTAAVFTP------- 549
Cdd:TIGR03443 577 PS-RSSDSTFLknlkdvmPAGKGMKNVQLLVVNRNDRTQTCGVgeVGEIYVRAGGLAEGYLGLPELNAEKFVNnwfvdps 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 550 --------AGGGERQ---------YRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEP 612
Cdd:TIGR03443 656 hwidldkeNNKPEREfwlgprdrlYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRR 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 613 GAGGSTRLAAYVVfadgdrPGVPAPAL------------------------------RDWLRERLPEFLVPARIVALDAF 662
Cdd:TIGR03443 736 DKDEEPTLVSYIV------PQDKSDELeefksevddeessdpvvkglikyrklikdiREYLKKKLPSYAIPTVIVPLKKL 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 663 PLTPNGKLDREALP-GSAAEEGALDENGAPEDALERF------LCELWAKVL--MVDSVGVDDDFFELGGHSLVAADLLG 733
Cdd:TIGR03443 810 PLNPNGKVDKPALPfPDTAQLAAVAKNRSASAADEEFtetereIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIF 889
|
650 660
....*....|....*....|....*
gi 502993053 734 QLQQDFGVELPARTFYLSPTIAELA 758
Cdd:TIGR03443 890 ELRKKLNVELPLGLIFKSPTIKGFA 914
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
183-670 |
2.54e-54 |
|
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: 195.12 E-value: 2.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 183 RLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRgdrtavpf 262
Cdd:cd05911 26 GLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDGLEKVK-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 263 datpTAATEPRSGER---TTGPLDAAAPEAAEPQPGPVLGDHALPPldanrraateplPGDLSPGTLAYVSYTSGSTGTP 339
Cdd:cd05911 98 ----EAAKELGPKDKiivLDDKPDGVLSIEDLLSPTLGEEDEDLPP------------PLKDGKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 340 KGVCVPHR---AVSRLVHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPpgRVDPAELGAVVAAEGVTV 416
Cdd:cd05911 162 KGVCLSHRnliANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMP--KFDSELFLDLIEKYKITF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 417 LWLTAGLFHQLVDHHL---DRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTEnTTFTTCATFGGPaARPGEA 493
Cdd:cd05911 240 LYLVPPIAAALAKSPLldkYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTE-TGGILTVNPDGD-DKPGSV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 494 gplpiGRPIRGTRVRVLDRLGRP-VPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLD 572
Cdd:cd05911 318 -----GRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDG----WLHTGDIGYFDEDGYLY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 573 FLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGSTRlaAYVVFADGDRpgVPAPALRDWLRERLPEF 650
Cdd:cd05911 389 IVDRKKELIKYKGFQVAPAELEAVLLEHPGVadAAVIGIPDEVSGELPR--AYVVRKPGEK--LTEKEVKDYVAKKVASY 464
|
490 500
....*....|....*....|..
gi 502993053 651 --LVpARIVALDAFPLTPNGKL 670
Cdd:cd05911 465 kqLR-GGVVFVDEIPKSASGKI 485
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
148-672 |
3.45e-50 |
|
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: 182.04 E-value: 3.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 148 VDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWP 227
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 228 DARLTGLLDDAGVRIVLADaqvagrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhalppld 307
Cdd:cd17631 81 PPEVAYILADSGAKVLFDD------------------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 308 anrraateplpgdlspgtLAYVSYTSGSTGTPKGVCVPHR-----AVSRLVHepdwLDAGPDDVFLQAAPIaFDASTLEI 382
Cdd:cd17631 100 ------------------LALLMYTSGTTGRPKGAMLTHRnllwnAVNALAA----LDLGPDDVLLVVAPL-FHIGGLGV 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 383 WA--SLSAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH-HLDR--LAGVRHLIAGGDVISPDAVRRLL 457
Cdd:cd17631 157 FTlpTLLRGGTVVILR--KFDPETVLDLIERHRVTSFFLVPTMIQALLQHpRFATtdLSSLRAVIYGGAPMPERLLRALQ 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 458 AAHPdlVFTNGYGPTENTTFTTCATFGGPAARPGEAGplpigRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYL 537
Cdd:cd17631 235 ARGV--KFVQGYGMTETSPGVTFLSPEDHRRKLGSAG-----RPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYW 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 538 GRPAVTAAVFtpAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAG 615
Cdd:cd17631 308 NRPEATAAAF--RDG---WFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVaeVAVIGVPDEKWG 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 502993053 616 gsTRLAAYVVFADGDRPgvPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDR 672
Cdd:cd17631 383 --EAVVAVVVPRPGAEL--DEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
143-677 |
7.75e-50 |
|
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: 183.44 E-value: 7.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 143 LVHDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLAL 222
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 223 PPDWPDARLTGLLDDAGVRIVLADAQvagRVRGDRTAVPfdATPTAATEPRSGERTTGPLDAaapeaaepqpgPVLGDHA 302
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSE---RLDLLHPALP--GCHDLRTLIIVGDPAHASEGH-----------PGEEPAS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 303 LPPLDANRRAATeplPGDLSPGTLAYVSYTSGSTGTPKGVCVPHR-AVSRLVHEPDWLDAGPDDVFLQAAPIAFDASTLE 381
Cdd:TIGR03098 145 WPKLLALGDADP---PHPVIDSDMAAILYTSGSTGRPKGVVLSHRnLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 382 IWASLSAGARLVLLppGRVDPAELGAVVAAEGVTVLWLTAGLFHQL--VDHHLDRLAGVRHLIAGGDVISPDAVRRLLAA 459
Cdd:TIGR03098 222 LTTAFYVGATVVLH--DYLLPRDVLKALEKHGITGLAAVPPLWAQLaqLDWPESAAPSLRYLTNSGGAMPRATLSRLRSF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 460 HPDLVFTNGYGPTENTTFTTCAtfggpaarPGEAG--PLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYL 537
Cdd:TIGR03098 300 LPNARLFLMYGLTEAFRSTYLP--------PEEVDrrPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYW 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 538 GRPAVTAAVFTPAGG-------GERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVA-- 608
Cdd:TIGR03098 372 NDPEKTAERFRPLPPfpgelhlPELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAfg 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502993053 609 LPEPGAGGSTRLaayVVFADGDRPGVPApALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPG 677
Cdd:TIGR03098 452 VPDPTLGQAIVL---VVTPPGGEELDRA-ALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
143-675 |
1.90e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 182.31 E-value: 1.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 143 LVHDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAgGAYLA- 221
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI-GAVLHp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 222 ----LPPDwpdaRLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPFDATPTAATEPrsgerttgpldaaapeAAEPQPGPV 297
Cdd:PRK06187 86 inirLKPE----EIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDG----------------PAAPLAPEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 298 LGDHALppLDAnrRAATEPLPgDLSPGTLAYVSYTSGSTGTPKGVCVPHR-AVSRLVHEPDWLDAGPDDVFLQAAPIaFD 376
Cdd:PRK06187 146 GEYEEL--LAA--ASDTFDFP-DIDENDAAAMLYTSGTTGHPKGVVLSHRnLFLHSLAVCAWLKLSRDDVYLVIVPM-FH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 377 ASTLEI-WASLSAGARLVLlpPGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDR---LAGVRHLIAGGDVISPDA 452
Cdd:PRK06187 220 VHAWGLpYLALMAGAKQVI--PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYfvdFSSLRLVIYGGAALPPAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 453 VRRLLAAHpDLVFTNGYGPTEnttfTT-CATFGGPAARPGEAGPLPI--GRPIRGTRVRVLDRLGRPVPP--GVVGDLYA 527
Cdd:PRK06187 298 LREFKEKF-GIDLVQGYGMTE----TSpVVSVLPPEDQLPGQWTKRRsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 528 LGEGLALGYLGRPAVTAAVFtpAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAA- 606
Cdd:PRK06187 373 RGPWLMQGYWNRPEATAETI--DGG---WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVa 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 607 -VALPEPGAGgsTRLAAYVVFADGDRPGvpAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK06187 448 vIGVPDEKWG--ERPVAVVVLKPGATLD--AKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
328-675 |
1.34e-48 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 179.32 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 328 YVSYTSGSTGTPKGVCVPHravSRLVHEPDW------LDAGPddVFLQAAPIAFDASTLEIWASLSAGARLVLLPPGRV- 400
Cdd:PRK04813 147 YIIFTSGTTGKPKGVQISH---DNLVSFTNWmledfaLPEGP--QFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTa 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 401 DPAELGAVVAAEGVTVlWLTAGLFHQ--LVDHHLD--RLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTT 476
Cdd:PRK04813 222 NFKQLFETLPQLPINV-WVSTPSFADmcLLDPSFNeeHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 477 FTT--------CATFGgpaarpgeagPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFT 548
Cdd:PRK04813 301 AVTsieitdemLDQYK----------RLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 549 PAGGgERQYRTGDLARWRtDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFAD 628
Cdd:PRK04813 371 TFDG-QPAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKE 448
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 502993053 629 GDRPGVPA--PALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK04813 449 EDFEREFEltKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
146-675 |
2.25e-48 |
|
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: 177.76 E-value: 2.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 146 DLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPD 225
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 226 WPDARLTGLLDDAGVRIVLadaqvagrvrgdrTAVPFDatptaateprsgerttgpldaaapeaaepqpgpvlgdhalpp 305
Cdd:cd05936 83 YTPRELEHILNDSGAKALI-------------VAVSFT------------------------------------------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 306 lDANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHR-----AVSRLVHEPDWLDagPDDVFLQAAPI--AFdAS 378
Cdd:cd05936 108 -DLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRnlvanALQIKAWLEDLLE--GDDVVLAALPLfhVF-GL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 379 TLEIWASLSAGARLVLLPpgRVDPAELGAVVAAEGVTVL----WLTAGLFHQLVDHHLDrLAGVRHLIAGGDVISPDAVR 454
Cdd:cd05936 184 TVALLLPLALGATIVLIP--RFRPIGVLKEIRKHRVTIFpgvpTMYIALLNAPEFKKRD-FSSLRLCISGGAPLPVEVAE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 455 RLLAAHPDLVFtNGYGPTENTTFTTCATFGGPAaRPGEagplpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLAL 534
Cdd:cd05936 261 RFEELTGVPIV-EGYGLTETSPVVAVNPLDGPR-KPGS-----IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 535 GYLGRPAVTAAVFTpaGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGA 614
Cdd:cd05936 334 GYWNRPEETAEAFV--DG---WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDP 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502993053 615 GGSTRLAAYVVFADGDRPGvpAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05936 409 YSGEAVKAFVVLKEGASLT--EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
146-675 |
3.52e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 178.56 E-value: 3.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 146 DLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPD 225
Cdd:PRK07656 9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 226 WPDARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVP----FDATPTAATEPRSGERTTGpldaaapeaaepqpgpvlgDH 301
Cdd:PRK07656 89 YTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPalehVVICETEEDDPHTEKMKTF-------------------TD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 302 ALPPLDANRRAATeplpgdLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHE-PDWLDAGPDDVFLQAAPI--AFdAS 378
Cdd:PRK07656 150 FLAAGDPAERAPE------VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADwAEYLGLTEGDRYLAANPFfhVF-GY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 379 TLEIWASLSAGARLVLLPpgRVDPAELGAVVAAEGVTVLwltAG---LFHQLVDH---HLDRLAGVRHLIAGGDVISPDA 452
Cdd:PRK07656 223 KAGVNAPLMRGATILPLP--VFDPDEVFRLIETERITVL---PGpptMYNSLLQHpdrSAEDLSSLRLAVTGAASMPVAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 453 VRRLLAAHPDLVFTNGYGPTENTTFTTCATFGGPAarpgEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGL 532
Cdd:PRK07656 298 LERFESELGVDIVLTGYGLSEASGVTTFNRLDDDR----KTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 533 ALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALP 610
Cdd:PRK07656 374 MKGYYDDPEATAAAIDADG----WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVaeAAVIGVP 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502993053 611 EPGAGGSTRlaAYVVFADGDRpgVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK07656 450 DERLGEVGK--AYVVLKPGAE--LTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
326-675 |
9.56e-44 |
|
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: 163.66 E-value: 9.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 326 LAYVSYTSGSTGTPKGVCVPHRA-VSRLVHEPDWLDAGPDDVFLQAAPIAFDASTL-EIWASLSAGARLVLLPPGRVDPA 403
Cdd:cd05972 83 PALIYFTSGTTGLPKGVLHTHSYpLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWsSFFGPWLLGATVFVYEGPRFDAE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 404 ELGAVVAAEGVTVLWLTAGLFHQL--VDHHLDRLAGVRHLIAGGDVISPDAVRRLLAaHPDLVFTNGYGPTEntTFTTCA 481
Cdd:cd05972 163 RILELLERYGVTSFCGPPTAYRMLikQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRA-ATGLPIRDGYGQTE--TGLTVG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 482 TFGGPAARPGEagplpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGE--GLALGYLGRPAVTAAVFtpaggGERQYRT 559
Cdd:cd05972 240 NFPDMPVKPGS-----MGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPppGLFLGYVGDPEKTEASI-----RGDYYLT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 560 GDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGSTRlaAYVVFADGDRPGVP-A 636
Cdd:cd05972 310 GDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVaeAAVVGSPDPVRGEVVK--AFVVLTSGYEPSEElA 387
|
330 340 350
....*....|....*....|....*....|....*....
gi 502993053 637 PALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05972 388 EELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
326-675 |
1.70e-42 |
|
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: 160.32 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 326 LAYVSYTSGSTGTPKGVCVPHRAVSRLVH--EPDWLDAGPDDVFLQAAPIAFDAST-LEIWASLSAGARlVLLPPGRVDP 402
Cdd:cd05919 93 IAYLLYSSGTTGPPKGVMHAHRDPLLFADamAREALGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGAS-AVLNPGWPTA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 403 AELGAVVAAEGVTVLWLTAGLFHQLV---DHHLDRLAGVRHLIAGGDVIsPDAVRRLLAAHPDLVFTNGYGPTENTTFTT 479
Cdd:cd05919 172 ERVLATLARFRPTVLYGVPTFYANLLdscAGSPDALRSLRLCVSAGEAL-PRGLGERWMEHFGGPILDGIGATEVGHIFL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 480 CAtfggpaaRPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFtpAGGgerQYRT 559
Cdd:cd05919 251 SN-------RPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF--NGG---WYRT 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 560 GDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDRP-GVPAPA 638
Cdd:cd05919 319 GDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPqESLARD 398
|
330 340 350
....*....|....*....|....*....|....*..
gi 502993053 639 LRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05919 399 IHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
184-676 |
5.61e-42 |
|
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: 160.76 E-value: 5.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 184 LVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVR--IVLADAQVAgrvrgdrtaVP 261
Cdd:cd17647 37 LIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRglIVIRAAGVV---------VG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 262 FDATPTaateprsgerttgpldaaapeaaepqpgpvlgdhalppldanrraateplpgdlspgtlayVSYTSGSTGTPKG 341
Cdd:cd17647 108 PDSNPT-------------------------------------------------------------LSFTSGSEGIPKG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 342 VCVPHRAvsrLVHEPDWL----DAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLlpPGRVD---PAELGAVVAAEGV 414
Cdd:cd17647 127 VLGRHFS---LAYYFPWMakrfNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLV--PTQDDigtPGRLAEWMAKYGA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 415 TVLWLTAGLFHQLVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTEN----TTFTTCATFGGPAARP 490
Cdd:cd17647 202 TVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETqravSYFEVPSRSSDPTFLK 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 491 GEAGPLPIGRPIRGTRVRVLDRLGRPVPPGV--VGDLYALGEGLALGYLGRPAVTAAVF--------------TPAGGG- 553
Cdd:cd17647 282 NLKDVMPAGRGMLNVQLLVVNRNDRTQICGIgeVGEIYVRAGGLAEGYRGLPELNKEKFvnnwfvepdhwnylDKDNNEp 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 554 ---------ERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYV 624
Cdd:cd17647 362 wrqfwlgprDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYI 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993053 625 V----------FADGDRPGVPAPA---------------LRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALP 676
Cdd:cd17647 442 VprfdkpddesFAQEDVPKEVSTDpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-675 |
5.96e-42 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 159.14 E-value: 5.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 187 AGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGA----YLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPf 262
Cdd:cd05922 13 AGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 263 DATPTAATEPRSGERTTgpldaaapeaaepqpgpvlgdhalppldanrRAATEPLPGDLspgtlAYVSYTSGSTGTPKGV 342
Cdd:cd05922 92 DPGTVLDADGIRAARAS-------------------------------APAHEVSHEDL-----ALLLYTSGSTGSPKLV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 343 CVPHRAV---SRLVHEpdWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPGRVDpAELGAVVAAEGVTVLWL 419
Cdd:cd05922 136 RLSHQNLlanARSIAE--YLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLD-DAFWEDLREHGATGLAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 420 TAGLFHQLVDHHLD--RLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTTFTTCAtfggPAARPGEAgPLP 497
Cdd:cd05922 213 VPSTYAMLTRLGFDpaKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYL----PPERILEK-PGS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 498 IGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAvftpAGGGERQYRTGDLARWRTDGSLDFLGRA 577
Cdd:cd05922 288 IGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRK----EGRGGGVLHTGDLARRDEDGFLFIVGRR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 578 DDQVKIKGYRVEPAEVAAALGAHPA--VTAAVALPEPgagGSTRLAAYVVFADGDRPGvpapALRDWLRERLPEFLVPAR 655
Cdd:cd05922 364 DRMIKLFGNRISPTEIEAAARSIGLiiEAAAVGLPDP---LGEKLALFVTAPDKIDPK----DVLRSLAERLPPYKVPAT 436
|
490 500
....*....|....*....|
gi 502993053 656 IVALDAFPLTPNGKLDREAL 675
Cdd:cd05922 437 VRVVDELPLTASGKVDYAAL 456
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
146-671 |
8.91e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 160.44 E-value: 8.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 146 DLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPD 225
Cdd:PRK07798 7 DLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 226 WPDARLTGLLDDAGVRIVLADAQVAGRVrgdrtAVPFDATPTAATEPRSGERTTGPLDAAapeaaepqpgpvlgdhALPP 305
Cdd:PRK07798 87 YVEDELRYLLDDSDAVALVYEREFAPRV-----AEVLPRLPKLRTLVVVEDGSGNDLLPG----------------AVDY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 306 LDANRRAATEPLPGDLSPGTLaYVSYTSGSTGTPKGVCVPHRAVSR------------LVHEPDWL----DAGPDDVFLQ 369
Cdd:PRK07798 146 EDALAAGSPERDFGERSPDDL-YLLYTGGTTGMPKGVMWRQEDIFRvllggrdfatgePIEDEEELakraAAGPGMRRFP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 370 AAPIAFDASTLEIWASLSAGARLVLLPPGRVDPAELGAVVAAEGVTVLWLTAGLFHQ-LVDHHLDR----LAGVRHLIAG 444
Cdd:PRK07798 225 APPLMHGAGQWAAFAALFSGQTVVLLPDVRFDADEVWRTIEREKVNVITIVGDAMARpLLDALEARgpydLSSLFAIASG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 445 GDVISPDAVRRLLAAHPDLVFTNGYGPTEnttfttcATFGGPAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPG--VV 522
Cdd:PRK07798 305 GALFSPSVKEALLELLPNVVLTDSIGSSE-------TGFGGSGTVAKGAVHTGGPRFTIGPRTVVLDEDGNPVEPGsgEI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 523 GDLyALGEGLALGYLGRPAVTAAVFtPAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPA 602
Cdd:PRK07798 378 GWI-ARRGHIPLGYYKDPEKTAETF-PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPD 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502993053 603 VTAA--VALPEPGAGgsTRLAAYVVFADGDRPGvpAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLD 671
Cdd:PRK07798 456 VADAlvVGVPDERWG--QEVVAVVQLREGARPD--LAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
325-676 |
2.31e-41 |
|
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: 156.68 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 325 TLAYVSYTSGSTGTPKGVCVPHRAVSRL-VHEPDWLDAGPDDVFLQAAPiAF--DASTLEIWASLSAGARLVLLPpgRVD 401
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAgYYSARRFGLGEDDVYLTVLP-LFhiNAQAVSVLAALSVGATLVLLP--RFS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 402 PAELGAVVAAEGVTVLWLTAGLFHQLV---DHHLDRLAGVRhlIAGGDVISPDAVRRLLAAHpDLVFTNGYGPTENTtft 478
Cdd:cd05934 159 ASRFWSDVRRYGATVTNYLGAMLSYLLaqpPSPDDRAHRLR--AAYGAPNPPELHEEFEERF-GVRLLEGYGMTETI--- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 479 tcatFGGPAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLY---ALGEGLALGYLGRPAVTAAVFtpAGGger 555
Cdd:cd05934 233 ----VGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVirgLRGWGFFKGYYNMPEATAEAM--RNG--- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 556 QYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDRPgvP 635
Cdd:cd05934 304 WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETL--D 381
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 502993053 636 APALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALP 676
Cdd:cd05934 382 PEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
145-675 |
4.07e-41 |
|
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: 158.39 E-value: 4.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 145 HDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGV-LGDRSAGLIAgLLAVLKAGGA-YLAL 222
Cdd:COG1021 28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVqLPNVAEFVIV-FFALFRAGAIpVFAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 223 PPDwPDARLTGLLDDAGVRIVLADAQVAGrvrgdrtavpFDATPTAATeprsgerttgpldaaapeAAEPQPGP----VL 298
Cdd:COG1021 107 PAH-RRAEISHFAEQSEAVAYIIPDRHRG----------FDYRALARE------------------LQAEVPSLrhvlVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 299 GDHA-LPPLDANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPH-------RAVSRLVHepdwLDAgpDDVFLQA 370
Cdd:COG1021 158 GDAGeFTSLDALLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHddylysvRASAEICG----LDA--DTVYLAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 371 APIA--FDASTLEIWASLSAGARLVLLPpgRVDPAELGAVVAAEGVTV---------LWLTAglfhqlVDHHLDRLAGVR 439
Cdd:COG1021 232 LPAAhnFPLSSPGVLGVLYAGGTVVLAP--DPSPDTAFPLIERERVTVtalvpplalLWLDA------AERSRYDLSSLR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 440 HLIAGGDVISPDAVRRL---LAAHPDLVFTNGYGP--------TENTTFTTCatfggpaarpgeagplpiGRPIR-GTRV 507
Cdd:COG1021 304 VLQVGGAKLSPELARRVrpaLGCTLQQVFGMAEGLvnytrlddPEEVILTTQ------------------GRPISpDDEV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 508 RVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYR 587
Cdd:COG1021 366 RIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDG----FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEK 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 588 VEPAEVAAALGAHPAVT--AAVALPEPGAGgsTRLAAYVVfADGDRPGvpAPALRDWLRER-LPEFLVPARIVALDAFPL 664
Cdd:COG1021 442 IAAEEVENLLLAHPAVHdaAVVAMPDEYLG--ERSCAFVV-PRGEPLT--LAELRRFLRERgLAAFKLPDRLEFVDALPL 516
|
570
....*....|.
gi 502993053 665 TPNGKLDREAL 675
Cdd:COG1021 517 TAVGKIDKKAL 527
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
156-675 |
8.85e-41 |
|
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: 155.71 E-value: 8.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 156 PDAPAL----TAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARL 231
Cdd:cd17654 1 PDRPALiidqTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 232 TGLLDDAGVRIVLADAQVAgrvrgdrtavpfdatptaaTEPRSGERTTgpldaaapeaaepqpgpvlgDHALPPLDANrr 311
Cdd:cd17654 81 LTVMKKCHVSYLLQNKELD-------------------NAPLSFTPEH--------------------RHFNIRTDEC-- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 312 aateplpgdlspgtLAYVSYTSGSTGTPKGVCVPHRAVSRL-VHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGA 390
Cdd:cd17654 120 --------------LAYVIHTSGTTGTPKIVAVPHKCILPNiQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 391 RLVLLPPG-RVDPAELGAVVAAE-GVTVLWLTAGLFHQ-----LVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAH-PD 462
Cdd:cd17654 186 TLLIVPTSvKVLPSKLADILFKRhRITVLQATPTLFRRfgsqsIKSTVLSATSSLRVLALGGEPFPSLVILSSWRGKgNR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 463 LVFTNGYGPTENTTFTTCATFggpaarPGEAGPLPIGRPIRGTRVRVLDRLGRPVpPGVVgdlyaLGEGLALGYLGRPAV 542
Cdd:cd17654 266 TRIFNIYGITEVSCWALAYKV------PEEDSPVQLGSPLLGTVIEVRDQNGSEG-TGQV-----FLGGLNRVCILDDEV 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 543 TAAVFTpagggerQYRTGDLARwRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAH-PAVTAAVALPEpgaggSTRLA 621
Cdd:cd17654 334 TVPKGT-------MRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESClGVESCAVTLSD-----QQRLI 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502993053 622 AYVVfadgdRPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd17654 401 AFIV-----GESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
136-670 |
3.16e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 156.27 E-value: 3.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 136 TAPAPARLVHDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRA-GVRPGEVVGVLGDRSAGLIAGLLAVLK 214
Cdd:PRK08314 4 SLTLPETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 215 AGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPFDATPTAATeprSGERTTGPLDAAAPEAAEPQP 294
Cdd:PRK08314 84 ANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQY---SDYLPAEPEIAVPAWLRAEPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 295 GPVLGDHALPPLDANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAV-SRLVHEPDWLDAGPDDVFLQAAPI 373
Cdd:PRK08314 161 LQALAPGGVVAWKEALAAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVmANAVGSVLWSNSTPESVVLAVLPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 374 aFDASTLE--IWASLSAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLfhqLVDH----HLDR--LAGVRHlIAGG 445
Cdd:PRK08314 241 -FHVTGMVhsMNAPIYAGATVVLMP--RWDREAAARLIERYRVTHWTNIPTM---VVDFlaspGLAErdLSSLRY-IGGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 446 DVISPDAVRRLLAAHPDLVFTNGYGPTEnttfTTCATFGGPAARPgeaGPLPIGRPIRGTRVRVLD-RLGRPVPPGVVGD 524
Cdd:PRK08314 314 GAAMPEAVAERLKELTGLDYVEGYGLTE----TMAQTHSNPPDRP---KLQCLGIPTFGVDARVIDpETLEELPPGEVGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 525 LYALGEGLALGYLGRPAVTAAVFTPAgGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT 604
Cdd:PRK08314 387 IVVHGPQVFKGYWNRPEATAEAFIEI-DGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQ 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 605 AA--VALPEPGAGGSTRlaAYVVFADGDRPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKL 670
Cdd:PRK08314 466 EAcvIATPDPRRGETVK--AVVVLRPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
152-682 |
5.96e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 155.58 E-value: 5.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 152 ARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARL 231
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 232 TGLLDDAGVRIVLADAQ---VAGRVRGDRTAVPFDATPTAATEPRsgeRTTGPLDAAAPEAAEPQPGPVlgdHALPPLDA 308
Cdd:PRK06178 123 SYELNDAGAEVLLALDQlapVVEQVRAETSLRHVIVTSLADVLPA---EPTLPLPDSLRAPRLAAAGAI---DLLPALRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 309 NRRAATEPLPgdlSPGTLAYVSYTSGSTGTPKGVCVPHR------AVSRLVHEPdwldAGPDDVFLQAAPIAFDA-STLE 381
Cdd:PRK06178 197 CTAPVPLPPP---ALDALAALNYTGGTTGMPKGCEHTQRdmvytaAAAYAVAVV----GGEDSVFLSFLPEFWIAgENFG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 382 IWASLSAGARLVLLppGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH---HLDRLAGVRHLIAGGDV--ISPDAVRRL 456
Cdd:PRK06178 270 LLFPLFSGATLVLL--ARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHprfAEYDLSSLRQVRVVSFVkkLNPDYRQRW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 457 LAAHPDLVFTNGYGPTENTTfttCATFggpaarpgEAG-----------PLPIGRPIRGTRVRVLD-RLGRPVPPGVVGD 524
Cdd:PRK06178 348 RALTGSVLAEAAWGMTETHT---CDTF--------TAGfqdddfdllsqPVFVGLPVPGTEFKICDfETGELLPLGAEGE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 525 LYALGEGLALGYLGRPAVTAAVFTpagggERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT 604
Cdd:PRK06178 417 IVVRTPSLLKGYWNKPEATAEALR-----DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVL 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 605 AAVALPEPGAGGSTRLAAYVVFADGdrPGVPAPALRDWLRERLPEFLVPaRIVALDAFPLTPNGKLDREALPGSAAEE 682
Cdd:PRK06178 492 GSAVVGRPDPDKGQVPVAFVQLKPG--ADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALAEEL 566
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
152-678 |
8.78e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 154.70 E-value: 8.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 152 ARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARL 231
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 232 TGLLDDAGVRIVLADAQVAGRVRGDRTAVP-FDATPTAATEPRSGERTTGPLDaaapeaaepqpgpvlgdhalpplDANR 310
Cdd:PRK07788 139 AEVAAREGVKALVYDDEFTDLLSALPPDLGrLRAWGGNPDDDEPSGSTDETLD-----------------------DLIA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 311 RAATEPLPGDLSPGTLayVSYTSGSTGTPKGvcVPHRAVSRLVHEPDWLDAGP---DDVFLQAAPIaFDASTLEIWA-SL 386
Cdd:PRK07788 196 GSSTAPLPKPPKPGGI--VILTSGTTGTPKG--APRPEPSPLAPLAGLLSRVPfraGETTLLPAPM-FHATGWAHLTlAM 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 387 SAGARLVLlpPGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAG-----VRHLIAGGDVISPDAVRRLLAAHP 461
Cdd:PRK07788 271 ALGSTVVL--RRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKydtssLKIIFVSGSALSPELATRALEAFG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 462 DLVFtNGYGPTENtTFTTCATFGGPAARPGEAgplpiGRPIRGTRVRVLDRLGRPVPPGVVGDLYaLGEGLAL-GYlgrp 540
Cdd:PRK07788 349 PVLY-NLYGSTEV-AFATIATPEDLAEAPGTV-----GRPPKGVTVKILDENGNEVPRGVVGRIF-VGNGFPFeGY---- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 541 avtaavftpAGGGERQ-----YRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPG 613
Cdd:PRK07788 417 ---------TDGRDKQiidglLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVveAAVIGVDDEE 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502993053 614 AGgsTRLAAYVVFADGDRPGvpAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGS 678
Cdd:PRK07788 488 FG--QRLRAFVVKAPGAALD--EDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
146-672 |
8.81e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 149.38 E-value: 8.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 146 DLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPD 225
Cdd:PRK05605 36 DLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 226 WPDARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPFDaTPTAATEPRSgerttgpldaaapeaaepqpGPVLGDHAL-- 303
Cdd:PRK05605 116 YTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLE-TIVSVNMIAA--------------------MPLLQRLALrl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 304 --PPLDANRRAATEPLPGDLS----------------------PGTLAYVSYTSGSTGTPKGVCVPHRAV-SRLVHEPDW 358
Cdd:PRK05605 175 piPALRKARAALTGPAPGTVPwetlvdaaiggdgsdvshprptPDDVALILYTSGTTGKPKGAQLTHRNLfANAAQGKAW 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 359 LDAGPDD--VFLQAAPIaFDAS--TLEIWASLSAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLVD----H 430
Cdd:PRK05605 255 VPGLGDGpeRVLAALPM-FHAYglTLCLTLAVSIGGELVLLP--APDIDLILDAMKKHPPTWLPGVPPLYEKIAEaaeeR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 431 HLDrLAGVRHLIAGGDVISPDAVRRLLAAHPDLVfTNGYGPTENTTFTTCATFgGPAARPGEagplpIGRPIRGTRVRVL 510
Cdd:PRK05605 332 GVD-LSGVRNAFSGAMALPVSTVELWEKLTGGLL-VEGYGLTETSPIIVGNPM-SDDRRPGY-----VGVPFPDTEVRIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 511 DR--LGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAgggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRV 588
Cdd:PRK05605 404 DPedPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-----WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 589 EPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDRpgVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNG 668
Cdd:PRK05605 479 YPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAA--LDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLG 556
|
....
gi 502993053 669 KLDR 672
Cdd:PRK05605 557 KVRR 560
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
323-670 |
1.54e-37 |
|
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: 145.99 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 323 PGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVH-EPDWLDAGPDDVFLQAAPIA-FDASTLEIWASLSAGARLVLLPpgRV 400
Cdd:cd05903 92 PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRqYAERLGLGPGDVFLVASPMAhQTGFVYGFTLPLLLGAPVVLQD--IW 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 401 DPAELGAVVAAEGVTVLWLTAGLFHQLVDHHL---DRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTnGYGPTENTTF 477
Cdd:cd05903 170 DPDKALALMREHGVTFMMGATPFLTDLLNAVEeagEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCS-AYGSTECPGA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 478 TTCATFGGPAARPGEAGplpigRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTpagggERQY 557
Cdd:cd05903 249 VTSITPAPEDRRLYTDG-----RPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-----EGWF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 558 RTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT--AAVALPEPGAGgsTRLAAYVVFADGDRPGVp 635
Cdd:cd05903 319 RTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIeaAVVALPDERLG--ERACAVVVTKSGALLTF- 395
|
330 340 350
....*....|....*....|....*....|....*.
gi 502993053 636 aPALRDWL-RERLPEFLVPARIVALDAFPLTPNGKL 670
Cdd:cd05903 396 -DELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
184-675 |
2.18e-37 |
|
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: 147.13 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 184 LVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPFD 263
Cdd:cd05959 46 LRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 264 ATPTAATEPRSGERTTGPLDAaapeaaepqpgpVLGDHAlPPLDANRRAATEPlpgdlspgtlAYVSYTSGSTGTPKGVC 343
Cdd:cd05959 126 LVVLIVSGGAGPEAGALLLAE------------LVAAEA-EQLKPAATHADDP----------AFWLYSSGSTGRPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 344 VPH---RAVSRLVHEPdWLDAGPDDVFLQAAPIAF-----DASTLeiwaSLSAGARLVLLPpGRVDPAELGAVVAAEGVT 415
Cdd:cd05959 183 HLHadiYWTAELYARN-VLGIREDDVCFSAAKLFFayglgNSLTF----PLSVGATTVLMP-ERPTPAAVFKRIRRYRPT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 416 VLWLTAGLFHQLV---DHHLDRLAGVRHLIAGGDVIsPDAVRRLLAAHPDLVFTNGYGPTENT-TFTTcatfggpaARPG 491
Cdd:cd05959 257 VFFGVPTLYAAMLaapNLPSRDLSSLRLCVSAGEAL-PAEVGERWKARFGLDILDGIGSTEMLhIFLS--------NRPG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 492 EAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTpaggGErQYRTGDLARWRTDGSL 571
Cdd:cd05959 328 RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ----GE-WTRTGDKYVRDDDGFY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 572 DFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADG-DRPGVPAPALRDWLRERLPEF 650
Cdd:cd05959 403 TYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGyEDSEALEEELKEFVKDRLAPY 482
|
490 500
....*....|....*....|....*
gi 502993053 651 LVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05959 483 KYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
156-675 |
3.26e-37 |
|
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: 146.30 E-value: 3.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 156 PDAPALTAAGKT--VPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTG 233
Cdd:cd05926 1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 234 LLDDAGVRIVLADAqvAGRVRGDRTAVPFDATPTAATEPRSGERTTGPldaaapeaaepqpGPVLGdhALPPLDANRRAA 313
Cdd:cd05926 81 YLADLGSKLVLTPK--GELGPASRAASKLGLAILELALDVGVLIRAPS-------------AESLS--NLLADKKNAKSE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 314 TEPLPGDLspgtlAYVSYTSGSTGTPKGVCVPHRAVSRLVHE-PDWLDAGPDDVFLQAAP----IAFDASTLeiwASLSA 388
Cdd:cd05926 144 GVPLPDDL-----ALILHTSGTTGRPKGVPLTHRNLAASATNiTNTYKLTPDDRTLVVMPlfhvHGLVASLL---STLAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 389 GARLVLlpPGRVDPAELGAVVAAEGVTvlWLTA-GLFHQ-LVDHHL----DRLAGVRHLIAGGDVISPDAVRRLLAAHPD 462
Cdd:cd05926 216 GGSVVL--PPRFSASTFWPDVRDYNAT--WYTAvPTIHQiLLNRPEpnpeSPPPKLRFIRSCSASLPPAVLEALEATFGA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 463 LVFtNGYGPTENTTFTTCATFGGPAARPGEagplpIGRPIrGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAV 542
Cdd:cd05926 292 PVL-EAYGMTEAAHQMTSNPLPPGPRKPGS-----VGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 543 TAAVFTPagggERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT--AAVALPEPGAGgsTRL 620
Cdd:cd05926 365 NAEAAFK----DGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLeaVAFGVPDEKYG--EEV 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502993053 621 AAYVVFADGDRpgVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05926 439 AAAVVLREGAS--VTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
313-675 |
5.15e-37 |
|
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: 144.57 E-value: 5.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 313 ATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHEPDW-LDAGPDDVFLQAAPIAFDASTLE-IWASLSAGA 390
Cdd:cd05969 78 TTEELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYvLDLHPDDIYWCTADPGWVTGTVYgIWAPWLNGV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 391 RLVLLPpGRVDPAELGAVVAAEGVTVlWLTAGLFHQLVDHHLDRLA------GVRHLIAGGDVISPDAVRRLLAAHpDLV 464
Cdd:cd05969 158 TNVVYE-GRFDAESWYGIIERVKVTV-WYTAPTAIRMLMKEGDELArkydlsSLRFIHSVGEPLNPEAIRWGMEVF-GVP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 465 FTNGYGPTENTTFTTCATFGGPAaRPGEagplpIGRPIRGTRVRVLDRLGRPVPPGVVGDLyALGEGL---ALGYLGRPA 541
Cdd:cd05969 235 IHDTWWQTETGSIMIANYPCMPI-KPGS-----MGKPLPGVKAAVVDENGNELPPGTKGIL-ALKPGWpsmFRGIWNDEE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 542 VTAAVFtPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGgsTR 619
Cdd:cd05969 308 RYKNSF-IDG----WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVaeAGVIGKPDPLRG--EI 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 502993053 620 LAAYVVFADGDRPGVP-APALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05969 381 IKAFISLKEGFEPSDElKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
156-675 |
2.19e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 141.28 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 156 PDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVL-GDRSAGLIAGLLAVLkAGGAYLALPPdwpdarLTGL 234
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLsLNRPEVLMAIGAAQL-AGLRRTALHP------LGSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 235 LDDAgvrIVLADAQVagrvrgdrTAVPFDATPTAateprsgERTTGPLDAAAPEAAEPQPGPVlgDHALPPLDANRRAAT 314
Cdd:PRK06188 99 DDHA---YVLEDAGI--------STLIVDPAPFV-------ERALALLARVPSLKHVLTLGPV--PDGVDLLAAAAKFGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 315 EPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVH----EPDWldagPDDV-FLQAAPIAFDASTLeIWASLSAG 389
Cdd:PRK06188 159 APLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQiqlaEWEW----PADPrFLMCTPLSHAGGAF-FLPTLLRG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 390 ARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDR---LAGVRHLIAGGDVISPDavrRLLAAHPDL--V 464
Cdd:PRK06188 234 GTVIVLA--KFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRtrdLSSLETVYYGASPMSPV---RLAEAIERFgpI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 465 FTNGYGPTE-NTTFTTCATFGGPAARPGEAGPlpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVT 543
Cdd:PRK06188 309 FAQYYGQTEaPMVITYLRKRDHDPDDPKRLTS--CGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEET 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 544 AAVFtpAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAA--VALPEPGAGGSTRla 621
Cdd:PRK06188 387 AEAF--RDG---WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVavIGVPDEKWGEAVT-- 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502993053 622 AYVVFadgdRPGVPAPA--LRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK06188 460 AVVVL----RPGAAVDAaeLQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
146-670 |
4.19e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 137.37 E-value: 4.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 146 DLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPD 225
Cdd:PRK08316 15 DILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 226 WPDARLTGLLDDAGVRIVLADAQVAGRVRG---DRTAVPFDATPTAATEPRSGERTtgPLDAAAPEAAEPQPGPVLGDha 302
Cdd:PRK08316 95 LTGEELAYILDHSGARAFLVDPALAPTAEAalaLLPVDTLILSLVLGGREAPGGWL--DFADWAEAGSVAEPDVELAD-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 303 lppldanrraateplpgdlspGTLAYVSYTSGSTGTPKGVCVPHRAvsrLVHE-----PDwLDAGPDDVFLQAAPI---- 373
Cdd:PRK08316 171 ---------------------DDLAQILYTSGTESLPKGAMLTHRA---LIAEyvsciVA-GDMSADDIPLHALPLyhca 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 374 AFDASTLEIwasLSAGARLVLLPpgRVDPAELGAVVAAEGVTVL------WLtAGLFHQLVDHHldRLAGVRHLIAGGDV 447
Cdd:PRK08316 226 QLDVFLGPY---LYVGATNVILD--APDPELILRTIEAERITSFfapptvWI-SLLRHPDFDTR--DLSSLRKGYYGASI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 448 ISPDAVRRLLAAHPDLVFTNGYGPTEnttFTTCATFGGP---AARPGEAgplpiGRPIRGTRVRVLDRLGRPVPPGVVGD 524
Cdd:PRK08316 298 MPVEVLKELRERLPGLRFYNCYGQTE---IAPLATVLGPeehLRRPGSA-----GRPVLNVETRVVDDDGNDVAPGEVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 525 LYALGEGLALGYLGRPAVTAAVFtpAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV- 603
Cdd:PRK08316 370 IVHRSPQLMLGYWDDPEKTAEAF--RGG---WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVa 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 604 -TAAVALPEPGAGGStrLAAYVVFADGDRpgVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKL 670
Cdd:PRK08316 445 eVAVIGLPDPKWIEA--VTAVVVPKAGAT--VTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
135-665 |
1.50e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 136.03 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 135 GTAPAPARLvHDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLK 214
Cdd:PRK06164 4 DAAPRADTL-ASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 215 AGGAYLALPPDWPDARLTGLLDDAGVRIVLadaqVAGRVRGDRTAVPFDATPTAAteprsgeRTTGPLDAAAPEAAEPQP 294
Cdd:PRK06164 83 LGATVIAVNTRYRSHEVAHILGRGRARWLV----VWPGFKGIDFAAILAAVPPDA-------LPPLRAIAVVDDAADATP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 295 GPVLGD-HALPPL-DANRRAATEPLPGDLSPGTLAYVsyTSGSTGTPKGVCVPHRAVSRLVHE-PDWLDAGPDDVFLQAA 371
Cdd:PRK06164 152 APAPGArVQLFALpDPAPPAAAGERAADPDAGALLFT--TSGTTSGPKLVLHRQATLLRHARAiARAYGYDPGAVLLAAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 372 PI--AFDASTLeiWASLSAGARLVLLPPgrVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH--------HLDRLAGVRHL 441
Cdd:PRK06164 230 PFcgVFGFSTL--LGALAGGAPLVCEPV--FDAARTARALRRHRVTHTFGNDEMLRRILDTageradfpSARLFGFASFA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 442 IAGGDVISpdavrrlLAAHPDLVFTNGYGPTENTTFTTCATFGGPAARPGEAGplpiGRPIRG-TRVRVLDRL-GRPVPP 519
Cdd:PRK06164 306 PALGELAA-------LARARGVPLTGLYGSSEVQALVALQPATDPVSVRIEGG----GRPASPeARVRARDPQdGALLPD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 520 GVVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGA 599
Cdd:PRK06164 375 GESGEIEIRAPSLMRGYLDNPDATARALTDDG----YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEA 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 600 HPAVTAAVALpepGA--GGSTRLAAYVVFADGDRPGvpAPALRDWLRERLPEFLVPARIVALDAFPLT 665
Cdd:PRK06164 451 LPGVAAAQVV---GAtrDGKTVPVAFVIPTDGASPD--EAGLMAACREALAGFKVPARVQVVEAFPVT 513
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
111-670 |
2.09e-33 |
|
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: 136.17 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 111 PSPRVSELDLASDAdrALVATFEGGTApapaRLVHDLVDERARLAPDAPAL------TAAGKTVPYRWLAEHAEALAARL 184
Cdd:cd17634 28 PYQKVKNTSFAPGA--PSIKWFEDATL----NLAANALDRHLRENGDRTAIiyegddTSQSRTISYRELHREVCRFAGTL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 185 VRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLAdaqVAGRVRGDRT----AV 260
Cdd:cd17634 102 LDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT---ADGGVRAGRSvplkKN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 261 PFDATPTAATEPRS---GERTTGPLDAaapeaaepQPGPVLGDHAL-----PPLDANRRAATEPLpgdlspgtlaYVSYT 332
Cdd:cd17634 179 VDDALNPNVTSVEHvivLKRTGSDIDW--------QEGRDLWWRDLiakasPEHQPEAMNAEDPL----------FILYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 333 SGSTGTPKGVCVPH--RAVSRLVHEPDWLDAGPDDVFLQAAPIAF-DASTLEIWASLSAGARLVLLP--PGRVDPAELGA 407
Cdd:cd17634 241 SGTTGKPKGVLHTTggYLVYAATTMKYVFDYGPGDIYWCTADVGWvTGHSYLLYGPLACGATTLLYEgvPNWPTPARMWQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 408 VVAAEGVTVLWLTAGLFHQLVDHHLDRLAG-----VRHLIAGGDVISPDAVRRLLAahpdlVFTNGYGPTENTTFTTCAT 482
Cdd:cd17634 321 VVDKHGVNILYTAPTAIRALMAAGDDAIEGtdrssLRILGSVGEPINPEAYEWYWK-----KIGKEKCPVVDTWWQTETG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 483 FGGPAARPGeAGPLPIG---RPIRGTRVRVLDRLGRPVPPGVVGDLyALGE---GLALGYLGRPAVTAAVFTPAGGGerQ 556
Cdd:cd17634 396 GFMITPLPG-AIELKAGsatRPVFGVQPAVVDNEGHPQPGGTEGNL-VITDpwpGQTRTLFGDHERFEQTYFSTFKG--M 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 557 YRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT--AAVALPEPGAGgsTRLAAYVVFadgdRPGV 634
Cdd:cd17634 472 YFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAeaAVVGIPHAIKG--QAPYAYVVL----NHGV 545
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 502993053 635 -PAPALRD----WLRERLPEFLVPARIVALDAFPLTPNGKL 670
Cdd:cd17634 546 ePSPELYAelrnWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
157-675 |
2.45e-33 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 133.95 E-value: 2.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 157 DAPALTAAGKTVPYRWLAEHAEALAARLVRAG-VRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLL 235
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 236 DDAGVRIVLADAQVAgrvrgdrtavpfdatptaateprsgerttgpldaaapeaaepqpgpvlgdhalppldanrraate 315
Cdd:cd05941 81 TDSEPSLVLDPALIL----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 316 plpgdlspgtlayvsYTSGSTGTPKGVCVPHRA----VSRLVHEPDWldaGPDDVFLQAAPI-----AFDASTleiwASL 386
Cdd:cd05941 96 ---------------YTSGTTGRPKGVVLTHANlaanVRALVDAWRW---TEDDVLLHVLPLhhvhgLVNALL----CPL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 387 SAGARLVLLPpgRVDPAELGAVVAAEGVTVLW--------LTAGLFHQLVDHHLDR---LAGVRHLIAGGDVISPDAVRR 455
Cdd:cd05941 154 FAGASVEFLP--KFDPKEVAISRLMPSITVFMgvptiytrLLQYYEAHFTDPQFARaaaAERLRLMVSGSAALPVPTLEE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 456 L--LAAHPDLvftNGYGPTENTTFTTCatfggPAArpGEAGPLPIGRPIRGTRVRVLDRL-GRPVPPGVVGDLYALGEGL 532
Cdd:cd05941 232 WeaITGHTLL---ERYGMTEIGMALSN-----PLD--GERRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSV 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 533 ALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGR-ADDQVKIKGYRVEPAEVAAALGAHPAVT--AAVAL 609
Cdd:cd05941 302 FKEYWNKPEATKEEFTDDG----WFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSecAVIGV 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502993053 610 PEPGAGgsTRLAAYVVFadgdRPGVPAPA---LRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05941 378 PDPDWG--ERVVAVVVL----RAGAAALSleeLKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
326-675 |
2.86e-33 |
|
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: 130.91 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 326 LAYVSYTSGSTGTPKGVCVPHR---AVSRLVHepDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPGRvdp 402
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAAnllASAAGLH--SRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQ--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 403 aELGAVVAAEGVTVLWLTAGLFHQLVDHHLDR--LAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTngYGPTEnttfTTC 480
Cdd:cd17630 77 -ALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPaaLKSLRAVLLGGAPIPPELLERAADRGIPLYTT--YGMTE----TAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 481 ATFGGPAARPGEAGplpIGRPIRGTRVRVLDRlgrpvppgvvGDLYALGEGLALGYLGRPAVtaavftPAGGGERQYRTG 560
Cdd:cd17630 150 QVATKRPDGFGRGG---VGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLV------PEFNEDGWFTTK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 561 DLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDRPGvpapALR 640
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPA----ELR 286
|
330 340 350
....*....|....*....|....*....|....*
gi 502993053 641 DWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd17630 287 AWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
331-672 |
7.25e-33 |
|
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: 130.48 E-value: 7.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 331 YTSGSTGTPKGVCVPHRAV---SRLVHEPdwLDAGPDDVFLQAAPI--AFdASTLEIWASLSAGARLVLLPPGrVDPAEL 405
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIvnnGYFIGER--LGLTEQDRLCIPVPLfhCF-GSVLGVLACLTHGATMVFPSPS-FDPLAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 406 GAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAGVRHL---IAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTTFTTCAT 482
Cdd:cd05917 85 LEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLrtgIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVSTQTR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 483 FGGPAARPGEAgplpIGRPIRGTRVRVLDRLGRPVPP-GVVGDLYALGEGLALGYLGRPAVTAAVFTpaggGERQYRTGD 561
Cdd:cd05917 165 TDDSIEKRVNT----VGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAID----GDGWLHTGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 562 LARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAA--VALPEPGAGgsTRLAAYVVFADGDRPgvPAPAL 639
Cdd:cd05917 237 LAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVqvVGVPDERYG--EEVCAWIRLKEGAEL--TEEDI 312
|
330 340 350
....*....|....*....|....*....|...
gi 502993053 640 RDWLRERLPEFLVPARIVALDAFPLTPNGKLDR 672
Cdd:cd05917 313 KAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
142-675 |
1.13e-32 |
|
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: 132.63 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 142 RLVHDLVDERARLAPDAPALT--AAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAY 219
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIAdpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 220 LALPPDWPDARLTGLLDDAGVR-IVLADAqvAGRVRGDRTAVpfdatptaateprsgerttgpldaaapeaaepqpGPVL 298
Cdd:cd05923 81 ALINPRLKAAELAELIERGEMTaAVIAVD--AQVMDAIFQSG----------------------------------VRVL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 299 GDHALPPLDANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRA----VSRLVHEPDwLDAGPDDVFLQAAP-- 372
Cdd:cd05923 125 ALSDLVGLGEPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAaesrVLFMSTQAG-LRHGRHNVVLGLMPly 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 373 --IAFDASTLeiwASLSAGARLVllPPGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHL---DRLAGVRHLIAGGDV 447
Cdd:cd05923 204 hvIGFFAVLV---AALALDGTYV--VVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEfagLKLSSLRHVTFAGAT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 448 IsPDAVRRLLAAHPDLVFTNGYGPTENTTFTTcatfgGPAARPGEAGplpigRPIRGTRVRVLDRLGRPV---PPGVVGD 524
Cdd:cd05923 279 M-PDAVLERVNQHLPGEKVNIYGTTEAMNSLY-----MRDARTGTEM-----RPGFFSEVRIVRIGGSPDealANGEEGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 525 LYALGEGLA--LGYLGRPAVTAAVFTpagggERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPA 602
Cdd:cd05923 348 LIVAAAADAafTGYLNQPEATAKKLQ-----DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPG 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502993053 603 VTAAVALPEPGAGGSTRLAAYVVFADGDrpgVPAPALRDWLRE-RLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05923 423 VTEVVVIGVADERWGQSVTACVVPREGT---LSADELDQFCRAsELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
328-671 |
2.09e-32 |
|
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: 129.42 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 328 YVSYTSGSTGTPKGVCVPH----------RAVSRLVHEPDWLD-----AGPDDVFLQAAPIAFDASTLEIWASLSAGARL 392
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQedifrmlmggADFGTGEFTPSEDAhkaaaAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 393 VLlPPGRVDPAELGAVVAAEGVTVLWLT-----AGLFHQLVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTN 467
Cdd:cd05924 87 VL-PDDRFDPEEVWRTIEKHKVTSMTIVgdamaRPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 468 GYGPTEnTTFTTcatFGGPAARPGEAGPlpigRPIRGTRVRVLDRLGRPVPPG--VVGDLYALGEgLALGYLGRPAVTAA 545
Cdd:cd05924 166 AFGSSE-TGFTG---SGHSAGSGPETGP----FTRANPDTVVLDDDGRVVPPGsgGVGWIARRGH-IPLGYYGDEAKTAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 546 VFtPAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVV 625
Cdd:cd05924 237 TF-PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQ 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 502993053 626 FADGdrPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLD 671
Cdd:cd05924 316 LREG--AGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
331-675 |
2.35e-32 |
|
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: 130.68 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 331 YTSGSTGTPKGVCVPHR---AVSRLvHEPDWLDAGPDDVFLQAAPIAFDAST-LEIWASLSAGARLVLLPpgRVDPAELG 406
Cdd:cd05958 104 FTSGTTGAPKATMHFHRdplASADR-YAVNVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLE--EATPDLLL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 407 AVVAAEGVTVLWlTAGLFHQLVDHHLDR----LAGVRHLIAGGDVIsPDAVRRLLAAHPDLVFTNGYGPTENTTFTTcat 482
Cdd:cd05958 181 SAIARYKPTVLF-TAPTAYRAMLAHPDAagpdLSSLRKCVSAGEAL-PAALHRAWKEATGIPIIDGIGSTEMFHIFI--- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 483 fggpAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEgLALGYLGRPAVTAAVftpagGGERQYrTGDL 562
Cdd:cd05958 256 ----SARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP-TGCRYLADKRQRTYV-----QGGWNI-TGDT 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 563 ARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT--AAVALPEPGAGGSTRlaAYVVFADGDRPG-VPAPAL 639
Cdd:cd05958 325 YSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAecAVVGHPDESRGVVVK--AFVVLRPGVIPGpVLAREL 402
|
330 340 350
....*....|....*....|....*....|....*.
gi 502993053 640 RDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05958 403 QDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
143-625 |
7.27e-32 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 130.43 E-value: 7.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 143 LVHDLVDERARLAPDAPAL--TAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYL 220
Cdd:cd05904 6 PLDSVSFLFASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 221 ALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRGdrTAVPFDATPTAateprsgerttgpldaaapeaaepqpgPVLGD 300
Cdd:cd05904 86 TANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLAS--LALPVVLLDSA---------------------------EFDSL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 301 HALPPLDANrrAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHR---AVSRLVHEPDWLDAGPDDVFLQAAPI---- 373
Cdd:cd05904 137 SFSDLLFEA--DEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRnliAMVAQFVAGEGSNSDSEDVFLCVLPMfhiy 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 374 AFDASTLeiwASLSAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLD---RLAGVRHLIAGGDVISP 450
Cdd:cd05904 215 GLSSFAL---GLLRLGATVVVMP--RFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVdkyDLSSLRQIMSGAAPLGK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 451 DAVRRLLAAHPDLVFTNGYGPTENTTFTT-CATFGGPAARPGEAGPLpigrpIRGTRVRVLD-RLGRPVPPGVVGDLYAL 528
Cdd:cd05904 290 ELIEAFRAKFPNVDLGQGYGMTESTGVVAmCFAPEKDRAKYGSVGRL-----VPNVEAKIVDpETGESLPPNQTGELWIR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 529 GEGLALGYLGRPAVTAAVFTPagggERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVA 608
Cdd:cd05904 365 GPSIMKGYLNNPEATAATIDK----EGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV 440
|
490
....*....|....*..
gi 502993053 609 LPEPGAGGSTRLAAYVV 625
Cdd:cd05904 441 IPYPDEEAGEVPMAFVV 457
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
326-675 |
1.31e-31 |
|
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: 128.70 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 326 LAYVSYTSGSTGTPKGVCVPHRAVsrLVHEPDW-----LDAGPDDVFLQAAPIAFDASTLEIW-ASLSAGARLVLLPPGR 399
Cdd:cd05971 90 PALIIYTSGTTGPPKGALHAHRVL--LGHLPGVqfpfnLFPRDGDLYWTPADWAWIGGLLDVLlPSLYFGVPVLAHRMTK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 400 VDPAELGAVVAAEGVTVLWLTAG---LFHQLVDHHLDRLAGVRHLIAGGDviSPDAVRRLLAA-HPDLVFTNGYGPTE-N 474
Cdd:cd05971 168 FDPKAALDLMSRYGVTTAFLPPTalkMMRQQGEQLKHAQVKLRAIATGGE--SLGEELLGWAReQFGVEVNEFYGQTEcN 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 475 TTFTTCATFGGPaaRPGEagplpIGRPIRGTRVRVLDRLGRPVPPGVVGDL-YALGEGLA-LGYLGRPAVTAAvfTPAGG 552
Cdd:cd05971 246 LVIGNCSALFPI--KPGS-----MGKPIPGHRVAIVDDNGTPLPPGEVGEIaVELPDPVAfLGYWNNPSATEK--KMAGD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 553 gerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGSTRlaAYVVFADGD 630
Cdd:cd05971 317 ---WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVlmAAVVGIPDPIRGEIVK--AFVVLNPGE 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 502993053 631 RPG-VPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05971 392 TPSdALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
184-675 |
2.78e-31 |
|
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: 128.90 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 184 LVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPFD 263
Cdd:cd12119 42 LRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 264 ATPTAATEPRSGERTTGPLDAAAPEAAEPQPGpvlgDHALPPLDANRRAATeplpgdlspgtlayvSYTSGSTGTPKGVC 343
Cdd:cd12119 122 EHVVVMTDDAAMPEPAGVGVLAYEELLAAESP----EYDWPDFDENTAAAI---------------CYTSGTTGNPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 344 VPHRAV---SRLVHEPDWLDAGPDDVFLQAAPIaFDASTleiW----ASLSAGARLVLlpPGR-VDPAELGAVVAAEGVT 415
Cdd:cd12119 183 YSHRSLvlhAMAALLTDGLGLSESDVVLPVVPM-FHVNA---WglpyAAAMVGAKLVL--PGPyLDPASLAELIEREGVT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 416 V------LWLtaGLFHQLVDHHLDRLAGVRhLIAGGDVISPDAVRRLLAAHPDlvFTNGYGPTENTTFTTCATFGGPAAR 489
Cdd:cd12119 257 FaagvptVWQ--GLLDHLEANGRDLSSLRR-VVIGGSAVPRSLIEAFEERGVR--VIHAWGMTETSPLGTVARPPSEHSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 490 PGEAGPLPI----GRPIRGTRVRVLDRLGRPVP--PGVVGDLYALGEGLALGYLGRPAVTAAVFtpAGGgerQYRTGDLA 563
Cdd:cd12119 332 LSEDEQLALrakqGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDEESEALT--EDG---WLRTGDVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 564 RWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGgsTRLAAYVVFADGDRPGvpAPALRD 641
Cdd:cd12119 407 TIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVaeAAVIGVPHPKWG--ERPLAVVVLKEGATVT--AEELLE 482
|
490 500 510
....*....|....*....|....*....|....
gi 502993053 642 WLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd12119 483 FLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
142-680 |
3.04e-31 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 129.40 E-value: 3.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 142 RLVHDLVDERARLAPDAPALTA------AGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKA 215
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 216 GGAYLALPPDWPDARLTGLLDDAGVRIVLadaqVAGRVRGdrtavpFDatptaatEPRSGERTTGPLDAAAPEAAEPQPG 295
Cdd:PRK13295 104 GAVLNPLMPIFRERELSFMLKHAESKVLV----VPKTFRG------FD-------HAAMARRLRPELPALRHVVVVGGDG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 296 PV-LGDHALPPLDANRRAATEPLPGD-LSPGTLAYVSYTSGSTGTPKGVCVPHR-AVSRLVHEPDWLDAGPDDVFLQAAP 372
Cdd:PRK13295 167 ADsFEALLITPAWEQEPDAPAILARLrPGPDDVTQLIYTSGTTGEPKGVMHTANtLMANIVPYAERLGLGADDVILMASP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 373 IAFDASTLE-IWASLSAGARLVLLppGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDR---LAGVRHLIAGGDVI 448
Cdd:PRK13295 247 MAHQTGFMYgLMMPVMLGATAVLQ--DIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESgrpVSSLRTFLCAGAPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 449 SPDAVRRLLAAHpDLVFTNGYGPTENTTFTTcatfggpaARPGEAGPLPI---GRPIRGTRVRVLDRLGRPVPPGVVGDL 525
Cdd:PRK13295 325 PGALVERARAAL-GAKIVSAWGMTENGAVTL--------TKLDDPDERASttdGCPLPGVEVRVVDADGAPLPAGQIGRL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 526 YALGEGLALGYLGRPAVTAavfTPAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT- 604
Cdd:PRK13295 396 QVRGCSNFGGYLKRPQLNG---TDADG---WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAq 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 605 -AAVALPEPGAGgsTRLAAYVVFadgdRPG--VPAPALRDWLRE-RLPEFLVPARIVALDAFPLTPNGKLD----REALP 676
Cdd:PRK13295 470 vAIVAYPDERLG--ERACAFVVP----RPGqsLDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQkfrlREMLR 543
|
....
gi 502993053 677 GSAA 680
Cdd:PRK13295 544 GEDA 547
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
329-675 |
7.92e-31 |
|
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: 128.00 E-value: 7.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 329 VSYTSGSTGTPKGVCVPHR-AVSRLVHEPDWLDAGPDDVFLQAAPIAF-DASTLEIWASLSAGARLVLLPPGRVDPAELG 406
Cdd:cd05970 190 VYFSSGTTGMPKMVEHDFTyPLGHIVTAKYWQNVREGGLHLTVADTGWgKAVWGKIYGQWIAGAAVFVYDYDKFDPKALL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 407 AVVAAEGVTVLWLTAGLFHQLVDHHLDR--LAGVRHLIAGGDVISPDAVRRLLAaHPDLVFTNGYGPTEnTTFTTcATFG 484
Cdd:cd05970 270 EKLSKYGVTTFCAPPTIYRFLIREDLSRydLSSLRYCTTAGEALNPEVFNTFKE-KTGIKLMEGFGQTE-TTLTI-ATFP 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 485 GPAARPGEagplpIGRPIRGTRVRVLDRLGRPVPPGVVGDL-YALGEGLALG----YLGRPAVTAAVFTpagggERQYRT 559
Cdd:cd05970 347 WMEPKPGS-----MGKPAPGYEIDLIDREGRSCEAGEEGEIvIRTSKGKPVGlfggYYKDAEKTAEVWH-----DGYYHT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 560 GDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGSTRlaAYVVFADGDRPG-VPA 636
Cdd:cd05970 417 GDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVleCAVTGVPDPIRGQVVK--ATIVLAKGYEPSeELK 494
|
330 340 350
....*....|....*....|....*....|....*....
gi 502993053 637 PALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05970 495 KELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
135-675 |
8.34e-31 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 127.95 E-value: 8.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 135 GTAPAPARLVHDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLK 214
Cdd:PRK06155 14 DPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 215 AGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRG---DRTAVP----FDATPTAATEPRSGertTGPLdaaap 287
Cdd:PRK06155 94 LGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAadpGDLPLPavwlLDAPASVSVPAGWS---TAPL----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 288 eaaepqpgpvlgdhalPPLDAnrrAATeplPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRL-VHEPDWLDAGPDDV 366
Cdd:PRK06155 166 ----------------PPLDA---PAP---AAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWgRNSAEDLEIGADDV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 367 FLQAAPIaFDASTLEIWAS-LSAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH---HLDRLAGVRHLI 442
Cdd:PRK06155 224 LYTTLPL-FHTNALNAFFQaLLAGATYVLEP--RFSASGFWPAVRRHGATVTYLLGAMVSILLSQparESDRAHRVRVAL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 443 AGGdviSPDAVRRLLAAHPDLVFTNGYGPTEnttftTCATFGG--PAARPGEAgplpiGRPIRGTRVRVLDRLGRPVPPG 520
Cdd:PRK06155 301 GPG---VPAALHAAFRERFGVDLLDGYGSTE-----TNFVIAVthGSQRPGSM-----GRLAPGFEARVVDEHDQELPDG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 521 VVGDLYALGE---GLALGYLGRPAVTAAVFTpagggERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAAL 597
Cdd:PRK06155 368 EPGELLLRADepfAFATGYFGMPEKTVEAWR-----NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVL 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 598 GAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDRpgVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK06155 443 LSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTA--LEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
150-674 |
1.47e-30 |
|
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: 126.97 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 150 ERARLAPDAPALT------AAGKTVPYRWLAEHAEALAARLVRAGvRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALP 223
Cdd:cd05931 1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 224 PDWP---DARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPFDATPTAATeprsgerttgpldaaapeaaepqpgpvlgd 300
Cdd:cd05931 80 PPTPgrhAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLV------------------------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 301 HALPPLDANRRAatepLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAV---SRLVHEPdwLDAGPDDVFLQAAPIAFD- 376
Cdd:cd05931 130 VDLLPDTSAADW----PPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLlanVRQIRRA--YGLDPGDVVVSWLPLYHDm 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 377 ASTLEIWASLSAGARLVLLPPGRV--DP-------AELGAVV----------AAEGVTVLWLTAglfhqlvdhhLDrLAG 437
Cdd:cd05931 204 GLIGGLLTPLYSGGPSVLMSPAAFlrRPlrwlrliSRYRATIsaapnfaydlCVRRVRDEDLEG----------LD-LSS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 438 VRHLIAGGDVISPDAVRRLLAA------HPDlVFTNGYGPTENTTFTTCATFG--------------GPAARPGEAGP-- 495
Cdd:cd05931 273 WRVALNGAEPVRPATLRRFAEAfapfgfRPE-AFRPSYGLAEATLFVSGGPPGtgpvvlrvdrdalaGRAVAVAADDPaa 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 496 ---LPIGRPIRGTRVRVLDR-LGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVF--TPAGGGERQYRTGDLARwRTDG 569
Cdd:cd05931 352 relVSCGRPLPDQEVRIVDPeTGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFgaLAATDEGGWLRTGDLGF-LHDG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 570 SLDFLGRADDQVKIKGYRVEPAEV-AAALGAHPAV----TAAVALPEPGAGgstRLAAyVVFADGDRPGVPAPALRDWLR 644
Cdd:cd05931 431 ELYITGRLKDLIIVRGRNHYPQDIeATAEEAHPALrpgcVAAFSVPDDGEE---RLVV-VAEVERGADPADLAAIAAAIR 506
|
570 580 590
....*....|....*....|....*....|....
gi 502993053 645 ERLP-EFLVPARIVAL---DAFPLTPNGKLDREA 674
Cdd:cd05931 507 AAVArEHGVAPADVVLvrpGSIPRTSSGKIQRRA 540
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
331-671 |
1.50e-30 |
|
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: 123.18 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 331 YTSGSTGTPKGVCVPHRAV-SRLVHEPDWLDAGPDDVFLQAAP---IAFDASTLeiwASLSAGARLVLLPpgRVDPAELG 406
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALlAQALVLAVLQAIDEGTVFLNSGPlfhIGTLMFTL---ATFHAGGTNVFVR--RVDAEEVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 407 AVVAAEGVTVLWLTAGLFHQLVD------HHLDRLAGVRHLIAGGDVISPDAvrrllaaHPDLVFTNGYGPTENTTFTTC 480
Cdd:cd17636 82 ELIEAERCTHAFLLPPTIDQIVElnadglYDLSSLRSSPAAPEWNDMATVDT-------SPWGRKPGGYGQTEVMGLATF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 481 ATFGGPAArpGEAGplpigRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFtpAGGGerqYRTG 560
Cdd:cd17636 155 AALGGGAI--GGAG-----RPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT--RGGW---HHTN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 561 DLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGSTRlaAYVVFADGDrpGVPAPA 638
Cdd:cd17636 223 DLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVadAAVIGVPDPRWAQSVK--AIVVLKPGA--SVTEAE 298
|
330 340 350
....*....|....*....|....*....|...
gi 502993053 639 LRDWLRERLPEFLVPARIVALDAFPLTPNGKLD 671
Cdd:cd17636 299 LIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
326-675 |
3.20e-30 |
|
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: 124.13 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 326 LAYVSYTSGSTGTPKGVCVPHRAVSRLVHEPD-WLDAGPDDVFLQAAPI----AFDASTLeiwASLSAGARLVLLppGRV 400
Cdd:cd05935 86 LALIPYTSGTTGLPKGCMHTHFSAAANALQSAvWTGLTPSDVILACLPLfhvtGFVGSLN---TAVYVGGTYVLM--ARW 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 401 DPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAGVRHL--IAGGDVISPDAVRRLLAAHPDLVFTNGYGPTEnttfT 478
Cdd:cd05935 161 DRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLkvLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTE----T 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 479 TCATFGGPAARPGEAGplpIGRPIRGTRVRVLD-RLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGGgERQY 557
Cdd:cd05935 237 MSQTHTNPPLRPKLQC---LGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKG-RRFF 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 558 RTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAA--VALPEPGAGGSTRlaAYVVFADGDRPGVP 635
Cdd:cd05935 313 RTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVcvISVPDERVGEEVK--AFIVLRPEYRGKVT 390
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 502993053 636 APALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05935 391 EEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
218-675 |
3.66e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 124.72 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 218 AYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRG-DRTAVpfDATPTAAT-----------------EPRSGERTT 279
Cdd:PRK07787 7 AAVAAAADIADAVRIGGRVLSRSDLAGAATAVAERVAGaRRVAV--LATPTLATvlavvgaliagvpvvpvPPDSGVAER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 280 GPLDAAAPEAAEPQPGPVlGDHALPPLDANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSR----LVHE 355
Cdd:PRK07787 85 RHILADSGAQAWLGPAPD-DPAGLPHVPVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAAdldaLAEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 356 PDWLdagPDDVFLQAAPI-AFDASTLEIWASLSAGARLVLLppGRVDPAELGAVVAAEGvTVLWLTAGLFHQLVD--HHL 432
Cdd:PRK07787 164 WQWT---ADDVLVHGLPLfHVHGLVLGVLGPLRIGNRFVHT--GRPTPEAYAQALSEGG-TLYFGVPTVWSRIAAdpEAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 433 DRLAGVRHLIAGGDVIsPDAVRRLLAAHPDLVFTNGYGPTEntTFTTCATFGGPAARPGEagplpIGRPIRGTRVRVLDR 512
Cdd:PRK07787 238 RALRGARLLVSGSAAL-PVPVFDRLAALTGHRPVERYGMTE--TLITLSTRADGERRPGW-----VGLPLAGVETRLVDE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 513 LGRPVP--PGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGR-ADDQVKIKGYRVE 589
Cdd:PRK07787 310 DGGPVPhdGETVGELQVRGPTLFDGYLNRPDATAAAFTADG----WFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 590 PAEVAAALGAHPAVT--AAVALPEPGAGgsTRLAAYVVFADgdrpGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPN 667
Cdd:PRK07787 386 AGEIETALLGHPGVReaAVVGVPDDDLG--QRIVAYVVGAD----DVAADELIDFVAQQLSVHKRPREVRFVDALPRNAM 459
|
....*...
gi 502993053 668 GKLDREAL 675
Cdd:PRK07787 460 GKVLKKQL 467
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
132-675 |
9.53e-30 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 124.61 E-value: 9.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 132 FEGGTAPAPARL---VHDLVDERARLAPDAPAL--TAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLI 206
Cdd:PRK05852 3 FMGGAAPMASDFgprIADLVEVAATRLPEAPALvvTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 207 AGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAG-RVRGDRTAVPFDATPTAATEPRSGErttgpldaa 285
Cdd:PRK05852 83 VALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHdRAEPTTRWWPLTVNVGGDSGPSGGT--------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 286 apeaaepqpgpvlgdhalppLDANRRAATEPLPGDLSPGTL----AYVSYTSGSTGTPKGVCVPHRAVSRLVHE-PDWLD 360
Cdd:PRK05852 154 --------------------LSVHLDAATEPTPATSTPEGLrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAiITGYR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 361 AGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPP-GRVDPAELGAVVAAEGVTvlWLTA-GLFHQLVDHHLD----- 433
Cdd:PRK05852 214 LSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPArGRFSAHTFWDDIKAVGAT--WYTAvPTIHQILLERAAtepsg 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 434 ----RLAGVRHLIAGGDVISPDAVRRLLAAhPDLVftnGYGPTENT--TFTTCATFGGPAARPGEAgPLPIGRPIrGTRV 507
Cdd:PRK05852 292 rkpaALRFIRSCSAPLTAETAQALQTEFAA-PVVC---AFGMTEAThqVTTTQIEGIGQTENPVVS-TGLVGRST-GAQI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 508 RVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTpagggERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYR 587
Cdd:PRK05852 366 RIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT-----DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 588 VEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVfadgdrPGVPAPALRDWL----RERLPEFLVPARIVALDAFP 663
Cdd:PRK05852 441 ISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV------PRESAPPTAEELvqfcRERLAAFEIPASFQEASGLP 514
|
570
....*....|..
gi 502993053 664 LTPNGKLDREAL 675
Cdd:PRK05852 515 HTAKGSLDRRAV 526
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
327-675 |
1.27e-29 |
|
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: 123.21 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 327 AYVSYTSGSTGTPKGVCVPHRAVSRLVHEP-DWLDAGPDDVFLQAAPIA--FDASTLEIWASLSAGARLVLLPPGrvDPA 403
Cdd:cd05920 142 ALFLLSGGTTGTPKLIPRTHNDYAYNVRASaEVCGLDQDTVYLAVLPAAhnFPLACPGVLGTLLAGGRVVLAPDP--SPD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 404 ELGAVVAAEGVTVLWLTAGLFHQLVDHHLDR---LAGVRHLIAGGDVISPDAVRRllaAHPDLVFT--NGYGPTEN-TTF 477
Cdd:cd05920 220 AAFPLIEREGVTVTALVPALVSLWLDAAASRradLSSLRLLQVGGARLSPALARR---VPPVLGCTlqQVFGMAEGlLNY 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 478 TtcatfggpaaRPGEAGPLPI---GRPI-RGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGgg 553
Cdd:cd05920 297 T----------RLDDPDEVIIhtqGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDG-- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 554 erQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT--AAVALPEPGAGgsTRLAAYVVFADgdr 631
Cdd:cd05920 365 --FYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHdaAVVAMPDELLG--ERSCAFVVLRD--- 437
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 502993053 632 PGVPAPALRDWLRER-LPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05920 438 PPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
120-677 |
2.34e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 123.18 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 120 LASDADRALVATfeGGTAPAPARLVHDLVDERAR--------LA------PDAPALTAAGKTVPYRWLAEHAEALAARLV 185
Cdd:PRK13383 1 VAPTAARALVRS--GLLNPPSPRAVLRLLREASRggtnpytlLAvtaarwPGRTAIIDDDGALSYRELQRATESLARRLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 186 RAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPFdAT 265
Cdd:PRK13383 79 RDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAV-ID 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 266 PTAATEPRSGERttgpldaaapeaaepqpgpvlgdhalppldanrraateplPGDLSPGTLayVSYTSGSTGTPKGVcvP 345
Cdd:PRK13383 158 PATAGAEESGGR----------------------------------------PAVAAPGRI--VLLTSGTTGKPKGV--P 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 346 HR-------AVSRLVHEPDWLDAGPDDVFlqAAPIAFDASTLEIWASLSAGARLVLLPPGRVDPAELGAVV-AAEGVTVL 417
Cdd:PRK13383 194 RApqlrsavGVWVTILDRTRLRTGSRISV--AMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASLhRADAFTAV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 418 WLTAGLFHQLVDHHLDR--LAGVRHLIAGGDVISPDAVRRLLAAHPDLVFtNGYGPTENTTfttcatfgGPAARPGEA-- 493
Cdd:PRK13383 272 PVVLARILELPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILY-NGYGSTEVGI--------GALATPADLrd 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 494 GPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGrpavtaavftpaGGGER----QYRTGDLARWRTDG 569
Cdd:PRK13383 343 APETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD------------GGGKAvvdgMTSTGDMGYLDNAG 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 570 SLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDrpGVPAPALRDWLRERLPE 649
Cdd:PRK13383 411 RLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGS--GVDAAQLRDYLKDRVSR 488
|
570 580
....*....|....*....|....*...
gi 502993053 650 FLVPARIVALDAFPLTPNGKLDREALPG 677
Cdd:PRK13383 489 FEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
328-672 |
7.87e-29 |
|
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: 117.89 E-value: 7.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 328 YVSYTSGSTGTPKGVCVPHR--AVSRLVHEPDWLDAGpDDVFLQAAPIAFDASTLEIWASLSAGARLVLLppGRVDPAEL 405
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERswIESFVCNEDLFNISG-EDAILAPGPLSHSLFLYGAISALYLGGTFIGQ--RKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 406 GAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAgVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTEnTTFTTcATFGG 485
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALARTLEPESK-IKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSE-LSFIT-YNFNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 486 PAARPGEagplpIGRPIRGTRVRVLDRLGrpvppGVVGDLYALGEGLALGYlgrpaVTAAVFTPAGggerQYRTGDLARW 565
Cdd:cd17633 158 ESRPPNS-----VGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGY-----VRGGFSNPDG----WMSVGDIGYV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 566 RTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVfadGDrpGVPAPALRDWLRE 645
Cdd:cd17633 219 DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GD--KLTYKQLKRFLKQ 293
|
330 340
....*....|....*....|....*..
gi 502993053 646 RLPEFLVPARIVALDAFPLTPNGKLDR 672
Cdd:cd17633 294 KLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
331-675 |
2.60e-28 |
|
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: 118.82 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 331 YTSGSTGTPKGVCVPHRA--VSRLvHEPDWLDAGPDDVFLQ-AAPIAFDASTLEIWASLSAGARLVLLPPGRVDPAELGA 407
Cdd:cd05974 92 FTSGTTSKPKLVEHTHRSypVGHL-STMYWIGLKPGDVHWNiSSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 408 VVAAEGVTVLWLTAGLFHQLVDHHLDRLA-GVRHLIAGGDVISPDAVRRLLAAHpDLVFTNGYGPTEnttftTCATFGGP 486
Cdd:cd05974 171 ALVRYGVTTLCAPPTVWRMLIQQDLASFDvKLREVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTE-----TTALVGNS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 487 AARPGEAGPLpiGRPIRGTRVRVLDRLGRPVPPG----VVGDLYALGegLALGYLGRPAVTAAVFtpaGGGerQYRTGDL 562
Cdd:cd05974 245 PGQPVKAGSM--GRPLPGYRVALLDPDGAPATEGevalDLGDTRPVG--LMKGYAGDPDKTAHAM---RGG--YYRTGDI 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 563 ARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAggsTRLA---AYVVFADGDRPGvPAPAL 639
Cdd:cd05974 316 AMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDP---VRLSvpkAFIVLRAGYEPS-PETAL 391
|
330 340 350
....*....|....*....|....*....|....*...
gi 502993053 640 R--DWLRERLPEFlVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05974 392 EifRFSRERLAPY-KRIRRLEFAELPKTISGKIRRVEL 428
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
119-691 |
6.53e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 119.67 E-value: 6.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 119 DLASDADralVATFEggTAPAPARLV----HDLVDERARLAPDAPALT----AAGKTVPYRWLAEHAEALAAR----LVR 186
Cdd:PRK07529 3 AFATLAD---IEAIE--AVPLAARDLpastYELLSRAAARHPDAPALSflldADPLDRPETWTYAELLADVTRtanlLHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 187 AGVRPGEVVGVLgdrSAGLIAGLLAVLKAGGAYLALPPDW---PDArLTGLLDDAGVRIVLA-----DAQVAGRVRGDRT 258
Cdd:PRK07529 78 LGVGPGDVVAFL---LPNLPETHFALWGGEAAGIANPINPllePEQ-IAELLRAAGAKVLVTlgpfpGTDIWQKVAEVLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 259 AVPfdaTPTAATEPRSGERTTGPLDAAAPEAAEPQPGPVLG-DHALPPLDANRR-AATEPLPGDLSpgtlAYVsYTSGST 336
Cdd:PRK07529 154 ALP---ELRTVVEVDLARYLPGPKRLAVPLIRRKAHARILDfDAELARQPGDRLfSGRPIGPDDVA----AYF-HTGGTT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 337 GTPKGVCVPHR-------AVSRLvhepdwLDAGPDDVFLQAAPIaF--DASTLEIWASLSAGARLVLLPP-GRVDP---A 403
Cdd:PRK07529 226 GMPKLAQHTHGnevanawLGALL------LGLGPGDTVFCGLPL-FhvNALLVTGLAPLARGAHVVLATPqGYRGPgviA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 404 ELGAVVAAEGVT----VLWLTAGLFHQLVDHHldRLAGVRHLIAGGDVIsPDAVRRLLAAHPDLVFTNGYGPTENTTFTT 479
Cdd:PRK07529 299 NFWKIVERYRINflsgVPTVYAALLQVPVDGH--DISSLRYALCGAAPL-PVEVFRRFEAATGVRIVEGYGLTEATCVSS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 480 CATFGGPAaRPGEagplpIGRPIRGTRVRVL-----DRLGRPVPPGVVGDLYALGEGLALGYLgRPAVTAAVFTpaggGE 554
Cdd:PRK07529 376 VNPPDGER-RIGS-----VGLRLPYQRVRVVilddaGRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL----ED 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 555 RQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT--AAVALPEPGAGgstRL-AAYVVFADGdr 631
Cdd:PRK07529 445 GWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVAlaAAVGRPDAHAG---ELpVAYVQLKPG-- 519
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502993053 632 PGVPAPALRDWLRERLPE-FLVPARIVALDAFPLTPNGKLDREALPGSAAE---EGALDENGAP 691
Cdd:PRK07529 520 ASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPALRRDAIRrvlRAALRDAGVE 583
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
267-675 |
9.71e-28 |
|
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: 117.48 E-value: 9.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 267 TAATEPRSGERTTGPLDAAAPEAAEPQPGPVLGDHALPPLDAnrrAATEPLPGDLSPGTlaYVSYTSGSTGTPKGVCVPH 346
Cdd:cd05929 73 SSRAPRAEACAIIEIKAAALVCGLFTGGGALDGLEDYEAAEG---GSPETPIEDEAAGW--KMLYSGGTTGRPKGIKRGL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 347 RAVSR----LVHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAG 422
Cdd:cd05929 148 PGGPPdndtLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLME--KFDPEEFLRLIERYRVTFAQFVPT 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 423 LFHQL------VDHHLDrLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFtNGYGPTENTTFTTCAtfggpaarpGE---A 493
Cdd:cd05929 226 MFVRLlklpeaVRNAYD-LSSLKRVIHAAAPCPPWVKEQWIDWGGPIIW-EYYGGTEGQGLTIIN---------GEewlT 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 494 GPLPIGRPIRGtRVRVLDRLGRPVPPGVVGDLYALGeGLALGYLGRPAVTAAVFTpagggERQYRT-GDLARWRTDGSLD 572
Cdd:cd05929 295 HPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARN-----EGGWSTlGDVGYLDEDGYLY 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 573 FLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGgsTRLAAYVVFADGDRPG-VPAPALRDWLRERLPE 649
Cdd:cd05929 368 LTDRRSDMIISGGVNIYPQEIENALIAHPKVldAAVVGVPDEELG--QRVHAVVQPAPGADAGtALAEELIAFLRDRLSR 445
|
410 420
....*....|....*....|....*.
gi 502993053 650 FLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05929 446 YKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
331-672 |
1.26e-27 |
|
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: 114.67 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 331 YTSGSTGTPKGVCVPHR----AVSRLVHEpdwLDAGPDDVFLQAAPIaFDASTLEI-WASLSAGARLVLLPpgRVDPAEL 405
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGnliaANLQLIHA---MGLTEADVYLNMLPL-FHIAGLNLaLATFHAGGANVVME--KFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 406 GAVVAAEGVTVLWLTAGLFHQLVDHHLD---RLAGVRHlIAGGDVisPDAVRRLLAaHPDLVFTNGYGPTENTTFttcAT 482
Cdd:cd17637 81 LELIEEEKVTLMGSFPPILSNLLDAAEKsgvDLSSLRH-VLGLDA--PETIQRFEE-TTGATFWSLYGQTETSGL---VT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 483 FGGPAARPGEAGplpigRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTpaGGgerQYRTGDL 562
Cdd:cd17637 154 LSPYRERPGSAG-----RPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFR--NG---WHHTGDL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 563 ARWRTDGSLDFLGRADDQVKIK--GYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDRPGvpAPALR 640
Cdd:cd17637 224 GRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLT--ADELI 301
|
330 340 350
....*....|....*....|....*....|..
gi 502993053 641 DWLRERLPEFLVPARIVALDAFPLTPNGKLDR 672
Cdd:cd17637 302 EFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
183-683 |
1.27e-27 |
|
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: 118.15 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 183 RLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPP----DWPDARLTGL------LDDAgvrIVLADAQVAGR 252
Cdd:cd05906 55 GLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVpptyDEPNARLRKLrhiwqlLGSP---VVLTDAELVAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 253 VRGDRT--AVPFDATPTAATEPRSGerttgpldaaapeaaepqpgpvlGDHALPPLDanrraateplpgdlsPGTLAYVS 330
Cdd:cd05906 132 FAGLETlsGLPGIRVLSIEELLDTA-----------------------ADHDLPQSR---------------PDDLALLM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 331 YTSGSTGTPKGVCVPHRAV-SRLVHEPDWLDAGPDDVFLQAAPIAFDASTLEI-WASLSAGARLVLLPPGRV--DPAELG 406
Cdd:cd05906 174 LTSGSTGFPKAVPLTHRNIlARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQVHVPTEEIlaDPLRWL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 407 AVVAAEGVTVLWLTAGLFHQLVDHhLDR-------LAGVRHLIAGGDVISPDAVRRLLAAH-----PDLVFTNGYGPTEn 474
Cdd:cd05906 254 DLIDRYRVTITWAPNFAFALLNDL-LEEiedgtwdLSSLRYLVNAGEAVVAKTIRRLLRLLepyglPPDAIRPAFGMTE- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 475 ttftTCA--TFGGPAARPGEAGPLP---IGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTP 549
Cdd:cd05906 332 ----TCSgvIYSRSFPTYDHSQALEfvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 550 AGggerQYRTGDLArWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAAL----GAHPAVTAAVALPEPGAgGSTRLAayVV 625
Cdd:cd05906 408 DG----WFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEPSFTAAFAVRDPGA-ETEELA--IF 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502993053 626 FA-DGDRPGVPAPALRDWLRERLPEF-LVPARIVAL--DAFPLTPNGKLDREALpGSAAEEG 683
Cdd:cd05906 480 FVpEYDLQDALSETLRAIRSVVSREVgVSPAYLIPLpkEEIPKTSLGKIQRSKL-KAAFEAG 540
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
323-681 |
1.82e-27 |
|
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: 114.50 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 323 PGTLAYVSYTSGSTGTPKgvCVPHRaVSRLVHEPdW-----LDAGPDDVFLQAAPI-AFDASTLEIWASLSAGARLVLL- 395
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPK--LAQHT-HSNEVYNA-WmlalnSLFDPDDVLLCGLPLfHVNGSVVTLLTPLASGAHVVLAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 396 PPGRVDPA---ELGAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPT 472
Cdd:cd05944 77 PAGYRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 473 ENTTFTTCATFGGPAaRPGEAG-PLPIGRpirgTRVRVLD---RLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVft 548
Cdd:cd05944 157 EATCLVAVNPPDGPK-RPGSVGlRLPYAR----VRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAF-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 549 pagGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFAD 628
Cdd:cd05944 230 ---VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKP 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 502993053 629 GDRpgVPAPALRDWLRERLPE-FLVPARIVALDAFPLTPNGKLDREALPGSAAE 681
Cdd:cd05944 307 GAV--VEEEELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADAIH 358
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
152-670 |
9.50e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 115.26 E-value: 9.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 152 ARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGayLALPPDWpdaRL 231
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGA--IAVPVNF---RL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 232 TG-----LLDDAGVRIVLADAQVAGRVRGDRTAVPFDATPTAAteprsgerttgpldaaapeaaepqpGPVLGDHALPPL 306
Cdd:PRK07786 102 TPpeiafLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVA-------------------------GGSSDDSVLGYE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 307 DANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVS--RLVHEPDWLDAGPDDVFLQAAPIAFDASTLEIWA 384
Cdd:PRK07786 157 DLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTgqAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 385 SLSAGARLVLLPPGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDhhlDRLAGVRHL----IAGGDVISPDAV-RRLLAA 459
Cdd:PRK07786 237 GLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCA---EQQARPRDLalrvLSWGAAPASDTLlRQMAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 460 HPDLVFTNGYGPTENTTfTTCATFGGPAARPGEAgplpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGR 539
Cdd:PRK07786 314 FPEAQILAAFGQTEMSP-VTCMLLGEDAIRKLGS----VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 540 PAVTAAVFtpAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAG-GST 618
Cdd:PRK07786 389 PEATAEAF--AGG---WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwGEV 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502993053 619 RLAAYVVFADGDRPGVpaPALRDWLRERLPEFLVPARIVALDAFPLTPNGKL 670
Cdd:PRK07786 464 PVAVAAVRNDDAALTL--EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
152-691 |
1.09e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 115.14 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 152 ARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLalPPDWpdaRL 231
Cdd:PRK07470 17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWV--PTNF---RQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 232 T-----GLLDDAGVRIVLADAQVAGRVRGDRTAVPFDATPTAATEPRSGErttgPLDAAAPEAAEPQPGPVLGDHALPpl 306
Cdd:PRK07470 92 TpdevaYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAGL----DYEALVARHLGARVANAAVDHDDP-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 307 danrraateplpgdlspgtlAYVSYTSGSTGTPKGVCVPHRAVSRLV--HEPDWL-DAGPDDVFLQAAPIAFDASTLEIw 383
Cdd:PRK07470 166 --------------------CWFFFTSGTTGRPKAAVLTHGQMAFVItnHLADLMpGTTEQDASLVVAPLSHGAGIHQL- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 384 ASLSAGARLVLLPPGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH-HLDRL--AGVRHLI-AGGDVISPDAVRRLLAA 459
Cdd:PRK07470 225 CQVARGAATVLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHpAVDRYdhSSLRYVIyAGAPMYRADQKRALAKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 460 HPDLVFTNGYGP-TENTTFTTCATFG---GPAARPGeagplPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALG 535
Cdd:PRK07470 305 GKVLVQYFGLGEvTGNITVLPPALHDaedGPDARIG-----TCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 536 YLGRPAVTAAVFTpagGGerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT--AAVALPEPG 613
Cdd:PRK07470 380 YYNNPEANAKAFR---DG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSevAVLGVPDPV 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 614 AGGSTrlAAYVVFADGDRPGvpAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAEEGALDENGAP 691
Cdd:PRK07470 455 WGEVG--VAVCVARDGAPVD--EAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEERGLLDLERAP 528
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
184-675 |
2.78e-26 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 114.07 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 184 LVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRGDRtavpfd 263
Cdd:PRK06087 66 LLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDL------ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 264 ATPTAATeprsgerttgpLDAAAPEAAEPQPGPVLGDHALPPLDANRRAATEPLP--GDlspgTLAYVSYTSGSTGTPKG 341
Cdd:PRK06087 140 ILPLQNQ-----------LPQLQQIVGVDKLAPATSSLSLSQIIADYEPLTTAITthGD----ELAAVLFTSGTEGLPKG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 342 VCVPHRAVsrLVHEPDW---LDAGPDDVFLQAAPIAFDASTLE-IWASLSAGARLVLLPpgRVDPAELGAVVAAEGVT-V 416
Cdd:PRK06087 205 VMLTHNNI--LASERAYcarLNLTWQDVFMMPAPLGHATGFLHgVTAPFLIGARSVLLD--IFTPDACLALLEQQRCTcM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 417 LWLTAGLFHQL--VDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVftNGYGPTENTTFTTCatfggPAARPGEAG 494
Cdd:PRK06087 281 LGATPFIYDLLnlLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLL--SVYGSTESSPHAVV-----NLDDPLSRF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 495 PLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFL 574
Cdd:PRK06087 354 MHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEG----WYYSGDLCRMDEAGYIKIT 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 575 GRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGgsTRLAAYVVFADGDRpgvpAPALRD---WL-RERLP 648
Cdd:PRK06087 430 GRKKDIIVRGGENISSREVEDILLQHPKIhdACVVAMPDERLG--ERSCAYVVLKAPHH----SLTLEEvvaFFsRKRVA 503
|
490 500
....*....|....*....|....*..
gi 502993053 649 EFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK06087 504 KYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
148-675 |
3.11e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 113.42 E-value: 3.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 148 VDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLV-RAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGayLALPPDW 226
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVEC--IAVPLNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 227 --PDARLTGLLDDAGVRIVLADAQVAGRVRgDRTAVPFDATPTAATEPRSGErttgpldaaapeaaepqpgpvlgDHAlp 304
Cdd:PRK06839 86 rlTENELIFQLKDSGTTVLFVEKTFQNMAL-SMQKVSYVQRVISITSLKEIE-----------------------DRK-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 305 PLDANRRAATEPLpgdlspgtlaYVSYTSGSTGTPKG-VCVPHRAVSRLVHEPDWLDAGPDDVFLQAAPIaFDASTLEIW 383
Cdd:PRK06839 140 IDNFVEKNESASF----------IICYTSGTTGKPKGaVLTQENMFWNALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 384 A--SLSAGARLVLlpPGRVDPAELGAVVAAEGVTVLwLTAGLFHQLVDHHLDR----LAGVRHLIAGGDVISPDAVRRLL 457
Cdd:PRK06839 209 AfpTLFAGGVIIV--PRKFEPTKALSMIEKHKVTVV-MGVPTIHQALINCSKFettnLQSVRWFYNGGAPCPEELMREFI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 458 aaHPDLVFTNGYGPTEnTTFTTCATFGGPAARPgeagPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYL 537
Cdd:PRK06839 286 --DRGFLFGQGFGMTE-TSPTVFMLSEEDARRK----VGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYW 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 538 GRPAVTAAVFTpagggERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAG 615
Cdd:PRK06839 359 NRPDATEETIQ-----DGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVyeVAVVGRQHVKWG 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 616 GSTRlaAYVVFADGdrPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK06839 434 EIPI--AFIVKKSS--SVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
184-670 |
5.16e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 112.69 E-value: 5.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 184 LVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALppDWpdaRLTG-----LLDDAGVRIVLADAQVAGRVRGDRT 258
Cdd:PRK08276 28 LRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPI--NW---HLTAaeiayIVDDSGAKVLIVSAALADTAAELAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 259 AVPFDATPTAAT-EPRSGERttgpldaaapeaaepqpgpvlgdhalpPLDANRRAATEPLPGDLSPGTLayVSYTSGSTG 337
Cdd:PRK08276 103 ELPAGVPLLLVVaGPVPGFR---------------------------SYEEALAAQPDTPIADETAGAD--MLYSSGTTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 338 TPKGVCVPhrAVSRLVHEPD---------WLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPpgRVDPAELGAV 408
Cdd:PRK08276 154 RPKGIKRP--LPGLDPDEAPgmmlallgfGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVME--KFDAEEALAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 409 VAAEGVTVLWLTAGLFHQL------VDHHLDrLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNgYGPTE--NTTFTTC 480
Cdd:PRK08276 230 IERYRVTHSQLVPTMFVRMlklpeeVRARYD-VSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEY-YASSEggGVTVITS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 481 ATFggpAARPGEAGplpigRPIRGtRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTG 560
Cdd:PRK08276 308 EDW---LAHPGSVG-----KAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHG----WVTVG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 561 DLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGgsTRLAAYVVFADGDRPG-VPAP 637
Cdd:PRK08276 375 DVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVadVAVFGVPDEEMG--ERVKAVVQPADGADAGdALAA 452
|
490 500 510
....*....|....*....|....*....|...
gi 502993053 638 ALRDWLRERLPEFLVPARIVALDAFPLTPNGKL 670
Cdd:PRK08276 453 ELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
184-675 |
6.36e-26 |
|
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: 111.46 E-value: 6.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 184 LVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAqvagrvrgdrtavpfd 263
Cdd:cd05973 17 LQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 264 atptaateprsgerttgpldaaapeaaepqpgpvlgdhalppldANRRaateplpgDLSPGTLAYVSyTSGSTGTPKGVC 343
Cdd:cd05973 81 --------------------------------------------ANRH--------KLDSDPFVMMF-TSGTTGLPKGVP 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 344 VPHRAVSRLV-HEPDWLDAGPDDVFLQAAPIAFdASTL--EIWASLSAGARLVLLPpGRVDPAELGAVVAAEGVTVLWLT 420
Cdd:cd05973 108 VPLRALAAFGaYLRDAVDLRPEDSFWNAADPGW-AYGLyyAITGPLALGHPTILLE-GGFSVESTWRVIERLGVTNLAGS 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 421 AGLFHQLVDHHLDRLAGV----RHLIAGGDVISPDaVRRLLAAHPDLVFTNGYGPTENTTFTtcATFGGPAaRPGEAGPL 496
Cdd:cd05973 186 PTAYRLLMAAGAEVPARPkgrlRRVSSAGEPLTPE-VIRWFDAALGVPIHDHYGQTELGMVL--ANHHALE-HPVHAGSA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 497 piGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLAL----GYLGRPavtaavfTPAGGGeRQYRTGDLARWRTDGSLD 572
Cdd:cd05973 262 --GRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLmwfrGYQLPD-------TPAIDG-GYYLTGDTVEFDPDGSFS 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 573 FLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDRPGVP-APALRDWLRERLPEFL 651
Cdd:cd05973 332 FIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAlADELQLHVKKRLSAHA 411
|
490 500
....*....|....*....|....
gi 502993053 652 VPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05973 412 YPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
329-670 |
1.17e-25 |
|
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: 108.74 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 329 VSYTSGSTGTPKGVCVPHRAVSRLVHEpdWLDAG---PDDVFLQAAPI----AFDASTLeiwASLSAGARLVllPPGRVD 401
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAA--WADCAdltEDDRYLIINPFfhtfGYKAGIV---ACLLTGATVV--PVAVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 402 PAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDR---LAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTTFT 478
Cdd:cd17638 78 VDAILEAIERERITVLPGPPTLFQSLLDHPGRKkfdLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 479 TCatfggpaaRPGEAGPL---PIGRPIRGTRVRVLDRlgrpvppgvvGDLYALGEGLALGYLGRPAVTAAVFTPAGgger 555
Cdd:cd17638 158 MC--------RPGDDAETvatTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADG---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 556 QYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGSTRlaAYVVFADGdrPG 633
Cdd:cd17638 216 WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVaqVAVIGVPDERMGEVGK--AFVVARPG--VT 291
|
330 340 350
....*....|....*....|....*....|....*..
gi 502993053 634 VPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKL 670
Cdd:cd17638 292 LTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
320-758 |
3.92e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 112.57 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 320 DLSPGTLAYVSYTSGSTGTPKGVCVPHR---AVSRLVHEPDWLDAGPDDVFLQAAPIAFDASTL-EIWASLSAGARLVLL 395
Cdd:PRK05691 162 ALQPDDIAFLQYTSGSTALPKGVQVSHGnlvANEQLIRHGFGIDLNPDDVIVSWLPLYHDMGLIgGLLQPIFSGVPCVLM 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 396 PPGRV--DPAELGAVVAAEGVTVlwlTAG------LFHQLV-DHHLDRL--AGVRHLIAGGDVISPDAVRRL---LAA-- 459
Cdd:PRK05691 242 SPAYFleRPLRWLEAISEYGGTI---SGGpdfayrLCSERVsESALERLdlSRWRVAYSGSEPIRQDSLERFaekFAAcg 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 460 -HPDLVFTNgYGPTENTTFTTCATFG-GPA-------------ARPGEAGPL-PIGRPIRGTRVRVLD-RLGRPVPPGVV 522
Cdd:PRK05691 319 fDPDSFFAS-YGLAEATLFVSGGRRGqGIPaleldaealarnrAEPGTGSVLmSCGRSQPGHAVLIVDpQSLEVLGDNRV 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 523 GDLYALGEGLALGYLGRPAVTAAVFTPAGGgERQYRTGDLARWRtDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPA 602
Cdd:PRK05691 398 GEIWASGPSIAHGYWRNPEASAKTFVEHDG-RTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 603 V-----TAAVALPEPGAGGstrLAAYVVFADGDRPGVPAPALRDWLRERLPEFL--VPARIVALD--AFPLTPNGKLDRE 673
Cdd:PRK05691 476 VvrkgrVAAFAVNHQGEEG---IGIAAEISRSVQKILPPQALIKSIRQAVAEACqeAPSVVLLLNpgALPKTSSGKLQRS 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 674 A---------------LPGSAAEEGALDEngAPEDALERFLCELWAKVLMVDSVGVDDDFFELGGHSLVAADLLGQLQQD 738
Cdd:PRK05691 553 AcrlrladgsldsyalFPALQAVEAAQTA--ASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDE 630
|
490 500
....*....|....*....|
gi 502993053 739 FGVELPARTFYLSPTIAELA 758
Cdd:PRK05691 631 LGIDLNLRQLFEAPTLAAFS 650
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
331-675 |
1.25e-24 |
|
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: 108.71 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 331 YTSGSTGTPKGVCVPHRA--VSRLVHEPDWLDAGPDDVFLQAAPIAFDASTL-EIWASLSAGARLVLLPPGRVDPAELGA 407
Cdd:cd05928 181 FTSGTTGSPKMAEHSHSSlgLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACVFVHHLPRFDPLVILK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 408 VVAAEGVTVLWLTAGLFHQLVDHHLDR--LAGVRHLIAGGDVISPDaVRRLLAAHPDLVFTNGYGPTEntTFTTCATFGG 485
Cdd:cd05928 261 TLSSYPITTFCGAPTVYRMLVQQDLSSykFPSLQHCVTGGEPLNPE-VLEKWKAQTGLDIYEGYGQTE--TGLICANFKG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 486 PAARPGEagplpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGE-----GLALGYLGRPAVTAAVFTpaggGERqYRTG 560
Cdd:cd05928 338 MKIKPGS-----MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIR----GDF-YLTG 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 561 DLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGSTRlaAYVVFA---DGDRPGVP 635
Cdd:cd05928 408 DRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVveSAVVSSPDPIRGEVVK--AFVVLApqfLSHDPEQL 485
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 502993053 636 APALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05928 486 TKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
152-675 |
1.91e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 107.59 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 152 ARLAPDAPAltAAGKTVPYRWLAEHAEALAARLV----RAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWP 227
Cdd:PRK09088 5 ARLQPQRLA--AVDLALGRRWTYAELDALVGRLAavlrRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 228 DARLTGLLDDAGVRIVLADAQVAGrvrGDRTAVPFDATPTAAteprsgerttgpldaaapeaaepqpgpvlgdhalpplD 307
Cdd:PRK09088 83 ASELDALLQDAEPRLLLGDDAVAA---GRTDVEDLAAFIASA-------------------------------------D 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 308 ANRRAATEPLPgdlsPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHEPDWLD-AGPDDVFLQAAPIAFDASTLEIWASL 386
Cdd:PRK09088 123 ALEPADTPSIP----PERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGrVDAHSSFLCDAPMFHIIGLITSVRPV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 387 SAGARLVLLPPGrVDPAELGAVVA--AEGVTVLWLTAGLFHQLVDHHLDRLAGVRHLIA---GGDVISPDAVRRLLAAHP 461
Cdd:PRK09088 199 LAVGGSILVSNG-FEPKRTLGRLGdpALGITHYFCVPQMAQAFRAQPGFDAAALRHLTAlftGGAPHAAEDILGWLDDGI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 462 DLVftNGYGPTE-NTTFTTCATFGGPAARPGEAG-PLPigrpirGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGR 539
Cdd:PRK09088 278 PMV--DGFGMSEaGTVFGMSVDCDVIRAKAGAAGiPTP------TVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 540 PAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGS 617
Cdd:PRK09088 350 PQATARAFTGDG----WFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIreCAVVGMADAQWGEV 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 618 TRLAayVVFADGDrpGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK09088 426 GYLA--IVPADGA--PLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
323-658 |
2.48e-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: 106.91 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 323 PGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHE-PDWLDAGPDDVFLQAAPIA--FdASTLEIWASLSAGARLVLLPP-- 397
Cdd:cd05907 86 PDDLATIIYTSGTTGRPKGVMLSHRNILSNALAlAERLPATEGDRHLSFLPLAhvF-ERRAGLYVPLLAGARIYFASSae 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 398 ------GRVDPAELGAV--------VAAEGVTVLWLTAGLFHQLVdhhLDRLagvRHLIAGGDVISPDAVRRLLAAhpDL 463
Cdd:cd05907 165 tllddlSEVRPTVFLAVprvwekvyAAIKVKAVPGLKRKLFDLAV---GGRL---RFAASGGAPLPAELLHFFRAL--GI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 464 VFTNGYGPTENTTFTTCATFGGPaaRPGEagplpIGRPIRGTRVRVLDRlgrpvppgvvGDLYALGEGLALGYLGRPAVT 543
Cdd:cd05907 237 PVYEGYGLTETSAVVTLNPPGDN--RIGT-----VGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEAT 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 544 AAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADD-QVKIKGYRVEPAEVAAALGAHPAVTAAvalpepgaggstrlaa 622
Cdd:cd05907 300 AEALDADG----WLHTGDLGEIDEDGFLHITGRKKDlIITSGGKNISPEPIENALKASPLISQA---------------- 359
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 502993053 623 yVVFADGdRPGVPA------PALRDWLRERLPEFLVPARIVA 658
Cdd:cd05907 360 -VVIGDG-RPFLVAlivpdpEALEAWAEEHGIAYTDVAELAA 399
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
133-646 |
3.24e-24 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 107.88 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 133 EGGTAPAPARLVhDLVDERARLAPDAPALT--AAGKTVPYRWLAEHAEALAAR--LVRAGVRPGEVVGVLGDRSAGLIAG 208
Cdd:COG1022 3 EFSDVPPADTLP-DLLRRRAARFPDRVALRekEDGIWQSLTWAEFAERVRALAagLLALGVKPGDRVAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 209 LLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLA-DAQVAGRVRGDRTAVP-------FDATptaatEPRSGERTTg 280
Cdd:COG1022 82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPslrhivvLDPR-----GLRDDPRLL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 281 PLDAAAPeaaepqpgpvLGDHALPPLDANRRAAteplpgDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHE-PDWL 359
Cdd:COG1022 156 SLDELLA----------LGREVADPAELEARRA------AVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARAlLERL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 360 DAGPDDVFLQAAPIA--FdASTLEIWAsLSAGARLVLLPpgrvDPAELGAVVAAEGVTVL-------------------- 417
Cdd:COG1022 220 PLGPGDRTLSFLPLAhvF-ERTVSYYA-LAAGATVAFAE----SPDTLAEDLREVKPTFMlavprvwekvyagiqakaee 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 418 --WLTAGLFHQLVD----HHLDRLAG-----------------------------VRHLIAGGDVISPDAVRRLLAAhpD 462
Cdd:COG1022 294 agGLKRKLFRWALAvgrrYARARLAGkspslllrlkhaladklvfsklrealggrLRFAVSGGAALGPELARFFRAL--G 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 463 LVFTNGYGPTENTTFTTCATFGGPaaRPGEagplpIGRPIRGTRVRVLDRlgrpvppgvvGDLYALGEGLALGYLGRPAV 542
Cdd:COG1022 372 IPVLEGYGLTETSPVITVNRPGDN--RIGT-----VGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEA 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 543 TAAVFTPAGGgerqYRTGDLARWRTDGSLDFLGRADDQvkIK---GYRVEPAEVAAALGAHPAVTAAvalpepgaggstr 619
Cdd:COG1022 435 TAEAFDADGW----LHTGDIGELDEDGFLRITGRKKDL--IVtsgGKNVAPQPIENALKASPLIEQA------------- 495
|
570 580 590
....*....|....*....|....*....|...
gi 502993053 620 laayVVFADGdRPGVPA------PALRDWLRER 646
Cdd:COG1022 496 ----VVVGDG-RPFLAAlivpdfEALGEWAEEN 523
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
118-675 |
4.17e-24 |
|
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: 107.58 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 118 LDLASDADRAlvATFEGGTApapaRLVHDLVDERARLAPDAPALTAAG-----KTVPYRWLAEHAEALAARLVRAGVRPG 192
Cdd:cd05968 43 LDLSGGKPWA--AWFVGGRM----NIVEQLLDKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 193 EVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVR-IVLADaqvaGRVRGDRTAVPFDATPTAA-- 269
Cdd:cd05968 117 DRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKaLITAD----GFTRRGREVNLKEEADKACaq 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 270 ---TEPRSGERTTGPLDAAAPEAAEPQPGPVlgdhALPPLDANRRAATEPLpgdlspgtlaYVSYTSGSTGTPKGvCV-- 344
Cdd:cd05968 193 cptVEKVVVVRHLGNDFTPAKGRDLSYDEEK----ETAGDGAERTESEDPL----------MIIYTSGTTGKPKG-TVhv 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 345 ----PHRAVSRLVHEpdwLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLP--PGRVDPAELGAVVAAEGVTVLW 418
Cdd:cd05968 258 hagfPLKAAQDMYFQ---FDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDgaPDHPKADRLWRMVEDHEITHLG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 419 LTAGLFHQLVDHHLDR-----LAGVRHLIAGGDVISPDA----VRRLLAAHPDLVftNGYGPTENTTFTTCATFGGPAAR 489
Cdd:cd05968 335 LSPTLIRALKPRGDAPvnahdLSSLRVLGSTGEPWNPEPwnwlFETVGKGRNPII--NYSGGTEISGGILGNVLIKPIKP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 490 PGEAGPLPigrpirGTRVRVLDRLGRPVPPgVVGDLYALGE--GLALGYLGRPAvtAAVFTPAGGGERQYRTGDLARWRT 567
Cdd:cd05968 413 SSFNGPVP------GMKADVLDESGKPARP-EVGELVLLAPwpGMTRGFWRDED--RYLETYWSRFDNVWVHGDFAYYDE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 568 DGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGgsTRLAAYVVFadgdRPGV-PAPALRDWLR 644
Cdd:cd05968 484 EGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVleSAAIGVPHPVKG--EAIVCFVVL----KPGVtPTEALAEELM 557
|
570 580 590
....*....|....*....|....*....|....*
gi 502993053 645 ERLPEF----LVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05968 558 ERVADElgkpLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
152-670 |
9.12e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 105.86 E-value: 9.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 152 ARLAPDAPALTAA--GKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDA 229
Cdd:PRK13390 7 AQIAPDRPAVIVAetGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 230 RLTGLLDDAGVRIVLADAQVAGRVrgdrtavpfdATPTAATEPR--SGERTTGpldaaapeaaepqpgpvLGDHALPPLD 307
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDGLA----------AKVGADLPLRlsFGGEIDG-----------------FGSFEAALAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 308 ANRRAATEPLPgdlspgtlAYVSYTSGSTGTPKGVC--VPHRAVSR-----LVHEPDWLDAGPDDVFLQAAPIaFDASTL 380
Cdd:PRK13390 140 AGPRLTEQPCG--------AVMLYSSGTTGFPKGIQpdLPGRDVDApgdpiVAIARAFYDISESDIYYSSAPI-YHAAPL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 381 EiWASL--SAGARLVLlpPGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVD--------HHLDRLAGVRHLIAGgdviSP 450
Cdd:PRK13390 211 R-WCSMvhALGGTVVL--AKRFDAQATLGHVERYRITVTQMVPTMFVRLLKldadvrtrYDVSSLRAVIHAAAP----CP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 451 DAVRRLLAAHPDLVFTNGYGPTENTTFTTCATfGGPAARPGEagplpIGRPIRGTrVRVLDRLGRPVPPGVVGDLYALGE 530
Cdd:PRK13390 284 VDVKHAMIDWLGPIVYEYYSSTEAHGMTFIDS-PDWLAHPGS-----VGRSVLGD-LHICDDDGNELPAGRIGTVYFERD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 531 GLALGYLGRPAVTAAVFTPAgggeRQYRT--GDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAA 606
Cdd:PRK13390 357 RLPFRYLNDPEKTAAAQHPA----HPFWTtvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVhdVAV 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502993053 607 VALPEPGAGgsTRLAAYVVFADGDRPGVP-APALRDWLRERLPEFLVPARIVALDAFPLTPNGKL 670
Cdd:PRK13390 433 IGVPDPEMG--EQVKAVIQLVEGIRGSDElARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
322-671 |
1.71e-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: 104.72 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 322 SPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHE-PDWLDAGPDDVFLQAAPI--AFdASTLEIWASLSAGARLVLLP-P 397
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQiTAIFDPNPEDVVFGALPFfhSF-GLTGCLWLPLLSGIKVVFHPnP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 398 grVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH-HLDRLAGVRHLIAGGDVIsPDAVRRLLAAHPDLVFTNGYGPTENTT 476
Cdd:cd05909 224 --LDYKKIPELIYDKKATILLGTPTFLRGYARAaHPEDFSSLRLVVAGAEKL-KDTLRQEFQEKFGIRILEGYGTTECSP 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 477 FTTCATfGGPAARPGEagplpIGRPIRGTRVRVLDRLGR-PVPPGVVGDLYALGEGLALGYLGRPAVTAAVFtpaggGER 555
Cdd:cd05909 301 VISVNT-PQSPNKEGT-----VGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-----GDG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 556 QYRTGDLARWRTDGSLDFLGRADDQVKIKG-----YRVEpaEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGD 630
Cdd:cd05909 370 WYDTGDIGKIDGEGFLTITGRLSRFAKIAGemvslEAIE--DILSEILPEDNEVAVVSVPDGRKGEKIVLLTTTTDTDPS 447
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 502993053 631 rpgvpapALRDWLRE-RLPEFLVPARIVALDAFPLTPNGKLD 671
Cdd:cd05909 448 -------SLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPD 482
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
151-675 |
3.32e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 103.89 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 151 RARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDAR 230
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 231 LTGLLDDAGVRIVLADAQVAGRVRGDrTAVPFDATPTAATEPRSgERTTGPLDaaapeaaepqpgpvlgdhalppldanr 310
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEAKLIPG-ISVKFAELMNGPKEEAE-IQEEFDLD--------------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 311 RAATeplpgdlspgtlayVSYTSGSTGTPKGVCVP-----HRAVSRL----VHEpdwldagpDDVFLQAAPIaFDASTLE 381
Cdd:PRK03640 142 EVAT--------------IMYTSGTTGKPKGVIQTygnhwWSAVGSAlnlgLTE--------DDCWLAAVPI-FHISGLS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 382 I-WASLSAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLvdhhLDRLAGVRHliaggdvisPDAVRRLLAah 460
Cdd:PRK03640 199 IlMRSVIYGMRVVLVE--KFDAEKINKLLQTGGVTIISVVSTMLQRL----LERLGEGTY---------PSSFRCMLL-- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 461 pdlvftnGYGPTENTTFTTCATFGGP--------------AARPGEAGPLPI---GRPIRGTRVRVLDRlGRPVPPGVVG 523
Cdd:PRK03640 262 -------GGGPAPKPLLEQCKEKGIPvyqsygmtetasqiVTLSPEDALTKLgsaGKPLFPCELKIEKD-GVVVPPFEEG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 524 DLYALGEGLALGYLGRPAVTAAVFtpAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV 603
Cdd:PRK03640 334 EIVVKGPNVTKGYLNREDATRETF--QDG---WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGV 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502993053 604 TAAVALPEPGAGGSTRLAAYVVfADGdrpGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK03640 409 AEAGVVGVPDDKWGQVPVAFVV-KSG---EVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
151-675 |
4.45e-23 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 103.80 E-value: 4.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 151 RARLA-PDAPAL-TAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPD 228
Cdd:PRK07514 10 RAAFAdRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 229 ARLTGLLDDAGVRIVLADAQVAGRVRgdrtavpfdatPTAAtepRSGERTTGPLDAAapeaaepqpgpvlGDHALPPLDA 308
Cdd:PRK07514 90 AELDYFIGDAEPALVVCDPANFAWLS-----------KIAA---AAGAPHVETLDAD-------------GTGSLLEAAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 309 NRRAATEPLPGDlsPGTLAYVSYTSGSTGTPKGVCVPHR-----AVSrLVHEPDWldaGPDDVFLQAAPI-----AFDAS 378
Cdd:PRK07514 143 AAPDDFETVPRG--ADDLAAILYTSGTTGRSKGAMLSHGnllsnALT-LVDYWRF---TPDDVLIHALPIfhthgLFVAT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 379 TLeiwaSLSAGARLVLLPpgRVDPAELGAVVAAegVTVLWLTAGLFHQLVDH-HLDR--LAGVRHLIAGGDVISPDAVRR 455
Cdd:PRK07514 217 NV----ALLAGASMIFLP--KFDPDAVLALMPR--ATVMMGVPTFYTRLLQEpRLTReaAAHMRLFISGSAPLLAETHRE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 456 LLA--AHPDLvftNGYGPTEnTTFTTCATFGGpAARPGEagplpIGRPIRGTRVRVLDR-LGRPVPPGVVGDLYALGEGL 532
Cdd:PRK07514 289 FQErtGHAIL---ERYGMTE-TNMNTSNPYDG-ERRAGT-----VGFPLPGVSLRVTDPeTGAELPPGEIGMIEVKGPNV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 533 ALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALP 610
Cdd:PRK07514 359 FKGYWRMPEKTAEEFRADG----FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVveSAVIGVP 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502993053 611 EP--GAGGstrlAAYVVfadgDRPGVP--APALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK07514 435 HPdfGEGV----TAVVV----PKPGAAldEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
331-675 |
6.70e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 103.82 E-value: 6.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 331 YTSGSTGTPKGVCVPHRAVSRLVHEPDW-LDAGPDDVF-LQAAPIAFDASTLEIWASLSAGARLVLLPpGRVDPAELGAV 408
Cdd:PRK04319 212 YTSGSTGKPKGVLHVHNAMLQHYQTGKYvLDLHEDDVYwCTADPGWVTGTSYGIFAPWLNGATNVIDG-GRFSPERWYRI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 409 VAAEGVTVlWLTA--------GLFHQLVDHHldRLAGVRHLIAGGDVISPDAVR---RLLaahpDLVFTNGYGPTEnTTF 477
Cdd:PRK04319 291 LEDYKVTV-WYTAptairmlmGAGDDLVKKY--DLSSLRHILSVGEPLNPEVVRwgmKVF----GLPIHDNWWMTE-TGG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 478 TTCATFGGPAARPGEagplpIGRPIRGTRVRVLDRLGRPVPPGVVGDLyALGEG---LALGYLGRPAVTAAVFtpAGGge 554
Cdd:PRK04319 363 IMIANYPAMDIKPGS-----MGKPLPGIEAAIVDDQGNELPPNRMGNL-AIKKGwpsMMRGIWNNPEKYESYF--AGD-- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 555 rQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAA--VALPEPGAGgsTRLAAYVVFadgdRP 632
Cdd:PRK04319 433 -WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAgvIGKPDPVRG--EIIKAFVAL----RP 505
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 502993053 633 GV-PAPALRDWL----RERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK04319 506 GYePSEELKEEIrgfvKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVL 553
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
146-686 |
1.35e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 102.54 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 146 DLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALaaRLVRA----GVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLA 221
Cdd:PRK12583 22 DAFDATVARFPDREALVVRHQALRYTWRQLADAVD--RLARGllalGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 222 LPPDWPDARLTGLLDDAGVR-IVLADAQVAGrvrgDRTAVPFDATPT-AATEPRSGERTTGPLDAAAPEAAEPQPGPVLG 299
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRwVICADAFKTS----DYHAMLQELLPGlAEGQPGALACERLPELRGVVSLAPAPPPGFLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 300 DHALPPL-DANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAV---SRLVHEPdwLDAGPDDVFLQAAPI-- 373
Cdd:PRK12583 176 WHELQARgETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNIlnnGYFVAES--LGLTEHDRLCVPVPLyh 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 374 AFdASTLEIWASLSAGARLVLlPPGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHlDR----LAGVRHLIAGGDVIS 449
Cdd:PRK12583 254 CF-GMVLANLGCMTVGACLVY-PNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHP-QRgnfdLSSLRTGIMAGAPCP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 450 PDAVRRLLAAHPDLVFTNGYGPTENTTFTTCATFGGPAARPGEAgplpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALG 529
Cdd:PRK12583 331 IEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVET----VGRTQPHLEVKVVDPDGATVPRGEIGELCTRG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 530 EGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVAL 609
Cdd:PRK12583 407 YSVMKGYWNNPEATAESIDEDG----WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVF 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502993053 610 PEPGAGGSTRLAAYVVFadgdRPGVPAPA--LRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAEEGALD 686
Cdd:PRK12583 483 GVPDEKYGEEIVAWVRL----HPGHAASEeeLREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEELALP 557
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
331-675 |
2.39e-22 |
|
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: 100.50 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 331 YTSGSTGTPKGVCVPHR-----AVSRLVHepdwLDAGPDDVFLQAAPIaFDASTLEI-WASLSAGARLVLLPpgRVDPAE 404
Cdd:cd05912 84 YTSGTTGKPKGVQQTFGnhwwsAIGSALN----LGLTEDDNWLCALPL-FHISGLSIlMRSVIYGMTVYLVD--KFDAEQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 405 LGAVVAAEGVTVLWLTAGLFHQLVDHHLDRL-AGVRHLIAGGDVISPDAVRRllAAHPDLVFTNGYGPTENTTFTTCATF 483
Cdd:cd05912 157 VLHLINSGKVTIISVVPTMLQRLLEILGEGYpNNLRCILLGGGPAPKPLLEQ--CKEKGIPVYQSYGMTETCSQIVTLSP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 484 GGPAARPGEAGplpigRPIRGTRVRVLDRLGrpvPPGVVGDLYALGEGLALGYLGRPAVTAAVFtpAGGgerQYRTGDLA 563
Cdd:cd05912 235 EDALNKIGSAG-----KPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESF--ENG---WFKTGDIG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 564 RWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVfadGDRPgVPAPALRDWL 643
Cdd:cd05912 302 YLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV---SERP-ISEEELIAYC 377
|
330 340 350
....*....|....*....|....*....|..
gi 502993053 644 RERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05912 378 SEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
310-673 |
8.53e-22 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 100.26 E-value: 8.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 310 RRAATEPLPgDLS--PGTLAYVSYTSGSTGTPKGVCVPHRA-VSRLVHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASL 386
Cdd:PLN02860 157 QRALGTTEL-DYAwaPDDAVLICFTSGTTGRPKGVTISHSAlIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAML 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 387 SAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDhhLDRLAG-------VRHLIAGGDVISPDAVRRLLAA 459
Cdd:PLN02860 236 MVGACHVLLP--KFDAKAALQAIKQHNVTSMITVPAMMADLIS--LTRKSMtwkvfpsVRKILNGGGSLSSRLLPDAKKL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 460 HPDLVFTNGYGPTE---NTTF-----TTCATFGGPAARPGEAGPLPIGRPiRGTRVrvldrlGRPVP----------PGV 521
Cdd:PLN02860 312 FPNAKLFSAYGMTEacsSLTFmtlhdPTLESPKQTLQTVNQTKSSSVHQP-QGVCV------GKPAPhvelkigldeSSR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 522 VGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHP 601
Cdd:PLN02860 385 VGRILTRGPHVMLGYWGQNSETASVLSNDG----WLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHP 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 602 AVTAAVALPEPGAGGSTRLAAYVVFADG---------DRPG---VPAPALRDWLRER-LPEFLVPARIVAL-DAFPLTPN 667
Cdd:PLN02860 461 GVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekeNAKKnltLSSETLRHHCREKnLSRFKIPKLFVQWrKPFPLTTT 540
|
....*.
gi 502993053 668 GKLDRE 673
Cdd:PLN02860 541 GKIRRD 546
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
278-774 |
1.13e-21 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 100.49 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 278 TTGPLDAAAPEAAEPQPGPVLGDHA-LPPLDanrraaTEPLPGDlspgTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHE- 355
Cdd:PRK06060 108 TSDALRDRFQPSRVAEAAELMSEAArVAPGG------YEPMGGD----ALAYATYTSGTTGPPKAAIHRHADPLTFVDAm 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 356 -PDWLDAGPDDVFLQAAPIAFdASTL--EIWASLSAGARLVllppgrVDPAELGAVVAAEGVT-----VLWLTAGLFHQL 427
Cdd:PRK06060 178 cRKALRLTPEDTGLCSARMYF-AYGLgnSVWFPLATGGSAV------INSAPVTPEAAAILSArfgpsVLYGVPNFFARV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 428 VDH-HLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTE-NTTFTTCATfggPAARPGEagplpIGRPIRGT 505
Cdd:PRK06060 251 IDScSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEvGQTFVSNRV---DEWRLGT-----LGRVLPPY 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 506 RVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPavtaavfTPAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKG 585
Cdd:PRK06060 323 EIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP-------DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 586 YRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDrpGVPAPALRDWLRE---RLPEFLVPARIVALDAF 662
Cdd:PRK06060 396 VNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGA--TIDGSVMRDLHRGllnRLSAFKVPHRFAVVDRL 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 663 PLTPNGKLDREALPGS---------------AAEEGALDE----------NGAPEDALERFLCELWAK--VLMVD----- 710
Cdd:PRK06060 474 PRTPNGKLVRGALRKQsptkpiwelsltepgSGVRAQRDDlsasnmtiagGNDGGATLRERLVALRQErqRLVVDavcae 553
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993053 711 -----------SVGVDDDFFELGGHSLVAADLLGQLQQDFGVELPARTFYLSPTIAELAEL--KELRPLRERFEAPL 774
Cdd:PRK06060 554 aakmlgepdpwSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYleAELAGGHGRLKSAG 630
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
322-601 |
1.50e-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: 98.59 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 322 SPGTLAYVSYTSGSTGTPKGVCVPHRA-VSRLVHEPDWLDAGPDDVFLqaapiafdaSTLEIWASLSAGARLVLLPPG-- 398
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHANlLHQIRSLSDIVPPQPGDRFL---------SILPIWHSYERSAEYFIFACGcs 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 399 ------RVDPAELGAVVAAEGVTV--LW--LTAGLFHQLVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFT-- 466
Cdd:cd17640 157 qaytsiRTLKDDLKRVKPHYIVSVprLWesLYSGIQKQVSKSSPIKQFLFLFFLSGGIFKFGISGGGALPPHVDTFFEai 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 467 -----NGYGPTENTTFTTCATFGGPAARPgeagplpIGRPIRGTRVRVLDRLGR-PVPPGVVGDLYALGEGLALGYLGRP 540
Cdd:cd17640 237 gievlNGYGLTETSPVVSARRLKCNVRGS-------VGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNP 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502993053 541 AVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQ-VKIKGYRVEPAEVAAALGAHP 601
Cdd:cd17640 310 EATSKVLDSDG----WFNTGDLGWLTCGGELVLTGRAKDTiVLSNGENVEPQPIEEALMRSP 367
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
152-677 |
6.31e-21 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 97.14 E-value: 6.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 152 ARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARL 231
Cdd:PRK13382 53 AQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPAL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 232 TGLLDDAGVRIVLADAQVAGRVRGDrtavpFDATPTAAtepRSGERTTGPLDAAAPEAAEPQPGpvlgdhaLPPLDANRR 311
Cdd:PRK13382 133 AEVVTREGVDTVIYDEEFSATVDRA-----LADCPQAT---RIVAWTDEDHDLTVEVLIAAHAG-------QRPEPTGRK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 312 AATEPLpgdlspgtlayvsyTSGSTGTPKGVcvPHRAVSRLVHEPDWLDAGP---DDVFLQAAPI--AFDASTLEIWASL 386
Cdd:PRK13382 198 GRVILL--------------TSGTTGTPKGA--RRSGPGGIGTLKAILDRTPwraEEPTVIVAPMfhAWGFSQLVLAASL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 387 sagaRLVLLPPGRVDPAELGAVVAAEGVTVLWLTAGLFH---QLVDHHLDRLAG--VRHLIAGGDVISPDAVRRLLAAHP 461
Cdd:PRK13382 262 ----ACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDrimDLPAEVRNRYSGrsLRFAAASGSRMRPDVVIAFMDQFG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 462 DLVFtNGYGPTENTTFTTcatfggpaARPGE--AGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYlgr 539
Cdd:PRK13382 338 DVIY-NNYNATEAGMIAT--------ATPADlrAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--- 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 540 pavtaavfTPagGGERQYR-----TGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGA 614
Cdd:PRK13382 406 --------TS--GSTKDFHdgfmaSGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDE 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502993053 615 GGSTRLAAYVVFADGdrPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPG 677
Cdd:PRK13382 476 QYGQRLAAFVVLKPG--ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
302-675 |
9.36e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 96.76 E-value: 9.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 302 ALPPLDANRRAATEPL-PGDLSPGTLAYVSYTSGSTGTPKGVCVPHR-AVSRLVHEPDWLDAGPDD---VFLQAAPI--- 373
Cdd:PRK05677 184 AVKFNDALAKGAGQPVtEANPQADDVAVLQYTGGTTGVAKGAMLTHRnLVANMLQCRALMGSNLNEgceILIAPLPLyhi 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 374 -AFdasTLEIWASLSAGARLVLLPPGRVDPA---ELGAVVAAEGVTVLWLTAGLFHQLVDHHLDrLAGVRHLIAGGDVIS 449
Cdd:PRK05677 264 yAF---TFHCMAMMLIGNHNILISNPRDLPAmvkELGKWKFSGFVGLNTLFVALCNNEAFRKLD-FSALKLTLSGGMALQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 450 PDAVRRLLAAHPDLVfTNGYGPTENTTFTTCATFGgpAARPGEagplpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALG 529
Cdd:PRK05677 340 LATAERWKEVTGCAI-CEGYGMTETSPVVSVNPSQ--AIQVGT-----IGIPVPSTLCKVIDDDGNELPLGEVGELCVKG 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 530 EGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAV 607
Cdd:PRK05677 412 PQVMKGYWQRPEATDEILDSDG----WLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVlqCAAI 487
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 608 ALPEPGAGGSTRLaaYVVFADGdrPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK05677 488 GVPDEKSGEAIKV--FVVVKPG--ETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
329-672 |
1.72e-20 |
|
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: 93.48 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 329 VSYTSGSTGTPKGVCVPHRAvsrLVHEPD-----WLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPgRVDPA 403
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKT---FFAVPDilqkeGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE-NTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 404 ELGAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAGVRHL---IAGGDVISPDAVRRLLAaHPDLVFTNGYGPTEnTTFTTC 480
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLrliGYGGSRAIAADVRFIEA-TGLTNTAQVYGLSE-TGTALC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 481 ATFGGPAARPGEagplpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTpagggERQYRTG 560
Cdd:cd17635 160 LPTDDDSIEINA-----VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-----DGWVNTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 561 DLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDRPGVpAPALR 640
Cdd:cd17635 230 DLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENA-IRALK 308
|
330 340 350
....*....|....*....|....*....|..
gi 502993053 641 DWLRERLPEFLVPARIVALDAFPLTPNGKLDR 672
Cdd:cd17635 309 HTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
144-675 |
4.50e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 94.71 E-value: 4.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 144 VHDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALP 223
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 224 PDWPDARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPFDATPTAatepRSGERTTGPLDAAAPEAAEPQPGPVLG---- 299
Cdd:PRK06710 106 PLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVT----RIADFLPFPKNLLYPFVQKKQSNLVVKvses 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 300 --DHALPPLDANRRAATEpLPGDlSPGTLAYVSYTSGSTGTPKGVCVPHR-AVSRLVHEPDWLD--AGPDDVFLQAAPIa 374
Cdd:PRK06710 182 etIHLWNSVEKEVNTGVE-VPCD-PENDLALLQYTGGTTGFPKGVMLTHKnLVSNTLMGVQWLYncKEGEEVVLGVLPF- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 375 FDASTLEIWASLS--AGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDR---LAGVRHLIAGGDVIs 449
Cdd:PRK06710 259 FHVYGMTAVMNLSimQGYKMVLIP--KFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKeydISSIRACISGSAPL- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 450 PDAVRRLLAAHPDLVFTNGYGPTENTTFTTcATFGGPAARPGEagplpIGRPIRGTRVRVLD-RLGRPVPPGVVGDLYAL 528
Cdd:PRK06710 336 PVEVQEKFETVTGGKLVEGYGLTESSPVTH-SNFLWEKRVPGS-----IGVPWPDTEAMIMSlETGEALPPGEIGEIVVK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 529 GEGLALGYLGRPAVTAAVFTpagggERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVA 608
Cdd:PRK06710 410 GPQIMKGYWNKPEETAAVLQ-----DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVT 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502993053 609 L--PEPGAGGSTRlaAYVVFADGDRpgVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK06710 485 IgvPDPYRGETVK--AFVVLKEGTE--CSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
466-679 |
5.52e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 94.50 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 466 TNGYGPTEnTTFTTCATFGGPAARPGEagplpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAA 545
Cdd:PRK12492 362 VEGYGLTE-TSPVASTNPYGELARLGT-----VGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAE 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 546 VFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT--AAVALPEPGAGGSTRLaaY 623
Cdd:PRK12492 436 ALDAEG----WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVAncAAIGVPDERSGEAVKL--F 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502993053 624 VVFADgdrPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSA 679
Cdd:PRK12492 510 VVARD---PGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
306-680 |
6.85e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 94.32 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 306 LDANRRAATEPLPgdLSPGTLAYVSYTSGSTGTPKGVCVPHR-AVSRLVHEPDWLDAG------PDD-VFLQAAPI--AF 375
Cdd:PRK07059 188 LAEGARQTFKPVK--LGPDDVAFLQYTGGTTGVSKGATLLHRnIVANVLQMEAWLQPAfekkprPDQlNFVCALPLyhIF 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 376 dASTLEIWASLSAGARLVLLPPGRVDPA---ELG--AVVAAEGVTVLWltAGLFHQLVDHHLDrLAGVRHLIAGG-DVIS 449
Cdd:PRK07059 266 -ALTVCGLLGMRTGGRNILIPNPRDIPGfikELKkyQVHIFPAVNTLY--NALLNNPDFDKLD-FSKLIVANGGGmAVQR 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 450 PDAVRRLLAAHPDLvfTNGYGPTENTTFTTCatfgGPAARPGEAGplPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALG 529
Cdd:PRK07059 342 PVAERWLEMTGCPI--TEGYGLSETSPVATC----NPVDATEFSG--TIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRG 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 530 EGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAV 607
Cdd:PRK07059 414 PQVMAGYWNRPDETAKVMTADG----FFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVleVAAV 489
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502993053 608 ALPEPGAGGSTRLaaYVVFADgdrPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAA 680
Cdd:PRK07059 490 GVPDEHSGEAVKL--FVVKKD---PALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDGKA 557
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
325-675 |
1.70e-19 |
|
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: 92.59 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 325 TLAYVSYTSGSTGTPKGVCVPHR-AVSRLVH--EPDWLDA-GPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPpgRV 400
Cdd:cd17642 185 QVALIMNSSGSTGLPKGVQLTHKnIVARFSHarDPIFGNQiIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMY--KF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 401 DPAELGAVVAAEGVTVLWLTAGLF-----HQLVDHHldRLAGVRHLIAGGDVISPDaVRRLLAAHPDLVFT-NGYGPTEn 474
Cdd:cd17642 263 EEELFLRSLQDYKVQSALLVPTLFaffakSTLVDKY--DLSNLHEIASGGAPLSKE-VGEAVAKRFKLPGIrQGYGLTE- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 475 ttfTTCATFGGPAA--RPGEAGPLpigrpIRGTRVRVLD-RLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAG 551
Cdd:cd17642 339 ---TTSAILITPEGddKPGAVGKV-----VPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDG 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 552 ggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV-TAAVA-LPEPGAGGSTrlAAYVVFADG 629
Cdd:cd17642 411 ----WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIfDAGVAgIPDEDAGELP--AAVVVLEAG 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 502993053 630 DR----------PGVPAPAlrDWLRerlpeflvpARIVALDAFPLTPNGKLDREAL 675
Cdd:cd17642 485 KTmtekevmdyvASQVSTA--KRLR---------GGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
152-675 |
3.69e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 91.49 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 152 ARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARL 231
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 232 TGLLDDAGVRIVLADAQVAgrvrgdrtAVPFDATPTAATEPRSGERTTgpldaaapeaaepqpgpVLGDHALPPLDANRR 311
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFD--------AIVALETPKIVIDAAAQADSR-----------------RLAQGGLEIPPQAAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 312 AateplpgdlsPGTLAYVSYTSGSTGTPKGVCVPHRAVS-RLVHEPDWLDAGPDDVFLQAAPI----AFDASTLeiwASL 386
Cdd:PRK06145 147 A----------PTDLVRLMYTSGTTDRPKGVMHSYGNLHwKSIDHVIALGLTASERLLVVGPLyhvgAFDLPGI---AVL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 387 SAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLV---DHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDL 463
Cdd:PRK06145 214 WVGGTLRIHR--EFDPEAVLAAIERHRLTCAWMAPVMLSRVLtvpDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 464 VFTNGYGPTENTTFTTCATFGGPAARPGEAGplpigRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVT 543
Cdd:PRK06145 292 RYIDAYGLTETCSGDTLMEAGREIEKIGSTG-----RALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 544 AAVFTpagggERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAY 623
Cdd:PRK06145 367 AEAFY-----GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAV 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502993053 624 VVFADGdrPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK06145 442 VVLNPG--ATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
183-675 |
5.39e-19 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 90.91 E-value: 5.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 183 RLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGgAYlALPPDW---PDaRLTGLLDDAGVRIVLADAQVAGRVRGD-RT 258
Cdd:PRK12406 27 GLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLG-AY-AVPVNWhfkPE-EIAYILEDSGARVLIAHADLLHGLASAlPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 259 AVPFDATPTAAtEPRSGERTtgpldaaapEAAEPQPGPvlGDHALPP-LDANRRAATEPLPGdlsPGTLAYvsyTSGSTG 337
Cdd:PRK12406 104 GVTVLSVPTPP-EIAAAYRI---------SPALLTPPA--GAIDWEGwLAQQEPYDGPPVPQ---PQSMIY---TSGTTG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 338 TPKGV----CVPHRAVS-----RLVH--EPDW--LDAGPddvFLQAAPIAFDAstleiwASLSAGARLVLLPpgRVDPAE 404
Cdd:PRK12406 166 HPKGVrraaPTPEQAAAaeqmrALIYglKPGIraLLTGP---LYHSAPNAYGL------RAGRLGGVLVLQP--RFDPEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 405 LGAVVAAEGVTVLWLTAGLFHQLVDHHLDR-----LAGVRHLIAGGDVISPDaVRRLLAAHPDLVFTNGYGPTENTTFTT 479
Cdd:PRK12406 235 LLQLIERHRITHMHMVPTMFIRLLKLPEEVrakydVSSLRHVIHAAAPCPAD-VKRAMIEWWGPVIYEYYGSTESGAVTF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 480 CaTFGGPAARPGEagplpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLAL-GYLGRPAVTAAVftpagggERQ-- 556
Cdd:PRK12406 314 A-TSEDALSHPGT-----VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEI-------DRGgf 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 557 YRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGStrLAAYVVFADGDRpgV 634
Cdd:PRK12406 381 ITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVhdCAVFGIPDAEFGEA--LMAVVEPQPGAT--L 456
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502993053 635 PAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK12406 457 DEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
499-681 |
8.63e-19 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 90.43 E-value: 8.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 499 GRPIRGT-RVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRA 577
Cdd:PRK10946 356 GRPMSPDdEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANG----FYCSGDLVSIDPDGYITVVGRE 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 578 DDQVKIKGYRVEPAEVAAALGAHPAVT--AAVALPEPGAGGSTrlAAYVVFADGDRPgvpaPALRDWLRER-LPEFLVPA 654
Cdd:PRK10946 432 KDQINRGGEKIAAEEIENLLLRHPAVIhaALVSMEDELMGEKS--CAFLVVKEPLKA----VQLRRFLREQgIAEFKLPD 505
|
170 180
....*....|....*....|....*..
gi 502993053 655 RIVALDAFPLTPNGKLDREALPGSAAE 681
Cdd:PRK10946 506 RVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
183-775 |
1.30e-18 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 90.92 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 183 RLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPF 262
Cdd:COG3319 7 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 263 DATPTAATEPRSGERTTGPLDAAAPEAAEPQPGPVLGDHALPPLDANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGV 342
Cdd:COG3319 87 ALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 343 CVPHRAVSRLVHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPPGRVDPAELGAVVAAEGVTVLWLTAG 422
Cdd:COG3319 167 VLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 423 LFHQLVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTTFTTCATFGGPAARPGEAGPLPIGRPI 502
Cdd:COG3319 247 LLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 503 RGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGGGERQYRTGDLARWRTDGSLDFLGRADDQVK 582
Cdd:COG3319 327 LLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 583 IKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVfadGDRPGVPAPALRDWLRERLPEFLVPARIVALDAF 662
Cdd:COG3319 407 RRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVV---AAAALAAAALLLLLLLLLLPPPLPPALLLLLLLL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 663 PLTPNGKLDREALPGSAAEEGALDEngAPEDALERFLCELWAKVLMVDSVGVDDDFFELGGHSLVAADLLGQLQQDFGVE 742
Cdd:COG3319 484 LLLLLAALLLAAAAPAAAAAAAAAP--APAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRL 561
|
570 580 590
....*....|....*....|....*....|...
gi 502993053 743 LPARTFYLSPTIAELAELKELRPLRERFEAPLP 775
Cdd:COG3319 562 LLLLALLLAPTLAALAAALAAAAAAAALSPLVP 594
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
320-675 |
1.96e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 89.73 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 320 DLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHEPDW-----LDAGPDDVFLqAAPI--AFdASTLEIWASLSAGARL 392
Cdd:PRK08974 202 ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAaygplLHPGKELVVT-ALPLyhIF-ALTVNCLLFIELGGQN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 393 VLLPPGRVDPA---ELGA--VVAAEGVTVL---WLTAGLFHQLVDHHLdrlagvrHLIAGGDVispdAVRRLLAAH-PDL 463
Cdd:PRK08974 280 LLITNPRDIPGfvkELKKypFTAITGVNTLfnaLLNNEEFQELDFSSL-------KLSVGGGM----AVQQAVAERwVKL 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 464 VFTN---GYGPTENTTFTTCAtfggPAARPGEAGPlpIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRP 540
Cdd:PRK08974 349 TGQYlleGYGLTECSPLVSVN----PYDLDYYSGS--IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRP 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 541 AVTAAVFTpagggERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGST 618
Cdd:PRK08974 423 EATDEVIK-----DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVleVAAVGVPSEVSGEAV 497
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 502993053 619 RLaaYVVFADgdrPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK08974 498 KI--FVVKKD---PSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
329-669 |
2.51e-18 |
|
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: 88.90 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 329 VSYTSGSTGTPKGVCVPHR-----AVSRLVHepdWlDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPpgRVDPA 403
Cdd:cd12118 138 LNYTSGTTGRPKGVVYHHRgaylnALANILE---W-EMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLR--KVDAK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 404 ELGAVVAAEGVTVLWLTAGLFHQLVDH-HLDRL---AGVRHLIAGGdviSPDAvrRLLAAHPDLVF--TNGYGPTENT-T 476
Cdd:cd12118 212 AIYDLIEKHKVTHFCGAPTVLNMLANApPSDARplpHRVHVMTAGA---PPPA--AVLAKMEELGFdvTHVYGLTETYgP 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 477 FTTCATFGGPAARPGEAGPLPIGRP----IRGTRVRVLD-RLGRPVP-PGV-VGDLYALGEGLALGYLGRPAVTAAVFtp 549
Cdd:cd12118 287 ATVCAWKPEWDELPTEERARLKARQgvryVGLEEVDVLDpETMKPVPrDGKtIGEIVFRGNIVMKGYLKNPEATAEAF-- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 550 AGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAA--VALPEPGAGGStrLAAYVVFA 627
Cdd:cd12118 365 RGG---WFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAavVARPDEKWGEV--PCAFVELK 439
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 502993053 628 DGDrpGVPAPALRDWLRERLPEFLVPaRIVALDAFPLTPNGK 669
Cdd:cd12118 440 EGA--KVTEEEIIAFCREHLAGFMVP-KTVVFGELPKTSTGK 478
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
321-675 |
2.88e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 88.97 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 321 LSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHEPDWLDA-GPDDVFLQAAPiAF--DASTLEIWASLSAGARLVLLPP 397
Cdd:PRK08008 170 LSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCAlRDDDVYLTVMP-AFhiDCQCTAAMAAFSAGATFVLLEK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 398 grvdpaelgavvaaegvtvlwLTAGLF-HQLVDHHldrlAGVRHLIaggdvisPDAVRRLLAAHP----------DLVF- 465
Cdd:PRK08008 249 ---------------------YSARAFwGQVCKYR----ATITECI-------PMMIRTLMVQPPsandrqhclrEVMFy 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 466 -------------------TNGYGPTEnttfttcaTFGGPAA-RPGEAGPLP-IGRPIRGTRVRVLDRLGRPVPPGVVGD 524
Cdd:PRK08008 297 lnlsdqekdafeerfgvrlLTSYGMTE--------TIVGIIGdRPGDKRRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 525 LYALGE-GLAL--GYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHP 601
Cdd:PRK08008 369 ICIKGVpGKTIfkEYYLDPKATAKVLEADG----WLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHP 444
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993053 602 AVTAAVALpepGAGGSTR---LAAYVVFADGDRpgVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK08008 445 KIQDIVVV---GIKDSIRdeaIKAFVVLNEGET--LSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
326-671 |
2.24e-17 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 87.29 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 326 LAYVSYTSGSTGTPKGVCVPHR-------AVSRLVHepdwldAGPDDVFLQAAPI--AFdASTLEIWASLSAGARLVLLP 396
Cdd:PRK08633 784 TATIIFSSGSEGEPKGVMLSHHnilsnieQISDVFN------LRNDDVILSSLPFfhSF-GLTVTLWLPLLEGIKVVYHP 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 397 -PgrVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH---HLDRLAGVRHLIAGGDVISP---DAVRRLLAAHPdlvfTNGY 469
Cdd:PRK08633 857 dP--TDALGIAKLVAKHRATILLGTPTFLRLYLRNkklHPLMFASLRLVVAGAEKLKPevaDAFEEKFGIRI----LEGY 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 470 GPTENTTFTTCATfggPAARPGEAGPLP------IGRPIRGTRVRVLD-RLGRPVPPGVVGDLYALGEGLALGYLGRPAV 542
Cdd:PRK08633 931 GATETSPVASVNL---PDVLAADFKRQTgskegsVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEK 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 543 TAAVFTPAGGgERQYRTGDLARWRTDGSLDFLGRADDQVKIKGY-----RVEpAEVAAALGAHPAVTAAVALPEPGAGgs 617
Cdd:PRK08633 1008 TAEVIKDIDG-IGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEmvplgAVE-EELAKALGGEEVVFAVTAVPDEKKG-- 1083
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 502993053 618 TRLAAYVVFADGDrpgvpAPALRDWLRE-RLPEFLVPARIVALDAFPLTPNGKLD 671
Cdd:PRK08633 1084 EKLVVLHTCGAED-----VEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
312-675 |
2.75e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 85.72 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 312 AATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHR---AVSRLVHEpDWlDAGPDDVflqaapiafDASTLEIWA--SL 386
Cdd:PRK09274 162 AAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGmfeAQIEALRE-DY-GIEPGEI---------DLPTFPLFAlfGP 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 387 SAGARLVLLP-----PGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDH---HLDRLAGVRHLIAGGDVISPDAVRRLLA 458
Cdd:PRK09274 231 ALGMTSVIPDmdptrPATVDPAKLFAAIERYGVTNLFGSPALLERLGRYgeaNGIKLPSLRRVISAGAPVPIAVIERFRA 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 459 A-HPDLVFTNGYGPTEN---TTFTTCATFGGPAARPGEAGPLPIGRPIRGTRVRVL---DRLG------RPVPPGVVGDL 525
Cdd:PRK09274 311 MlPPDAEILTPYGATEAlpiSSIESREILFATRAATDNGAGICVGRPVDGVEVRIIaisDAPIpewddaLRLATGEIGEI 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 526 YALGEGLALGYLGRPAVTAAVFTPAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV-- 603
Cdd:PRK09274 391 VVAGPMVTRSYYNRPEATRLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVkr 470
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993053 604 TAAVALPEPGAggsTRLAAYVVFADGDRpgVPAPALRDWLRERLPEFLVPARIVAL---DAFPLTP--NGKLDREAL 675
Cdd:PRK09274 471 SALVGVGVPGA---QRPVLCVELEPGVA--CSKSALYQELRALAAAHPHTAGIERFlihPSFPVDIrhNAKIFREKL 542
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
328-675 |
5.15e-17 |
|
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: 85.31 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 328 YVSYTSGSTGTPKGVCvpHRAVSRLVHEP---DW-LDAGPDDVFLQAAPIAF-DASTLEIWASLSAGARLVLLP--PGRV 400
Cdd:cd05966 235 FILYTSGSTGKPKGVV--HTTGGYLLYAAttfKYvFDYHPDDIYWCTADIGWiTGHSYIVYGPLANGATTVMFEgtPTYP 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 401 DPAELGAVVAAEGVTVLWlTAG----LFHQLVDHHLDR--LAGVRHLIAGGDVISPDAVR--RLLAAHPDLVFTNGYGPT 472
Cdd:cd05966 313 DPGRYWDIVEKHKVTIFY-TAPtairALMKFGDEWVKKhdLSSLRVLGSVGEPINPEAWMwyYEVIGKERCPIVDTWWQT 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 473 ENTTFTTCATFGGPAARPGEAGplpigRPIRGTRVRVLDRLGRPVPPGVVGDLYALGE--GLALGYLGRPA-VTAAVFTP 549
Cdd:cd05966 392 ETGGIMITPLPGATPLKPGSAT-----RPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHErYEDTYFSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 550 AGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGStrLAAYVVFA 627
Cdd:cd05966 467 FPG---YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVaeAAVVGRPHDIKGEA--IYAFVTLK 541
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 502993053 628 DGDRP-GVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05966 542 DGEEPsDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
151-669 |
1.14e-16 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 84.24 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 151 RARLAPDAPALTAA--GKTVPYRWLA--EHAEALAARLVRAGVRPGE-VVGVLGDRSAGLIAgLLAVLKAGGAYLALPPD 225
Cdd:cd05943 78 RHADADDPAAIYAAedGERTEVTWAElrRRVARLAAALRALGVKPGDrVAGYLPNIPEAVVA-MLATASIGAIWSSCSPD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 226 WPDArltGLLDDAG---VRIVLADAQV--AGRV--RGDRTAVPFDATPT-AATEPRSGERTTGPLDAAAPEAAEPQPGpV 297
Cdd:cd05943 157 FGVP---GVLDRFGqiePKVLFAVDAYtyNGKRhdVREKVAELVKGLPSlLAVVVVPYTVAAGQPDLSKIAKALTLED-F 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 298 LGDHALPPLDANRRAATEPLpgdlspgtlaYVSYTSGSTGTPKgvCVPHRAVSRLV-----HEPDWlDAGPDDVFLQaap 372
Cdd:cd05943 233 LATGAAGELEFEPLPFDHPL----------YILYSSGTTGLPK--CIVHGAGGTLLqhlkeHILHC-DLRPGDRLFY--- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 373 iaFDASTLEIW----ASLSAGARLVLL--PPGRVDPAELGAVVAAEGVTVLWLTAGLFH-----QLVDHHLDRLAGVRHL 441
Cdd:cd05943 297 --YTTCGWMMWnwlvSGLAVGATIVLYdgSPFYPDTNALWDLADEEGITVFGTSAKYLDalekaGLKPAETHDLSSLRTI 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 442 IAGGDVISPDAVRRLL-AAHPDLVFTNGYGPTEnttFTTCATFGGPAA--RPGEagplpIGRPIRGTRVRVLDRLGRPVP 518
Cdd:cd05943 375 LSTGSPLKPESFDYVYdHIKPDVLLASISGGTD---IISCFVGGNPLLpvYRGE-----IQCRGLGMAVEAFDEEGKPVW 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 519 pGVVGDLYALGE--GLALGYLGRPAVT---AAVFTPAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEV 593
Cdd:cd05943 447 -GEKGELVCTKPfpSMPVGFWNDPDGSryrAAYFAKYPG---VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEI 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993053 594 AAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDRPGVP-APALRDWLRERLPEFLVPARIVALDAFPLTPNGK 669
Cdd:cd05943 523 YRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDElRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
311-684 |
1.20e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 83.68 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 311 RAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAvsrlvhepdWLDA----------GPDDVFLQAAPIAfdaSTL 380
Cdd:PRK07638 130 KYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQS---------WLHSfdcnvhdfhmKREDSVLIAGTLV---HSL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 381 EIWASLSA---GARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLVdhhldRLAGVRH----LIAGGDVISPDAV 453
Cdd:PRK07638 198 FLYGAISTlyvGQTVHLMR--KFIPNQVLDKLETENISVMYTVPTMLESLY-----KENRVIEnkmkIISSGAKWEAEAK 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 454 RRLLAAHPDLVFTNGYGPTEnTTFTTCATFGGPAARPGEAGplpigRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLA 533
Cdd:PRK07638 271 EKIKNIFPYAKLYEFYGASE-LSFVTALVDEESERRPNSVG-----RPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFF 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 534 LGYLGRPAVTAAVftPAGGGERQYRTGDLARwrtDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPG 613
Cdd:PRK07638 345 MGYIIGGVLAREL--NADGWMTVRDVGYEDE---EGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPD 419
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502993053 614 AGGSTRLAAYVvfaDGDRPgvpAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPgSAAEEGA 684
Cdd:PRK07638 420 SYWGEKPVAII---KGSAT---KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK-SWIENQE 483
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
126-658 |
1.43e-16 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 83.77 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 126 RALVATFegGTAPAPARLVHDLVDERARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGL 205
Cdd:PRK08279 23 RGLKRTA--LITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 206 IAGLLAVLKAGGAylalppdwpdarlTGLLDDAGVRIVLA------DAQVAgrVRGDRTAVPFDATPTAATEPRSgertt 279
Cdd:PRK08279 101 LAAWLGLAKLGAV-------------VALLNTQQRGAVLAhslnlvDAKHL--IVGEELVEAFEEARADLARPPR----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 280 gpldaaAPEAAEPQPGPVLGDHALPPLDANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRavsRLVHEPDW- 358
Cdd:PRK08279 161 ------LWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHM---RWLKAMGGf 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 359 ---LDAGPDDVFLQAAPIAFDASTLEIWAS-LSAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLVD---HH 431
Cdd:PRK08279 232 gglLRLTPDDVLYCCLPLYHNTGGTVAWSSvLAAGATLALRR--KFSASRFWDDVRRYRATAFQYIGELCRYLLNqppKP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 432 LDRLAGVRHLIAGGdvISPD---------AVRRLLaahpdlvftNGYGPTE-NTTFTTcaTFGgpaaRPGEAG--PLPIG 499
Cdd:PRK08279 310 TDRDHRLRLMIGNG--LRPDiwdefqqrfGIPRIL---------EFYAASEgNVGFIN--VFN----FDGTVGrvPLWLA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 500 RPIR--------GTRVRVLDRLGRPVPPGVVgdlyalgeGLALGYLGR---------PAVTAA-----VFTPaggGERQY 557
Cdd:PRK08279 373 HPYAivkydvdtGEPVRDADGRCIKVKPGEV--------GLLIGRITDrgpfdgytdPEASEKkilrdVFKK---GDAWF 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 558 RTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVA--LPEPGAGGSTRLAAYVVfadGDRPGVP 635
Cdd:PRK08279 442 NTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygVEVPGTDGRAGMAAIVL---ADGAEFD 518
|
570 580
....*....|....*....|....*
gi 502993053 636 APALRDWLRERLPEFLVPA--RIVA 658
Cdd:PRK08279 519 LAALAAHLYERLPAYAVPLfvRLVP 543
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
327-679 |
4.07e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 81.74 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 327 AYVSYTSGSTGTPKGVCVPHRAVSRLVHE-PDWLDAGPDDVFLQAAP-IAFDASTLEIWASLSAgarLVLLPPGRVDPAE 404
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRHGTFAAQIDAlRQLYGIRPGEVDLATFPlFALFGPALGLTSVIPD---MDPTRPARADPQK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 405 LGAVVAAEGVTVLWLTAGLFHQLVDH---HLDRLAGVRHLIAGGDVISPDAVRRLLAA-HPDLVFTNGYGPTENTTFTTC 480
Cdd:cd05910 165 LVGAIRQYGVSIVFGSPALLERVARYcaqHGITLPSLRRVLSAGAPVPIALAARLRKMlSDEAEILTPYGATEALPVSSI 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 481 AT---FGGPAARPGEAGPLPIGRPIRGTRVRVLDRLGRP---------VPPGVVGDLYALGEGLALGYLGRPAVTAAVFT 548
Cdd:cd05910 245 GSrelLATTTAATSGGAGTCVGRPIPGVRVRIIEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKI 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 549 PAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGaggsTRLAAYVVF 626
Cdd:cd05910 325 DDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVrrSALVGVGKPG----CQLPVLCVE 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 627 AdgdRPGV--PAPALRDWLRERLPEFLVPARIVAL---DAFPLTP--NGKLDREALPGSA 679
Cdd:cd05910 401 P---LPGTitPRARLEQELRALAKDYPHTQRIGRFlihPSFPVDIrhNAKIFREKLAVWA 457
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
151-675 |
5.81e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 81.66 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 151 RARLAPDAPALTAA--GKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPD 228
Cdd:PRK13391 6 HAQTTPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 229 ARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPfdatptaateprsgeRTTGPLDaaapeaaepqpgpVLGDHALPPLDa 308
Cdd:PRK13391 86 AEAAYIVDDSGARALITSAAKLDVARALLKQCP---------------GVRHRLV-------------LDGDGELEGFV- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 309 NRRAATEPLPG----DLSPGTLayVSYTSGSTGTPKGVC--VPHRAVSR-----LVHEPDWlDAGPDDVFLQAAPIAFDA 377
Cdd:PRK13391 137 GYAEAVAGLPAtpiaDESLGTD--MLYSSGTTGRPKGIKrpLPEQPPDTplpltAFLQRLW-GFRSDMVYLSPAPLYHSA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 378 STLEIWASLSAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQLVD--------HHLDRLAGVRHLIAGgdviS 449
Cdd:PRK13391 214 PQRAVMLVIRLGGTVIVME--HFDAEQYLALIEEYGVTHTQLVPTMFSRMLKlpeevrdkYDLSSLEVAIHAAAP----C 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 450 PDAVRRLLAAHPDLVFTNGYGPTENTTFTTCATFGGpAARPGEagplpIGRPIRGTrVRVLDRLGRPVPPGVVGDLYaLG 529
Cdd:PRK13391 288 PPQVKEQMIDWWGPIIHEYYAATEGLGFTACDSEEW-LAHPGT-----VGRAMFGD-LHILDDDGAELPPGEPGTIW-FE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 530 EGLALGYLGRPAVTAAVFTPAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT-AAV- 607
Cdd:PRK13391 360 GGRPFEYLNDPAKTAEARHPDGT---WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVAdAAVf 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502993053 608 ALPEPGAGGSTRlaAYVVFADGDRPGVP-APALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK13391 437 GVPNEDLGEEVK--AVVQPVDGVDPGPAlAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
479-760 |
7.70e-16 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 79.02 E-value: 7.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 479 TCATFGGPAARPGEAGPLPIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGGGERQYR 558
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 559 TGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDrPGVPAPA 638
Cdd:COG3433 81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAA-LDGLAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 639 LRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAEE----GALDENGAPEDALERFLCELWAKVLMV--DSV 712
Cdd:COG3433 160 AALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEallaAASPAPALETALTEEELRADVAELLGVdpEEI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 502993053 713 GVDDDFFELGGHSLVAADLLGQLQQDfGVELPARTFYLSPTIAELAEL 760
Cdd:COG3433 240 DPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWAL 286
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
690-760 |
1.90e-15 |
|
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: 71.81 E-value: 1.90e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502993053 690 APEDALERFLCELWAKVLMVD--SVGVDDDFF-ELGGHSLVAADLLGQLQQDFGVELPARTFYLSPTIAELAEL 760
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDpeEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADY 74
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
697-756 |
1.95e-15 |
|
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: 71.06 E-value: 1.95e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502993053 697 RFLCELWAKVLMVD--SVGVDDDFFELGGHSLVAADLLGQLQQDFGVELPARTFYLSPTIAE 756
Cdd:pfam00550 1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
320-675 |
2.20e-15 |
|
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: 79.57 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 320 DLSPGTLAYVSYTSGSTGTPKGVCVPHR-------AVSRLVhePDWLdaGPDDVFLQAAPIA----FDASTLeiwaSLSA 388
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTHGnlvagiaGLGDRV--PELL--GPDDRYLAYLPLAhifeLAAENV----CLYR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 389 GAR--------------------LVLLPP----------GRVDPAELGAVVAAEGV--TVLWL-------------TAGL 423
Cdd:cd17639 156 GGTigygsprtltdkskrgckgdLTEFKPtlmvgvpaiwDTIRKGVLAKLNPMGGLkrTLFWTayqsklkalkegpGTPL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 424 FHQLVDHHLDRLAG--VRHLIAGGDVISPDAVRRLLAAHPDLVftNGYGPTEnttftTCAtfGGPAARPGEAGPLPIGRP 501
Cdd:cd17639 236 LDELVFKKVRAALGgrLRYMLSGGAPLSADTQEFLNIVLCPVI--QGYGLTE-----TCA--GGTVQDPGDLETGRVGPP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 502 IRGTRVRVLD--RLG----RPVPPG--VVGdlyalGEGLALGYLGRPAVTAAVFTpaggGERQYRTGDLARWRTDGSLDF 573
Cdd:cd17639 307 LPCCEIKLVDweEGGystdKPPPRGeiLIR-----GPNVFKGYYKNPEKTKEAFD----GDGWFHTGDIGEFHPDGTLKI 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 574 LGRADDQVKIK-GYRVEPAEVAAALGAHPAV-----------TAAVALPEPGAGGSTRLAAYVVFADGD------RPGVP 635
Cdd:cd17639 378 IDRKKDLVKLQnGEYIALEKLESIYRSNPLVnnicvyadpdkSYPVAIVVPNEKHLTKLAEKHGVINSEweelceDKKLQ 457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 502993053 636 APALRDwLRE-----RLPEFLVPARIVALDaFPLTP-NG------KLDREAL 675
Cdd:cd17639 458 KAVLKS-LAEtaraaGLEKFEIPQGVVLLD-EEWTPeNGlvtaaqKLKRKEI 507
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
553-676 |
3.29e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 78.54 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 553 GERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVAL--PEPGAGgsTRLAAYVVfadgD 630
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgKDPVAG--ERVKAKVI----S 362
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 502993053 631 RPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALP 676
Cdd:PRK08308 363 HEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
299-670 |
6.02e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 78.59 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 299 GDHALPPLDANrraateplpgdlspgTLAYVSYTSGSTGTPKGVCVPHRavSRLVHE-----PDWLDAGPDDVFLQAAPI 373
Cdd:PRK07008 166 GDYDWPRFDEN---------------QASSLCYTSGTTGNPKGALYSHR--STVLHAygaalPDAMGLSARDAVLPVVPM 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 374 aFDASTLEI-WASLSAGARLVlLPPGRVDPAELGAVVAAEGVT------VLWLtaGLFHQLVDHHLdRLAGVRHLIAGGD 446
Cdd:PRK07008 229 -FHVNAWGLpYSAPLTGAKLV-LPGPDLDGKSLYELIEAERVTfsagvpTVWL--GLLNHMREAGL-RFSTLRRTVIGGS 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 447 VISPDAVRRLLAAHpDLVFTNGYGPTENTTF-TTCATFGGPAARPGEAGP---LPIGRPIRGTRVRVLDRLGRPVP-PGV 521
Cdd:PRK07008 304 ACPPAMIRTFEDEY-GVEVIHAWGMTEMSPLgTLCKLKWKHSQLPLDEQRkllEKQGRVIYGVDMKIVGDDGRELPwDGK 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 522 V-GDLYALGEGLALGYLGRPAvtaavfTPAGGGerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAH 600
Cdd:PRK07008 383 AfGDLQVRGPWVIDRYFRGDA------SPLVDG--WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAH 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 601 PAV--TAAVALPEPGAGGSTRLAayVVfadgDRPGVpapalrDWLRERLPEFL--------VPARIVALDAFPLTPNGKL 670
Cdd:PRK07008 455 PAVaeAACIACAHPKWDERPLLV--VV----KRPGA------EVTREELLAFYegkvakwwIPDDVVFVDAIPHTATGKL 522
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
310-571 |
3.25e-14 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 76.10 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 310 RRAATEPLPGDlsPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHEPDWL-----DAGPDDVFLQAAPIA--FDAstLEI 382
Cdd:cd05927 102 KKNKVPPPPPK--PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKIleilnKINPTDVYISYLPLAhiFER--VVE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 383 WASLSAGARL--------VLLP----------PG------RVDPAELGAVVAAEGVT-----------VLWLTAG----- 422
Cdd:cd05927 178 ALFLYHGAKIgfysgdirLLLDdikalkptvfPGvprvlnRIYDKIFNKVQAKGPLKrklfnfalnykLAELRSGvvras 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 423 -LFHQLVDHHLDRLAG--VRHLIAGGDVISPDAVRRLLAAhPDLVFTNGYGPTEnttfTTCATFggpAARPGEAGPLPIG 499
Cdd:cd05927 258 pFWDKLVFNKIKQALGgnVRLMLTGSAPLSPEVLEFLRVA-LGCPVLEGYGQTE----CTAGAT---LTLPGDTSVGHVG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 500 RPIRGTRVRVLDrlgrpVP--------PGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSL 571
Cdd:cd05927 330 GPLPCAEVKLVD-----VPemnydakdPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDG----WLHTGDIGEWLPNGTL 400
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
301-680 |
4.72e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 75.68 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 301 HALPPLDanrraateplpgdLSPGTLAYVSYTSGSTGTPKGVCVPHR-AVSRLVHEPDWLDAGPD-----DVFLQAAPI- 373
Cdd:PRK08751 198 HSMPTLQ-------------IEPDDIAFLQYTGGTTGVAKGAMLTHRnLVANMQQAHQWLAGTGKleegcEVVITALPLy 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 374 ---AFDASTLeIWASLSAGARLVLLP---PGRVDPAELGAVVAAEGVTVLWltAGLFHQLVDHHLDrLAGVRHLIAGGdv 447
Cdd:PRK08751 265 hifALTANGL-VFMKIGGCNHLISNPrdmPGFVKELKKTRFTAFTGVNTLF--NGLLNTPGFDQID-FSSLKMTLGGG-- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 448 ispDAVRRLLAAH----PDLVFTNGYGPTEnttfTTCATFGGPAARPGEAGplPIGRPIRGTRVRVLDRLGRPVPPGVVG 523
Cdd:PRK08751 339 ---MAVQRSVAERwkqvTGLTLVEAYGLTE----TSPAACINPLTLKEYNG--SIGLPIPSTDACIKDDAGTVLAIGEIG 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 524 DLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV 603
Cdd:PRK08751 410 ELCIKGPQVMKGYWKRPEETAKVMDADG----WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGV 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502993053 604 --TAAVALPEPGAGGSTRlaayVVFADGDrPGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAA 680
Cdd:PRK08751 486 leVAAVGVPDEKSGEIVK----VVIVKKD-PALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
186-675 |
5.00e-14 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 75.65 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 186 RAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRGDRtaVPFDAT 265
Cdd:PLN02574 86 VMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLG--VPVIGV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 266 PTAATEpRSGERTTGPLDAAAPEAAEPQPGPVLGDHalpplDAnrraateplpgdlspgtlAYVSYTSGSTGTPKGVCVP 345
Cdd:PLN02574 164 PENYDF-DSKRIEFPKFYELIKEDFDFVPKPVIKQD-----DV------------------AAIMYSSGTTGASKGVVLT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 346 HRAVSRLVH------EPDWLDAGPDDVFLQAAPIaFDASTLEIWAS--LSAGARLVLLPpgRVDPAELGAVVAAEGVT-- 415
Cdd:PLN02574 220 HRNLIAMVElfvrfeASQYEYPGSDNVYLAALPM-FHIYGLSLFVVglLSLGSTIVVMR--RFDASDMVKVIDRFKVThf 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 416 --VLWLTAGLFHQLVDHHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTTFTTCATFGGPAARPGEA 493
Cdd:PLN02574 297 pvVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYSSV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 494 GPLPigrpiRGTRVRVLD-RLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLD 572
Cdd:PLN02574 377 GLLA-----PNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDG----WLRTGDIAYFDEDGYLY 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 573 FLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFADGDrpGVPAPALRDWLRERLPEFLV 652
Cdd:PLN02574 448 IVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGS--TLSQEAVINYVAKQVAPYKK 525
|
490 500
....*....|....*....|...
gi 502993053 653 PARIVALDAFPLTPNGKLDREAL 675
Cdd:PLN02574 526 VRKVVFVQSIPKSPAGKILRREL 548
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
329-675 |
7.05e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 75.06 E-value: 7.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 329 VSYTSGSTGTPKGVCVPHRA--VSRLVHEPDWlDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLPpgRVDPAELG 406
Cdd:PLN03102 191 LNYTSGTTADPKGVVISHRGayLSTLSAIIGW-EMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMR--HVTAPEIY 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 407 AVVAAEGVTVLWLTAGLFHQLVDHH---LDRLAGVRHLIAGGDviSPDAVrrLLAAHPDLVF--TNGYGPTENTtfttca 481
Cdd:PLN03102 268 KNIEMHNVTHMCCVPTVFNILLKGNsldLSPRSGPVHVLTGGS--PPPAA--LVKKVQRLGFqvMHAYGLTEAT------ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 482 tfgGP---AARPGEAGPLPIGRPI-----RGTRVRVLDRL---------GRPVPPGVVGDLYALGEGLALGYLGRPAVTA 544
Cdd:PLN03102 338 ---GPvlfCEWQDEWNRLPENQQMelkarQGVSILGLADVdvknketqeSVPRDGKTMGEIVIKGSSIMKGYLKNPKATS 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 545 AVFTPAgggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGSTrlAA 622
Cdd:PLN03102 415 EAFKHG-----WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVleTAVVAMPHPTWGETP--CA 487
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502993053 623 YVVFADGDRPGVPAPA--------LRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PLN03102 488 FVVLEKGETTKEDRVDklvtrerdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
325-653 |
7.57e-14 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 74.70 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 325 TLAYVSYTSGSTGTPKGVCVPH-RAVSRLVHEPDWLDAGPDDVFLQAAPIAFD-ASTLEIWASLSAGARLVLlppGRVDP 402
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHrRAWRGGAFFAGSGGALPSDVLYTCLPLYHStALIVGWSACLASGATLVI---RKKFS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 403 A-ELGAVVAAEGVTVLWLTAGLFHQLVD---HHLDRLAGVRHLIAGGdvISPDAVRRLLAAHPDLVFTNGYGPTE-NTTF 477
Cdd:cd05940 159 AsNFWDDIRKYQATIFQYIGELCRYLLNqppKPTERKHKVRMIFGNG--LRPDIWEEFKERFGVPRIAEFYAATEgNSGF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 478 TTCATFGGPAARPG----EAGPLPI-------GRPIRGTRVRVldrlgRPVPPGVVGDLyaLGEGLAL----GYLGRPAV 542
Cdd:cd05940 237 INFFGKPGAIGRNPsllrKVAPLALvkydlesGEPIRDAEGRC-----IKVPRGEPGLL--ISRINPLepfdGYTDPAAT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 543 TAAVFTPA-GGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAV--ALPEPGAGGSTR 619
Cdd:cd05940 310 EKKILRDVfKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANvyGVQVPGTDGRAG 389
|
330 340 350
....*....|....*....|....*....|....
gi 502993053 620 LAAYVVFADGDRPGvpaPALRDWLRERLPEFLVP 653
Cdd:cd05940 390 MAAIVLQPNEEFDL---SALAAHLEKNLPGYARP 420
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
184-624 |
1.35e-13 |
|
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: 74.38 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 184 LVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQ--------VAGRVRG 255
Cdd:cd17641 28 LLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDEeqvdklleIADRIPS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 256 DRTAVPFDatptaatePRSGERTTGPL-----DAAAPEAAEPQPGPVLGDHALppldanrrAATeplpgdlSPGTLAYVS 330
Cdd:cd17641 108 VRYVIYCD--------PRGMRKYDDPRlisfeDVVALGRALDRRDPGLYEREV--------AAG-------KGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 331 YTSGSTGTPKGVCVPHRAVSRlvHEPDWLDA---GPDDVFLQAAPIAF----------------------DASTL----- 380
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFLG--HCAAYLAAdplGPGDEYVSVLPLPWigeqmysvgqalvcgfivnfpeEPETMmedlr 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 381 EIwaslsaGARLVLLPP-----------------GRVDPA--ELGAVVAAEGV----------TVLWLTAGLFHQLVDHH 431
Cdd:cd17641 243 EI------GPTFVLLPPrvwegiaadvrarmmdaTPFKRFmfELGMKLGLRALdrgkrgrpvsLWLRLASWLADALLFRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 432 L-DRL--AGVRHLIAGGDVISPDAVRRLLAAHPDLvfTNGYGPTENTTFTTcatfggpAARPGEAGPLPIGRPIRGTRVR 508
Cdd:cd17641 317 LrDRLgfSRLRSAATGGAALGPDTFRFFHAIGVPL--KQLYGQTELAGAYT-------VHRDGDVDPDTVGVPFPGTEVR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 509 VLDrlgrpvppgvVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKI-KGYR 587
Cdd:cd17641 388 IDE----------VGEILVRSPGVFVGYYKNPEATAEDFDEDG----WLHTGDAGYFKENGHLVVIDRAKDVGTTsDGTR 453
|
490 500 510
....*....|....*....|....*....|....*..
gi 502993053 588 VEPAEVAAALGAHPAVTAAVALpepgAGGSTRLAAYV 624
Cdd:cd17641 454 FSPQFIENKLKFSPYIAEAVVL----GAGRPYLTAFI 486
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
138-675 |
1.62e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 73.86 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 138 PAPARL-VHDLVDERARLAPDAPALTAA--GKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSA--GLIAglLAV 212
Cdd:PLN02330 23 PVPDKLtLPDFVLQDAELYADKVAFVEAvtGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAeyGIVA--LGI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 213 LKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRGdrtavpfdatptaateprsgerttgpldaaapeaaEP 292
Cdd:PLN02330 101 MAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKG-----------------------------------LG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 293 QPGPVLGDHALPP-------LDANRRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHR-AVSRLVHEpdWLDAGPD 364
Cdd:PLN02330 146 LPVIVLGEEKIEGavnwkelLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRnLVANLCSS--LFSVGPE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 365 DV----FLQAAPIAFDASTLEI-WASLSAGARLVLLppGRVD-PAELGAVVAAEgVTVLWLTAGLFHQLV------DHHL 432
Cdd:PLN02330 224 MIgqvvTLGLIPFFHIYGITGIcCATLRNKGKVVVM--SRFElRTFLNALITQE-VSFAPIVPPIILNLVknpiveEFDL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 433 DRLAgVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGYGPTENTTFTTcaTFGGPAARPGEAGPLPIGRPIRGTRVRVLD- 511
Cdd:PLN02330 301 SKLK-LQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITL--THGDPEKGHGIAKKNSVGFILPNLEVKFIDp 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 512 RLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPA 591
Cdd:PLN02330 378 DTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDG----WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 592 EVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVF------ADGDRPGVPAPALRDWLRERLPEFlvparivaLDAFPLT 665
Cdd:PLN02330 454 ELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVInpkakeSEEDILNFVAANVAHYKKVRVVQF--------VDSIPKS 525
|
570
....*....|
gi 502993053 666 PNGKLDREAL 675
Cdd:PLN02330 526 LSGKIMRRLL 535
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
312-675 |
2.24e-13 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 73.50 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 312 AATEPLpgdlspgtlaYVSYTSGSTGTPKGV-------CVPHRAVSRLVHepdwlDAGPDDVFLQAAPIAFDAS-TLEIW 383
Cdd:cd05967 228 AATDPL----------YILYTSGTTGKPKGVvrdngghAVALNWSMRNIY-----GIKPGDVWWAASDVGWVVGhSYIVY 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 384 ASLSAGARLVL---LPPGRVDPAELGAVVAAEGVTVLWL--TA----------GLFHQLVDhhldrLAGVRHLIAGGDVI 448
Cdd:cd05967 293 GPLLHGATTVLyegKPVGTPDPGAFWRVIEKYQVNALFTapTAirairkedpdGKYIKKYD-----LSSLRTLFLAGERL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 449 SPDAVRRLLAAHPDLVFTNgYGPTEN--TTFTTCATFGGPAARPGEAGplpigRPIRGTRVRVLDRLGRPVPPGVVGDL- 525
Cdd:cd05967 368 DPPTLEWAENTLGVPVIDH-WWQTETgwPITANPVGLEPLPIKAGSPG-----KPVPGYQVQVLDEDGEPVGPNELGNIv 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 526 --YALGEGLALG-YLGRPAVTAAVFTPAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPA 602
Cdd:cd05967 442 ikLPLPPGCLLTlWKNDERFKKLYLSKFPG---YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPA 518
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993053 603 VT--AAVALPEPGAGgsTRLAAYVVFADGDRPGVPA--PALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:cd05967 519 VAecAVVGVRDELKG--QVPLGLVVLKEGVKITAEEleKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
326-672 |
2.54e-13 |
|
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: 72.86 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 326 LAYVSYTSGSTGTPKGVCVPHRavsRLVHEPDWLDA----GPDDVFL------QAAPIAFDASTleiwaSLSAGARLVLL 395
Cdd:cd05914 91 VALINYTSGTTGNSKGVMLTYR---NIVSNVDGVKEvvllGKGDKILsilplhHIYPLTFTLLL-----PLLNGAHVVFL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 396 ---PPGRVDPAELGAVVAAEGVTVLW---------------LTAGLF------------HQLVDHHLDRLAG-VRHLIAG 444
Cdd:cd05914 163 dkiPSAKIIALAFAQVTPTLGVPVPLviekifkmdiipkltLKKFKFklakkinnrkirKLAFKKVHEAFGGnIKEFVIG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 445 GDVISPDAVRRLLAAhpDLVFTNGYGPTENTTFTTcatfggpAARPGEAGPLPIGRPIRGTRVRVLDrlgrPVPPGVVGD 524
Cdd:cd05914 243 GAKINPDVEEFLRTI--GFPYTIGYGMTETAPIIS-------YSPPNRIRLGSAGKVIDGVEVRIDS----PDPATGEGE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 525 LYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQ-VKIKGYRVEPAEVAAALGAHPAV 603
Cdd:cd05914 310 IIVRGPNVMKGYYKNPEATAEAFDKDG----WFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 604 -TAAVALPEpgagGSTRLAAYVVFADGDRPGVPAP--------ALRDWLRERLPEF--LVPARIVALDaFPLTPNGKLDR 672
Cdd:cd05914 386 lESLVVVQE----KKLVALAYIDPDFLDVKALKQRniidaikwEVRDKVNQKVPNYkkISKVKIVKEE-FEKTPKGKIKR 460
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
152-675 |
2.60e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 72.98 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 152 ARLAPDAPALTAAGKTVPYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARL 231
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 232 TGLLDDAGVRIVLADaqvagrvrgdrtavpfdatptaateprSGERTTGPLDAAapeaaepQPGPVLGDHALPPldanrr 311
Cdd:PRK09029 93 EELLPSLTLDFALVL---------------------------EGENTFSALTSL-------HLQLVEGAHAVAW------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 312 aateplpgdlSPGTLAYVSYTSGSTGTPKGV---CVPHRAVSRLVHEpdWLDAGPDDVFLQAAPIaFDASTLEI-WASLS 387
Cdd:PRK09029 133 ----------QPQRLATMTLTSGSTGLPKAAvhtAQAHLASAEGVLS--LMPFTAQDSWLLSLPL-FHVSGQGIvWRWLY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 388 AGARLVLlppgrvdPAELGAVVAAEGVTVLWLTAGLFHQLVDHHLDRLAgVRHLIAGGDVIsPDAVRRLLAAHPDLVFTn 467
Cdd:PRK09029 200 AGATLVV-------RDKQPLEQALAGCTHASLVPTQLWRLLDNRSEPLS-LKAVLLGGAAI-PVELTEQAEQQGIRCWC- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 468 GYGPTENTTfTTCATfggpaarpgEAGPLP-IGRPIRGTRVRVLDrlgrpvppgvvGDLYALGEGLALGYL--GRPavta 544
Cdd:PRK09029 270 GYGLTEMAS-TVCAK---------RADGLAgVGSPLPGREVKLVD-----------GEIWLRGASLALGYWrqGQL---- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 545 avfTPAGGGERQYRTGDLARWRtDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYV 624
Cdd:PRK09029 325 ---VPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 502993053 625 VFADgdrpGVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK09029 401 ESDS----EAAVVNLAEWLQDKLARFQQPVAYYLLPPELKNGGIKISRQAL 447
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
312-629 |
2.72e-13 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 73.09 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 312 AATEPLPG-DLSPGTLAYVSYTSGSTGTPKGVCVPHR----AVSRLV--HEPDwLDAGPDDVFLQAAPIaFDASTLE--I 382
Cdd:PLN02246 166 ADENELPEvEISPDDVVALPYSSGTTGLPKGVMLTHKglvtSVAQQVdgENPN-LYFHSDDVILCVLPM-FHIYSLNsvL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 383 WASLSAGARLVLLPpgRVDPAELGAVVAAEGVTVLWLTAGLFHQL-----VDHHldRLAGVRHLIAGGdviSP------D 451
Cdd:PLN02246 244 LCGLRVGAAILIMP--KFEIGALLELIQRHKVTIAPFVPPIVLAIakspvVEKY--DLSSIRMVLSGA---APlgkeleD 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 452 AVRRLLaahPDLVFTNGYGPTE-NTTFTTCATFggpAARPGEAGPLPIGRPIRGTRVRVLD-RLGRPVPPGVVGDLYALG 529
Cdd:PLN02246 317 AFRAKL---PNAVLGQGYGMTEaGPVLAMCLAF---AKEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRG 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 530 EGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT--AAV 607
Cdd:PLN02246 391 PQIMKGYLNDPEATANTIDKDG----WLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIAdaAVV 466
|
330 340
....*....|....*....|..
gi 502993053 608 ALPEPGAGGSTrlAAYVVFADG 629
Cdd:PLN02246 467 PMKDEVAGEVP--VAFVVRSNG 486
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
330-687 |
4.57e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 72.29 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 330 SYTSGSTGTPKGVCVPHR-----AVSRLVHepdWlDAGPDDVFLQAAPI------AFDastleiWASLSAGARLVLLPpg 398
Cdd:PRK08162 188 NYTSGTTGNPKGVVYHHRgaylnALSNILA---W-GMPKHPVYLWTLPMfhcngwCFP------WTVAARAGTNVCLR-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 399 RVDPAELGAVVAAEGVTVLwLTAGLFHQ-LVDHHLDRLAGVRH----LIAGGDviSPDAVrrlLAAHPDLVF--TNGYGP 471
Cdd:PRK08162 256 KVDPKLIFDLIREHGVTHY-CGAPIVLSaLINAPAEWRAGIDHpvhaMVAGAA--PPAAV---IAKMEEIGFdlTHVYGL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 472 TEntTFttcatfgGPA---ARPGEAGPLPIGRPIR-----GTR------VRVLDR-LGRPVPPG--VVGDLYALGEGLAL 534
Cdd:PRK08162 330 TE--TY-------GPAtvcAWQPEWDALPLDERAQlkarqGVRyplqegVTVLDPdTMQPVPADgeTIGEIMFRGNIVMK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 535 GYLGRPAVTAAVFtpAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAA--VALPEP 612
Cdd:PRK08162 401 GYLKNPKATEEAF--AGG---WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAavVAKPDP 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502993053 613 GAGGSTrlAAYVVFADGdrPGVPAPALRDWLRERLPEFLVPARIVaLDAFPLTPNGKLDREALPGSAAEEGALDE 687
Cdd:PRK08162 476 KWGEVP--CAFVELKDG--ASATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVLREQAKSLKAIDL 545
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
188-675 |
6.12e-13 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 72.12 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 188 GVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGR----------VRGDR 257
Cdd:PRK05620 60 GITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQlgeilkecpcVRAVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 258 TAVPFDATPTAATEPRSGErttgpldaaapeaaepqpgpVLGDHALppLDAnrRAATEPLPgDLSPGTLAYVSYTSGSTG 337
Cdd:PRK05620 140 FIGPSDADSAAAHMPEGIK--------------------VYSYEAL--LDG--RSTVYDWP-ELDETTAAAICYSTGTTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 338 TPKGVCVPHRAV---SRLVHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLlpPGR-VDPAELGAVVA--- 410
Cdd:PRK05620 195 APKGVVYSHRSLylqSLSLRTTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVF--PGPdLSAPTLAKIIAtam 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 411 ---AEGVTVLWLtaGLFHQLVDHHLDRLAgVRHLIAGGDVISPdAVRRLLAAHPDLVFTNGYGPTENTTFTTCATfgGPA 487
Cdd:PRK05620 273 prvAHGVPTLWI--QLMVHYLKNPPERMS-LQEIYVGGSAVPP-ILIKAWEERYGVDVVHVWGMTETSPVGTVAR--PPS 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 488 ARPGEA--------GPLPIGRPIR----GTRVRVLDRLGRPVP---PGVVGDLY----ALGEGLALGYLGRPAVTAA-VF 547
Cdd:PRK05620 347 GVSGEArwayrvsqGRFPASLEYRivndGQVMESTDRNEGEIQvrgNWVTASYYhsptEEGGGAASTFRGEDVEDANdRF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 548 TPAGggerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVVFA 627
Cdd:PRK05620 427 TADG----WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLA 502
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502993053 628 DGDRPGV-PAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK05620 503 PGIEPTReTAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
189-674 |
7.04e-13 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 72.08 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 189 VRPGEVVGVLGDRSAGLIAGLLAVLKAGGayLALP---PDWPD--ARLTGLLDDAGVRIVLADAQVAGRVRGdrtavpFD 263
Cdd:PRK12476 89 AGPGDRVAILAPQGIDYVAGFFAAIKAGT--IAVPlfaPELPGhaERLDTALRDAEPTVVLTTTAAAEAVEG------FL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 264 ATPTAATEPRsgerttgpldaaapeaaepqpgpVLGDHALPPldanrRAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVC 343
Cdd:PRK12476 161 RNLPRLRRPR-----------------------VIAIDAIPD-----SAGESFVPVELDTDDVSHLQYTSGSTRPPVGVE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 344 VPHRAVS----RLVHEPDWLDAGPDDVflQAAPIAFDASTLEIWASLSAGARLVLLP-------PGR-----VDPAELGA 407
Cdd:PRK12476 213 ITHRAVGtnlvQMILSIDLLDRNTHGV--SWLPLYHDMGLSMIGFPAVYGGHSTLMSptafvrrPQRwikalSEGSRTGR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 408 VVAAEGVTVLWLTA--GLFHQLVDHHLDRLAgvrhLIAGGDVISPDAVRRLLAAH-----PDLVFTNGYGPTENTTFTtc 480
Cdd:PRK12476 291 VVTAAPNFAYEWAAqrGLPAEGDDIDLSNVV----LIIGSEPVSIDAVTTFNKAFapyglPRTAFKPSYGIAEATLFV-- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 481 ATFgGPAARP------------GEAGPLP-----------IGRPIRGT-RVRVLDRLGRPVPPGVVGDLYALGEGLALGY 536
Cdd:PRK12476 365 ATI-APDAEPsvvyldreqlgaGRAVRVAadapnavahvsCGQVARSQwAVIVDPDTGAELPDGEVGEIWLHGDNIGRGY 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 537 LGRPAVTAAVF-------TPAGG-------GERQYRTGDLARWRtDGSLDFLGRADDQVKIKGYRVEPAEVAAALG-AHP 601
Cdd:PRK12476 444 WGRPEETERTFgaklqsrLAEGShadgaadDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAeASP 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 602 AV----TAAVALPepgAGGSTRLAAYVVFADGDRPGVPAP---ALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREA 674
Cdd:PRK12476 523 MVrrgyVTAFTVP---AEDNERLVIVAERAAGTSRADPAPaidAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRA 599
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
183-674 |
1.36e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 70.80 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 183 RLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAgrVRGDrtavPF 262
Cdd:PRK07768 45 GLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLRVIGMIGAKAV--VVGE----PF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 263 DATptaateprsgerttgpldaaapeaaepqpGPVLGDHALPPLDANRRAATEPL-PGDLSPGTLAYVSYTSGSTGTPKG 341
Cdd:PRK07768 119 LAA-----------------------------APVLEEKGIRVLTVADLLAADPIdPVETGEDDLALMQLTSGSTGSPKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 342 VCVPHR--------AVSRLVHEPDwldagpDDVFLQAAPIAFDASTLEIWAS-LSAGARLVLLPPGR--VDP---AEL-- 405
Cdd:PRK07768 170 VQITHGnlyanaeaMFVAAEFDVE------TDVMVSWLPLFHDMGMVGFLTVpMYFGAELVKVTPMDflRDPllwAELis 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 406 ---GAVVAAEGVTVLWLTAGLFHQLVDHHLDrLAGVRHLIAGGDVISPDAVRRLLAA------HPDlVFTNGYGPTENTT 476
Cdd:PRK07768 244 kyrGTMTAAPNFAYALLARRLRRQAKPGAFD-LSSLRFALNGAEPIDPADVEDLLDAgarfglRPE-AILPAYGMAEATL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 477 FTTCATFGGPA---------------ARPGEAGPL----PIGRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYL 537
Cdd:PRK07768 322 AVSFSPCGAGLvvdevdadllaalrrAVPATKGNTrrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 538 grpavTAAVFTPAGGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTA--AVALPEPGAG 615
Cdd:PRK07768 402 -----TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPgnAVAVRLDAGH 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502993053 616 GSTRLAAYVVFADGDRPGVPAPALRDWLRERLPEFLVPARIVAL---DAFPLTPNGKLDREA 674
Cdd:PRK07768 477 SREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVlgpGSIPKTPSGKLRRAN 538
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
319-675 |
2.09e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 70.17 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 319 GDLSPGTLAYVSYTSGSTGTPKGVCVPHRavSRLVH-----EPDWLDAGPDDVFLQAAPIaFDASTLEI-WASLSAGARL 392
Cdd:PRK06018 172 KTFDENTAAGMCYTSGTTGDPKGVLYSHR--SNVLHalmanNGDALGTSAADTMLPVVPL-FHANSWGIaFSAPSMGTKL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 393 VlLPPGRVDPAELGAVVAAEGVTV------LWLtagLFHQLVDHHLDRLAGVRHLIAGGDVISpdavRRLLAAHPDL--- 463
Cdd:PRK06018 249 V-MPGAKLDGASVYELLDTEKVTFtagvptVWL---MLLQYMEKEGLKLPHLKMVVCGGSAMP----RSMIKAFEDMgve 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 464 VFtNGYGPTENTTFTTCATFGGPAAR-PGEAG---PLPIGRPIRGTRVRVLDRLGRPVPpgvvgdlyalGEGLALGYL-- 537
Cdd:PRK06018 321 VR-HAWGMTEMSPLGTLAALKPPFSKlPGDARldvLQKQGYPPFGVEMKITDDAGKELP----------WDGKTFGRLkv 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 538 GRPAVTAAVFTPAG---GGERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGA 614
Cdd:PRK06018 390 RGPAVAAAYYRVDGeilDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHP 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502993053 615 GGSTRLAAYVVFADGDRPgVPAPALrDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK06018 470 KWDERPLLIVQLKPGETA-TREEIL-KYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
302-675 |
3.58e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 68.53 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 302 ALPPLDANRRAATEPLPGDLSPG-----TLAYVSYTSGSTGTPKGVCVPHRAV--------SRLVHEPDWLDAGPddvfl 368
Cdd:PRK07824 8 ALLPVPAQDERRAALLRDALRVGepiddDVALVVATSGTTGTPKGAMLTAAALtasadathDRLGGPGQWLLALP----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 369 qAAPIAFDASTLEiwaSLSAGAR-LVLLPPGRVDPAELGAVVAAEGVTVLWltAGLFHQLVDHHLDRLAGVRHL------ 441
Cdd:PRK07824 83 -AHHIAGLQVLVR---SVIAGSEpVELDVSAGFDPTALPRAVAELGGGRRY--TSLVPMQLAKALDDPAATAALaeldav 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 442 IAGGDVISPDAVRRLLAAHPDLVFTngYGPTEnttftTCAtfggpaarpgeaGPLPIGRPIRGTRVRVLDrlgrpvppgv 521
Cdd:PRK07824 157 LVGGGPAPAPVLDAAAAAGINVVRT--YGMSE-----TSG------------GCVYDGVPLDGVRVRVED---------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 522 vGDLYALGEGLALGYlgRPAVTAAVFTPAGggerQYRTGDLARWrTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHP 601
Cdd:PRK07824 208 -GRIALGGPTLAKGY--RNPVDPDPFAEPG----WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHP 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502993053 602 AVTAA--VALPEPGAGgsTRLAAYVVFADGDRPGVpaPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK07824 280 AVADCavFGLPDDRLG--QRVVAAVVGDGGPAPTL--EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
498-669 |
2.91e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 66.76 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 498 IGRPIRGTRVRVLD-RLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLGR 576
Cdd:PRK08315 373 VGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADG----WMHTGDLAVMDEEGYVNIVGR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 577 ADDQVkIKG----YrvePAEVAAALGAHPAVTAA--VALPEPGAGgsTRLAAYVVFadgdRPGVPAPA--LRDWLRERLP 648
Cdd:PRK08315 449 IKDMI-IRGgeniY---PREIEEFLYTHPKIQDVqvVGVPDEKYG--EEVCAWIIL----RPGATLTEedVRDFCRGKIA 518
|
170 180
....*....|....*....|.
gi 502993053 649 EFLVPARIVALDAFPLTPNGK 669
Cdd:PRK08315 519 HYKIPRYIRFVDEFPMTVTGK 539
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
169-672 |
6.14e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 65.80 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 169 PYRWLAEHAEALAARLVRAGVRPGEVVGVLGDRSAGLIAGLLAVLKAGG--AYLALPPDWPD-----ARLTGLLDDAGVR 241
Cdd:PRK09192 51 PYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLvpVPLPLPMGFGGresyiAQLRGMLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 242 IVLADAQVAGRVrgdrtavpfdatpTAATEprsgerttgpldaaapeaaePQPGPVLGDHALppLDAnRRAATEPLPgDL 321
Cdd:PRK09192 131 AIITPDELLPWV-------------NEATH--------------------GNPLLHVLSHAW--FKA-LPEADVALP-RP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 322 SPGTLAYVSYTSGSTGTPKGVCVPHRAV-SRLV-HEPDWLDAGPDDVFLQAAPIAFDAStleiwaslsagarLV--LLPP 397
Cdd:PRK09192 174 TPDDIAYLQYSSGSTRFPRGVIITHRALmANLRaISHDGLKVRPGDRCVSWLPFYHDMG-------------LVgfLLTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 398 grvdpaelgavvAAEGVTVLWLTAGLF----HQLVD-----------------------------HHLD----RLAGVrh 440
Cdd:PRK09192 241 ------------VATQLSVDYLPTRDFarrpLQWLDlisrnrgtisysppfgyelcarrvnskdlAELDlscwRVAGI-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 441 liaGGDVISPDAVRRLLAAHPDL-----VFTNGYGPTENTTFTTCATFGG---------------PAARPGEAGPLPI-- 498
Cdd:PRK09192 307 ---GADMIRPDVLHQFAEAFAPAgfddkAFMPSYGLAEATLAVSFSPLGSgivveevdrdrleyqGKAVAPGAETRRVrt 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 499 ----GRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPaVTAAVFTPAGggerQYRTGDLArWRTDGSLDFL 574
Cdd:PRK09192 384 fvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDE-ESQDVLAADG----WLDTGDLG-YLLDGYLYIT 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 575 GRADDQVKIKGYRVEPAEVAAALGAHPAV----TAAVALPEPGAGGSTRLAAYVVFADGDRpgvpaPALRDWLRERL-PE 649
Cdd:PRK09192 458 GRAKDLIIINGRNIWPQDIEWIAEQEPELrsgdAAAFSIAQENGEKIVLLVQCRISDEERR-----GQLIHALAALVrSE 532
|
570 580 590
....*....|....*....|....*....|
gi 502993053 650 F-------LVPARivaldAFPLTPNGKLDR 672
Cdd:PRK09192 533 FgveaaveLVPPH-----SLPRTSSGKLSR 557
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
592-669 |
1.83e-10 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 57.55 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 592 EVAAALGAHPAVT--AAVALPEPGAGgsTRLAAYVVFADGDRPgvPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGK 669
Cdd:pfam13193 1 EVESALVSHPAVAeaAVVGVPDELKG--EAPVAFVVLKPGVEL--LEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
323-686 |
3.71e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 63.58 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 323 PGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHEPDWL-DAGPDDVFLQAAPI--AFdASTLEIWASLSAGARLVLLPPG- 398
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIaDFTPNDRFMSALPLfhSF-GLTVGLFTPLLTGAEVFLYPSPl 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 399 --RVDPaELgavVAAEGVTVLWLTAG-LFHQLVDHHLDRLAGVRHLIAGGDVISpDAVRRLLAAHPDLVFTNGYGPTEnt 475
Cdd:PRK08043 443 hyRIVP-EL---VYDRNCTVLFGTSTfLGNYARFANPYDFARLRYVVAGAEKLQ-ESTKQLWQDKFGLRILEGYGVTE-- 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 476 tfttCA---TFGGP-AARPGEagplpIGRPIRGTRVRVLdrlgrPVpPGVV--GDLYALGEGLALGYL--GRPAVTAAVF 547
Cdd:PRK08043 516 ----CApvvSINVPmAAKPGT-----VGRILPGMDARLL-----SV-PGIEqgGRLQLKGPNIMNGYLrvEKPGVLEVPT 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 548 TPAGGGERQ---YRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAA-ALGAHP-AVTAAVALPEPGAGgstrlAA 622
Cdd:PRK08043 581 AENARGEMErgwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPdKQHATAIKSDASKG-----EA 655
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502993053 623 YVVFADGdrPGVPAPALRDWLRER-LPEFLVPARIVALDAFPLTPNGKLDREALPGSAAEEGALD 686
Cdd:PRK08043 656 LVLFTTD--SELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQHD 718
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
302-651 |
4.80e-10 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 62.87 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 302 ALPPLDANR--------RAATEPLPGDLSPGT--LAYVSYTSGSTGTPKGVCVPHR----AVSRLVHEpdwLDAGPDDVF 367
Cdd:cd05932 105 SLPPPSAANcqyqwddlIAQHPPLEERPTRFPeqLATLIYTSGTTGQPKGVMLTFGsfawAAQAGIEH---IGTEENDRM 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 368 LQAAPIAFDASTLEIW-ASLSAGARLVLlppgrvdPAELGAVVAAE---------GVTVLW--LTAGLFHQLVDHHLDRL 435
Cdd:cd05932 182 LSYLPLAHVTERVFVEgGSLYGGVLVAF-------AESLDTFVEDVqrarptlffSVPRLWtkFQQGVQDKIPQQKLNLL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 436 -------AGVRHLIAGGdvISPDAVRRLLAAH----PDLV---------FTNGYGPTENTTFTTcatfggpAARPGEAGP 495
Cdd:cd05932 255 lkipvvnSLVKRKVLKG--LGLDQCRLAGCGSapvpPALLewyrslglnILEAYGMTENFAYSH-------LNYPGRDKI 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 496 LPIGRPIRGTRVRVLDRlgrpvppgvvGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARWRTDGSLDFLG 575
Cdd:cd05932 326 GTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADG----FLRTGDKGELDADGNLTITG 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502993053 576 RADDQVKI-KGYRVEPAEVAAALGAHPAVTAAVALPEpgagGSTRLAAYVVFADGDRPGVPAPAlRDWLRERLPEFL 651
Cdd:cd05932 392 RVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGS----GLPAPLALVVLSEEARLRADAFA-RAELEASLRAHL 463
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
314-603 |
7.01e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 62.44 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 314 TEPLPGDL-SPGTLAYVSYTSGSTGTPKGVCVPHR-------AVSRLVhePDwldAGPDDVFLQAAPIAF------DAST 379
Cdd:PLN02387 239 ENPVDPDLpSPNDIAVIMYTSGSTGLPKGVMMTHGnivatvaGVMTVV--PK---LGKNDVYLAYLPLAHilelaaESVM 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 380 LEIWASLSAGARLVL-----------------LPP----------GRVDPAELGAVVAAEGVTVL--------------- 417
Cdd:PLN02387 314 AAVGAAIGYGSPLTLtdtsnkikkgtkgdasaLKPtlmtavpailDRVRDGVRKKVDAKGGLAKKlfdiaykrrlaaieg 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 418 -WLTAG-----LFHQLVDHHLDRLAG--VRHLIAGGDVISPDAVRrllaahpdlvFTN---------GYGPTEnttftTC 480
Cdd:PLN02387 394 sWFGAWgleklLWDALVFKKIRAVLGgrIRFMLSGGAPLSGDTQR----------FINiclgapigqGYGLTE-----TC 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 481 AtfGGPAARPGEAGPLPIGRPIRGTRVRVLD-------RLGRPVPPG--VVGdlyalGEGLALGYLGRPAVTAAVFTPAG 551
Cdd:PLN02387 459 A--GATFSEWDDTSVGRVGPPLPCCYVKLVSweeggylISDKPMPRGeiVIG-----GPSVTLGYFKNQEKTDEVYKVDE 531
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 502993053 552 GGERQYRTGDLARWRTDGSLDFLGRADDQVKIK-GYRVEPAEVAAALGAHPAV 603
Cdd:PLN02387 532 RGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYV 584
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
331-685 |
7.38e-10 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 62.17 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 331 YTSGSTGTPKGVCVPHRA--VSRLVHEPDW-LDAGPddVFLQAAPIAFDASTLEIWaSLSA--GARLVLLppgRVDPAEL 405
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGayLMALSNALIWgMNEGA--VYLWTLPMFHCNGWCFTW-TLAAlcGTNICLR---QVTAKAI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 406 GAVVAAEGVTVLWLTAGLFHQLVDHHLDR----LAGVRHLIAGGDVISPDavrrLLAAHPDLVF--TNGYGPTEntTF-- 477
Cdd:PLN02479 276 YSAIANYGVTHFCAAPVVLNTIVNAPKSEtilpLPRVVHVMTAGAAPPPS----VLFAMSEKGFrvTHTYGLSE--TYgp 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 478 -TTCATfggpaaRPgEAGPLPIGRPIR-----GTRVRVLDRL-------GRPVPP--GVVGDLYALGEGLALGYLGRPAV 542
Cdd:PLN02479 350 sTVCAW------KP-EWDSLPPEEQARlnarqGVRYIGLEGLdvvdtktMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKA 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 543 TAAVFtpAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAA--VALPEPGAGGSTrl 620
Cdd:PLN02479 423 NEEAF--ANG---WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEAsvVARPDERWGESP-- 495
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 621 AAYVVFADG-DRPGVPAPA--LRDWLRERLPEFLVPARIVaLDAFPLTPNGKLDREALPGSAAEEGAL 685
Cdd:PLN02479 496 CAFVTLKPGvDKSDEAALAedIMKFCRERLPAYWVPKSVV-FGPLPKTATGKIQKHVLRAKAKEMGPV 562
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
328-689 |
2.56e-09 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 60.68 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 328 YVSYTSGSTGTPKGVCvpHRAVSRLVHEPDWL----DAGPDDVFLQAAPIAF-DASTLEIWASLSAGARLVLLP--PGRV 400
Cdd:PLN02654 279 FLLYTSGSTGKPKGVL--HTTGGYMVYTATTFkyafDYKPTDVYWCTADCGWiTGHSYVTYGPMLNGATVLVFEgaPNYP 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 401 DPAELGAVVAAEGVTVLWLTAGLFHQLV---DHHLDRLA--GVRHLIAGGDVISPDAVRRLLAAHPD--LVFTNGYGPTE 473
Cdd:PLN02654 357 DSGRCWDIVDKYKVTIFYTAPTLVRSLMrdgDEYVTRHSrkSLRVLGSVGEPINPSAWRWFFNVVGDsrCPISDTWWQTE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 474 NTTFTTCATFGGPAARPGEAGplpigRPIRGTRVRVLDRLGRPVppgvvgdlyalgEGLALGYLGRPAVTAAVFTPAGGG 553
Cdd:PLN02654 437 TGGFMITPLPGAWPQKPGSAT-----FPFFGVQPVIVDEKGKEI------------EGECSGYLCVKKSWPGAFRTLYGD 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 554 ERQYRT------------GDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHP-AVTAAVALPEPGAGGSTrL 620
Cdd:PLN02654 500 HERYETtyfkpfagyyfsGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPqCAEAAVVGIEHEVKGQG-I 578
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502993053 621 AAYVVFADgdrpGVP-APALRDWL----RERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAEEgaLDENG 689
Cdd:PLN02654 579 YAFVTLVE----GVPySEELRKSLiltvRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQ--LDELG 646
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
692-759 |
3.39e-09 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 54.18 E-value: 3.39e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502993053 692 EDALERFLCELWAKVLMVDS---VGVDDDFFELGGHSLVAADLLGQLQQDFGVELPARTFYLSPTIAELAE 759
Cdd:smart00823 10 RRLLLDLVREQVAAVLGHAAaeaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAE 80
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
124-389 |
1.04e-08 |
|
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: 58.62 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 124 ADRALVAT--FEGGTAPAPARLVHDLVDERArlapdapaltaagkTVPYR-WLAEHAEALAARLVRAGVRPGEVVGVLGD 200
Cdd:cd17632 36 ADRPALGQraTELVTDPATGRTTLRLLPRFE--------------TITYAeLWERVGAVAAAHDPEQPVRPGDFVAVLGF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 201 RSAGLIAGLLAVLKAGGAYLALPPDWPDARLTGLLDDAGVRIVLADA-------QVAGRVRGDRTAVPFDATPTAATEPR 273
Cdd:cd17632 102 TSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAehldlavEAVLEGGTPPRLVVFDHRPEVDAHRA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 274 SGERTTGPLdaaapeaaEPQPGPVLGDHALPPLDANRRAAtEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLV 353
Cdd:cd17632 182 ALESARERL--------AAVGIPVTTLTLIAVRGRDLPPA-PLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFW 252
|
250 260 270
....*....|....*....|....*....|....*...
gi 502993053 354 HEPDWLDAG--PDDVFLQAAPIAFDASTLEIWASLSAG 389
Cdd:cd17632 253 LKVSSIQDIrpPASITLNFMPMSHIAGRISLYGTLARG 290
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
327-671 |
1.19e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 58.82 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 327 AYVSYTSGSTGTPKGVCVPHR--------AVSRLvhepdwlDAGPDDVFLQAAPI----AFDASTLeiwASLSAGARLVL 394
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRnllanraqVAARI-------DFSPEDKVFNALPVfhsfGLTGGLV---LPLLSGVKVFL 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 395 LPPG---RVDPAelgaVVAAEGVTVLWLT----AGlfHQLVDHHLDrLAGVRHLIAGGDVISpDAVRRLLAAHPDLVFTN 467
Cdd:PRK06814 866 YPSPlhyRIIPE----LIYDTNATILFGTdtflNG--YARYAHPYD-FRSLRYVFAGAEKVK-EETRQTWMEKFGIRILE 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 468 GYGPTENTTFTTCATfggPAA-RPGEagplpIGRPIRGTRVRVLdrlgrPVPpGVV--GDLYALGEGLALGYLgRPAVTA 544
Cdd:PRK06814 938 GYGVTETAPVIALNT---PMHnKAGT-----VGRLLPGIEYRLE-----PVP-GIDegGRLFVRGPNVMLGYL-RAENPG 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 545 AVFTPAGGgerQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEV-AAALGAHP-AVTAAVALPEPGAGgsTRLAA 622
Cdd:PRK06814 1003 VLEPPADG---WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVeELAAELWPdALHAAVSIPDARKG--ERIIL 1077
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 502993053 623 YVVFADGDRPgvpapALRDWLRER-LPEFLVPARIVALDAFPLTPNGKLD 671
Cdd:PRK06814 1078 LTTASDATRA-----AFLAHAKAAgASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
499-683 |
2.28e-08 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 57.44 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 499 GRPIRGTRVRVLDRLGRPVPPGVVGDLYALGEGLALGYLGRPAVTAA-----VFTPaggGERQYRTGDLARWRTDGSLDF 573
Cdd:cd05937 280 DDPIRDPKTGFCVRAPVGEPGEMLGRVPFKNREAFQGYLHNEDATESklvrdVFRK---GDIYFRTGDLLRQDADGRWYF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 574 LGRADDQVKIKGYRVEPAEVAAALGAHPAVTAA--VALPEPGAGGSTRLAAYVVfadGDRPGVPAP----ALRDWLRERL 647
Cdd:cd05937 357 LDRLGDTFRWKSENVSTTEVADVLGAHPDIAEAnvYGVKVPGHDGRAGCAAITL---EESSAVPTEftksLLASLARKNL 433
|
170 180 190
....*....|....*....|....*....|....*.
gi 502993053 648 PEFLVPARIVALDAFPLTPNGKLDREALpgsaAEEG 683
Cdd:cd05937 434 PSYAVPLFLRLTEEVATTDNHKQQKGVL----RDEG 465
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
138-675 |
2.55e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 57.38 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 138 PAPARLVHDLVDERARLapDAPALTAAGKTVPYRWLAEHAEALAARLvRAGVRPGEV--VGVLGDRSAGLIAGLLAVLKA 215
Cdd:PRK07867 1 TSSAPTVAELLLPLAED--DDRGLYFEDSFTSWREHIRGSAARAAAL-RARLDPTRPphVGVLLDNTPEFSLLLGAAALS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 216 GGAYLALPPDWPDARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPFDATPTAATEPRsgerttgpldaaapeaaepqpg 295
Cdd:PRK07867 78 GIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADE---------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 296 pvlgdhalppLDANRRAatEPLPGDLSPGTLAYVSYTSGSTGTPKGV-CVPHRAVSRLVHEPDWLDAGPDDVFLQAAPIA 374
Cdd:PRK07867 136 ----------LAAHRDA--EPPFRVADPDDLFMLIFTSGTSGDPKAVrCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 375 FDASTLEIWA-SLSAGARLVLlpPGRVDPAELGAVVAAEGVTVL-WLTAGLFHQLVDHHL--DRLAGVRhlIAGGDVISP 450
Cdd:PRK07867 204 HSNAVMAGWAvALAAGASIAL--RRKFSASGFLPDVRRYGATYAnYVGKPLSYVLATPERpdDADNPLR--IVYGNEGAP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 451 DAVRRlLAAHPDLVFTNGYGPTEnttfTTCATFGGPAARPGEAGPLPIGrpirgtrVRVLD-RLGRPVPPGVVGDLYALG 529
Cdd:PRK07867 280 GDIAR-FARRFGCVVVDGFGSTE----GGVAITRTPDTPPGALGPLPPG-------VAIVDpDTGTECPPAEDADGRLLN 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 530 EGLALGYL----GRPAVTAAVFTPAGGGER----QYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHP 601
Cdd:PRK07867 348 ADEAIGELvntaGPGGFEGYYNDPEADAERmrggVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYP 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502993053 602 AVTAAVALPEPGAGGSTRLAAYVVFADGdRPGVPApALRDWLRER--LPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK07867 428 DATEVAVYAVPDPVVGDQVMAALVLAPG-AKFDPD-AFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
196-585 |
4.31e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 56.49 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 196 GVLGDRSA-----GL--IAGLLAVLKAGGAYLALPPDWP---DARLTGLLDDAGVRIVLADAQVAGRVRGDRTAVPFDAT 265
Cdd:PRK05850 56 GSTGDRAVilapqGLeyIVAFLGALQAGLIAVPLSVPQGgahDERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 266 PTAAteprsgerttgpldaaapeaaepqpgpvlgdhALPPLDANRRAATEPLPGDLsPGTlAYVSYTSGSTGTPKGVCVP 345
Cdd:PRK05850 136 PPVI--------------------------------EVDLLDLDSPRGSDARPRDL-PST-AYLQYTSGSTRTPAGVMVS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 346 HRAV---------SRLVHEPDwlDAGPDDVFLQAAPIAFDAS-TLEIWASLSAGARLVLLPPgrvdpaelgavvaaegVT 415
Cdd:PRK05850 182 HRNVianfeqlmsDYFGDTGG--VPPPDTTVVSWLPFYHDMGlVLGVCAPILGGCPAVLTSP----------------VA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 416 VLWLTAGLFHQLVDHH-------------------------LDrLAGVRHLIAGGDVISPDAVRRLLA--AH---PDLVF 465
Cdd:PRK05850 244 FLQRPARWMQLLASNPhafsaapnfafelavrktsdddmagLD-LGGVLGIISGSERVHPATLKRFADrfAPfnlRETAI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 466 TNGYGPTENTTFTTCATFGGPA-ARPGEAGPLPIGRPIR-----GTR-----------VRVLD-RLGRPVPPGVVGDLYA 527
Cdd:PRK05850 323 RPSYGLAEATVYVATREPGQPPeSVRFDYEKLSAGHAKRcetggGTPlvsygsprsptVRIVDpDTCIECPAGTVGEIWV 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502993053 528 LGEGLALGYLGRPAVTAAVF-----TPAGGGERQ--YRTGDLArWRTDGSLDFLGRADDQVKIKG 585
Cdd:PRK05850 403 HGDNVAAGYWQKPEETERTFgatlvDPSPGTPEGpwLRTGDLG-FISEGELFIVGRIKDLLIVDG 466
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
484-672 |
8.85e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 55.53 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 484 GGPAARPGEAGplpigRPIRGTRVRVLDRLGRPVPPGVVGDLyALGE---GLALGYLGRPavtaavftpagggER----- 555
Cdd:PRK00174 417 GATPLKPGSAT-----RPLPGIQPAVVDEEGNPLEGGEGGNL-VIKDpwpGMMRTIYGDH-------------ERfvkty 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 556 ------QYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVALPEPGAGGStrLAAYVVFA 627
Cdd:PRK00174 478 fstfkgMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVaeAAVVGRPDDIKGQG--IYAFVTLK 555
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502993053 628 DGDRPGVP-APALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDR 672
Cdd:PRK00174 556 GGEEPSDElRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMR 601
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
320-585 |
1.85e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 54.44 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 320 DLSPGTLAYVSYTSGSTGTPKGVCVPHRavSRLVHEP---DWLDAGPDDVFLQAAP----IAFDASTLeiwASLSAGARL 392
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHA--NLLANQRaclKFFSPKEDDVMMSFLPpfhaYGFNSCTL---FPLLSGVPV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 393 VLlPPGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVD---HHLDRLAGVRHLIAGGDVISPDAVRRLLAAHPDLVFTNGY 469
Cdd:PRK06334 254 VF-AYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKtakKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGY 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 470 GPTENTTFTTCATFGGPAARPGeagplpIGRPIRGTRVRVLDRLGR-PVPPGVVGDLYALGEGLALGYLGRPAVTAAVFT 548
Cdd:PRK06334 333 GTTECSPVITINTVNSPKHESC------VGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVEL 406
|
250 260 270
....*....|....*....|....*....|....*..
gi 502993053 549 pagGGERQYRTGDLARWRTDGSLDFLGRADDQVKIKG 585
Cdd:PRK06334 407 ---GGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGA 440
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
529-681 |
2.03e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 54.23 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 529 GEGLALGYLgrPAVTAAvftpagggERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAA 606
Cdd:PRK07445 308 AQSLALGYY--PQILDS--------QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVqdVCV 377
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502993053 607 VALPEPGAGgsTRLAAYVVFADGDrpgVPAPALRDWLRERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAE 681
Cdd:PRK07445 378 LGLPDPHWG--EVVTAIYVPKDPS---ISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQ 447
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
311-684 |
3.23e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 53.86 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 311 RAATEPLPGDLSPgtLAYVsYTSGSTGTPKGVCVPHR---AVSRLVHEP-----DWLDAGPDDVFLQAAPIAfdastlEI 382
Cdd:PRK05857 159 SLAGNADQGSEDP--LAMI-FTSGTTGEPKAVLLANRtffAVPDILQKEglnwvTWVVGETTYSPLPATHIG------GL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 383 WASLSAGARLVLLPPGRVDPAELGAVVAAEGVTVLWLTAGLFHQLVDHHldRLAGV-----RHLIAGGD-VISPDaVRRL 456
Cdd:PRK05857 230 WWILTCLMHGGLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSEL--KSANAtvpslRLVGYGGSrAIAAD-VRFI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 457 LAAhpDLVFTNGYGPTENTTFTTCATFGGPAARPGEAGplPIGRPIRGTRVRVLDRLGR-PVPPGVV-----GDLYALGE 530
Cdd:PRK05857 307 EAT--GVRTAQVYGLSETGCTALCLPTDDGSIVKIEAG--AVGRPYPGVDVYLAATDGIgPTAPGAGpsasfGTLWIKSP 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 531 GLALGYLGRPAVTAAVFTpagggERQYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAV--TAAVA 608
Cdd:PRK05857 383 ANMLGYWNNPERTAEVLI-----DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVreAACYE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 609 LPEPGAGGSTRLAayvVFADGDRPGVPAPALRDWL----RERLPEFLVPARIVALDAFPLTPNGKLDREALPGSAAEEGA 684
Cdd:PRK05857 458 IPDEEFGALVGLA---VVASAELDESAARALKHTIaarfRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKA 534
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
328-670 |
1.37e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 51.72 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 328 YVSYTSGSTGTPK-------GVCVPHRAVSRLvHepdwLDAGPDDVFLqaapiaFDASTleIW-------ASLSAGARLV 393
Cdd:PRK03584 267 WILYSSGTTGLPKcivhghgGILLEHLKELGL-H----CDLGPGDRFF------WYTTC--GWmmwnwlvSGLLVGATLV 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 394 LL--PPGRVDPAELGAVVAAEGVTVLWLTAGLFHQL--------VDHHLDRLagvRHLIAGGDVISPDA---VRRllAAH 460
Cdd:PRK03584 334 LYdgSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACekaglvpgETHDLSAL---RTIGSTGSPLPPEGfdwVYE--HVK 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 461 PDLVFTNGYGPTEnttFTTCATFGGP--AARPGEagplpIGRPIRGTRVRVLDRLGRPVpPGVVGDLyalgeglalgylg 538
Cdd:PRK03584 409 ADVWLASISGGTD---ICSCFVGGNPllPVYRGE-----IQCRGLGMAVEAWDEDGRPV-VGEVGEL------------- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 539 rpAVTAAV------FTPAGGGERqYRT------------GDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAH 600
Cdd:PRK03584 467 --VCTKPFpsmplgFWNDPDGSR-YRDayfdtfpgvwrhGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEAL 543
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502993053 601 PAVTAAVALPEPGAGGSTRLAAYVVFADGdrpgvpaPALRDWLRERL---------PEFlVPARIVALDAFPLTPNGKL 670
Cdd:PRK03584 544 PEVLDSLVIGQEWPDGDVRMPLFVVLAEG-------VTLDDALRARIrttirtnlsPRH-VPDKIIAVPDIPRTLSGKK 614
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
138-650 |
1.69e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 51.59 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 138 PAPARLVHDLvDERARLAPDAPALtaAGKTVPYRWLAEHAEALAARLVRA--------GVRPGEVVGVLGDRS--AGLIA 207
Cdd:PRK12582 46 PYPRSIPHLL-AKWAAEAPDRPWL--AQREPGHGQWRKVTYGEAKRAVDAlaqalldlGLDPGRPVMILSGNSieHALMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 208 glLAVLKAG-------GAYLALPPDWpdARLTGLLDDAGVRIVLADaQVAGRVRGDRTAVPFDATPTAATEPRSGERTTG 280
Cdd:PRK12582 123 --LAAMQAGvpaapvsPAYSLMSHDH--AKLKHLFDLVKPRVVFAQ-SGAPFARALAALDLLDVTVVHVTGPGEGIASIA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 281 pldaaapeaaepqpgpvLGDHALPPLDANRRAATEPLpgdlSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVhepdwld 360
Cdd:PRK12582 198 -----------------FADLAATPPTAAVAAAIAAI----TPDTVAKYLFTSGSTGMPKAVINTQRMMCANI------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 361 AGPDDVFLQAA----PIAFD--------ASTLEIWASLSAGARLvLLPPGRVDPAELGAVVAA--EGVTVLWLTAGLFHQ 426
Cdd:PRK12582 250 AMQEQLRPREPdpppPVSLDwmpwnhtmGGNANFNGLLWGGGTL-YIDDGKPLPGMFEETIRNlrEISPTVYGNVPAGYA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 427 LVDHHLDRLAGVRH-------LIA-GGDVISPDAVRRL--LAAHPD---LVFTNGYGPTEnTTFTTCATFGgPAARPGEA 493
Cdd:PRK12582 329 MLAEAMEKDDALRRsffknlrLMAyGGATLSDDLYERMqaLAVRTTghrIPFYTGYGATE-TAPTTTGTHW-DTERVGLI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 494 G-PLPigrpirGTRVRVldrlgrpVPPGVVGDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARW----RTD 568
Cdd:PRK12582 407 GlPLP------GVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEG----FYRLGDAARFvdpdDPE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 569 GSLDFLGRADDQVKI-KGYRV-----EPAEVAAALG-AHPAVTA--------AVALPEPGAggstrLAAYVVFADG-DRP 632
Cdd:PRK12582 470 KGLIFDGRVAEDFKLsTGTWVsvgtlRPDAVAACSPvIHDAVVAgqdrafigLLAWPNPAA-----CRQLAGDPDAaPED 544
|
570
....*....|....*...
gi 502993053 633 GVPAPALRDWLRERLPEF 650
Cdd:PRK12582 545 VVKHPAVLAILREGLSAH 562
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
194-672 |
2.80e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 50.53 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 194 VVGVLGDRSAGLIAGLLAVLKAGGAYLALP--------PDWPDARLTGLLDdAGVRIVLADAQVAGRVRGDRTAVPFDAT 265
Cdd:PRK05851 56 AVGLVGEPTVELVAAIQGAWLAGAAVSILPgpvrgaddGRWADATLTRFAG-IGVRTVLSHGSHLERLRAVDSSVTVHDL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 266 PTAATEPRSGerttgpldaaapeaaepqpgpvlgdhALPPLDanrraateplpgdlsPGTLAYVSYTSGSTGTPKGVCVP 345
Cdd:PRK05851 135 ATAAHTNRSA--------------------------SLTPPD---------------SGGPAVLQGTAGSTGTPRTAILS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 346 HRAV-SRLVHEPDWLDAGPD-DVFLQAAPIAFDASTLEIWASLSAGARLVLLPPgrvdpaelGAVVAAEGVTVLWLT--- 420
Cdd:PRK05851 174 PGAVlSNLRGLNARVGLDAAtDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPT--------TAFSASPFRWLSWLSdsr 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 421 AGLF------HQLVDHHLDRLAGV-----RHLIAGGDVISPDAVRRLLAAHPDLVFTNG-----YGPTEnttfTTCATfg 484
Cdd:PRK05851 246 ATLTaapnfaYNLIGKYARRVSDVdlgalRVALNGGEPVDCDGFERFATAMAPFGFDAGaaapsYGLAE----STCAV-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 485 gPAARPG----------EAGPLP-----IGRPIRGTRVRVLDRLG-RPVPPGVVGDLYALGEGLALGYLGRPAVTAavft 548
Cdd:PRK05851 320 -TVPVPGiglrvdevttDDGSGArrhavLGNPIPGMEVRISPGDGaAGVAGREIGEIEIRGASMMSGYLGQAPIDP---- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 549 pagggERQYRTGDLArWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT--AAVALPEPGAGGSTRLAAYVVF 626
Cdd:PRK05851 395 -----DDWFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVRegAVVAVGTGEGSARPGLVIAAEF 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 502993053 627 ADGDRPGVpapalRDWLRERLPEF--LVPARIVALD--AFPLTPNGKLDR 672
Cdd:PRK05851 469 RGPDEAGA-----RSEVVQRVASEcgVVPSDVVFVApgSLPRTSSGKLRR 513
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
190-610 |
7.70e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 49.34 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 190 RPGEVVGVLGDRSAGLIAGLLAVLKAGGayLALP---PDWPD--ARLTGLLDDAGVRIVLADAQVAGRVRGdrtavpFDA 264
Cdd:PRK07769 77 KPGDRVAILAPQNLDYLIAFFGALYAGR--IAVPlfdPAEPGhvGRLHAVLDDCTPSAILTTTDSAEGVRK------FFR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 265 TPTAATEPRsgerttgpldaaapeaaepqpgpVLGDHALPpldaNRRAATEpLPGDLSPGTLAYVSYTSGSTGTPKGVCV 344
Cdd:PRK07769 149 ARPAKERPR-----------------------VIAVDAVP----DEVGATW-VPPEANEDTIAYLQYTSGSTRIPAGVQI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 345 PHRAV-SRLVHEPDWLDAGPDDVFLQAAPIAFDASTLEIWASLSAGARLVLLP-------PGR------VDPAELGAVVA 410
Cdd:PRK07769 201 THLNLpTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSpaafvrrPGRwirelaRKPGGTGGTFS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 411 AEGVTVLWLTA--GLFHQlVDHHLDrLAGVRHLIAGGDVISPDAVRRLLAAH-----PDLVFTNGYGPTENTTFTTCATF 483
Cdd:PRK07769 281 AAPNFAFEHAAarGLPKD-GEPPLD-LSNVKGLLNGSEPVSPASMRKFNEAFapyglPPTAIKPSYGMAEATLFVSTTPM 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 484 GG--------------------PAARPGEAGPLPIGRPIRGTRVRVLD-RLGRPVPPGVVGDLYALGEGLALGYLGRPAV 542
Cdd:PRK07769 359 DEeptviyvdrdelnagrfvevPADAPNAVAQVSAGKVGVSEWAVIVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 543 TAAVF-------------TPAGGGERQYRTGDLARWrTDGSLDFLGRADDQVKIKGYRVEPAEV-AAALGAHPAV----T 604
Cdd:PRK07769 439 TAATFqnilksrlseshaEGAPDDALWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLeYTAQEATKALrtgyV 517
|
....*.
gi 502993053 605 AAVALP 610
Cdd:PRK07769 518 AAFSVP 523
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
514-672 |
9.19e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 48.99 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 514 GRPVPPGVVGDLyalgeglalgylgrpavtaaVFTPAGggeRQ------YRTGDLARWRTDGS--------LDF-LGRAD 578
Cdd:COG1541 271 GEPVPEGEEGEL--------------------VVTTLT---KEamplirYRTGDLTRLLPEPCpcgrthprIGRiLGRAD 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 579 DQVKIKGYRVEPAEVAAALGAHPAVTAAVALPEPGAGGSTRLAAYVvfadGDRPGVPAPALRDWLRERLPEFL-VPARI- 656
Cdd:COG1541 328 DMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRV----ELAPGASLEALAEAIAAALKAVLgLRAEVe 403
|
170
....*....|....*..
gi 502993053 657 -VALDAFPLTPnGKLDR 672
Cdd:COG1541 404 lVEPGSLPRSE-GKAKR 419
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
311-650 |
5.27e-05 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 46.66 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 311 RAATEPLPGDLSPGTLAYVSYTSGSTGTPKGVCVPHR--AVSRLVHEPDWLDAGPDD-VFLQAAPiafdastleiWASLS 387
Cdd:cd05921 152 TAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRmlCANQAMLEQTYPFFGEEPpVLVDWLP----------WNHTF 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 388 AGAR---LVL-------LPPGRVDPAELGAVVA--AEGVTVLWLTAGLFHQLVDHHLDR--------LAGVRHLIAGGDV 447
Cdd:cd05921 222 GGNHnfnLVLynggtlyIDDGKPMPGGFEETLRnlREISPTVYFNVPAGWEMLVAALEKdealrrrfFKRLKLMFYAGAG 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 448 ISP---DAVRRLLAAHPD--LVFTNGYGPTENTTFTTCATFggPAARPGEagplpIGRPIRGTRVRVldrlgrpVPPGVV 522
Cdd:cd05921 302 LSQdvwDRLQALAVATVGerIPMMAGLGATETAPTATFTHW--PTERSGL-----IGLPAPGTELKL-------VPSGGK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 523 GDLYALGEGLALGYLGRPAVTAAVFTPAGggerQYRTGDLARW----RTDGSLDFLGRADDQVKIKG---YRVEPAEVAA 595
Cdd:cd05921 368 YEVRVKGPNVTPGYWRQPELTAQAFDEEG----FYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASgtwVSVGPLRARA 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502993053 596 ALGAHPAVTAAV----------ALPEPGAGGSTRLAAYVVFADGDrpGVPAPALRDWLRERLPEF 650
Cdd:cd05921 444 VAACAPLVHDAVvagedraevgALVFPDLLACRRLVGLQEASDAE--VLRHAKVRAAFRDRLAAL 506
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
328-675 |
1.25e-04 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 45.32 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 328 YVSYTSGSTGTPKGVcvpHR-----AVSRLVHEPDWLDAGPDDVFLQAAPIAFDAS-TLEIWASLSAGARLVLLP--PGR 399
Cdd:PRK10524 237 YILYTSGTTGKPKGV---QRdtggyAVALATSMDTIFGGKAGETFFCASDIGWVVGhSYIVYAPLLAGMATIMYEglPTR 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 400 VDPAELGAVVAAEGVTVLWL--TA--GLFHQ----LVDHHLDRLagvRHL-IAGGDVISPDAvrRLLAAHPDLVFTNGYG 470
Cdd:PRK10524 314 PDAGIWWRIVEKYKVNRMFSapTAirVLKKQdpalLRKHDLSSL---RALfLAGEPLDEPTA--SWISEALGVPVIDNYW 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 471 PTEnTTFTTCATFGGPAARPGEAG-PlpiGRPIRGTRVRVLDRL-GRPVPPGVVGDLYALGeglalgylgrPAVTAAVFT 548
Cdd:PRK10524 389 QTE-TGWPILAIARGVEDRPTRLGsP---GVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEG----------PLPPGCMQT 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 549 PAGGGER------------QYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVT--AAVALPEPGA 614
Cdd:PRK10524 455 VWGDDDRfvktywslfgrqVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAevAVVGVKDALK 534
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 615 GgstRLA-AYVVFADGDRPGVPAPALR------DWLRERLPEFLVPARIVALDAFPLTPNGKLDREAL 675
Cdd:PRK10524 535 G---QVAvAFVVPKDSDSLADREARLAlekeimALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAI 599
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
514-605 |
2.24e-04 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 44.54 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 514 GRPVPPGVVGDLyalgeglalgylgrpavTAAVFTPAGGGERQYRTGDLARW--------RTDGSLD-FLGRADDQVKIK 584
Cdd:cd05913 267 GEPVPPGEVGEL-----------------VFTTLTKEAMPLIRYRTRDITRLlpgpcpcgRTHRRIDrITGRSDDMLIIR 329
|
90 100
....*....|....*....|.
gi 502993053 585 GYRVEPAEVAAALGAHPAVTA 605
Cdd:cd05913 330 GVNVFPSQIEDVLLKIPGLGP 350
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
308-374 |
4.53e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 43.55 E-value: 4.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502993053 308 ANRRAATEPLPGDLspgtlAYVSYTSGSTGTPKGVCVPHRA-VSRLVHEPDWLDAGPDDVFLQAAPIA 374
Cdd:PLN02736 210 SSPQPFRPPKPEDV-----ATICYTSGTTGTPKGVVLTHGNlIANVAGSSLSTKFYPSDVHISYLPLA 272
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
501-675 |
6.75e-04 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 43.14 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 501 PIRGTRVRVLDRLGRPVPPGVVGdlyaLGEgLALGylgrPAVTAAVFT--------------PAGGGERQYRTGDLARWR 566
Cdd:PLN03052 530 PAMGCKLFILDDSGNPYPDDAPC----TGE-LALF----PLMFGASSTllnadhykvyfkgmPVFNGKILRRHGDIFERT 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 567 TDGSLDFLGRADDQVKIKGYRVEPAEVAAALG-AHPAV--TAAVALPEPGaGGSTRLAAYVVFADgDRPGVPAPALrdwL 643
Cdd:PLN03052 601 SGGYYRAHGRADDTMNLGGIKVSSVEIERVCNaADESVleTAAIGVPPPG-GGPEQLVIAAVLKD-PPGSNPDLNE---L 675
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502993053 644 RERL---------PEFLVPArIVALDAFPLTPNGKLDREAL 675
Cdd:PLN03052 676 KKIFnsaiqkklnPLFKVSA-VVIVPSFPRTASNKVMRRVL 715
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
463-663 |
1.18e-03 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 42.17 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 463 LVFTNGYGPTENTTFTTCATFggPAARPGEagplpIGRPIRGTRVRVldrlgrpVPpgvVGDLYAL---GEGLALGYLGR 539
Cdd:PRK08180 366 IRMMTGLGMTETAPSATFTTG--PLSRAGN-----IGLPAPGCEVKL-------VP---VGGKLEVrvkGPNVTPGYWRA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 540 PAVTAAVFTPAGggerQYRTGDLARW----RTDGSLDFLGRADDQVKIKG---YRVEPAEVAAALGAHPAVTAAV----- 607
Cdd:PRK08180 429 PELTAEAFDEEG----YYRSGDAVRFvdpaDPERGLMFDGRIAEDFKLSSgtwVSVGPLRARAVSAGAPLVQDVVitghd 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502993053 608 -----ALPEPGAGGSTRLAAYVVFADgDRPGVPAPALRDWLRERLPEF--------LVPARIVALDAFP 663
Cdd:PRK08180 505 rdeigLLVFPNLDACRRLAGLLADAS-LAEVLAHPAVRAAFRERLARLnaqatgssTRVARALLLDEPP 572
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
310-630 |
2.51e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 41.17 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 310 RRAATEPLPgDLSPGTLAYVSYTSGSTGTPKGVCVPHRAVSRLVHE-PDWLDAGPDDVFLQAAPIAFDASTLEIWA-SLS 387
Cdd:PRK13388 137 AAGALTPHR-EVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRAlTERFGLTRDDVCYVSMPLFHSNAVMAGWApAVA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 388 AGARLVLlpPGRVDPAELGAVVAAEGVTVL-WLTAGLFHQLVDHHLDRLAGVRHLIAGGDVISPD---AVRRLLAAHpdl 463
Cdd:PRK13388 216 SGAAVAL--PAKFSASGFLDDVRRYGATYFnYVGKPLAYILATPERPDDADNPLRVAFGNEASPRdiaEFSRRFGCQ--- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 464 vFTNGYGPTENttfttcatfGGPAARPGEAGPLPIGRPIRGTR-----------VRVLDRLGRPV-PPGVVGDLY-ALGE 530
Cdd:PRK13388 291 -VEDGYGSSEG---------AVIVVREPGTPPGSIGRGAPGVAiynpetltecaVARFDAHGALLnADEAIGELVnTAGA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502993053 531 GLALGYLGRPAVTAavftpagggER----QYRTGDLARWRTDGSLDFLGRADDQVKIKGYRVEPAEVAAALGAHPAVTAA 606
Cdd:PRK13388 361 GFFEGYYNNPEATA---------ERmrhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRV 431
|
330 340
....*....|....*....|....
gi 502993053 607 VALPEPGAGGSTRLAAYVVFADGD 630
Cdd:PRK13388 432 AVYAVPDERVGDQVMAALVLRDGA 455
|
|
| |
