|
Name |
Accession |
Description |
Interval |
E-value |
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
8-1433 |
0e+00 |
|
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: 2056.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 8 RVLSRLQNLPSISLPTDYPRPTgANKLIESVHTAQLSEQTSlsllklalysededheeeeedveSSHKRPSAFHLLLAAF 87
Cdd:TIGR03443 1 RWSERLDNPTLSVLPHDYLRPA-NNRLVEATYSLQLPSAEV-----------------------TAGGGSTPFIILLAAF 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 88 IVLLHRYTGDTDIVVGSSSASAREPLILRLSVDPADPYWAVVRHVQQTEKEAEADA-LPYDVITQALNKGKEDSLDRPLF 166
Cdd:TIGR03443 57 AALVYRLTGDEDIVLGTSSNKSGRPFVLRLNITPELSFLQLYAKVSEEEKEGASDIgVPFDELSEHIQAAKKLERTPPLF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 167 RVRFFDETDEPTNNFigSTSVTSDLTVFITrpPAStrasiaPRLSLRVLYNSLLFTSARITSFLDQLSVFLRKVAATPLS 246
Cdd:TIGR03443 137 RLAFQDAPDNQQTTY--STGSTTDLTVFLT--PSS------PELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 247 PVGSVPLLTPSQKAVLPNPTGDLNWCGWKGAITDVFSRNARQNPDRPCVIQSLPTESPDKPQgkVIFSYGAILRASNVLA 326
Cdd:TIGR03443 207 PIGKVSLITPSQKSLLPDPTKDLDWSGFRGAIHDIFADNAEKHPDRTCVVETPSFLDPSSKT--RSFTYKQINEASNILA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 327 HHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPRGLIMLKGAGTISPTVREFLA 406
Cdd:TIGR03443 285 HYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEKAGTLDQLVRDYID 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 407 QELKIKVEVPGLEVFPDGHIVGGLDPVGE-DVLRAHNHLGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFF 485
Cdd:TIGR03443 365 KELELRTEIPALALQDDGSLVGGSLEGGEtDVLAPYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 486 PWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQA 565
Cdd:TIGR03443 445 PWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAQA 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 566 TRQIPTLLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAVSYFAIPPVSQDSTFLATQKDIMPAGEGMIDVQL 645
Cdd:TIGR03443 525 TTPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETQRAVSYFEIPSRSSDSTFLKNLKDVMPAGKGMKNVQL 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 646 LVVNRNDRNVPCAVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWFaVNAPPRKDTIlhPEEGfaGPESRYWKGIRDRM 724
Cdd:TIGR03443 605 LVVNRNDRTQTCGVGEVGEIYVRAGGLAEGYLGLpELNAEKFVNNWF-VDPSHWIDLD--KENN--KPEREFWLGPRDRL 679
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 725 YRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVP-LEGSALEGY 803
Cdd:TIGR03443 680 YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPqDKSDELEEF 759
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 804 ASNVPDDEDDGkGLVKGMKKYRRLIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALPFPDTAQASYAAGPSA 883
Cdd:TIGR03443 760 KSEVDDEESSD-PVVKGLIKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAVAKNRS 838
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 884 PGA-----SATEIAMQKIWSTILPNAPQPIPTDESFFDLGGHSILATRLIFEIRKVFVVNAPLGLIFEKPTIAGLVEAVD 958
Cdd:TIGR03443 839 ASAadeefTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVD 918
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 959 ALRNADlgfaykepsaasagatTSADVKNAGVAA--AAPHVEYGQDYLNLIEKLQPSYAPLPADFNDHPITVFLTGATGF 1036
Cdd:TIGR03443 919 RLKKGE----------------ELADEGDSEIEEeeTVLELDYAKDAKTLVDSLPKSYPSRKELDASTPITVFLTGATGF 982
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1037 LGAFVLYDLLSR-TDRVKKVICLVRGKTVEQGLERLKEGSTDRNVWSDSWVSsgRLEVVTGDLGLDNFGLSQETWNNVAN 1115
Cdd:TIGR03443 983 LGSFILRDLLTRrSNSNFKVFAHVRAKSEEAGLERLRKTGTTYGIWDEEWAS--RIEVVLGDLSKEKFGLSDEKWSDLTN 1060
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1116 EADVVLHNGALVHWVFPYEKLRSPNVLGTLTAVNLASTGKQKVFVFVSSTSAIDTEHYVQLSESLArgSTDSKGVPESDD 1195
Cdd:TIGR03443 1061 EVDVIIHNGALVHWVYPYSKLRDANVIGTINVLNLCAEGKAKQFSFVSSTSALDTEYYVNLSDELV--QAGGAGIPESDD 1138
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1196 LEGAKSALKTGYGQSKWVSEKLLFEAGKRGLRGHIVRPGYVVGDSHTAVTNTDDFIWRLVKGCVQLGLVPDINNSINMVP 1275
Cdd:TIGR03443 1139 LMGSSKGLGTGYGQSKWVAEYIIREAGKRGLRGCIVRPGYVTGDSKTGATNTDDFLLRMLKGCIQLGLIPNINNTVNMVP 1218
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1276 VDHVARITSLAAVSPLPDAPLSVCHVTARPLPTFNGMLSSLVQYGFPTESCEYVVWRRKLEQHVMEVG-DNALFPLLHFV 1354
Cdd:TIGR03443 1219 VDHVARVVVAAALNPPKESELAVAHVTGHPRIRFNDFLGTLKTYGYDVEIVDYVHWRKSLERFVIERSeDNALFPLLHFV 1298
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1355 LDDLPTSTKSPELDDSNTVAVLRQG----GAQLSATVGDD--LMGLYLAWLVGAGFLPSPSLpSPQKALPTLA-NAGNIK 1427
Cdd:TIGR03443 1299 LDDLPQSTKAPELDDTNAATSLKADaawtGVDVSSGAGVTeeQIGIYIAYLVKVGFLPAPTK-TGALPLPKIEiSEAQLK 1377
|
1450
....*....|
gi 2234869976 1428 ----AAGRTG 1433
Cdd:TIGR03443 1378 liasAGGRGS 1387
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
290-870 |
0e+00 |
|
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: 849.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 290 PDRPCVIqslptESPDKPQGKV-IFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVD 368
Cdd:cd17647 2 PERTCVV-----ETPSLNSSKTrSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 369 PAYPPSRQIIYLGVAKPRGLIMLKGAGtisptvreflaqelkikvevpglevfpdghivggldpvgedvlrahnhlgetd 448
Cdd:cd17647 77 PAYPPARQNIYLGVAKPRGLIVIRAAG----------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 449 pnVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVP 528
Cdd:cd17647 104 --VVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVP 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 529 TADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTET 608
Cdd:cd17647 182 TQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTET 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 609 QRAVSYFAIPPVSQDSTFLATQKDIMPAGEGMIDVQLLVVNRNDRNVPCAVGEVGEIYVRSGGLAEGYLD-QDASAEKFV 687
Cdd:cd17647 262 QRAVSYFEVPSRSSDPTFLKNLKDVMPAGRGMLNVQLLVVNRNDRTQICGIGEVGEIYVRAGGLAEGYRGlPELNKEKFV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 688 NNWFAvnappRKDTILHPEEGFAGPESRYWKGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQ 767
Cdd:cd17647 342 NNWFV-----EPDHWNYLDKDNNEPWRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQ 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 768 HPLVRENVTLVRRDKDEEKILVSYFVP-LEGSALEGYASNVPDDEDDGKGLVKGMKKYRRLIKDIREHLKQKLPKHSVPS 846
Cdd:cd17647 417 HPLVRENITLVRRDKDEEPTLVSYIVPrFDKPDDESFAQEDVPKEVSTDPIVKGLIGYRKLIKDIREFLKKRLASYAIPS 496
|
570 580
....*....|....*....|....
gi 2234869976 847 LFVPLSKMPLNPNGKIDKPALPFP 870
Cdd:cd17647 497 LIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2-961 |
7.21e-146 |
|
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: 479.74 E-value: 7.21e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 2 ADQRLERVLSRLQNLPSI-SLPTDYPRPTGANKLIESvHTAQLSEQTSLSLLKLAlysededheeeeedvesSHKRPSAF 80
Cdd:COG1020 204 LARQLAYWRQQLAGLPPLlELPTDRPRPAVQSYRGAR-VSFRLPAELTAALRALA-----------------RRHGVTLF 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 81 HLLLAAFIVLLHRYTGDTDIVVGSSSA----SAREPLI--------LRLSVDPADPYWAVVRHVQQTEKEAEA-DALPYD 147
Cdd:COG1020 266 MVLLAAFALLLARYSGQDDVVVGTPVAgrprPELEGLVgffvntlpLRVDLSGDPSFAELLARVRETLLAAYAhQDLPFE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 148 VITQALNKgkEDSLDR-PLFRVRF-FDETDEPTNNFIGST-------SVTS--DLTVFITRPPAstrasiapRLSLRVLY 216
Cdd:COG1020 346 RLVEELQP--ERDLSRnPLFQVMFvLQNAPADELELPGLTlepleldSGTAkfDLTLTVVETGD--------GLRLTLEY 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 217 NSLLFTSARITSFLDQLSVFLRKVAATPLSPVGSVPLLTPSQKAVL---------PNPTGDLnwcgwkgaITDVFSRNAR 287
Cdd:COG1020 416 NTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLlaewnataaPYPADAT--------LHELFEAQAA 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 288 QNPDRPCVI---QSLptespdkpqgkvifSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATF 364
Cdd:COG1020 488 RTPDAVAVVfgdQSL--------------TYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 365 SVVDPAYPPSRqIIYlgvakprgliMLKGAGtisptVREFLAQElkikvevpglevfpdgHIVGGLDPVGEDVLR----A 440
Cdd:COG1020 554 VPLDPAYPAER-LAY----------MLEDAG-----ARLVLTQS----------------ALAARLPELGVPVLAldalA 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 441 HNHLGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLF 520
Cdd:COG1020 602 LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALL 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 521 LGAQLHVPTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRLQALAANVRII 600
Cdd:COG1020 682 SGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLV 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 601 NMYGTTETQRAVSYFAIPPVSQDStflatqkDIMPAGEGMIDVQLLVVNRNDRnvPCAVGEVGEIYVRSGGLAEGYLDQ- 679
Cdd:COG1020 762 NLYGPTETTVDSTYYEVTPPDADG-------GSVPIGRPIANTRVYVLDAHLQ--PVPVGVPGELYIGGAGLARGYLNRp 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 680 DASAEKFVNNWFavnapprkdtilhpeeGFAGpesrywkgirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELG 759
Cdd:COG1020 833 ELTAERFVADPF----------------GFPG----------ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELG 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 760 EIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALEGYAsnvpddeddgkglvkgmkkyrrlikdIREHLKQKL 839
Cdd:COG1020 887 EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAAL--------------------------LRLALALLL 940
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 840 PKHSVPSLFVPLSKMPLNPNGKIDKPALPFPDTAQASYAAGPSAPGASATEIAMQKIWstilpnAPQPIPTDESFFDLGG 919
Cdd:COG1020 941 PPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLL------LVVVVGDDDFFFFGGG 1014
|
970 980 990 1000
....*....|....*....|....*....|....*....|..
gi 2234869976 920 HSILATRLIFEIRKVFVVNAPLGLIFEKPTIAGLVEAVDALR 961
Cdd:COG1020 1015 LGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAA 1056
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
313-867 |
1.75e-128 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 405.37 E-value: 1.75e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 313 FSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRqIIYLgvakprglimlk 392
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER-LAYI------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 393 gagtisptvreflaqelkikvevpglevfpdghivggldpvgedvlrahnhLGETDPNVVL-GPDSIGTLSFTSGSTGIP 471
Cdd:cd05930 80 ---------------------------------------------------LEDSGAKLVLtDPDDLAYVIYTSGSTGKP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 472 KGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVT 551
Cdd:cd05930 109 KGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 552 HLTPAM-GQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAVSYFAIPPVsqdstflATQ 630
Cdd:cd05930 189 HLTPSLlRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPD-------DEE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 631 KDIMPAGEGMIDVQLLVVNRNDRnvPCAVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWFavnapprkdtilhpeegf 709
Cdd:cd05930 262 DGRVPIGRPIPNTRVYVLDENLR--PVPPGVPGELYIGGAGLARGYLNRpELTAERFVPNPF------------------ 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 710 agpesrywkGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILV 789
Cdd:cd05930 322 ---------GPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLV 392
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2234869976 790 SYFVPLEGSALEgyasnvpddeddgkglvkgmkkyrrlIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05930 393 AYVVPDEGGELD--------------------------EEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
314-775 |
4.23e-121 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 384.31 E-value: 4.23e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 314 SYGAILRASNVLAHHLI-MNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPRGLIMLk 392
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 393 gagtisptvreflaqelkikvevPGLEVFPDGHIVGGLDPVGEDVLRAHNHLGETDPNVVLGPDSIGTLSFTSGSTGIPK 472
Cdd:TIGR01733 80 -----------------------SALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 473 GVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRL-AEWMAESEVTVT 551
Cdd:TIGR01733 137 GVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAALIAEHPVTVL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 552 HLTPAMGQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAVSYFAIPPVsqdstfLATQK 631
Cdd:TIGR01733 217 NLTPSLLALLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPD------DAPRE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 632 DIMPAGEGMIDVQLLVVNRNDRnvPCAVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWFavnapprkdtilhpeegfa 710
Cdd:TIGR01733 291 SPVPIGRPLANTRLYVLDDDLR--PVPVGVVGELYIGGPGVARGYLNRpELTAERFVPDPF------------------- 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2234869976 711 gpesryWKGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENV 775
Cdd:TIGR01733 350 ------AGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAV 408
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
17-960 |
1.63e-118 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 412.63 E-value: 1.63e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 17 PSISLPTDYPRPT-----GANkliesvHTAQLSEQTSLSLLKLAlysededheeeeedvesshKRPSA--FHLLLAAFIV 89
Cdd:PRK12467 252 TVLELPTDRPRPAvpsyrGAR------LRVDLPQALSAGLKALA-------------------QREGVtlFMVLLASFQT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 90 LLHRYTGDTDIVVGSSSA----SAREPLI--------LRLSVDPADPYWAVVRHVQQTEKEAEA-DALPYDVITQALNKg 156
Cdd:PRK12467 307 LLHRYSGQSDIRIGVPNAnrnrVETERLIgffvntqvLKAEVDPQASFLELLQQVKRTALGAQAhQDLPFEQLVEALQP- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 157 kEDSLDR-PLFRVRFFDETD-EPTNNFIGST--------------SVTSDLTVFITRPPASTRASIAprlslrvlYNSLL 220
Cdd:PRK12467 386 -ERSLSHsPLFQVMFNHQNTaTGGRDREGAQlpgltveelswarhTAQFDLALDTYESAQGLWAAFT--------YATDL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 221 FTSARITSFLDQLSVFLRKVAATPLSPVGSVPLL--TPSQKAVLPNPTGDLNWCGwkGAITDVFSRNARQNPDRPCVIQs 298
Cdd:PRK12467 457 FEATTIERLATHWRNLLEAIVAEPRRRLGELPLLdaEERARELVRWNAPATEYAP--DCVHQLIEAQARQHPERPALVF- 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 299 lptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRqII 378
Cdd:PRK12467 534 ----------GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDR-LA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 379 YlgvakprgliMLKGAGtisptVREFLAQElkikvEVPGLEVFPDGHIVGGLDPVGEDVlrahNHLGETDPNVVLGPDSI 458
Cdd:PRK12467 603 Y----------MLDDSG-----VRLLLTQS-----HLLAQLPVPAGLRSLCLDEPADLL----CGYSGHNPEVALDPDNL 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 459 GTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGR 538
Cdd:PRK12467 659 AYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEA 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 539 LAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLNAFFVGDVLTKRDCL-RLQALAANVRIINMYGTTETQRAVSYFAI 617
Cdd:PRK12467 739 FAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLaRVRALGPGARLINHYGPTETTVGVSTYEL 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 618 PPVSQDStflatqkDIMPAGEGMIDVQLLVVNrNDRNvPCAVGEVGEIYVRSGGLAEGYLDQDA-SAEKFVNNWFAVNAp 696
Cdd:PRK12467 819 SDEERDF-------GNVPIGQPLANLGLYILD-HYLN-PVPVGVVGELYIGGAGLARGYHRRPAlTAERFVPDPFGADG- 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 697 prkdtilhpeegfagpesrywkgirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVT 776
Cdd:PRK12467 889 -------------------------GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 777 LVrRDKDEEKILVSYFVPLEGSalegyasnvpddeDDGKGLVKGmkkyrrliKDIREHLKQKLPKHSVPSLFVPLSKMPL 856
Cdd:PRK12467 944 LA-QPGDAGLQLVAYLVPAAVA-------------DGAEHQATR--------DELKAQLRQVLPDYMVPAHLLLLDSLPL 1001
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 857 NPNGKIDKPALPFPD--TAQASYAAgPSAPgasaTEIAMQKIWSTILpnAPQPIPTDESFFDLGGHSILATRLIFEIRKV 934
Cdd:PRK12467 1002 TPNGKLDRKALPKPDasAVQATFVA-PQTE----LEKRLAAIWADVL--KVERVGLTDNFFELGGHSLLATQVISRVRQR 1074
|
970 980
....*....|....*....|....*.
gi 2234869976 935 FVVNAPLGLIFEKPTIAGLVEAVDAL 960
Cdd:PRK12467 1075 LGIQVPLRTLFEHQTLAGFAQAVAAQ 1100
|
|
| SDR_e1 |
cd05235 |
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ... |
1027-1331 |
7.21e-107 |
|
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins identified as putative polyketide sythases fatty acid synthases (FAS), and nonribosomal peptide synthases, among others. However, unlike the usual ketoreductase modules of FAS and polyketide synthase, these domains are related to the extended SDRs, and have canonical NAD(P)-binding motifs and an active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187546 [Multi-domain] Cd Length: 290 Bit Score: 340.78 E-value: 7.21e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1027 TVFLTGATGFLGAFVLYDLLSRTDrVKKVICLVRGKTVEQGLERLKE--GSTDRNVWSDSWVSsgRLEVVTGDLGLDNFG 1104
Cdd:cd05235 1 TVLLTGATGFLGAYLLRELLKRKN-VSKIYCLVRAKDEEAALERLIDnlKEYGLNLWDELELS--RIKVVVGDLSKPNLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1105 LSQETWNNVANEADVVLHNGALVHWVFPYEKLRSPNVLGTLTAVNLASTGKQKVFVFVSSTSAIDTEHYVQLSESlargs 1184
Cdd:cd05235 78 LSDDDYQELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAATGKLKPLHFVSTLSVFSAEEYNALDDE----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1185 tdskgvpESDDLEGAKSALKTGYGQSKWVSEKLLFEAGKRGLRGHIVRPGYVVGDSHTAVTNTDDFIWRLVKGCVQLGLV 1264
Cdd:cd05235 153 -------ESDDMLESQNGLPNGYIQSKWVAEKLLREAANRGLPVAIIRPGNIFGDSETGIGNTDDFFWRLLKGCLQLGIY 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2234869976 1265 PDINNSINMVPVDHVARITSLAAVSplPDAPLSVCHVTARPLPTFNGMLSSLVQYGFPTESCEYVVW 1331
Cdd:cd05235 226 PISGAPLDLSPVDWVARAIVKLALN--ESNEFSIYHLLNPPLISLNDLLDALEEKGYSIKEVSYEEW 290
|
|
| Thioester-redct |
TIGR01746 |
thioester reductase domain; This model includes the terminal domain from the fungal alpha ... |
1027-1404 |
1.41e-104 |
|
thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.
Pssm-ID: 273787 [Multi-domain] Cd Length: 367 Bit Score: 337.46 E-value: 1.41e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1027 TVFLTGATGFLGAFVLYDLLSRTDRvKKVICLVRGKTVEQGLERLKEGSTDRNVWSDSWVSSgRLEVVTGDLGLDNFGLS 1106
Cdd:TIGR01746 1 TVLLTGATGFLGAYLLEELLRRSTR-AKVICLVRADSEEHAMERLREALRSYRLWHENLAME-RIEVVAGDLSKPRLGLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1107 QETWNNVANEADVVLHNGALVHWVFPYEKLRSPNVLGTLTAVNLASTGKQKVFVFVSSTSAIDTEHYvqlseslargstd 1186
Cdd:TIGR01746 79 DAEWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAASGRAKPLHYVSTISVGAAIDL------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1187 SKGVPESDDLEGAKSALKTGYGQSKWVSEKLLFEAGKRGLRGHIVRPGYVVGDSHTAVTNTDDFIWRLVKGCVQLGLVPD 1266
Cdd:TIGR01746 146 STGVTEDDATVTPYPGLAGGYTQSKWVAELLVREASDRGLPVTIVRPGRILGDSYTGAWNSSDILWRMVKGCLALGAYPQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1267 IN-NSINMVPVDHVAR-ITSLAAVsPLPDAPLSVCHVTARPLPTFNGMLSSLVQYGFPTESCEYVVWRRKLEQHVMEVGD 1344
Cdd:TIGR01746 226 SPeLTEDLTPVDFVARaIVALSSR-PAASAGGIVFHVVNPNPVPLDEFLEWLERAGYNLRLVSFDEWLQRLEDSDTAKRD 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2234869976 1345 ---NALFPLLHFVLD-DLPTSTKSPELDDSNTVAVLRQGGAQlSATVGDDLMGLYLAWLVGAGF 1404
Cdd:TIGR01746 305 srrYPLLPLLHFTGDaFESDETDTRNLDSRSTAEALEGDGIR-EPSITAPLLHLYLQYLKEIGF 367
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-964 |
1.48e-100 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 357.73 E-value: 1.48e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 82 LLLAAFIVLLHRYTGDTDIVVGSSSASAREPL------------ILRLSVDPAdPYWAVVRHVQQTEKEA----EADALP 145
Cdd:PRK12316 4342 LVQAAWLLLLQRYTGQDTVAFGATVAGRPAELpgiegqiglfinTLPVIATPR-AQQSVVEWLQQVQRQNlalrEHEHTP 4420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 146 YDVITQALNKGKEDSLDRPL-FRVRFFDET-DEPTNNFIGSTSVTS-DLTVFitrpPASTRASIAPRLSLRVLYNSLLFT 222
Cdd:PRK12316 4421 LYEIQRWAGQGGEALFDSLLvFENYPVSEAlQQGAPGGLRFGEVTNhEQTNY----PLTLAVGLGETLSLQFSYDRGHFD 4496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 223 SARITSFLDQLSVFLRKVAATPLSPVGSVPLLTPSQKAvlpnptgdlnwcgwkgAITDVFSRNARQNPDRPCV---IQSL 299
Cdd:PRK12316 4497 AATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQ----------------RIVALWNRTDAGYPATRCVhqlVAER 4560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 300 PTESPDKPqgKVIF-----SYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPps 374
Cdd:PRK12316 4561 ARMTPDAV--AVVFdeeklTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYP-- 4636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 375 rqiiylgvaKPRGLIMLKGAGTISPTVREFLAQELKIkvevpglevfPDGHIVGGLDPVGEdvlraHNHLGETDPNVVLG 454
Cdd:PRK12316 4637 ---------RERLAYMMEDSGAALLLTQSHLLQRLPI----------PDGLASLALDRDED-----WEGFPAHDPAVRLH 4692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 455 PDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPtADDIG 534
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIR-DDSLW 4771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 535 TPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQ--IPTLLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAV 612
Cdd:PRK12316 4772 DPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDgePPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTV 4851
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 613 SYFAIPPvsqdstFLATQKDIMPAGEGMIDVQLLVVnrNDRNVPCAVGEVGEIYVRSGGLAEGYLDQDA-SAEKFVNNWF 691
Cdd:PRK12316 4852 LLWKARD------GDACGAAYMPIGTPLGNRSGYVL--DGQLNPLPVGVAGELYLGGEGVARGYLERPAlTAERFVPDPF 4923
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 692 AvnapprkdtilhpEEGfagpesrywkgirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLV 771
Cdd:PRK12316 4924 G-------------APG-------------GRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4977
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 772 RENVtLVRRDKDEEKILVSYFVPLEgSALegyasnVPDDEDDGKglvkgmkkyrrLIKDIREHLKQKLPKHSVPSLFVPL 851
Cdd:PRK12316 4978 REAV-VIAQEGAVGKQLVGYVVPQD-PAL------ADADEAQAE-----------LRDELKAALRERLPEYMVPAHLVFL 5038
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 852 SKMPLNPNGKIDKPALPFPDT--AQASYAAgPSapgaSATEIAMQKIWSTILpnAPQPIPTDESFFDLGGHSILATRLIF 929
Cdd:PRK12316 5039 ARMPLTPNGKLDRKALPQPDAslLQQAYVA-PR----SELEQQVAAIWAEVL--QLERVGLDDNFFELGGHSLLAIQVTS 5111
|
890 900 910
....*....|....*....|....*....|....*
gi 2234869976 930 EIRKVFVVNAPLGLIFEKPTIAGLVEAVDALRNAD 964
Cdd:PRK12316 5112 RIQLELGLELPLRELFQTPTLAAFVELAAAAGSGD 5146
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-956 |
2.99e-100 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 356.57 E-value: 2.99e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 17 PSISLPTDYPRPTgANKLIESVHTAQLSEQTSLSLLKLAlysededheeeeedvesSHKRPSAFHLLLAAFIVLLHRYTG 96
Cdd:PRK12316 252 PVLELPTDHPRPA-VPSYRGSRYEFSIDPALAEALRGTA-----------------RRQGLTLFMLLLGAFNVLLHRYSG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 97 DTDIVVGSSSASAR----EPLI--------LRLSVDPADPYWAVVRHVQQTEKEAEA-DALPYDVITQALNKgkEDSLDR 163
Cdd:PRK12316 314 QTDIRVGVPIANRNraevEGLIgffvntqvLRSVFDGRTRVATLLAGVKDTVLGAQAhQDLPFERLVEALKV--ERSLSH 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 164 -PLFRVRFfdeTDEPTNNFIGSTSVTSDLTV-FITRPPASTRASIA-------PRLSLRVLYNSLLFTSARITSFLDQLS 234
Cdd:PRK12316 392 sPLFQVMY---NHQPLVADIEALDTVAGLEFgQLEWKSRTTQFDLTldtyekgGRLHAALTYATDLFEARTVERMARHWQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 235 VFLRKVAATPLSPVGSVPLLTPSQKAVLPNptgdlnwcGWKGAitdvfsrnARQNPDRPCV---IQSLPTESPDKPQ--- 308
Cdd:PRK12316 469 NLLRGMVENPQARVDELPMLDAEERGQLVE--------GWNAT--------AAEYPLQRGVhrlFEEQVERTPEAPAlaf 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 309 GKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIylgvakprgl 388
Cdd:PRK12316 533 GEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAY---------- 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 389 iMLKGAGTISPTVREFLAQELKikvevpglevFPDGHIVGGLDPVGEDvLRAHNhlgETDPNVVLGPDSIGTLSFTSGST 468
Cdd:PRK12316 603 -MLEDSGVQLLLSQSHLGRKLP----------LAAGVQVLDLDRPAAW-LEGYS---EENPGTELNPENLAYVIYTSGST 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 469 GIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESEV 548
Cdd:PRK12316 668 GKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGV 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 549 TVTHLTPAMGQ-LLSAQATRQIPTLLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAVSYFaippvsqdsTFL 627
Cdd:PRK12316 748 DTLHFVPSMLQaFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHW---------TCV 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 628 ATQKDIMPAGEGMIDVQLLVVNRNDRnvPCAVGEVGEIYVRSGGLAEGYLDQDA-SAEKFVNNWFAvnapprkdtilhpe 706
Cdd:PRK12316 819 EEGGDSVPIGRPIANLACYILDANLE--PVPVGVLGELYLAGRGLARGYHGRPGlTAERFVPSPFV-------------- 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 707 egfAGpesrywkgirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRrdkdEEK 786
Cdd:PRK12316 883 ---AG----------ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGK 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 787 ILVSYFVPlegsalegyasnvpddEDDGKGLVKGMKkyrrlikdirEHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPA 866
Cdd:PRK12316 946 QLVGYVVL----------------ESEGGDWREALK----------AHLAASLPEYMVPAQWLALERLPLTPNGKLDRKA 999
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 867 LPFPDTAQAsyAAGPSAPgASATEIAMQKIWSTILpnAPQPIPTDESFFDLGGHSILATRLIFEIRKVFVVNAPLGLiFE 946
Cdd:PRK12316 1000 LPAPEASVA--QQGYVAP-RNALERTLAAIWQDVL--GVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDL-FQ 1073
|
970
....*....|
gi 2234869976 947 KPTIAGLVEA 956
Cdd:PRK12316 1074 HQTIRSLALV 1083
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
17-953 |
3.46e-100 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 356.39 E-value: 3.46e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 17 PSISLPTDYPRPtGANKLIESVHTAQLSEQTSLSLLKLAlysededheeeeedvesSHKRPSAFHLLLAAFIVLLHRYTG 96
Cdd:PRK12467 1317 PVLELPTDRPRP-AVQSHRGARLAFELPPALAEGLRALA-----------------RREGVTLFMLLLASFQTLLHRYSG 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 97 DTDIVVGSSSA----SAREPLI--------LRLSVDPADPYWAVVRHVQQTEKEAEADA-LPYDVITQALNKgkEDSLDR 163
Cdd:PRK12467 1379 QDDIRVGVPIAnrnrAETEGLIgffvntqvLRAEVDGQASFQQLLQQVKQAALEAQAHQdLPFEQLVEALQP--ERSLSH 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 164 -PLFRVRFFDET-DEPTNNFIGSTSVTS----------DLTVFITRPPASTRASIAprlslrvlYNSLLFTSARITSFLD 231
Cdd:PRK12467 1457 sPLFQVMFNHQRdDHQAQAQLPGLSVESlswesqtaqfDLTLDTYESSEGLQASLT--------YATDLFEASTIERLAG 1528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 232 QLSVFLRKVAATPLSPVGSVPLLTPSQKAVLP---NPTGDlnwcGWKGA--ITDVFSRNARQNPDRPCVIQslptespdk 306
Cdd:PRK12467 1529 HWLNLLQGLVADPERRLGELDLLDEAERRQILegwNATHT----GYPLArlVHQLIEDQAAATPEAVALVF--------- 1595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 307 pqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRqIIYlgvakpr 386
Cdd:PRK12467 1596 --GEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRER-LAY------- 1665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 387 gliMLKGAGTISPTVREFLAQELKIKVEVPGLEvfpdghivggLDPvGEDVLRAHnhlGETDPNVVLGPDSIGTLSFTSG 466
Cdd:PRK12467 1666 ---MIEDSGIELLLTQSHLQARLPLPDGLRSLV----------LDQ-EDDWLEGY---SDSNPAVNLAPQNLAYVIYTSG 1728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 467 STGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAES 546
Cdd:PRK12467 1729 STGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQ 1808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 547 EVTVTHLTPAMGQLLsAQATRQI---PTLLNAFFVGDVLtKRDCLRlQALAA--NVRIINMYGTTETQRAVSYFAIPPVS 621
Cdd:PRK12467 1809 QVTTLHFVPSMLQQL-LQMDEQVehpLSLRRVVCGGEAL-EVEALR-PWLERlpDTGLFNLYGPTETAVDVTHWTCRRKD 1885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 622 QdstflaTQKDIMPAGEGMIDVQLLVVNrNDRNvPCAVGEVGEIYVRSGGLAEGYLDQDA-SAEKFVNNWFAVNApprkd 700
Cdd:PRK12467 1886 L------EGRDSVPIGQPIANLSTYILD-ASLN-PVPIGVAGELYLGGVGLARGYLNRPAlTAERFVADPFGTVG----- 1952
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 701 tilhpeegfagpesrywkgirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVrR 780
Cdd:PRK12467 1953 ---------------------SRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-Q 2010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 781 DKDEEKILVSYFVPLEgsalegyASNVPDDEDDGkglvkgmkKYRRLIKDireHLKQKLPKHSVPSLFVPLSKMPLNPNG 860
Cdd:PRK12467 2011 DGANGKQLVAYVVPTD-------PGLVDDDEAQV--------ALRAILKN---HLKASLPEYMVPAHLVFLARMPLTPNG 2072
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 861 KIDKPALPFPDTAQASYAAgpSAPgASATEIAMQKIWSTILpNAPQpIPTDESFFDLGGHSILATRLIFEIRKVFVVNAP 940
Cdd:PRK12467 2073 KLDRKALPAPDASELQQAY--VAP-QSELEQRLAAIWQDVL-GLEQ-VGLHDNFFELGGDSIISIQVVSRARQAGIRFTP 2147
|
970
....*....|...
gi 2234869976 941 LGLiFEKPTIAGL 953
Cdd:PRK12467 2148 KDL-FQHQTVQSL 2159
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
205-954 |
1.48e-96 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 345.22 E-value: 1.48e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 205 SIAPRLSLRVLYNSLLFTSARITSFLDQLSVFLRKVAATPLSPVGSVPLLTPSQKAVLP---NPTGDLNWCGwkGAITDV 281
Cdd:PRK12467 3023 GLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLhawNATAAAYPSE--RLVHQL 3100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 282 FSRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAG 361
Cdd:PRK12467 3101 IEAQVARTPEAPALVF-----------GDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAG 3169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 362 ATFSVVDPAYPPSRQiiylgvakprgLIMLKGAGtisptVREFLAQELKikvevpgLEVFPDGHIVGGLDpVGEDVLrah 441
Cdd:PRK12467 3170 GAYVPLDPEYPRERL-----------AYMIEDSG-----VKLLLTQAHL-------LEQLPAPAGDTALT-LDRLDL--- 3222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 442 NHLGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFL 521
Cdd:PRK12467 3223 NGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLIC 3302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 522 GAQLHVpTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQ-IPTLLNAFFVGDVLTKRDCLRLQALAANVRII 600
Cdd:PRK12467 3303 GGCLVV-RDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGAdCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLT 3381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 601 NMYGTTETQRAVSYFAIPpvsQDSTFLATQkdiMPAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQ- 679
Cdd:PRK12467 3382 NGYGPTEAVVTVTLWKCG---GDAVCEAPY---APIGRPVAGRSIYVLDGQLNPVP--VGVAGELYIGGVGLARGYHQRp 3453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 680 DASAEKFVNNWFAVNApprkdtilhpeegfagpesrywkgirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELG 759
Cdd:PRK12467 3454 SLTAERFVADPFSGSG--------------------------GRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELG 3507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 760 EIDTHLSQHPLVRENVTLVRrDKDEEKILVSYFVPlegsalegyasnvpDDEDDGkglvkgmkkyrrLIKDIREHLKQKL 839
Cdd:PRK12467 3508 EIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP--------------ADPQGD------------WRETLRDHLAASL 3560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 840 PKHSVPSLFVPLSKMPLNPNGKIDKPALPFPDTAQASYAAGPsapgASATEIAMQKIWSTILpnAPQPIPTDESFFDLGG 919
Cdd:PRK12467 3561 PDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVAP----RSEVEQQLAAIWADVL--GVEQVGVTDNFFELGG 3634
|
730 740 750
....*....|....*....|....*....|....*
gi 2234869976 920 HSILATRLIFEIRKVFVVNAPLGLIFEKPTIAGLV 954
Cdd:PRK12467 3635 DSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA 3669
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
82-967 |
1.83e-93 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 330.47 E-value: 1.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 82 LLLAAFIVLLHRYTGDTDIVVG------SSSASAREP------LILRLSVDPADPYWAVVRHVQQTEKEAEADALpYDV- 148
Cdd:PRK10252 254 LALALVALWLGRLCGRMDYAAGfifmrrLGSAALTATgpvlnvLPLRVHIAAQETLPELATRLAAQLKKMRRHQR-YDAe 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 149 -ITQALNK-GKEDSLDRPLFRVRFFDETDEptnnFIGSTSVT--------SDLTVFITRPPASTrasiaprLSLRVLYNS 218
Cdd:PRK10252 333 qIVRDSGRaAGDEPLFGPVLNIKVFDYQLD----FPGVQAQThtlatgpvNDLELALFPDEHGG-------LSIEILANP 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 219 LLFTSARITSFLDQLSVFLRKVAATPLSPVGSVPLLTPSQKA----------VLPNPTgdlnwcgwkgaITDVFSRNARQ 288
Cdd:PRK10252 402 QRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAqlaqvnatavEIPETT-----------LSALVAQQAAK 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 289 NPDRPCVIQSLPTespdkpqgkviFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVD 368
Cdd:PRK10252 471 TPDAPALADARYQ-----------FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLD 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 369 PAYPPSRQIIYLGVAKPRGLImlkgagtispTVREFLAQelkikvevpglevFPDGhivGGLDPVGEDVLRAhnhLGETD 448
Cdd:PRK10252 540 TGYPDDRLKMMLEDARPSLLI----------TTADQLPR-------------FADV---PDLTSLCYNAPLA---PQGAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 449 PNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVP 528
Cdd:PRK10252 591 PLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMA 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 529 TADDIGTPGRLAEWMAESEVTVTHLTPAM-----GQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRLQALaANVRIINMY 603
Cdd:PRK10252 671 EPEAHRDPLAMQQFFAEYGVTTTHFVPSMlaafvASLTPEGARQSCASLRQVFCSGEALPADLCREWQQL-TGAPLHNLY 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 604 GTTETQRAVSYFaipPVSQDSTFLATQKDImPAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQ-DAS 682
Cdd:PRK10252 750 GPTEAAVDVSWY---PAFGEELAAVRGSSV-PIGYPVWNTGLRILDARMRPVP--PGVAGDLYLTGIQLAQGYLGRpDLT 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 683 AEKFVNNWFAvnapprkdtilhPEEgfagpesrywkgirdRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEID 762
Cdd:PRK10252 824 ASRFIADPFA------------PGE---------------RMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEID 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 763 THLSQHPLVRENVTLVR------RDKDEEKILVSYFVPlegsalegyASNVPDDEDdgkglvkgmkkyrrlikDIREHLK 836
Cdd:PRK10252 877 RAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVS---------QSGLPLDTS-----------------ALQAQLR 930
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 837 QKLPKHSVPSLFVPLSKMPLNPNGKIDKPALPFPDTAQASYAAGPSAPgasaTEIAMQKIWSTILPNAPQPIptDESFFD 916
Cdd:PRK10252 931 ERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTG----TETIIAAAFSSLLGCDVVDA--DADFFA 1004
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 2234869976 917 LGGHSILATRLIFEIRKVFVVNAPLGLIFEKPTIAGLVEAVDA--LRNADLGF 967
Cdd:PRK10252 1005 LGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAeeDESRRLGF 1057
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
280-867 |
1.04e-92 |
|
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: 308.75 E-value: 1.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 280 DVFSRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLK 359
Cdd:cd12117 1 ELFEEQAARTPDAVAVVY-----------GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 360 AGATFSVVDPAYPPSRQIIYLGVAKPRGLIMLKGAgtisptvreflaqelkiKVEVPGLEVFPDghIVGGLDPVGEDVlr 439
Cdd:cd12117 70 AGAAYVPLDPELPAERLAFMLADAGAKVLLTDRSL-----------------AGRAGGLEVAVV--IDEALDAGPAGN-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 440 ahnhlgetdPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFF---PWMSerfgLDETSKFTMLSGIAHDPIQRDMF 516
Cdd:cd12117 129 ---------PAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVkntNYVT----LGPDDRVLQTSPLAFDASTFEIW 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 517 TPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRLQALAAN 596
Cdd:cd12117 196 GALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 597 VRIINMYGTTETQRAVSYFAIPPvsqdstfLATQKDIMPAGEGMIDVQLLVVNRNDRnvPCAVGEVGEIYVRSGGLAEGY 676
Cdd:cd12117 276 LRLVNGYGPTENTTFTTSHVVTE-------LDEVAGSIPIGRPIANTRVYVLDEDGR--PVPPGVPGELYVGGDGLALGY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 677 LDQDA-SAEKFVnnwfavnapprkdtilhpEEGFAGPEsrywkgirdRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFR 755
Cdd:cd12117 347 LNRPAlTAERFV------------------ADPFGPGE---------RLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFR 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 756 IELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGsalegyasnVPDDEddgkglvkgmkkyrrlikdIREHL 835
Cdd:cd12117 400 IELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA---------LDAAE-------------------LRAFL 451
|
570 580 590
....*....|....*....|....*....|..
gi 2234869976 836 KQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd12117 452 RERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
282-871 |
1.13e-92 |
|
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: 308.87 E-value: 1.13e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 282 FSRNARQNPDRPCVI---QSLptespdkpqgkvifSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVL 358
Cdd:cd17655 3 FEEQAEKTPDHTAVVfedQTL--------------TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGIL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 359 KAGATFSVVDPAYPPSRqIIYlgvakprgliMLKGAGTisptvREFLAQElkikvevpglEVFPDGHIVGGLDPVGEDVL 438
Cdd:cd17655 69 KAGGAYLPIDPDYPEER-IQY----------ILEDSGA-----DILLTQS----------HLQPPIAFIGLIDLLDEDTI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 439 RahnHLGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTP 518
Cdd:cd17655 123 Y---HEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFAS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 519 LFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRLQAL-AANV 597
Cdd:cd17655 200 LLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELfGTNP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 598 RIINMYGTTETQRAVSYFAIPPVsqdstflATQKDIMPAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYL 677
Cdd:cd17655 280 TITNAYGPTETTVDASIYQYEPE-------TDQQVSVPIGKPLGNTRIYILDQYGRPQP--VGVAGELYIGGEGVARGYL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 678 DQ-DASAEKFVNNWFAVNapprkdtilhpeegfagpesrywkgirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRI 756
Cdd:cd17655 351 NRpELTAEKFVDDPFVPG---------------------------ERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRI 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 757 ELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVplegsalegyasnvpdDEDDGKglvkgmkkyrrlIKDIREHLK 836
Cdd:cd17655 404 ELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV----------------SEKELP------------VAQLREFLA 455
|
570 580 590
....*....|....*....|....*....|....*
gi 2234869976 837 QKLPKHSVPSLFVPLSKMPLNPNGKIDKPALPFPD 871
Cdd:cd17655 456 RELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
279-867 |
1.68e-92 |
|
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: 308.44 E-value: 1.68e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 279 TDVFSRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVL 358
Cdd:cd17646 1 HALVAEQAARTPDAPAVVD-----------EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 359 KAGATFSVVDPAYPPSRQIIYLGVAKPRglIMLKGAGTisptvreflaqelkikvevpgLEVFPDGHIVGGLDPVGEDvl 438
Cdd:cd17646 70 KAGAAYLPLDPGYPADRLAYMLADAGPA--VVLTTADL---------------------AARLPAGGDVALLGDEALA-- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 439 rahnHLGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTP 518
Cdd:cd17646 125 ----APPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 519 LFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTHLTPAM-GQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRLQALaANV 597
Cdd:cd17646 201 LVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMlRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLAL-PGA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 598 RIINMYGTTETQRAVSYFAIPPVSQDSTflatqkdiMPAGEGMIDVQLLVVnrNDRNVPCAVGEVGEIYVRSGGLAEGYL 677
Cdd:cd17646 280 ELHNLYGPTEAAIDVTHWPVRGPAETPS--------VPIGRPVPNTRLYVL--DDALRPVPVGVPGELYLGGVQLARGYL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 678 DQDA-SAEKFVNNWFAvnapprkdtilhpeegfAGPesrywkgirdRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRI 756
Cdd:cd17646 350 GRPAlTAERFVPDPFG-----------------PGS----------RMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRV 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 757 ELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSAlegyasnVPDDEddgkglvkgmkkyrrlikDIREHLK 836
Cdd:cd17646 403 EPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAA-------GPDTA------------------ALRAHLA 457
|
570 580 590
....*....|....*....|....*....|.
gi 2234869976 837 QKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd17646 458 ERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
282-868 |
2.00e-91 |
|
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: 305.42 E-value: 2.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 282 FSRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAG 361
Cdd:cd17651 1 FERQAARTPDAPALVA-----------EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 362 ATFSVVDPAYPPsrqiiylgvakPRGLIMLKGAGtisPTVreFLAQElkikVEVPGLEVfpdghivgGLDPVGEDVLRAH 441
Cdd:cd17651 70 AAYVPLDPAYPA-----------ERLAFMLADAG---PVL--VLTHP----ALAGELAV--------ELVAVTLLDQPGA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 442 NHLGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFL 521
Cdd:cd17651 122 AAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 522 GAQLHVPTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQI---PTLLNAFFVGDVLTKRDCLRlQALAA--N 596
Cdd:cd17651 202 GATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGvrlAALRYLLTGGEQLVLTEDLR-EFCAGlpG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 597 VRIINMYGTTETQRAVSYfaipPVSQDStflATQKDIMPAGEGMIDVQLLVVNRNDRnvPCAVGEVGEIYVRSGGLAEGY 676
Cdd:cd17651 281 LRLHNHYGPTETHVVTAL----SLPGDP---AAWPAPPPIGRPIDNTRVYVLDAALR--PVPPGVPGELYIGGAGLARGY 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 677 L-DQDASAEKFVNNWFAVNApprkdtilhpeegfagpesrywkgirdRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFR 755
Cdd:cd17651 352 LnRPELTAERFVPDPFVPGA---------------------------RMYRTGDLARWLPDGELEFLGRADDQVKIRGFR 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 756 IELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPlegsalegyasnVPDDEDDGKGLvkgmkkyrrlikdiREHL 835
Cdd:cd17651 405 IELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVG------------DPEAPVDAAEL--------------RAAL 458
|
570 580 590
....*....|....*....|....*....|...
gi 2234869976 836 KQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALP 868
Cdd:cd17651 459 ATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
278-867 |
4.82e-90 |
|
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: 301.00 E-value: 4.82e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPDRPCViqslptESPDKPqgkviFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAV 357
Cdd:cd05918 1 VHDLIEERARSQPDAPAV------CAWDGS-----LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 358 LKAGATFSVVDPAYPPSRqiiylgvakprglimlkgagtisptvREFLAQELKIKVevpglevfpdghivggldpvgedV 437
Cdd:cd05918 70 LKAGGAFVPLDPSHPLQR--------------------------LQEILQDTGAKV-----------------------V 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 438 LrahnhlgetdpnvVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFT 517
Cdd:cd05918 101 L-------------TSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 518 PLFLGAQLHVPTADDIgtPGRLAEWMAESEVTVTHLTPAMGQLLSAQatrQIPTLLNAFFVGDVLTKRDclrLQALAANV 597
Cdd:cd05918 168 TLAAGGCLCIPSEEDR--LNDLAGFINRLRVTWAFLTPSVARLLDPE---DVPSLRTLVLGGEALTQSD---VDTWADRV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 598 RIINMYGTTETqravsyfAIPPVSQDSTFLATQKDImpaGEGmIDVQLLVVNRNDRNVPCAVGEVGEIYVRSGGLAEGYL 677
Cdd:cd05918 240 RLINAYGPAEC-------TIAATVSPVVPSTDPRNI---GRP-LGATCWVVDPDNHDRLVPIGAVGELLIEGPILARGYL 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 678 -DQDASAEKFVNN--WFAVNAPPRkdtilhpeegfagpesrywkgiRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGF 754
Cdd:cd05918 309 nDPEKTAAAFIEDpaWLKQEGSGR----------------------GRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQ 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 755 RIELGEIDTHLSQHPLVRENVT---LVRRDKDEEKILVSyFVPLEGSALEGYASNVPDDEDDgkglvkgmKKYRRLIKDI 831
Cdd:cd05918 367 RVELGEIEHHLRQSLPGAKEVVvevVKPKDGSSSPQLVA-FVVLDGSSSGSGDGDSLFLEPS--------DEFRALVAEL 437
|
570 580 590
....*....|....*....|....*....|....*.
gi 2234869976 832 REHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05918 438 RSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| Lys2b |
COG3320 |
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ... |
1027-1310 |
2.08e-89 |
|
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 442549 [Multi-domain] Cd Length: 265 Bit Score: 290.96 E-value: 2.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1027 TVFLTGATGFLGAFVLYDLLSRTDRvkKVICLVRGKTVEQGLERLKEGSTDRNVWSDswVSSGRLEVVTGDLGLDNFGLS 1106
Cdd:COG3320 2 TVLLTGATGFLGAHLLRELLRRTDA--RVYCLVRASDEAAARERLEALLERYGLWLE--LDASRVVVVAGDLTQPRLGLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1107 QETWNNVANEADVVLHNGALVHWVFPYEKLRSPNVLGTLTAVNLASTGKQKVFVFVSSTSAIdtehyvqlseslarGSTD 1186
Cdd:COG3320 78 EAEFQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRLKPFHYVSTIAVA--------------GPAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1187 SKGVPESDDLEGAKSaLKTGYGQSKWVSEKLLFEAGKRGLRGHIVRPGYVVGDSHTAVTNTDDFIWRLVKGCVQLGLVPD 1266
Cdd:COG3320 144 RSGVFEEDDLDEGQG-FANGYEQSKWVAEKLVREARERGLPVTIYRPGIVVGDSRTGETNKDDGFYRLLKGLLRLGAAPG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2234869976 1267 INNS-INMVPVDHVARitSLAAVSPLPDAPLSVCHVTARPLPTFN 1310
Cdd:COG3320 223 LGDArLNLVPVDYVAR--AIVHLSRQPEAAGRTFHLTNPQPLSLG 265
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-957 |
8.11e-89 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 321.14 E-value: 8.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 17 PSISLPTDYPRPTGANKLIESVHTaQLSEQTSLSLLKLAlysededheeeeedvesSHKRPSAFHLLLAAFIVLLHRYTG 96
Cdd:PRK12316 2801 PVLELPLDRPRPALQSHRGARLDV-ALDVALSRELLALA-----------------RREGVTLFMLLLASFQVLLHRYSG 2862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 97 DTDIVVGSSSASAREP------------LILRLSVDPADPYWAVVRHVQQTEKEAEA-DALPYDVITQALNKGKEDSlDR 163
Cdd:PRK12316 2863 QSDIRVGVPIANRNRAeterligffvntQVLRAQVDAQLAFRDLLGQVKEQALGAQAhQDLPFEQLVEALQPERSLS-HS 2941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 164 PLFRVRFFDETDE---PTNNFIGSTSVTSDLTVFITRPPASTRASiAPRLSLRVLYNSLLFTSARITSFLDQLSVFLRKV 240
Cdd:PRK12316 2942 PLFQVMYNHQSGEraaAQLPGLHIESFAWDGAATQFDLALDTWES-AEGLGASLTYATDLFDARTVERLARHWQNLLRGM 3020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 241 AATPLSPVGSVPLLTPSQKAVLPNptgdlnwcGWkgaitdvfSRNARQNPDRPCVIQSLPTESPDKPQ------GKVIFS 314
Cdd:PRK12316 3021 VENPQRSVDELAMLDAEERGQLLE--------AW--------NATAAEYPLERGVHRLFEEQVERTPDavalafGEQRLS 3084
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 315 YGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIylgvakprgliMLKGA 394
Cdd:PRK12316 3085 YAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAY-----------MLEDS 3153
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 395 GtisptVREFLAQELKIKVEVPGLEVFpdghivggldpvgeDVLRAHNHLGETDPNVVLGPDSIGTLSFTSGSTGIPKGV 474
Cdd:PRK12316 3154 G-----AQLLLSQSHLRLPLAQGVQVL--------------DLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGV 3214
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 475 RGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTHLT 554
Cdd:PRK12316 3215 GIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAY 3294
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 555 PAMGQLLSAQATRQIPTLLNAFFVGDVLTKRDCLrlQALAANVRIINMYGTTETqravsyfAIPPVSQDSTflATQKDIM 634
Cdd:PRK12316 3295 PSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQ--QQVFAGLPLYNLYGPTEA-------TITVTHWQCV--EEGKDAV 3363
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 635 PAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWFAVNApprkdtilhpeegfagpe 713
Cdd:PRK12316 3364 PIGRPIANRACYILDGSLEPVP--VGALGELYLGGEGLARGYHNRpGLTAERFVPDPFVPGE------------------ 3423
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 714 srywkgirdRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLvrrdKDEEKILVSYFV 793
Cdd:PRK12316 3424 ---------RLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVV 3490
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 794 PLEGSAlegyasnvpddeddgkglvkgmkKYRRLIKdirEHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALPFPDTA 873
Cdd:PRK12316 3491 PEDEAG-----------------------DLREALK---AHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAA 3544
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 874 QASyaAGPSAPgASATEIAMQKIWSTILpNAPQpIPTDESFFDLGGHSILATRLIFEIRKVFVVNAPLGLiFEKPTIAGL 953
Cdd:PRK12316 3545 LLQ--QDYVAP-VNELERRLAAIWADVL-KLEQ-VGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDL-FQHQTIQGL 3618
|
....
gi 2234869976 954 VEAV 957
Cdd:PRK12316 3619 ARVA 3622
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-963 |
2.04e-87 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 316.51 E-value: 2.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 82 LLLAAFIVLLHRYTGDTDIVVGSSSASAREPL----------ILRLSVDPA-DPYWAVVRHVQQTekeaeadalpydvit 150
Cdd:PRK12316 1794 LVQAAWLLLLQRYTGQETVAFGATVAGRPAELpgieqqiglfINTLPVIAApRPDQSVADWLQEV--------------- 1858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 151 QALNKGKEDSLDRPLFRVRFFDEtdeptnnfIGSTSVTSDLTVFITRPPASTRASIAP---------------------- 208
Cdd:PRK12316 1859 QALNLALREHEHTPLYDIQRWAG--------QGGEALFDSLLVFENYPVAEALKQGAPaglvfgrvsnheqtnypltlav 1930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 209 ----RLSLRVLYNSLLFTSARITSFLDQLSVFLRKVAATPLSPVGSVPLLTPSQKAVLpnptgDLNWCGWKGA------I 278
Cdd:PRK12316 1931 tlgeTLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRI-----LADWDRTPEAyprgpgV 2005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 279 TDVFSRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVL 358
Cdd:PRK12316 2006 HQRIAEQAARAPEAIAVVF-----------GDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVL 2074
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 359 KAGATFSVVDPAYPPSRqIIYlgvakprgliMLKGAGTISPTVREFLAQELKIKVEVPGLEvfpdghivggLDPVGEdvL 438
Cdd:PRK12316 2075 KAGGAYVPLDPNYPAER-LAY----------MLEDSGAALLLTQRHLLERLPLPAGVARLP----------LDRDAE--W 2131
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 439 RAHnhlGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTP 518
Cdd:PRK12316 2132 ADY---PDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHP 2208
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 519 LFLGAQLHVpTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQ--IPTLLNAFFVGDVLTKRDCLRLQALAAN 596
Cdd:PRK12316 2209 LLNGARVLI-RDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDgrPPAVRVYCFGGEAVPAASLRLAWEALRP 2287
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 597 VRIINMYGTTETQRAVSYFAIPPVSQDSTFLatqkdiMPAGEGMIDVQLLVVNrNDRNvPCAVGEVGEIYVRSGGLAEGY 676
Cdd:PRK12316 2288 VYLFNGYGPTEAVVTPLLWKCRPQDPCGAAY------VPIGRALGNRRAYILD-ADLN-LLAPGMAGELYLGGEGLARGY 2359
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 677 LDQDA-SAEKFVNNWFAvnapprkdtilhpeegfagpesrywkGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFR 755
Cdd:PRK12316 2360 LNRPGlTAERFVPDPFS--------------------------ASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFR 2413
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 756 IELGEIDTHLSQHPLVRENVtLVRRDKDEEKILVSYFVPlegsalegyasnvpddeDDGKGLvkgmkkyrrLIKDIREHL 835
Cdd:PRK12316 2414 IELGEIEARLQAHPAVREAV-VVAQDGASGKQLVAYVVP-----------------DDAAED---------LLAELRAWL 2466
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 836 KQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALPFPDTAQASYAAgpsAPGASATEIAMQKIWSTILpnAPQPIPTDESFF 915
Cdd:PRK12316 2467 AARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAY---VAPQEGLEQRLAAIWQAVL--KVEQVGLDDHFF 2541
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 2234869976 916 DLGGHSILATRLIFEIRKVFVVNAPLGLIFEKPTIAGLVEAVDALRNA 963
Cdd:PRK12316 2542 ELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTS 2589
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
314-867 |
3.58e-84 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 283.43 E-value: 3.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 314 SYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPRGLImlkg 393
Cdd:cd17643 14 TYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLL---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 394 agtisptvreflaqelkikvevpglevfpdghivggldpvgedvlrahnhlgeTDPnvvlgpDSIGTLSFTSGSTGIPKG 473
Cdd:cd17643 90 -----------------------------------------------------TDP------DDLAYVIYTSGSTGRPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 474 VRGRHFSLTHFFpWMSER-FGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTH 552
Cdd:cd17643 111 VVVSHANVLALF-AATQRwFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLN 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 553 LTP-AMGQLLSA--QATRQIPTLLNAFFVGDVLTKRdclRLQALAANV-----RIINMYGTTETQRAVSYFaipPVSQDS 624
Cdd:cd17643 190 QTPsAFYQLVEAadRDGRDPLALRYVIFGGEALEAA---MLRPWAGRFgldrpQLVNMYGITETTVHVTFR---PLDAAD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 625 TFLATQKDImpaGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQDA-SAEKFVNNWFavNAPPRkdtil 703
Cdd:cd17643 264 LPAAAASPI---GRPLPGLRVYVLDADGRPVP--PGVVGELYVSGAGVARGYLGRPElTAERFVANPF--GGPGS----- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 704 hpeegfagpesrywkgirdRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKD 783
Cdd:cd17643 332 -------------------RMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEP 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 784 EEKILVSYFVPLEGSAlegyasnvpddeddgkglvkgmkkyrRLIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKID 863
Cdd:cd17643 393 GDTRLVAYVVADDGAA--------------------------ADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLD 446
|
....
gi 2234869976 864 KPAL 867
Cdd:cd17643 447 RAAL 450
|
|
| NAD_binding_4 |
pfam07993 |
Male sterility protein; This family represents the C-terminal region of the male sterility ... |
1030-1283 |
9.97e-84 |
|
Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.
Pssm-ID: 462334 [Multi-domain] Cd Length: 257 Bit Score: 274.49 E-value: 9.97e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1030 LTGATGFLGAFVLYDLLSRTDRVKKVICLVRGKTVEQGLERLKEGSTDRNVWSDSWVS-SGRLEVVTGDLGLDNFGLSQE 1108
Cdd:pfam07993 1 LTGATGFLGKVLLEKLLRSTPDVKKIYLLVRAKDGESALERLRQELEKYPLFDALLKEaLERIVPVAGDLSEPNLGLSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1109 TWNNVANEADVVLHNGALVHWVFPYEKLRSPNVLGTLTAVNLASTGKQK-VFVFVsSTSAIDTEHYVQLSESLARGSTDs 1187
Cdd:pfam07993 81 DFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQLkPFHHV-STAYVNGERGGLVEEKPYPEGED- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1188 kGVPESDDLEGAKSALKTGYGQSKWVSEKLLFEAGKRGLRGHIVRPGYVVGDSHTAVTNTDDFIWRLVKGCVQLGLVPDI 1267
Cdd:pfam07993 159 -DMLLDEDEPALLGGLPNGYTQTKWLAEQLVREAARRGLPVVIYRPSIITGEPKTGWINNFDFGPRGLLGGIGKGVLPSI 237
|
250 260
....*....|....*....|
gi 2234869976 1268 NNS----INMVPVDHVARIT 1283
Cdd:pfam07993 238 LGDpdavLDLVPVDYVANAI 257
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
16-963 |
3.94e-80 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 293.61 E-value: 3.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 16 LPSISLPTDYPRpTGANKLIESVHTAQLSEQTSLSLLKLALysededheeeeedvessHKRPSAFHLLLAAFIVLLHRYT 95
Cdd:PRK05691 877 QPVLELATDHPR-SARQAHSAARYSLRVDASLSEALRGLAQ-----------------AHQATLFMVLLAAFQALLHRYS 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 96 GDTDIVVGSSSASAREP------------LILRLSVDPADPYWAVVRHVQQTEKEAEADA-LPYDVITQALNKGKEDSLd 162
Cdd:PRK05691 939 GQGDIRIGVPNANRPRLetqglvgffintQVLRAQLDGRLPFTALLAQVRQATLGAQAHQdLPFEQLVEALPQAREQGL- 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 163 rplFRVRFFDETDEPtnnfigstSVTSDLTVFITR--PPASTRASI----------APRLSLRVLYNSLLFTSARITSFL 230
Cdd:PRK05691 1018 ---FQVMFNHQQRDL--------SALRRLPGLLAEelPWHSREAKFdlqlhseedrNGRLTLSFDYAAELFDAATIERLA 1086
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 231 DQLSVFLRKVAATPLSPVGSVPLLTPSQKAVLpnptgdLNWCGWKGA-----ITDVFSRNARQNPDRPCVIQslptespd 305
Cdd:PRK05691 1087 EHFLALLEQVCEDPQRALGDVQLLDAAERAQL------AQWGQAPCApaqawLPELLNEQARQTPERIALVW-------- 1152
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 306 kpQGKVIfSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRqIIYlgvakp 385
Cdd:PRK05691 1153 --DGGSL-DYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER-LAY------ 1222
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 386 rgliMLKGAGTisptvrEFLAQELKIKVEVPGLEvfpdghivgGLDPVGEDVLRAHNHlGETDPNVVLGPDSIGTLSFTS 465
Cdd:PRK05691 1223 ----MLADSGV------ELLLTQSHLLERLPQAE---------GVSAIALDSLHLDSW-PSQAPGLHLHGDNLAYVIYTS 1282
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 466 GSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAE 545
Cdd:PRK05691 1283 GSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQ 1362
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 546 SEVTVTHLTPAMGQL-----LSAQATRqiptLLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAVSYFAIPpv 620
Cdd:PRK05691 1363 YGVTTLHFVPPLLQLfidepLAAACTS----LRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQ-- 1436
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 621 sqdstflATQKDIMPAGEGMIDVQLLVvnRNDRNVPCAVGEVGEIYVRSGGLAEGYLDQDA-SAEKFVNNWFAvnapprk 699
Cdd:PRK05691 1437 -------AEDGERSPIGRPLGNVLCRV--LDAELNLLPPGVAGELCIGGAGLARGYLGRPAlTAERFVPDPLG------- 1500
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 700 dtilhpEEGfagpesrywkgirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVR 779
Cdd:PRK05691 1501 ------EDG-------------ARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR 1561
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 780 RDkdeekilvsyfvpLEGSALEGY--ASNVPDDEDDgkglvkgmkkyrrlikDIREHLKQKLPKHSVPSLFVPLSKMPLN 857
Cdd:PRK05691 1562 EG-------------AAGAQLVGYytGEAGQEAEAE----------------RLKAALAAELPEYMVPAQLIRLDQMPLG 1612
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 858 PNGKIDKPALPFPDTAQASYAAgPSapgasaTEIAMQ--KIWSTILpNAPQpIPTDESFFDLGGHSILATRLIFEIRKVF 935
Cdd:PRK05691 1613 PSGKLDRRALPEPVWQQREHVE-PR------TELQQQiaAIWREVL-GLPR-VGLRDDFFALGGHSLLATQIVSRTRQAC 1683
|
970 980
....*....|....*....|....*...
gi 2234869976 936 VVNAPLGLIFEKPTIAGLVEAVDALRNA 963
Cdd:PRK05691 1684 DVELPLRALFEASELGAFAEQVARIQAA 1711
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
313-867 |
1.15e-79 |
|
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: 271.09 E-value: 1.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 313 FSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPRGLImlk 392
Cdd:cd12116 13 LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 393 gagtISPTVREFLAqelkikvevpglevfpdgHIVGGLDPVGEDVLRAHNHLGETDPnvvlgPDSIGTLSFTSGSTGIPK 472
Cdd:cd12116 90 ----TDDALPDRLP------------------AGLPVLLLALAAAAAAPAAPRTPVS-----PDDLAYVIYTSGSTGRPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 473 GVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTH 552
Cdd:cd12116 143 GVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 553 LTPAMGQLLSAQATRQIPTLlNAFFVGDVLTKRDCLRLQALAAnvRIINMYGTTETqravsyfaippvsqdsTFLATQKD 632
Cdd:cd12116 223 ATPATWRMLLDAGWQGRAGL-TALCGGEALPPDLAARLLSRVG--SLWNLYGPTET----------------TIWSTAAR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 633 I------MPAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQDA-SAEKFVNNWFAvnaPPRKdtilhp 705
Cdd:cd12116 284 VtaaagpIPIGRPLANTQVYVLDAALRPVP--PGVPGELYIGGDGVAQGYLGRPAlTAERFVPDPFA---GPGS------ 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 706 eegfagpesrywkgirdRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDkDEE 785
Cdd:cd12116 353 -----------------RLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRED-GGD 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 786 KILVSYFVPLEGSALegyasnvpdDEDdgkglvkgmkkyrrlikDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKP 865
Cdd:cd12116 415 RRLVAYVVLKAGAAP---------DAA-----------------ALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRK 468
|
..
gi 2234869976 866 AL 867
Cdd:cd12116 469 AL 470
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
286-867 |
2.43e-79 |
|
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: 269.50 E-value: 2.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 286 ARQNPDRPCVIqslptESPDKpqgkviFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFS 365
Cdd:cd05945 1 AAANPDRPAVV-----EGGRT------LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 366 VVDPAYPPSRQIIYLGVAKPRGLImlkgagtisptvreflaqelkikvevpgleVFPDghivggldpvgedvlrahnhlg 445
Cdd:cd05945 70 PLDASSPAERIREILDAAKPALLI------------------------------ADGD---------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 446 etDPNVVLgpdsigtlsFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQL 525
Cdd:cd05945 98 --DNAYII---------FTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 526 HVPTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQATR---QIPTLLNAFFVGDVLTKRDCLRLQALAANVRIINM 602
Cdd:cd05945 167 VPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFtpeSLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNT 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 603 YGTTETQRAVSYFAIPPVSqdstflATQKDIMPAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYL-DQDA 681
Cdd:cd05945 247 YGPTEATVAVTYIEVTPEV------LDGYDRLPIGYAKPGAKLVILDEDGRPVP--PGEKGELVISGPSVSKGYLnNPEK 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 682 SAEKFvnnwfavnapprkdtilHPEEGfagpesrywkgirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEI 761
Cdd:cd05945 319 TAAAF-----------------FPDEG-------------QRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEI 368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 762 DTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSAlegyasnvpddeddgkglvkgmkkyRRLIKDIREHLKQKLPK 841
Cdd:cd05945 369 EAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAE-------------------------AGLTKAIKAELAERLPP 423
|
570 580
....*....|....*....|....*.
gi 2234869976 842 HSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05945 424 YMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
304-868 |
1.07e-78 |
|
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: 267.70 E-value: 1.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 304 PDKP---QGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRqIIYl 380
Cdd:cd17649 1 PDAValvFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAER-LRY- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 381 gvakprgliMLKGAGtisptVREFLAQElkikvevpglevfpdghivggldpvgedvlrahnhlgetdpnvvlgPDSIGT 460
Cdd:cd17649 79 ---------MLEDSG-----AGLLLTHH----------------------------------------------PRQLAY 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 461 LSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLA 540
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELA 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 541 EWMAESEVTVTHLTPAMGQLLSAQA---TRQIPTLLNAFFVGDVLTKRDCLRlQALAANVRIINMYGTTETQRAVSYFAI 617
Cdd:cd17649 179 EMVRELGVTVLDLPPAYLQQLAEEAdrtGDGRPPSLRLYIFGGEALSPELLR-RWLKAPVRLFNAYGPTEATVTPLVWKC 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 618 PPvsqDSTFLATQkdiMPAGEGMIDVQLLVVNrNDRNvPCAVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVnnwfavnap 696
Cdd:cd17649 258 EA---GAARAGAS---MPIGRPLGGRSAYILD-ADLN-PVPVGVTGELYIGGEGLARGYLGRpELTAERFV--------- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 697 prkdtilhpEEGFAGPESRywkgirdrMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVREnVT 776
Cdd:cd17649 321 ---------PDPFGAPGSR--------LYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVRE-AA 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 777 LVRRDKDEEKILVSYFVPLEGSALEgyasnvpddEDDGKglvkgmkkyrrlikdIREHLKQKLPKHSVPSLFVPLSKMPL 856
Cdd:cd17649 383 VVALDGAGGKQLVAYVVLRAAAAQP---------ELRAQ---------------LRTALRASLPDYMVPAHLVFLARLPL 438
|
570
....*....|..
gi 2234869976 857 NPNGKIDKPALP 868
Cdd:cd17649 439 TPNGKLDRKALP 450
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
309-868 |
3.10e-78 |
|
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: 266.04 E-value: 3.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 309 GKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRqIIYLgvakprgl 388
Cdd:cd17652 9 GDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAER-IAYM-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 389 imlkgagtisptvreflaqelkikvevpglevfpdghivggldpvgedvlrahnhLGETDPNVVLG-PDSIGTLSFTSGS 467
Cdd:cd17652 80 -------------------------------------------------------LADARPALLLTtPDNLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 468 TGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESE 547
Cdd:cd17652 105 TGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 548 VTVTHLTPAmgqLLSAQATRQIPTLLNAFFVGDV----LTKRdclrlqaLAANVRIINMYGTTETQRAVSYFAIPPVSqd 623
Cdd:cd17652 185 ITHVTLPPA---ALAALPPDDLPDLRTLVVAGEAcpaeLVDR-------WAPGRRMINAYGPTETTVCATMAGPLPGG-- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 624 stflatqkDIMPAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVnnwfavnapprkdti 702
Cdd:cd17652 253 --------GVPPIGRPVPGTRVYVLDARLRPVP--PGVPGELYIAGAGLARGYLNRpGLTAERFV--------------- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 703 LHPeegFAGPESRywkgirdrMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDK 782
Cdd:cd17652 308 ADP---FGAPGSR--------MYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDR 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 783 DEEKILVSYFVPlegsalegyasnVPDDEDDGKGLvkgmkkyrrlikdiREHLKQKLPKHSVPSLFVPLSKMPLNPNGKI 862
Cdd:cd17652 377 PGDKRLVAYVVP------------APGAAPTAAEL--------------RAHLAERLPGYMVPAAFVVLDALPLTPNGKL 430
|
....*.
gi 2234869976 863 DKPALP 868
Cdd:cd17652 431 DRRALP 436
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
280-867 |
5.56e-76 |
|
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: 259.94 E-value: 5.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 280 DVFSRNARQNPDRPCVIQslptespdkPQGKVifSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLK 359
Cdd:cd12115 3 DLVEAQAARTPDAIALVC---------GDESL--TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 360 AGATFSVVDPAYPPSRQiiylgvakprglimlkgagtisptvreflaqelkikvevpglevfpdGHIVggldpvgEDVLR 439
Cdd:cd12115 72 AGAAYVPLDPAYPPERL-----------------------------------------------RFIL-------EDAQA 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 440 AHnhlgetdpnVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDEtskftmLSGI-AHDPIQRD---- 514
Cdd:cd12115 98 RL---------VLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEE------LAGVlASTSICFDlsvf 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 515 -MFTPLFLGAQLHVptADDIGTPGRLAewmAESEVTVTHLTP-AMGQLLSAQAtrqIPTLLNAF-FVGDVLTKRDCLRLQ 591
Cdd:cd12115 163 eLFGPLATGGKVVL--ADNVLALPDLP---AAAEVTLINTVPsAAAELLRHDA---LPASVRVVnLAGEPLPRDLVQRLY 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 592 ALAANVRIINMYGTTETQRAVSYFAIPPVSQDSTflatqkdimPAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGG 671
Cdd:cd12115 235 ARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEV---------SIGRPLANTQAYVLDRALQPVP--LGVPGELYIGGAG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 672 LAEGYLDQ-DASAEKFVNNWFAVNApprkdtilhpeegfagpesrywkgirdRMYRSGDLGRYLPDGTVECSGRADDQVK 750
Cdd:cd12115 304 VARGYLGRpGLTAERFLPDPFGPGA---------------------------RLYRTGDLVRWRPDGLLEFLGRADNQVK 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 751 IRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALegyasnvpddeddgkglvkgmkkyrrLIKD 830
Cdd:cd12115 357 VRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG--------------------------LVED 410
|
570 580 590
....*....|....*....|....*....|....*..
gi 2234869976 831 IREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd12115 411 LRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
314-867 |
7.72e-75 |
|
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: 256.63 E-value: 7.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 314 SYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQiiylgvakprgLIMLKG 393
Cdd:cd17650 14 TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL-----------QYMLED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 394 AGTisptvreflaqelkikvevpglevfpdghivggldpvgedvlrahnhlgetdPNVVLGPDSIGTLSFTSGSTGIPKG 473
Cdd:cd17650 83 SGA----------------------------------------------------KLLLTQPEDLAYVIYTSGTTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 474 VRGRHFSLTH-FFPWmSERFGLDE-TSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVT 551
Cdd:cd17650 111 VMVEHRNVAHaAHAW-RREYELDSfPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLM 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 552 HLTPAMGQLLSAQATRQIPTL--LNAFFVG-DVLTKRDCLRLQA-LAANVRIINMYGTTETQRAVSYFaippvsQDSTFL 627
Cdd:cd17650 190 ESTPALIRPVMAYVYRNGLDLsaMRLLIVGsDGCKAQDFKTLAArFGQGMRIINSYGVTEATIDSTYY------EEGRDP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 628 ATQKDIMPAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYL-DQDASAEKFVNNWFAVNApprkdtilhpe 706
Cdd:cd17650 264 LGDSANVPIGRPLPNTAMYVLDERLQPQP--VGVAGELYIGGAGVARGYLnRPELTAERFVENPFAPGE----------- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 707 egfagpesrywkgirdRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEK 786
Cdd:cd17650 331 ----------------RMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEA 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 787 ILVSYFVPlegsalegyaSNVPDdeddgkglvkgmkkyrrlIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPA 866
Cdd:cd17650 395 RLCAYVVA----------AATLN------------------TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRA 446
|
.
gi 2234869976 867 L 867
Cdd:cd17650 447 L 447
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
322-868 |
2.35e-74 |
|
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: 255.82 E-value: 2.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 322 SNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRqIIYlgvakprgliMLKGAGtisptV 401
Cdd:cd17644 35 ANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQER-LTY----------ILEDAQ-----I 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 402 REFLAQelkikvevpglevfpdghivggldpvgedvlrahnhlgetdpnvvlgPDSIGTLSFTSGSTGIPKGVRGRHFSL 481
Cdd:cd17644 99 SVLLTQ-----------------------------------------------PENLAYVIYTSGSTGKPKGVMIEHQSL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 482 THFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLL 561
Cdd:cd17644 132 VNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 562 S---AQATRQIPTLLNAFFVG--DVLTKRDCLRLQALAANVRIINMYGTTETQRAVSYFAIppvSQDSTFLATQkdiMPA 636
Cdd:cd17644 212 VlelLLSTIDLPSSLRLVIVGgeAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRL---TQLTERNITS---VPI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 637 GEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWFAVNAPprkdtilhpeegfagpesr 715
Cdd:cd17644 286 GRPIANTQVYILDENLQPVP--VGVPGELHIGGVGLARGYLNRpELTAEKFISHPFNSSES------------------- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 716 ywkgirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPl 795
Cdd:cd17644 345 ------ERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVP- 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2234869976 796 egsalegYASNVPDdeddgkglvkgmkkyrrlIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALP 868
Cdd:cd17644 418 -------HYEESPS------------------TVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
278-867 |
9.48e-68 |
|
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: 236.25 E-value: 9.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAV 357
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF-----------GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 358 LKAGATFSVVDPAYPPsRQIIYLgvakprglimlkgagtisptvreflaqelkikvevpglevfpdghivggldpvgedv 437
Cdd:COG0318 70 LRAGAVVVPLNPRLTA-EELAYI--------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 438 lrahnhLGETDPNVVLgpdsIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHD-PIQRDMF 516
Cdd:COG0318 92 ------LEDSGARALV----TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLL 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 517 TPLFLGAQLHVPTADDigtPGRLAEWMAESEVTVTHLTPAMGQLLSAQ---ATRQIPTLLNAFFVGDVLTKRDCLRLQAL 593
Cdd:COG0318 162 APLLAGATLVLLPRFD---PERVLELIERERVTVLFGVPTMLARLLRHpefARYDLSSLRLVVSGGAPLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 594 aANVRIINMYGTTETQRAVSYfaiPPVSQDSTFLATqkdimpAGEGMIDVQLLVVNRNDRnvPCAVGEVGEIYVRSGGLA 673
Cdd:COG0318 239 -FGVRIVEGYGLTETSPVVTV---NPEDPGERRPGS------VGRPLPGVEVRIVDEDGR--ELPPGEVGEIVVRGPNVM 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 674 EGYL-DQDASAEKFVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLGRYLPDGTVECSGRADDQVKIR 752
Cdd:COG0318 307 KGYWnDPEATAEAFRDGWL----------------------------------RTGDLGRLDEDGYLYIVGRKKDMIISG 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 753 GFRIELGEIDTHLSQHPLVRE-NVTLVRRDKDEEKILVsYFVPLEGSALegyasnvpdDEDdgkglvkgmkkyrrlikDI 831
Cdd:COG0318 353 GENVYPAEVEEVLAAHPGVAEaAVVGVPDEKWGERVVA-FVVLRPGAEL---------DAE-----------------EL 405
|
570 580 590
....*....|....*....|....*....|....*.
gi 2234869976 832 REHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:COG0318 406 RAFLRERLARYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
314-868 |
5.11e-67 |
|
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: 235.06 E-value: 5.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 314 SYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLgvakprglimlkg 393
Cdd:cd17656 15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 394 agtISPTVREFLAQ-ELKIKVEVPGLEVFPDGHIVGGLDPVGEDVLRAHNHLGetdpnvvlgpdsigTLSFTSGSTGIPK 472
Cdd:cd17656 82 ---LDSGVRVVLTQrHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLL--------------YIIYTSGTTGKPK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 473 GVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTH 552
Cdd:cd17656 145 GVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 553 LTPAMGQLLSA--QATRQIPTLL-NAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQrAVSYFAIPPVsqdstflAT 629
Cdd:cd17656 225 LPVAFLKFIFSerEFINRFPTCVkHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETH-VVTTYTINPE-------AE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 630 QKDIMPAGEGMIDVQLLVVNRNDRNVPCavGEVGEIYVRSGGLAEGYLDQDA-SAEKFVNNWFAVNApprkdtilhpeeg 708
Cdd:cd17656 297 IPELPPIGKPISNTWIYILDQEQQLQPQ--GIVGELYISGASVARGYLNRQElTAEKFFPDPFDPNE------------- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 709 fagpesrywkgirdRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKIL 788
Cdd:cd17656 362 --------------RMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYL 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 789 VSYFVPLEgsalegyasNVPddeddgkglvkgmkkyrrlIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALP 868
Cdd:cd17656 428 CAYFVMEQ---------ELN-------------------ISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
80-953 |
2.84e-66 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 248.93 E-value: 2.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 80 FHLLLAAFIVLLHRYTGDTDIVVGSSSASAREP----LI--------LRLSVDPADPYWAVVRHVQQTEKEAEADA-LPY 146
Cdd:PRK05691 1976 FMTMTATLAALLYRYSGQRDLRIGAPVANRIRPesegLIgaflntqvLRCQLDGQMSVSELLEQVRQTVIEGQSHQdLPF 2055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 147 DVITQALNKGKEDSLDrPLFRV-----RF-FDETDE----PTNNFIGSTSVTS-DLTVFITrppastraSIAPRLSLRVL 215
Cdd:PRK05691 2056 DHLVEALQPPRSAAYN-PLFQVmcnvqRWeFQQSRQlagmTVEYLVNDARATKfDLNLEVT--------DLDGRLGCCLT 2126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 216 YNSLLFTSARITSFLDQLSVFLRKVAATPLSPVGSVPLLTPSQKAVLPNPTG------DLNWCgwkgaITDVFSRNARQN 289
Cdd:PRK05691 2127 YSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAgeageaRLDQT-----LHGLFAAQAART 2201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 290 PDRPCVIQSLPTespdkpqgkviFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDP 369
Cdd:PRK05691 2202 PQAPALTFAGQT-----------LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDP 2270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 370 AYPPSRqIIYLgvAKPRGLIMLKGAGTISPTVREFLAQELKIKVE--VPGLEVFPDGHIvggldpvgedvlrahnhlget 447
Cdd:PRK05691 2271 EYPLER-LHYM--IEDSGIGLLLSDRALFEALGELPAGVARWCLEddAAALAAYSDAPL--------------------- 2326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 448 dPNVVLgPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLhV 527
Cdd:PRK05691 2327 -PFLSL-PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARV-V 2403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 528 PTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLS---AQATRQIPTLLnAFFVGDVLTKRDCLRLQALAANVRIINMYG 604
Cdd:PRK05691 2404 LRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAqwlAGQGEQLPVRM-CITGGEALTGEHLQRIRQAFAPQLFFNAYG 2482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 605 TTETqravsyfAIPPVSqdstflATQKDIMPAGEGMIDVQLLVVNR-----NDRNVPCAVGEVGEIYVRSGGLAEGYLDQ 679
Cdd:PRK05691 2483 PTET-------VVMPLA------CLAPEQLEEGAASVPIGRVVGARvayilDADLALVPQGATGELYVGGAGLAQGYHDR 2549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 680 -DASAEKFVNNWFAVNApprkdtilhpeegfagpesrywkgirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIEL 758
Cdd:PRK05691 2550 pGLTAERFVADPFAADG--------------------------GRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIEL 2603
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 759 GEIDTHLSQHPLVRENVTLVrRDKDEEKILVSYFVplegsalegyaSNVPDDEDDGKGLVKgmkkyrrliKDIREHLKQK 838
Cdd:PRK05691 2604 GEIESRLLEHPAVREAVVLA-LDTPSGKQLAGYLV-----------SAVAGQDDEAQAALR---------EALKAHLKQQ 2662
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 839 LPKHSVPSLFVPLSKMPLNPNGKIDKPALPFPDTAQASYAAgpSAPgASATEIAMQKIWSTILpNAPQpIPTDESFFDLG 918
Cdd:PRK05691 2663 LPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAY--QAP-RSELEQQLAQIWREVL-NVER-VGLGDNFFELG 2737
|
890 900 910
....*....|....*....|....*....|....*
gi 2234869976 919 GHSILATRLIFEIRKVFVVNAPLGLiFEKPTIAGL 953
Cdd:PRK05691 2738 GDSILSIQVVSRARQLGIHFSPRDL-FQHQTVQTL 2771
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
281-868 |
1.89e-65 |
|
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: 229.36 E-value: 1.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 281 VFSRNARQNPDRPCVI---QSLptespdkpqgkvifSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAV 357
Cdd:cd17645 3 LFEEQVERTPDHVAVVdrgQSL--------------TYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 358 LKAGATFSVVDPAYPPSRQiiylgvakprglimlkgagtisptvrEFLAQELKIKVevpglevfpdghivggldpvgedv 437
Cdd:cd17645 69 LKAGGAYVPIDPDYPGERI--------------------------AYMLADSSAKI------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 438 lrahnhlgetdpnVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFT 517
Cdd:cd17645 99 -------------LLTNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFP 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 518 PLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTHL-TPAMGQLLSAQATrQIPTLLNAffvGDVLTKrdclrlqALAAN 596
Cdd:cd17645 166 HLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLpTGAAEQFMQLDNQ-SLRVLLTG---GDKLKK-------IERKG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 597 VRIINMYGTTETQRAVSYFAIPPVSQDstflatqkdiMPAGEGMIDVQLLVVNRNdrNVPCAVGEVGEIYVRSGGLAEGY 676
Cdd:cd17645 235 YKLVNNYGPTENTVVATSFEIDKPYAN----------IPIGKPIDNTRVYILDEA--LQLQPIGVAGELCIAGEGLARGY 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 677 LDQ-DASAEKFVNNWFAvnapprkdtilhPEEgfagpesrywkgirdRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFR 755
Cdd:cd17645 303 LNRpELTAEKFIVHPFV------------PGE---------------RMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYR 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 756 IELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPlegsalegyasnvPDDEDDGKglvkgmkkyrrlikdIREHL 835
Cdd:cd17645 356 IEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA-------------PEEIPHEE---------------LREWL 407
|
570 580 590
....*....|....*....|....*....|...
gi 2234869976 836 KQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALP 868
Cdd:cd17645 408 KNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
290-867 |
2.00e-64 |
|
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: 227.54 E-value: 2.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 290 PDRPCVIQSLPTespdkpqgkviFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDP 369
Cdd:cd12114 1 PDATAVICGDGT-----------LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 370 AYPPSRQIIYLGVAKPRGLIMLKGagtisptvrefLAQELkikVEVPGLEVFPDGHIVGGLDPvgedvlrahnhlgetdP 449
Cdd:cd12114 70 DQPAARREAILADAGARLVLTDGP-----------DAQLD---VAVFDVLILDLDALAAPAPP----------------P 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 450 NVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPT 529
Cdd:cd12114 120 PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 530 ADDIGTPGRLAEWMAESEVTVTHLTPAMGQLL---SAQATRQIPTLLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTT 606
Cdd:cd12114 200 EARRRDPAHWAELIERHGVTLWNSVPALLEMLldvLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGAT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 607 ETQRAVSYFAIPPVSQDstflatQKDImPAGEGMIDVQLLVVNRNDRnvPCAVGEVGEIYVRSGGLAEGYL-DQDASAEK 685
Cdd:cd12114 280 EASIWSIYHPIDEVPPD------WRSI-PYGRPLANQRYRVLDPRGR--DCPDWVPGELWIGGRGVALGYLgDPELTAAR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 686 FVNnwfavnapprkdtilHPEEGfagpesrywkgirdRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHL 765
Cdd:cd12114 351 FVT---------------HPDGE--------------RLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAAL 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 766 SQHPLVRENVTLVRRDkDEEKILVSYFVPLEGSAlegyasnvPDDEDdgkglvkgmkkyrrlikDIREHLKQKLPKHSVP 845
Cdd:cd12114 402 QAHPGVARAVVVVLGD-PGGKRLAAFVVPDNDGT--------PIAPD-----------------ALRAFLAQTLPAYMIP 455
|
570 580
....*....|....*....|..
gi 2234869976 846 SLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd12114 456 SRVIALEALPLTANGKVDRAAL 477
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
282-752 |
4.93e-64 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 224.11 E-value: 4.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 282 FSRNARQNPDRPCVIqslptespdkPQGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAG 361
Cdd:pfam00501 1 LERQAARTPDKTALE----------VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 362 ATFSVVDPAYPPSRQIIYLGVAKPRGLImlkgagtispTVREFLAQELKI---KVEVPGLEVFPDGHIVGGLDPVGEDVL 438
Cdd:pfam00501 71 AVYVPLNPRLPAEELAYILEDSGAKVLI----------TDDALKLEELLEalgKLEVVKLVLVLDRDPVLKEEPLPEEAK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 439 RAHNHLgetDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMS----ERFGLDETSKFTMLSGIAHD-PIQR 513
Cdd:pfam00501 141 PADVPP---PPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDfGLSL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 514 DMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLL---SAQATRQIPTLLNAFFVGDVLTKRDCLRL 590
Cdd:pfam00501 218 GLLGPLLAGATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLleaGAPKRALLSSLRLVLSGGAPLPPELARRF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 591 QALAANVrIINMYGTTETqrAVSYFAIPPVSQDSTFLATQKDIMPagegmiDVQLLVVNRNDRNvPCAVGEVGEIYVRSG 670
Cdd:pfam00501 298 RELFGGA-LVNGYGLTET--TGVVTTPLPLDEDLRSLGSVGRPLP------GTEVKIVDDETGE-PVPPGEPGELCVRGP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 671 GLAEGYLDQ-DASAEKFVNnwfavnapprkdtilhpeegfagpesrywkgirDRMYRSGDLGRYLPDGTVECSGRADDQV 749
Cdd:pfam00501 368 GVMKGYLNDpELTAEAFDE---------------------------------DGWYRTGDLGRRDEDGYLEIVGRKKDQI 414
|
...
gi 2234869976 750 KIR 752
Cdd:pfam00501 415 KLG 417
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
290-868 |
2.08e-63 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 223.82 E-value: 2.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 290 PDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQR-EDVVMVYAHRSVDLVVAVMAVLKAGATFSVVD 368
Cdd:cd17648 1 PDRVAVVY-----------GDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 369 PAYPPSRQIIYLGVAKPRGLIMlkgagtisptvreflaqelkikvevpglevfpdghivggldpvgedvlrahnhlgetd 448
Cdd:cd17648 70 PSYPDERIQFILEDTGARVVIT---------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 449 pnvvlGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTML--SGIAHDPIQRDMFTPLFLGAQLH 526
Cdd:cd17648 92 -----NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLffSNYVFDFFVEQMTLALLNGQKLV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 527 VPTADDIGTPGRLAEWMAESEVTVTHLTPAmgqLLSAQATRQIPTLLNAFFVGDVLTKRDCLRLQALAANvRIINMYGTT 606
Cdd:cd17648 167 VPPDEMRFDPDRFYAYINREKVTYLSGTPS---VLQQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAG-LIINAYGPT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 607 ETqrAVSyfaippvSQDSTFLATQKDIMPAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQDA-SAEK 685
Cdd:cd17648 243 ET--TVT-------NHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVP--VGAVGELYLGGDGVARGYLNRPElTAER 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 686 FVNNWFAVnapprkdtilhpeegfagpESRYWKGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHL 765
Cdd:cd17648 312 FLPNPFQT-------------------EQERARGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAAL 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 766 SQHPLVRENVTLVRRDKD-----EEKILVSYFVPLEGSALEGyasnvpddeddgkglvkgmkkyrrlikDIREHLKQKLP 840
Cdd:cd17648 373 ASYPGVRECAVVAKEDASqaqsrIQKYLVGYYLPEPGHVPES---------------------------DLLSFLRAKLP 425
|
570 580
....*....|....*....|....*...
gi 2234869976 841 KHSVPSLFVPLSKMPLNPNGKIDKPALP 868
Cdd:cd17648 426 RYMVPARLVRLEGIPVTINGKLDVRALP 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
313-965 |
1.56e-57 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 220.81 E-value: 1.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 313 FSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPRGLImlk 392
Cdd:PRK05691 3746 WSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLV--- 3822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 393 gagtISPTVREfLAQELkikvevpgLEVFPdghivGGLDP---VGEDVlrAHNHLGETDPNVVLGPDSIGTLSFTSGSTG 469
Cdd:PRK05691 3823 ----CSAACRE-QARAL--------LDELG-----CANRPrllVWEEV--QAGEVASHNPGIYSGPDNLAYVIYTSGSTG 3882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 470 IPKGVrgrhfslthffpwMSERFGL--DETSKFTMLSGIAHDPIQRD------------MFTPLFlGAQLHVPTADDIGT 535
Cdd:PRK05691 3883 LPKGV-------------MVEQRGMlnNQLSKVPYLALSEADVIAQTasqsfdisvwqfLAAPLF-GARVEIVPNAIAHD 3948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 536 PGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLNAFFVGDV----LTKRDCLRLQALAanvrIINMYGTTETQRA 611
Cdd:PRK05691 3949 PQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAmppeLARQWLQRYPQIG----LVNAYGPAECSDD 4024
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 612 VSYFAIPPVSQDSTFLatqkdimPAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYL-DQDASAEKFVNNW 690
Cdd:PRK05691 4025 VAFFRVDLASTRGSYL-------PIGSPTDNNRLYLLDEALELVP--LGAVGELCVAGTGVGRGYVgDPLRTALAFVPHP 4095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 691 FAvnapprkdtilhpeegfagpesrywkGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPL 770
Cdd:PRK05691 4096 FG--------------------------APGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAE 4149
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 771 VRENVTLVrRDKDEEKILVSYFVPLEGSALEGyasnvpddeddgkglvkgmkkyrRLIKDIREHLKQKLPKHSVPSLFVP 850
Cdd:PRK05691 4150 VREAAVAV-QEGVNGKHLVGYLVPHQTVLAQG-----------------------ALLERIKQRLRAELPDYMVPLHWLW 4205
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 851 LSKMPLNPNGKIDKPALPFPDTAQASYAAgPSAPGaSATEIAMQKIWSTILpnAPQPIPTDESFFDLGGHSILATRLIFE 930
Cdd:PRK05691 4206 LDRLPLNANGKLDRKALPALDIGQLQSQA-YLAPR-NELEQTLATIWADVL--KVERVGVHDNFFELGGHSLLATQIASR 4281
|
650 660 670
....*....|....*....|....*....|....*
gi 2234869976 931 IRKVFVVNAPLGLIFEKPTIAGLVEAVDALRNADL 965
Cdd:PRK05691 4282 VQKALQRNVPLRAMFECSTVEELAEYIEGLAGSAI 4316
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
280-867 |
2.49e-56 |
|
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: 202.54 E-value: 2.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 280 DVFSRNARQNPDrpcviqSLPTESPDkpqGKVifSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLK 359
Cdd:cd17653 1 DAFERIAAAHPD------AVAVESLG---GSL--TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 360 AGATFSVVDPAYPPSRQIIylgvakprgliMLKGAGtisptvreflaqelkikvevPGLEVFPDGhivggldpvgedvlr 439
Cdd:cd17653 70 AGAAYVPLDAKLPSARIQA-----------ILRTSG--------------------ATLLLTTDS--------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 440 ahnhlgetdpnvvlgPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPL 519
Cdd:cd17653 104 ---------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 520 FLGAQLHVPT-ADDIGTPGRlaewmaesEVTVTHLTPAMGQLLSAQatrQIPTLLNAFFVGDVLTKRdclRLQALAANVR 598
Cdd:cd17653 169 CNGGTLVLADpSDPFAHVAR--------TVDALMSTPSILSTLSPQ---DFPNLKTIFLGGEAVPPS---LLDRWSPGRR 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 599 IINMYGTTETQRAVSYFAIPPVSQdstflatqkdiMPAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLD 678
Cdd:cd17653 235 LYNAYGPTECTISSTMTELLPGQP-----------VTIGKPIPNSTCYILDADLQPVP--EGVVGEICISGVQVARGYLG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 679 QDA-SAEKFVNNWFavnapprkdtilhpeegfagpesryWKGirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIE 757
Cdd:cd17653 302 NPAlTASKFVPDPF-------------------------WPG--SRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRIN 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 758 LGEI-DTHLSQHPLVRENVTLVRRDKdeekiLVSyFVplegsalegyasnVPDDEDdgkglvkgmkkyrrlIKDIREHLK 836
Cdd:cd17653 355 LEEIeEVVLQSQPEVTQAAAIVVNGR-----LVA-FV-------------TPETVD---------------VDGLRSELA 400
|
570 580 590
....*....|....*....|....*....|.
gi 2234869976 837 QKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd17653 401 KHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
278-867 |
1.26e-50 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 187.80 E-value: 1.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSR---NARQNPDRPCVIQslptespdkpQGKVIfSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAV 354
Cdd:PRK04813 1 IMDIIETieeFAQTQPDFPAYDY----------LGEKL-TYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 355 MAVLKAGATFSVVDPAYPPSR--QIIylGVAKPRGLIMLKGAGTISPTVREFLAQELkikvevpglevfpdghivggldp 432
Cdd:PRK04813 70 LGAVKAGHAYIPVDVSSPAERieMII--EVAKPSLIIATEELPLEILGIPVITLDEL----------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 433 vgEDVLRAHNHLGETDPnvVLGPDSIGTLsFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFtmlsgIAHDPIQ 512
Cdd:PRK04813 125 --KDIFATGNPYDFDHA--VKGDDNYYII-FTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQF-----LNQAPYS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 513 RDM-----FTPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTHLTPA---MGQLLSAQATRQIPTLLNAFFVGDVLTK 584
Cdd:PRK04813 195 FDLsvmdlYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSfadMCLLDPSFNEEHLPNLTHFLFCGEELPH 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 585 RDCLRLQALAANVRIINMYGTTETQRAVSyfAIPpVSQDstfLATQKDIMPAGEGMIDVQLLVVNRNDRNVPcaVGEVGE 664
Cdd:PRK04813 275 KTAKKLLERFPSATIYNTYGPTEATVAVT--SIE-ITDE---MLDQYKRLPIGYAKPDSPLLIIDEEGTKLP--DGEQGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 665 IYVRSGGLAEGYLdqdasaekfvnnwfavNAPPRKDTILHPEEGFagpesrywkgirdRMYRSGDLGrYLPDGTVECSGR 744
Cdd:PRK04813 347 IVISGPSVSKGYL----------------NNPEKTAEAFFTFDGQ-------------PAYHTGDAG-YLEDGLLFYQGR 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 745 ADDQVKIRGFRIELGEIDTHLSQHPLVRENVTlVRRDKDeEKI--LVSYFVPLEGsalegyasnvpDDEDDGKglvkgmk 822
Cdd:PRK04813 397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAVV-VPYNKD-HKVqyLIAYVVPKEE-----------DFEREFE------- 456
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2234869976 823 kyrrLIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:PRK04813 457 ----LTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
463-863 |
4.77e-46 |
|
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: 169.39 E-value: 4.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 463 FTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDigtPGRLAEW 542
Cdd:cd04433 7 YTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFD---PEAALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 543 MAESEVTVTHLTPAMGQLL---SAQATRQIPTLLNAFFVGDVLTKRDCLRLQAlAANVRIINMYGTTETQRAVSyfAIPP 619
Cdd:cd04433 84 IEREKVTILLGVPTLLARLlkaPESAGYDLSSLRALVSGGAPLPPELLERFEE-APGIKLVNGYGLTETGGTVA--TGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 620 VSQDSTFlatqKDIMPAGEGmidVQLLVVNRNDRnvPCAVGEVGEIYVRSGGLAEGYLDQDASAEKFvnnwfavnapprk 699
Cdd:cd04433 161 DDDARKP----GSVGRPVPG---VEVRIVDPDGG--ELPPGEIGELVVRGPSVMKGYWNNPEATAAV------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 700 dtilhpeegfagpesrywkgIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVR 779
Cdd:cd04433 219 --------------------DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 780 RDKDEEKILVSYFVPLEGSALegyasnvpdDEDdgkglvkgmkkyrrlikDIREHLKQKLPKHSVPSLFVPLSKMPLNPN 859
Cdd:cd04433 279 PDPEWGERVVAVVVLRPGADL---------DAE-----------------ELRAHVRERLAPYKVPRRVVFVDALPRTAS 332
|
....
gi 2234869976 860 GKID 863
Cdd:cd04433 333 GKID 336
|
|
| MupV_like_SDR_e |
cd05263 |
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ... |
1028-1304 |
3.41e-37 |
|
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187573 [Multi-domain] Cd Length: 293 Bit Score: 142.51 E-value: 3.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1028 VFLTGATGFLGAFVLYDLLSRTdrvKKVICLVRGKTVEQGLERLKEGSTDRNvwsdswvssgRLEVVTGDLGLDNFGLSQ 1107
Cdd:cd05263 1 VFVTGGTGFLGRHLVKRLLENG---FKVLVLVRSESLGEAHERIEEAGLEAD----------RVRVLEGDLTQPNLGLSA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1108 ETWNNVANEADVVLHNGALVHWVFPYEKLRSPNVLGTLTAVNLASTGKQKVFVFVSSTsaidtehYVqlseslargSTDS 1187
Cdd:cd05263 68 AASRELAGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARLDIQRFHYVSTA-------YV---------AGNR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1188 KG-VPESDDLEGAKsaLKTGYGQSKWVSEKLLFEAGKRgLRGHIVRPGYVVGDSHTAVTNTDDFIWRLVKGCVQLGLVP- 1265
Cdd:cd05263 132 EGnIRETELNPGQN--FKNPYEQSKAEAEQLVRAAATQ-IPLTVYRPSIVVGDSKTGRIEKIDGLYELLNLLAKLGRWLp 208
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2234869976 1266 ---DINNSINMVPVDHVARitSLAAVSPLPDAPLSVCHVTAR 1304
Cdd:cd05263 209 mpgNKGARLNLVPVDYVAD--AIVYLSKKPEANGQIFHLTDP 248
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
265-862 |
2.28e-35 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 143.33 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 265 PTGDLNWCgwkgaiTDVFSRNARQNPDRPCVIqslpteSPDKPQGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYA 344
Cdd:COG0365 4 VGGRLNIA------YNCLDRHAEGRGDKVALI------WEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 345 HRSVDLVVAVMAVLKAGATFSVVDPAYPPsRQIIY-LGVAKPRGLI----MLKGAGTIS--PTVREFLAQ--ELKIKVEV 415
Cdd:COG0365 72 PNIPEAVIAMLACARIGAVHSPVFPGFGA-EALADrIEDAEAKVLItadgGLRGGKVIDlkEKVDEALEElpSLEHVIVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 416 PGLEvfPDGHIVGGLDPvgEDVLRAHnhlGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSER-FGL 494
Cdd:COG0365 151 GRTG--ADVPMEGDLDW--DELLAAA---SAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 495 DETSKF---------TMLSGIahdpiqrdMFTPLFLGA-QLHVPTADDIGTPGRLAEWMAESEVTVTHLTpamgqllsaq 564
Cdd:COG0365 224 KPGDVFwctadigwaTGHSYI--------VYGPLLNGAtVVLYEGRPDFPDPGRLWELIEKYGVTVFFTA---------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 565 atrqiPTLLNAF--FVGDVLTKRDCLRLQALAA-----------------NVRIINMYGTTETqraVSYFAIPPVSQDST 625
Cdd:COG0365 286 -----PTAIRALmkAGDEPLKKYDLSSLRLLGSageplnpevwewwyeavGVPIVDGWGQTET---GGIFISNLPGLPVK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 626 FLATQKdimpAGEGMiDVQLLvvnrNDRNVPCAVGEVGEIYVRSG--GLAEGYLDQDasaEKFVNNWFavnapprkdtil 703
Cdd:COG0365 358 PGSMGK----PVPGY-DVAVV----DEDGNPVPPGEEGELVIKGPwpGMFRGYWNDP---ERYRETYF------------ 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 704 hpeEGFAGpesrywkgirdrMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVREN-VTLVrrdK 782
Cdd:COG0365 414 ---GRFPG------------WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAaVVGV---P 475
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 783 DEEK--ILVSYFVPLEGSAlegyasnvPDDEddgkglvkgmkkyrrLIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNG 860
Cdd:COG0365 476 DEIRgqVVKAFVVLKPGVE--------PSDE---------------LAKELQAHVREELGPYAYPREIEFVDELPKTRSG 532
|
..
gi 2234869976 861 KI 862
Cdd:COG0365 533 KI 534
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
278-867 |
3.94e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 138.78 E-value: 3.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAV 357
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYF-----------DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 358 LKAGATFSVVDPAYPPSrQIIY-LGVAKPRGLImlkgagtISPtvrEFLAQELKIKVEVPGLE---VFPDGHIVGGLDPV 433
Cdd:PRK06187 77 PKIGAVLHPINIRLKPE-EIAYiLNDAEDRVVL-------VDS---EFVPLLAAILPQLPTVRtviVEGDGPAAPLAPEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 434 G--EDVLRAHNhlgETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKF--------TML 503
Cdd:PRK06187 146 GeyEELLAAAS---DTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYlvivpmfhVHA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 504 SGIahdpiqrdMFTPLFLGAQLHVPTADDigtPGRLAEWMAESEVTVTHLTPAMGQ-LLSAQATRQI------------- 569
Cdd:PRK06187 223 WGL--------PYLALMAGAKQVIPRRFD---PENLLDLIETERVTFFFAVPTIWQmLLKAPRAYFVdfsslrlviygga 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 570 ---PTLLNAFfvgdvLTKRDClrlqalaanvRIINMYGTTETQRAVSyFAIPP--VSQDSTFLATqkdimpAGEGMIDVQ 644
Cdd:PRK06187 292 alpPALLREF-----KEKFGI----------DLVQGYGMTETSPVVS-VLPPEdqLPGQWTKRRS------AGRPLPGVE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 645 LLVVNRNDRNVPCAVGEVGEIYVRSGGLAEGYL-DQDASAEKFVNNWfavnapprkdtilhpeegfagpesrywkgirdr 723
Cdd:PRK06187 350 ARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWnRPEATAETIDGGW--------------------------------- 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 724 mYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVREN-VTLVRRDKDEEKILVsYFVPLEGSALeg 802
Cdd:PRK06187 397 -LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVaVIGVPDEKWGERPVA-VVVLKPGATL-- 472
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2234869976 803 yasnvpdDEddgkglvkgmkkyrrliKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:PRK06187 473 -------DA-----------------KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
284-864 |
5.66e-32 |
|
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: 130.81 E-value: 5.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 284 RNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGAT 363
Cdd:cd17631 3 RRARRHPDRTALVF-----------GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 364 FSVVDPayppsrqiiylgvakprgliMLKGAgtisptvrEFLAQelkikvevpglevfpdghivggldpvgedvlrahnh 443
Cdd:cd17631 72 FVPLNF--------------------RLTPP--------EVAYI------------------------------------ 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 444 LGETDPNVVLgpDSIGTLSFTSGSTGIPKGVRGRHFSLThffpWMserfgldetskfTMLSGIAHDPIQRDMF---TPLF 520
Cdd:cd17631 88 LADSGAKVLF--DDLALLMYTSGTTGRPKGAMLTHRNLL----WN------------AVNALAALDLGPDDVLlvvAPLF 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 521 LGAQLHVPTADDI---GT--------PGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTL--LNAFFVGDVLTkRDC 587
Cdd:cd17631 150 HIGGLGVFTLPTLlrgGTvvilrkfdPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLssLRAVIYGGAPM-PER 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 588 LRLQALAANVRIINMYGTTETQRAVSyfAIPPVSQDSTFLAtqkdimpAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYV 667
Cdd:cd17631 229 LLRALQARGVKFVQGYGMTETSPGVT--FLSPEDHRRKLGS-------AGRPVFFVEVRIVDPDGREVP--PGEVGEIVV 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 668 RSGGLAEGYLDQ-DASAEKFVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLGRYLPDGTVECSGRAD 746
Cdd:cd17631 298 RGPHVMAGYWNRpEATAAAFRDGWF----------------------------------HTGDLGRLDEDGYLYIVDRKK 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 747 DQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALegyasnvpdDEDdgkglvkgmkkyrr 826
Cdd:cd17631 344 DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAEL---------DED-------------- 400
|
570 580 590
....*....|....*....|....*....|....*...
gi 2234869976 827 likDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDK 864
Cdd:cd17631 401 ---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
313-862 |
3.22e-29 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 123.48 E-value: 3.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 313 FSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPsRQIIY-LGVAKPRGLIml 391
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTA-DELAHqLKISKPKVIF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 392 kGAGTISPTVREFLAQELKI-KVEVPGLEVFPDGHIVGGLDPVgedvlrahnhLGETDPNVVL----GPDSIGTLSFTSG 466
Cdd:cd05911 88 -TDPDGLEKVKEAAKELGPKdKIIVLDDKPDGVLSIEDLLSPT----------LGEEDEDLPPplkdGKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 467 STGIPKGV--RGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAH---DPIqrdMFTPLFLGAQLHVPTADDIGTPGRLAE 541
Cdd:cd05911 157 TTGLPKGVclSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHiygLFT---TLASLLNGATVIIMPKFDSELFLDLIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 542 wmaESEVTVTHLTPAMGQLL--SAQATR-QIPTLLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAVSYFAIP 618
Cdd:cd05911 234 ---KYKITFLYLVPPIAAALakSPLLDKyDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 619 PVSQDSTflatqkdimpaGEGMIDVQLLVVNRNDRNVpCAVGEVGEIYVRSGGLAEGYL-DQDASAEkfvnnwfavnapp 697
Cdd:cd05911 311 DDKPGSV-----------GRLLPNVEAKIVDDDGKDS-LGPNEPGEICVRGPQVMKGYYnNPEATKE------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 698 rkdtiLHPEEGFagpesrywkgirdrmYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVREnvtl 777
Cdd:cd05911 366 -----TFDEDGW---------------LHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVAD---- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 778 vrrdkdeekilVSYF-VPLEgsalegYASNVPddeddgKGLVKGMKKYRRLIKDIREHLKQKLPKH-----SVpsLFVPl 851
Cdd:cd05911 422 -----------AAVIgIPDE------VSGELP------RAYVVRKPGEKLTEKEVKDYVAKKVASYkqlrgGV--VFVD- 475
|
570
....*....|.
gi 2234869976 852 sKMPLNPNGKI 862
Cdd:cd05911 476 -EIPKSASGKI 485
|
|
| FAR-N_SDR_e |
cd05236 |
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ... |
1027-1303 |
1.38e-28 |
|
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187547 [Multi-domain] Cd Length: 320 Bit Score: 118.17 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1027 TVFLTGATGFLGAFVLYDLLSRTDRVKKVICLVRGKTVEQGLERLKE---------GSTDRNVWSDswvssgRLEVVTGD 1097
Cdd:cd05236 2 SVLITGATGFLGKVLLEKLLRSCPDIGKIYLLIRGKSGQSAEERLREllkdklfdrGRNLNPLFES------KIVPIEGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1098 LGLDNFGLSQETWNNVANEADVVLHNGALVHWVFPYEKLRSPNVLGTLTAVNLASTGKQ-KVFVFVSSTsaidtehYV-- 1174
Cdd:cd05236 76 LSEPNLGLSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKlKAFVHVSTA-------YVng 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1175 ---QLSESLARGSTDSKGVPES----DDLEGAKSALKTGYGQ------SKWVSEKLLFEAGKrGLRGHIVRPGYVVG--- 1238
Cdd:cd05236 149 drqLIEEKVYPPPADPEKLIDIlelmDDLELERATPKLLGGHpntytfTKALAERLVLKERG-NLPLVIVRPSIVGAtlk 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2234869976 1239 -------DSHTAVTntddfiwRLVKGCvQLGLVPDINNSINM----VPVDHVAR--ITSLAAVSPLPDAPLSVCHVTA 1303
Cdd:cd05236 228 epfpgwiDNFNGPD-------GLFLAY-GKGILRTMNADPNAvadiIPVDVVANalLAAAAYSGVRKPRELEVYHCGS 297
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
276-867 |
9.68e-27 |
|
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: 116.31 E-value: 9.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 276 GAITDVFSRNARQNPDRPCVIqslptespdKPQGKVifSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVM 355
Cdd:cd05959 4 NAATLVDLNLNEGRGDKTAFI---------DDAGSL--TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 356 AVLKAGATFSVVDPAYPPSRQIIYLGVAKPRGLIMlkgAGTISPTVREFLAQELKIKVEVpgleVFPDGHIVGGLDPVGE 435
Cdd:cd05959 73 GAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV---SGELAPVLAAALTKSEHTLVVL----IVSGGAGPEAGALLLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 436 DVLRAHNHLGETDPNvvlGPDSIGTLSFTSGSTGIPKGVRGRHFSLThffpWMSERFGLDetskftmLSGIAHDpiqrDM 515
Cdd:cd05959 146 ELVAAEAEQLKPAAT---HADDPAFWLYSSGSTGRPKGVVHLHADIY----WTAELYARN-------VLGIRED----DV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 516 F---TPLF----LGAQLHVPTAddIG----------TPGRLAEWMAESEVTVTHltpamgqllsaqatrQIPTLLNAFFV 578
Cdd:cd05959 208 CfsaAKLFfaygLGNSLTFPLS--VGattvlmperpTPAAVFKRIRRYRPTVFF---------------GVPTLYAAMLA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 579 GDVLTKRDCLRL-------QALAANV----------RIINMYGTTE--------TQRAVSYfaippvsqdstflATQKDI 633
Cdd:cd05959 271 APNLPSRDLSSLrlcvsagEALPAEVgerwkarfglDILDGIGSTEmlhiflsnRPGRVRY-------------GTTGKP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 634 MPAGEgmidVQLlvvnRNDRNVPCAVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWfavnapprkdtilhpeegfagp 712
Cdd:cd05959 338 VPGYE----VEL----RDEDGGDVADGEPGELYVRGPSSATMYWNNrDKTRDTFQGEW---------------------- 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 713 esrywkgirdrmYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVREnVTLVRRDKDEEKILVSYF 792
Cdd:cd05959 388 ------------TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLE-AAVVGVEDEDGLTKPKAF 454
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2234869976 793 VplegsalegyasnVPDDEDDGKGLvkgmkkyrrLIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05959 455 V-------------VLRPGYEDSEA---------LEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
290-867 |
8.06e-26 |
|
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: 112.57 E-value: 8.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 290 PDRPCVIQslptespDKPQGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDP 369
Cdd:cd17654 1 PDRPALII-------DQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 370 AYPPSRQiiylgvakprgLIMLKGAGTISPTVREFLAQELKIKVEvpglevfpdghivggldpvgedvlrAHNHLgetdp 449
Cdd:cd17654 74 ASPEQRS-----------LTVMKKCHVSYLLQNKELDNAPLSFTP-------------------------EHRHF----- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 450 NVVLGPDSIGTLsFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQL-HVP 528
Cdd:cd17654 113 NIRTDECLAYVI-HTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLlIVP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 529 TADDIgTPGRLAEWMAES-EVTVTHLTPAM----------GQLLSAQATRQIPTLLNAFFVGDVLTKrdCLRLQALaaNV 597
Cdd:cd17654 192 TSVKV-LPSKLADILFKRhRITVLQATPTLfrrfgsqsikSTVLSATSSLRVLALGGEPFPSLVILS--SWRGKGN--RT 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 598 RIINMYGTTETQRAVSYFAIPpvSQDSTflatqkdiMPAGEGMIDVQLLVVNRNDRNVPcavgevGEIYVrsGGLAEGYL 677
Cdd:cd17654 267 RIFNIYGITEVSCWALAYKVP--EEDSP--------VQLGSPLLGTVIEVRDQNGSEGT------GQVFL--GGLNRVCI 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 678 DQDasaekfvnnwfavnapprkdtilhpEEGfaGPESrywkgirdRMYRSGDLGRyLPDGTVECSGRADDQVKIRGFRIE 757
Cdd:cd17654 329 LDD-------------------------EVT--VPKG--------TMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRIN 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 758 LGEIDTHLSQH-PLVRENVTLVRRDKdeekiLVSYFVPLEGSAlegyasnvpddeddgkglvkgmkkyrRLIKDIREHLk 836
Cdd:cd17654 373 LDLIQQVIESClGVESCAVTLSDQQR-----LIAFIVGESSSS--------------------------RIHKELQLTL- 420
|
570 580 590
....*....|....*....|....*....|.
gi 2234869976 837 qkLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd17654 421 --LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
313-868 |
1.51e-23 |
|
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: 105.45 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 313 FSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYppsrqiiylgvakprglimlk 392
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTAL--------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 393 gagtisptVREFLAqelkikvevpglevfpdgHIVGGLDPvgedvlrahnHLGETDPNVVLgpdsigtlsFTSGSTGIPK 472
Cdd:cd05934 63 --------RGDELA------------------YIIDHSGA----------QLVVVDPASIL---------YTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 473 GVRGRHFSLTHFFPWMSERFGLDEtsKFTMLSgiahdpiqrdmFTPLF-LGAQLH-VPTADDIGTPGRLAE-------W- 542
Cdd:cd05934 98 GVVITHANLTFAGYYSARRFGLGE--DDVYLT-----------VLPLFhINAQAVsVLAALSVGATLVLLPrfsasrfWs 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 543 -MAESEVTVTHLTPAMGQLLSAQATRQIPtllnaffvgdvltKRDCLRLQALAAN-------------VRIINMYGTTET 608
Cdd:cd05934 165 dVRRYGATVTNYLGAMLSYLLAQPPSPDD-------------RAHRLRAAYGAPNppelheefeerfgVRLLEGYGMTET 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 609 QRAVsyfAIPPVSQDSTflatqkdiMPAGEGMIDVQLLVVNRNDRnvPCAVGEVGEIYVRSG---GLAEGYLDQ-DASAE 684
Cdd:cd05934 232 IVGV---IGPRDEPRRP--------GSIGRPAPGYEVRIVDDDGQ--ELPAGEPGELVIRGLrgwGFFKGYYNMpEATAE 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 685 KFVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTH 764
Cdd:cd05934 299 AMRNGWF----------------------------------HTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERA 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 765 LSQHPLVRE-NVTLVRRDKDEEKILVsYFVPLEGSALEgyasnvPDdeddgkglvkgmkkyrrlikDIREHLKQKLPKHS 843
Cdd:cd05934 345 ILRHPAVREaAVVAVPDEVGEDEVKA-VVVLRPGETLD------PE--------------------ELFAFCEGQLAYFK 397
|
570 580
....*....|....*....|....*
gi 2234869976 844 VPSLFVPLSKMPLNPNGKIDKPALP 868
Cdd:cd05934 398 VPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
273-867 |
2.01e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 106.37 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 273 GWKG--AITDVFSRNARQNPDRPCVIQSLPTEspdkpqgkviFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDL 350
Cdd:PRK06087 18 GYWGdaSLADYWQQTARAMPDKIAVVDNHGAS----------YTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 351 VVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPRGLImlkgagtiSPTV---REFLAQELKIKVEVPGLEvfpdgHIV 427
Cdd:PRK06087 88 TIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFF--------APTLfkqTRPVDLILPLQNQLPQLQ-----QIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 428 G--GLDPVGEDVLRAH----NHLGETDPNVvlGPDSIGTLSFTSGSTGIPKGVRgrhfsLTHFFPWMSERF---GLDETS 498
Cdd:PRK06087 155 GvdKLAPATSSLSLSQiiadYEPLTTAITT--HGDELAAVLFTSGTEGLPKGVM-----LTHNNILASERAycaRLNLTW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 499 KFTML--------SGIAHDPIqrdmfTPLFLGAQLhvpTADDIGTPGRLAEWMAESEVTVTH-LTPAMGQLLSA--QATR 567
Cdd:PRK06087 228 QDVFMmpaplghaTGFLHGVT-----APFLIGARS---VLLDIFTPDACLALLEQQRCTCMLgATPFIYDLLNLleKQPA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 568 QIPTLlnAFFV--GDVLTKRdcLRLQALAANVRIINMYGTTETqraVSYFAIPPVSQDSTFLATqkdimpAGEGMIDVQL 645
Cdd:PRK06087 300 DLSAL--RFFLcgGTTIPKK--VARECQQRGIKLLSVYGSTES---SPHAVVNLDDPLSRFMHT------DGYAAAGVEI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 646 LVVNRNDRNVPCavGEVGEIYVRSGGLAEGYLDqdasaekfvnnwfavnAPPRKDTILHpEEGfagpesryWkgirdrmY 725
Cdd:PRK06087 367 KVVDEARKTLPP--GCEGEEASRGPNVFMGYLD----------------EPELTARALD-EEG--------W-------Y 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 726 RSGDLGRYLPDGTVECSGRADDqVKIRGFR-IELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPlegsalegya 804
Cdd:PRK06087 413 YSGDLCRMDEAGYIKITGRKKD-IIVRGGEnISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVL---------- 481
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2234869976 805 snvpddeddgkglvkgMKKYRRL-IKDIREHL-KQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:PRK06087 482 ----------------KAPHHSLtLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
280-867 |
5.95e-23 |
|
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: 104.18 E-value: 5.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 280 DVFSRNARQNPDRPCVIQslptespdkpQGKVIfSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLK 359
Cdd:cd05936 3 DLLEEAARRFPDKTALIF----------MGRKL-TYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 360 AGATFSVVDPAYPPsRQIIY-LGVAKPRGLImlkgagtispTVREFlaqelkikvevpglevfpdghivggldpvgEDVL 438
Cdd:cd05936 72 AGAVVVPLNPLYTP-RELEHiLNDSGAKALI----------VAVSF------------------------------TDLL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 439 RAhnhLGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGI---------AHd 509
Cdd:cd05936 111 AA---GAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDVVLAALplfhvfgltVA- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 510 piqrdMFTPLFLGA-QLHVPTADDIGTpgrLAEwMAESEVTVTHLTPAMGQLLSAQATRQ---IPTLLNAFFVGDVLTKR 585
Cdd:cd05936 187 -----LLLPLALGAtIVLIPRFRPIGV---LKE-IRKHRVTIFPGVPTMYIALLNAPEFKkrdFSSLRLCISGGAPLPVE 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 586 DCLRLQALAaNVRIINMYGTTETQravsyfaipPVSQDSTFLATQKdimpagEGMI-----DVQLLVVNRNDRNVPCavG 660
Cdd:cd05936 258 VAERFEELT-GVPIVEGYGLTETS---------PVVAVNPLDGPRK------PGSIgiplpGTEVKIVDDDGEELPP--G 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 661 EVGEIYVRSGGLAEGYL-DQDASAEKFVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLGRYLPDGTV 739
Cdd:cd05936 320 EVGELWVRGPQVMKGYWnRPEETAEAFVDGWL----------------------------------RTGDIGYMDEDGYF 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 740 ECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALegyasnvpdDEDdgkglvk 819
Cdd:cd05936 366 FIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASL---------TEE------- 429
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2234869976 820 gmkkyrrlikDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05936 430 ----------EIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| WcaG |
COG0451 |
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
1027-1290 |
1.11e-22 |
|
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 100.05 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1027 TVFLTGATGFLGAFVLYDLLSRTDRvkkVICLVRGKTVEQGLERLKegstdrnvwsdswvssgRLEVVTGDLgldnfgLS 1106
Cdd:COG0451 1 RILVTGGAGFIGSHLARRLLARGHE---VVGLDRSPPGAANLAALP-----------------GVEFVRGDL------RD 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1107 QETWNNVANEADVVLHNGALVH-WVFPYEKLRSPNVLGTLTAVNLASTGKQKVFVFVSSTSAIDtehyvqlseslargsT 1185
Cdd:COG0451 55 PEALAAALAGVDAVVHLAAPAGvGEEDPDETLEVNVEGTLNLLEAARAAGVKRFVYASSSSVYG---------------D 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1186 DSKGVPESDDLEGAksalkTGYGQSKWVSEKLLFEAGKR-GLRGHIVRPGYVVGDSHTAVTNtdDFIWRLVKGcVQLGLV 1264
Cdd:COG0451 120 GEGPIDEDTPLRPV-----SPYGASKLAAELLARAYARRyGLPVTILRPGNVYGPGDRGVLP--RLIRRALAG-EPVPVF 191
|
250 260
....*....|....*....|....*.
gi 2234869976 1265 PDINNSINMVPVDHVARITSLAAVSP 1290
Cdd:COG0451 192 GDGDQRRDFIHVDDVARAIVLALEAP 217
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
285-868 |
5.26e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 101.93 E-value: 5.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 285 NARQNPDRPCVIQSLPTespdkpqgkviFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATF 364
Cdd:PRK07788 58 AARRAPDRAALIDERGT-----------LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 365 SVVDPAYPPsRQIIylGVAKPRGLIMLkgagtisptV--REFLAQELKIKVEVPGLEVFP----DGHIVGGLDPVGEDVL 438
Cdd:PRK07788 127 ILLNTGFSG-PQLA--EVAAREGVKAL---------VydDEFTDLLSALPPDLGRLRAWGgnpdDDEPSGSTDETLDDLI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 439 RAHnhlGETDPNVVLGPDSIGTLsfTSGSTGIPKGVRgrhfslthffpwmseRfglDETSKFTMLSGI-AHDPIQRDMFT 517
Cdd:PRK07788 195 AGS---STAPLPKPPKPGGIVIL--TSGTTGTPKGAP---------------R---PEPSPLAPLAGLlSRVPFRAGETT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 518 ----PLF--LG-AQLHVPTAddigtpgrlaewMAESEVTVTHLTPAmgQLLSAQATRQI------PTLLNAFF--VGDVL 582
Cdd:PRK07788 252 llpaPMFhaTGwAHLTLAMA------------LGSTVVLRRRFDPE--ATLEDIAKHKAtalvvvPVMLSRILdlGPEVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 583 TKRDCLRLQ-------ALAANV----------RIINMYGTTEtqraVSYFAIppvsqdstflATQKD--IMP--AGEGMI 641
Cdd:PRK07788 318 AKYDTSSLKiifvsgsALSPELatraleafgpVLYNLYGSTE----VAFATI----------ATPEDlaEAPgtVGRPPK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 642 DVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDqdasaekfvnnwfavnaPPRKDTIlhpeegfagpesrywkgir 721
Cdd:PRK07788 384 GVTVKILDENGNEVP--RGVVGRIFVGNGFPFEGYTD-----------------GRDKQII------------------- 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 722 DRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALe 801
Cdd:PRK07788 426 DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAAL- 504
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2234869976 802 gyasnvpdDEDDgkglvkgmkkyrrlikdIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALP 868
Cdd:PRK07788 505 --------DEDA-----------------IKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
274-867 |
7.03e-22 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 101.38 E-value: 7.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 274 WKGA-ITDVFSRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVV 352
Cdd:COG1021 22 WRGEtLGDLLRRRAERHPDRIAVVD-----------GERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 353 AVMAVLKAGATfsvvdP--AYPPSRQ--IIYL-GVAKPRGLImlkgagtISPTVREF----LAQELKIkvEVPGLE-VFp 422
Cdd:COG1021 91 VFFALFRAGAI-----PvfALPAHRRaeISHFaEQSEAVAYI-------IPDRHRGFdyraLARELQA--EVPSLRhVL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 423 dghIVGGLDP-VGEDVLRAHnhlGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRH----FSLTHffpwMSERFGLDET 497
Cdd:COG1021 156 ---VVGDAGEfTSLDALLAA---PADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHddylYSVRA----SAEICGLDAD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 498 SKFTMLSGIAHDpiqrdmFT---PLFLGAqLHV-------PTADdigtPGRLAEWMAESEVTVTHLTPAM---------- 557
Cdd:COG1021 226 TVYLAALPAAHN------FPlssPGVLGV-LYAggtvvlaPDPS----PDTAFPLIERERVTVTALVPPLallwldaaer 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 558 --------------GQLLSAQATRQIPTLLNAffvgdvltkrdclRLQalaanvriiNMYGTTETqrAVSYfaIPPVSQD 623
Cdd:COG1021 295 srydlsslrvlqvgGAKLSPELARRVRPALGC-------------TLQ---------QVFGMAEG--LVNY--TRLDDPE 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 624 STFLATQ-KDIMPAGEgmidvqLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQDasaekfvnnwfAVNAppRKDTi 702
Cdd:COG1021 349 EVILTTQgRPISPDDE------VRIVDEDGNPVP--PGEVGELLTRGPYTIRGYYRAP-----------EHNA--RAFT- 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 703 lhpEEGFagpesrywkgirdrmYRSGDLGRYLPDGTVECSGRADDQVkIRGfrielGE------IDTHLSQHPLVReNVT 776
Cdd:COG1021 407 ---PDGF---------------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GEkiaaeeVENLLLAHPAVH-DAA 461
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 777 LVRRDkDE---EKILVsyFVPLEGSALEgyasnvpddeddgkglvkgmkkyrrlIKDIREHLKQK-LPKHSVPSLFVPLS 852
Cdd:COG1021 462 VVAMP-DEylgERSCA--FVVPRGEPLT--------------------------LAELRRFLRERgLAAFKLPDRLEFVD 512
|
650
....*....|....*
gi 2234869976 853 KMPLNPNGKIDKPAL 867
Cdd:COG1021 513 ALPLTAVGKIDKKAL 527
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
320-867 |
2.83e-21 |
|
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: 98.67 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 320 RASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVV----DPAYPPSrQIIYLG-VAKPRGLIMLKGA 394
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVfvplNPTLKES-VLRYLVaDAGGRIVLADAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 395 GTisptvreflaqELKikvevPGLEVFPDGHIVggldpVGEDVLRAHNHLGetdPNVVLGPDSIGTLSFTSGSTGIPKGV 474
Cdd:cd05922 80 AD-----------RLR-----DALPASPDPGTV-----LDADGIRAARASA---PAHEVSHEDLALLLYTSGSTGSPKLV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 475 RGRHFSLTHFFPWMSERFGLDETSK-FTMLSgIAHDPIQRDMFTPLFLGAQLhVPTADdiGTPGRlAEWMAESEVTVTHL 553
Cdd:cd05922 136 RLSHQNLLANARSIAEYLGITADDRaLTVLP-LSYDYGLSVLNTHLLRGATL-VLTND--GVLDD-AFWEDLREHGATGL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 554 T--PAMGQLLS--AQATRQIPTLLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAVSYfaIPPVSQDSTFLAT 629
Cdd:cd05922 211 AgvPSTYAMLTrlGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTY--LPPERILEKPGSI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 630 QKDImPAGEgmIDVqllvvnRNDRNVPCAVGEVGEIYVRSGGLAEGYLDQDASAEKfvnnwfavnaPPRKDTILHpeegf 709
Cdd:cd05922 289 GLAI-PGGE--FEI------LDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRK----------EGRGGGVLH----- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 710 agpesrywkgirdrmyrSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILV 789
Cdd:cd05922 345 -----------------TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLAL 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2234869976 790 syFVplegsalegyasnVPDDEDDgkglvkgmkkyrrlIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05922 408 --FV-------------TAPDKID--------------PKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
313-864 |
4.50e-21 |
|
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: 97.84 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 313 FSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPRGLImlk 392
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 393 gagtisptvreflaqelkikveVPglevfpdghivggldpvgeDVLRAHNHLGEtdpnvvlgPDSIGTLSFTSGSTGIPK 472
Cdd:cd05903 79 ----------------------VP-------------------ERFRQFDPAAM--------PDAVALLLFTSGTTGEPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 473 GVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDP-IQRDMFTPLFLGAQLHVptaDDIGTPGRLAEWMAESEVTVT 551
Cdd:cd05903 110 GVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTgFVYGFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTFM 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 552 H-LTPAMGQLLSA--QATRQIPTlLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAVSyfaIPPVSQDSTFLA 628
Cdd:cd05903 187 MgATPFLTDLLNAveEAGEPLSR-LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVT---SITPAPEDRRLY 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 629 TQKDIMPAgegmidVQLLVVnrNDRNVPCAVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWFavnapprkdtilhpee 707
Cdd:cd05903 263 TDGRPLPG------VEIKVV--DDTGATLAPGVEGELLSRGPSVFLGYLDRpDLTADAAPEGWF---------------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 708 gfagpesrywkgirdrmyRSGDLGRYLPDGTVECSGRADDqVKIR-GFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEK 786
Cdd:cd05903 319 ------------------RTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGE 379
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2234869976 787 ILVSYFVPLEGSALEgyasnvpddeddgkglvkgmkkyrrlIKDIREHL-KQKLPKHSVPSLFVPLSKMPLNPNGKIDK 864
Cdd:cd05903 380 RACAVVVTKSGALLT--------------------------FDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
307-867 |
1.17e-20 |
|
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: 97.38 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 307 PQGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPR 386
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 387 GLIMLKGA-GTISPTVREFLAQELKIKVEVPGLEVFPDGHIVGGLDPVGEDVLRAHNHLGEtDPNVVLgpdsigtlsFTS 465
Cdd:cd05926 89 LVLTPKGElGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPD-DLALIL---------HTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 466 GSTGIPKGVRGRHFSL---------THffpwmseRFGLDETSKFTMlsgiahdPiqrdMF----------TPLFLGAQLH 526
Cdd:cd05926 159 GTTGRPKGVPLTHRNLaasatnitnTY-------KLTPDDRTLVVM-------P----LFhvhglvasllSTLAAGGSVV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 527 VPtaddigtPGRLA----EWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLNAF-FVgdvltkRDC---LRLQALAA--- 595
Cdd:cd05926 221 LP-------PRFSAstfwPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLrFI------RSCsasLPPAVLEAlea 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 596 --NVRIINMYGTTETQRAVSYFAIPPvsqdstflaTQKDIMPAGEGmIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLA 673
Cdd:cd05926 288 tfGAPVLEAYGMTEAAHQMTSNPLPP---------GPRKPGSVGKP-VGVEVRILDEDGEILP--PGVVGEICLRGPNVT 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 674 EGYL-DQDASAEK-FVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLGRYLPDGTVECSGRADDQVKI 751
Cdd:cd05926 356 RGYLnNPEANAEAaFKDGWF----------------------------------RTGDLGYLDADGYLFLTGRIKELINR 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 752 RGFRIELGEIDTHLSQHPLVRENVTL-VRRDKDEEKIlVSYFVPLEGSALegyasnvpddeddgkglvkgmkkyrrLIKD 830
Cdd:cd05926 402 GGEKISPLEVDGVLLSHPAVLEAVAFgVPDEKYGEEV-AAAVVLREGASV--------------------------TEEE 454
|
570 580 590
....*....|....*....|....*....|....*..
gi 2234869976 831 IREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05926 455 LRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
320-867 |
1.28e-20 |
|
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: 96.64 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 320 RASNVLAHHlimnGIQREDVVMVYAHRSVDLVVAVMAVLKAGAtfsvvdpayppsrqiiylgvakprglIMLKGAGTISP 399
Cdd:cd05972 12 KAANVLAKL----GLRKGDRVAVLLPRVPELWAVILAVIKLGA--------------------------VYVPLTTLLGP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 400 TVREFLAQELKIKVevpglevfpdghivggldpvgedvlrahnhlgetdpnVVLGPDSIGTLSFTSGSTGIPKGVRGRHF 479
Cdd:cd05972 62 KDIEYRLEAAGAKA-------------------------------------IVTDAEDPALIYFTSGTTGLPKGVLHTHS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 480 SLTHFFPWMSERFGLDETSKFTMLSgiahDP-----IQRDMFTPLFLGAQLHVPTADDIgTPGRLAEWMAESEVTVTHLT 554
Cdd:cd05972 105 YPLGHIPTAAYWLGLRPDDIHWNIA----DPgwakgAWSSFFGPWLLGATVFVYEGPRF-DAERILELLERYGVTSFCGP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 555 PAMGQLLSAQ--ATRQIPTLLNAFFVGDVLTkRDCLRLQALAANVRIINMYGTTETQRAVSYFAIPPVSQDSTFLATqkd 632
Cdd:cd05972 180 PTAYRMLIKQdlSSYKFSHLRLVVSAGEPLN-PEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPT--- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 633 imPAgegmIDVQLLvvnrNDRNVPCAVGEVGEIyvrsgglaegyldqdasaekfvnnwfAVNAPPrkdtiLHPEEGFAGP 712
Cdd:cd05972 256 --PG----YDVAII----DDDGRELPPGEEGDI--------------------------AIKLPP-----PGLFLGYVGD 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 713 ESRYWKGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDkdeekilvsyf 792
Cdd:cd05972 295 PEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPD----------- 363
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2234869976 793 vPLEGSALEGYASnvpddeddgkgLVKGMKKYRRLIKDIREHLKQKLPKHSVPSL--FVPlsKMPLNPNGKIDKPAL 867
Cdd:cd05972 364 -PVRGEVVKAFVV-----------LTSGYEPSEELAEELQGHVKKVLAPYKYPREieFVE--ELPKTISGKIRRVEL 426
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
311-867 |
3.71e-20 |
|
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: 96.20 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 311 VIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPayPPSRQIIYLGVAKPRGLIM 390
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTV--PPTYDEPNARLRKLRHIWQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 391 LKGagtiSPTV--REFLAQELKIKVEVPGLEVFPDGHIVGGLDPVGEDVLRAhnhlgetdpnvvLGPDSIGTLSFTSGST 468
Cdd:cd05906 116 LLG----SPVVltDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQ------------SRPDDLALLMLTSGST 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 469 GIPKGVRGRHFSLTH----------------FFPWMserfGLDEtskftmLSGIAHDPIQrdmftPLFLGA-QLHVPTAD 531
Cdd:cd05906 180 GFPKAVPLTHRNILArsagkiqhngltpqdvFLNWV----PLDH------VGGLVELHLR-----AVYLGCqQVHVPTEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 532 DIGTPGRLAEWMAESEVTVThLTPAMGQLLSAQATRQIPT----------LLNAFFVGDVLTKRDCLRLQA---LAANVr 598
Cdd:cd05906 245 ILADPLRWLDLIDRYRVTIT-WAPNFAFALLNDLLEEIEDgtwdlsslryLVNAGEAVVAKTIRRLLRLLEpygLPPDA- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 599 IINMYGTTETQRAVSY---FAIPPVSQDSTFLATqkdimpaGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEG 675
Cdd:cd05906 323 IRPAFGMTETCSGVIYsrsFPTYDHSQALEFVSL-------GRPIPGVSMRIVDDEGQLLP--EGEVGRLQVRGPVVTKG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 676 YL-DQDASAEKFVN-NWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLGrYLPDGTVECSGRADDQVKIRG 753
Cdd:cd05906 394 YYnNPEANAEAFTEdGWF----------------------------------RTGDLG-FLDNGNLTITGRTKDTIIVNG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 754 FRIELGEIDTHLSQHPLVRENVTL---VRRDKDEEKILVSYFVPlegsalegyaSNVPDDEDDgkglvkgmkkyrRLIKD 830
Cdd:cd05906 439 VNYYSHEIEAAVEEVPGVEPSFTAafaVRDPGAETEELAIFFVP----------EYDLQDALS------------ETLRA 496
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2234869976 831 IREHLKQKL---PKHSVPslfVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05906 497 IRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
277-864 |
2.13e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 90.38 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 277 AITDVFSRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMA 356
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVF-----------GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 357 VLKAGATFSVVDPAYPPSrQIIY-LGVAKPRGLIMlkgAGTISPTVREFLAQelkIKVEVPGLEVFPDGHIVGGLDpvgE 435
Cdd:PRK08316 81 CARAGAVHVPVNFMLTGE-ELAYiLDHSGARAFLV---DPALAPTAEAALAL---LPVDTLILSLVLGGREAPGGW---L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 436 DVLRAHNHLGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHffPWMSERFGLDETSKFTMLSGIahdPI---- 511
Cdd:PRK08316 151 DFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIA--EYVSCIVAGDMSADDIPLHAL---PLyhca 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 512 QRDMF--TPLFLGAQLHVPTADDigtPGRLAEWMAESEVTVTHLTPA--MGQLLSAQ-ATRQIPTLLNAFFVGDVLTKRD 586
Cdd:PRK08316 226 QLDVFlgPYLYVGATNVILDAPD---PELILRTIEAERITSFFAPPTvwISLLRHPDfDTRDLSSLRKGYYGASIMPVEV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 587 CLRLQALAANVRIINMYGTTEtqravsyfaIPPvsqdstfLAT-----QKDIMP--AGEGMIDVQLLVVNRNDRNVPcaV 659
Cdd:PRK08316 303 LKELRERLPGLRFYNCYGQTE---------IAP-------LATvlgpeEHLRRPgsAGRPVLNVETRVVDDDGNDVA--P 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 660 GEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLGRYLPDGT 738
Cdd:PRK08316 365 GEVGEIVHRSPQLMLGYWDDpEKTAEAFRGGWF----------------------------------HSGDLGVMDEEGY 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 739 VECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRE-NVTLVRRDKDEEKIlVSYFVPLEGSALegyasnvpdDEDDgkgl 817
Cdd:PRK08316 411 ITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEvAVIGLPDPKWIEAV-TAVVVPKAGATV---------TEDE---- 476
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2234869976 818 vkgmkkyrrLIkdirEHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDK 864
Cdd:PRK08316 477 ---------LI----AHCRARLAGFKVPKRVIFVDELPRNPSGKILK 510
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
451-867 |
2.32e-18 |
|
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: 89.44 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 451 VVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFP-WMSERFGLDE------TSKFTMLSGIAHDpiqrdMFTPLFLGA 523
Cdd:cd05919 86 VVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADaMAREALGLTPgdrvfsSAKMFFGYGLGNS-----LWFPLAVGA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 524 QLHVptADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQAT---RQIPTLLNAFFVGDVLTKRDCLRLQAlAANVRII 600
Cdd:cd05919 161 SAVL--NPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAgspDALRSLRLCVSAGEALPRGLGERWME-HFGGPIL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 601 NMYGTTETQRavsyfaippvsqdsTFLATQKDIMPAGEGMIDV---QLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYl 677
Cdd:cd05919 238 DGIGATEVGH--------------IFLSNRPGAWRLGSTGRPVpgyEIRLVDEEGHTIP--PGEEGDLLVRGPSAAVGY- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 678 dqdasaekfvnnWfavNAPPRkdtilhPEEGFAGPesryWkgirdrmYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIE 757
Cdd:cd05919 301 ------------W---NNPEK------SRATFNGG----W-------YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVS 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 758 LGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALEGyasnvpddeddgkglvkgmkkyrRLIKDIREHLKQ 837
Cdd:cd05919 349 PVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQE-----------------------SLARDIHRHLLE 405
|
410 420 430
....*....|....*....|....*....|
gi 2234869976 838 KLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05919 406 RLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
304-867 |
8.03e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 88.50 E-value: 8.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 304 PDKPQ---GKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYL 380
Cdd:PRK06188 26 PDRPAlvlGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 381 GVAKPRGLImlkgagtISPTvrEFLAQELKIKVEVPGLE-VFPDGHIVGGLDPVGEDVLRAHNHLGETDpnvvlGPDSIG 459
Cdd:PRK06188 106 EDAGISTLI-------VDPA--PFVERALALLARVPSLKhVLTLGPVPDGVDLLAAAAKFGPAPLVAAA-----LPPDIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 460 TLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHdpIQRDMFTP-LFLGAQLHVPTADDigtPGR 538
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH--AGGAFFLPtLLRGGTVIVLAKFD---PAE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 539 LAEWMAESEVTVTHLTPAMgqllsaqatrqIPTLLNAffvgDVLTKRDCLRLQALA------ANVRII-----------N 601
Cdd:PRK06188 247 VLRAIEEQRITATFLVPTM-----------IYALLDH----PDLRTRDLSSLETVYygaspmSPVRLAeaierfgpifaQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 602 MYGTTETQRAVSYFA-IPPVSQDSTFLATQKDIMPAgegmIDVQLLvvNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQ- 679
Cdd:PRK06188 312 YYGQTEAPMVITYLRkRDHDPDDPKRLTSCGRPTPG----LRVALL--DEDGREVA--QGEVGEICVRGPLVMDGYWNRp 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 680 DASAEKFVNNWfavnapprkdtiLHpeegfagpesrywkgirdrmyrSGDLGRYLPDGTVECSGRADDQVKIRGFRIELG 759
Cdd:PRK06188 384 EETAEAFRDGW------------LH----------------------TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPR 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 760 EIDTHLSQHPLVRE-NVTLVRRDKDEEKIlVSYFVPLEGSAlegyasnvPDDEddgkglvkgmkkyrrlikDIREHLKQK 838
Cdd:PRK06188 430 EVEDVLAEHPAVAQvAVIGVPDEKWGEAV-TAVVVLRPGAA--------VDAA------------------ELQAHVKER 482
|
570 580
....*....|....*....|....*....
gi 2234869976 839 LPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:PRK06188 483 KGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
313-867 |
8.66e-18 |
|
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: 87.87 E-value: 8.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 313 FSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGAtfsvvdpayppsrqiiylgvakprglimlk 392
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGA------------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 393 gagtisptvreflaqelkIKVEVPGLevfpdghivggldpVGEDVLRahNHLGETDPNVVL--GPDSIGTLSFTSGSTGI 470
Cdd:cd05971 57 ------------------IAVPLFAL--------------FGPEALE--YRLSNSGASALVtdGSDDPALIIYTSGTTGP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 471 PKGVRGRH-FSLTH---------FFPWMSERFGldETSKFTMLSGIAhdpiqrDMFTP-LFLGAQL--HVPTADDigtPG 537
Cdd:cd05971 103 PKGALHAHrVLLGHlpgvqfpfnLFPRDGDLYW--TPADWAWIGGLL------DVLLPsLYFGVPVlaHRMTKFD---PK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 538 RLAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLN--AFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAVSYF 615
Cdd:cd05971 172 AALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKlrAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNC 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 616 AippvsqdstflatqkDIMPAGEGMI-------DVQLLvvnrNDRNVPCAVGEVGEIYVR---SGGLAEGYLDQDASAEK 685
Cdd:cd05971 252 S---------------ALFPIKPGSMgkpipghRVAIV----DDNGTPLPPGEVGEIAVElpdPVAFLGYWNNPSATEKK 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 686 FVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHL 765
Cdd:cd05971 313 MAGDWL----------------------------------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECL 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 766 SQHPLVReNVTLVRRDKDEEKILVSYFVPLEgsalegyASNVPDDEddgkglvkgmkkyrrLIKDIREHLKQKLPKHSVP 845
Cdd:cd05971 359 LKHPAVL-MAAVVGIPDPIRGEIVKAFVVLN-------PGETPSDA---------------LAREIQELVKTRLAAHEYP 415
|
570 580
....*....|....*....|..
gi 2234869976 846 SLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05971 416 REIEFVNELPRTATGKIRRREL 437
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
278-867 |
1.03e-17 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 88.57 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPDRPCVIqslpteSPDKPQGKVI-FSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMA 356
Cdd:PRK13295 26 INDDLDACVASCPDKTAVT------AVRLGTGAPRrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 357 VLKAGAtfsVVDPAYPPSRQiiylgvakpRGL-IMLKGAGT---ISP-TVREF----LAQELKikVEVPGLEvfpdgHI- 426
Cdd:PRK13295 100 CSRIGA---VLNPLMPIFRE---------RELsFMLKHAESkvlVVPkTFRGFdhaaMARRLR--PELPALR-----HVv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 427 -VGG----------LDPVGEDVLRAHNHLGETDPnvvlGPDSIGTLSFTSGSTGIPKGVrgRHFSLTHF---FPWmSERF 492
Cdd:PRK13295 161 vVGGdgadsfeallITPAWEQEPDAPAILARLRP----GPDDVTQLIYTSGTTGEPKGV--MHTANTLManiVPY-AERL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 493 GLDETSKFTMLSGIAHDP-IQRDMFTPLFLGAQLhvpTADDIGTPGRLAEWMAESEVTVTHL-TPAMGQLLSAQAT--RQ 568
Cdd:PRK13295 234 GLGADDVILMASPMAHQTgFMYGLMMPVMLGATA---VLQDIWDPARAAELIRTEGVTFTMAsTPFLTDLTRAVKEsgRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 569 IPTlLNAFFVGDVLTKRDCLR--LQALAANvrIINMYGTTETQrAVSyfAIPPVSQDSTFLATQKDIMPAgegmidVQLL 646
Cdd:PRK13295 311 VSS-LRTFLCAGAPIPGALVEraRAALGAK--IVSAWGMTENG-AVT--LTKLDDPDERASTTDGCPLPG------VEVR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 647 VVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQDasaekfvnNWFAVNApprkdtilhpeEGfagpesryWkgirdrmYR 726
Cdd:PRK13295 379 VVDADGAPLP--AGQIGRLQVRGCSNFGGYLKRP--------QLNGTDA-----------DG--------W-------FD 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 727 SGDLGRYLPDGTVECSGRADDqVKIRGFR-IELGEIDTHLSQHPLVREnVTLVRRdKDE---EKIlVSYFVPLEGSALEg 802
Cdd:PRK13295 423 TGDLARIDADGYIRISGRSKD-VIIRGGEnIPVVEIEALLYRHPAIAQ-VAIVAY-PDErlgERA-CAFVVPRPGQSLD- 497
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2234869976 803 yasnvpddeddgkglVKGMKKYRRlikdirehlKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:PRK13295 498 ---------------FEEMVEFLK---------AQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
278-867 |
1.44e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 87.65 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPDRPCVIQslptespdkpqGKVIFSYG----AILRASNVLAHHlimnGIQREDVVMVYAHRSVDLVVA 353
Cdd:PRK07656 7 LPELLARAARRFGDKEAYVF-----------GDQRLTYAelnaRVRRAAAALAAL----GIGKGDRVAIWAPNSPHWVIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 354 VMAVLKAGATFSVVDPAYPPSrQIIY-LGVAKPRGLIMLKGagtisptvreFLAQELKIKVEVPGLEvfpdgHIV----G 428
Cdd:PRK07656 72 ALGALKAGAVVVPLNTRYTAD-EAAYiLARGDAKALFVLGL----------FLGVDYSATTRLPALE-----HVVicetE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 429 GLDPVGEDVLRAHNHLGETDPN---VVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFtmlsg 505
Cdd:PRK07656 136 EDDPHTEKMKTFTDFLAAGDPAeraPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRY----- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 506 IAHDPiqrdMF----------TPLFLGAQ-LHVPTADdigtPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQ------ 568
Cdd:PRK07656 211 LAANP----FFhvfgykagvnAPLMRGATiLPLPVFD----PDEVFRLIETERITVLPGPPTMYNSLLQHPDRSaedlss 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 569 ----------IP-TLLNAFfvgdvltkRDCLRLQalaanvRIINMYGTTEtqrAVSYFAIPPVSQDSTFLATQkdimpAG 637
Cdd:PRK07656 283 lrlavtgaasMPvALLERF--------ESELGVD------IVLTGYGLSE---ASGVTTFNRLDDDRKTVAGT-----IG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 638 EGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQ-DASAEkfvnnwfAVnappRKDTILHpeegfagpesry 716
Cdd:PRK07656 341 TAIAGVENKIVNELGEEVP--VGEVGELLVRGPNVMKGYYDDpEATAA-------AI----DADGWLH------------ 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 717 wkgirdrmyrSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLE 796
Cdd:PRK07656 396 ----------TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKP 465
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2234869976 797 GSALegyasnvpdDEDDgkglvkgmkkyrrLIKDIREHLKqklpKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:PRK07656 466 GAEL---------TEEE-------------LIAYCREHLA----KYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1-244 |
3.51e-17 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 85.87 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1 MADQRLERVLS----RLQNLPSI-SLPTDYPRPT-----GAnkliesVHTAQLSEQTSLSLLKLAlysededheeeeedv 70
Cdd:cd19531 183 LQGEVLERQLAywreQLAGAPPVlELPTDRPRPAvqsfrGA------RVRFTLPAELTAALRALA--------------- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 71 esshKRPSA--FHLLLAAFIVLLHRYTGDTDIVVGSSSASaR-----EPLI--------LRLSVDPADPYWAVVRHVQQT 135
Cdd:cd19531 242 ----RREGAtlFMTLLAAFQVLLHRYSGQDDIVVGTPVAG-RnraelEGLIgffvntlvLRTDLSGDPTFRELLARVRET 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 136 EKEAEA--DaLPYDVITQALNkgKEDSLDR-PLFRVRF-FDETDEPTNNFIGST-------SVTS--DLTVFITRPPAst 202
Cdd:cd19531 317 ALEAYAhqD-LPFEKLVEALQ--PERDLSRsPLFQVMFvLQNAPAAALELPGLTveplevdSGTAkfDLTLSLTETDG-- 391
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2234869976 203 rasiapRLSLRVLYNSLLFTSARITSFLDQLSVFLRKVAATP 244
Cdd:cd19531 392 ------GLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
312-867 |
3.57e-17 |
|
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: 86.19 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 312 IFSYGAILRASNVLAHHLI-MNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPRGLIm 390
Cdd:cd05941 11 SITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 391 lkgagtisptvreflaqelkikvevpglevfpdghivggldpvgedvlrahnhlgetDPNVVLgpdsigtlsFTSGSTGI 470
Cdd:cd05941 90 ---------------------------------------------------------DPALIL---------YTSGTTGR 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 471 PKGVRGRHFSLTHffpwMSErfGLDETSKFTMLSGIAHD-PIQR------DMFTPLFLGAQLHVPTADDigtPGRLAEWM 543
Cdd:cd05941 104 PKGVVLTHANLAA----NVR--ALVDAWRWTEDDVLLHVlPLHHvhglvnALLCPLFAGASVEFLPKFD---PKEVAISR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 544 AESEVTVTHLTPAMGQLLSAQATRQIPTLLnafFVGDVLTKRdcLRL-----QALAANV----------RIINMYGTTET 608
Cdd:cd05941 175 LMPSITVFMGVPTIYTRLLQYYEAHFTDPQ---FARAAAAER--LRLmvsgsAALPVPTleeweaitghTLLERYGMTEI 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 609 QRAVSyfaiPPVSQDStflatqkdiMPAGEGMI--DVQLLVVNRNdRNVPCAVGEVGEIYVRSGGLAEGYLDQ-DASAEK 685
Cdd:cd05941 250 GMALS----NPLDGER---------RPGTVGMPlpGVQARIVDEE-TGEPLPRGEVGEIQVRGPSVFKEYWNKpEATKEE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 686 FVNnwfavnapprkdtilhpeegfagpesrywkgirDRMYRSGDLGRYLPDGTVECSGR-ADDQVKIRGFRIELGEIDTH 764
Cdd:cd05941 316 FTD---------------------------------DGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERV 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 765 LSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSAlegyasnvPDDEDdgkglvkgmkkyrrlikDIREHLKQKLPKHSV 844
Cdd:cd05941 363 LLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAA--------ALSLE-----------------ELKEWAKQRLAPYKR 417
|
570 580
....*....|....*....|...
gi 2234869976 845 PSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05941 418 PRRLILVDELPRNAMGKVNKKEL 440
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
284-753 |
5.47e-17 |
|
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: 86.14 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 284 RNARQNPDRPCViqslpTESPDKPQGKVIFSYGAILRASNVLAHHLIMNGiQREDVVMVYAHRSVDLVVAVMAVLKAGAt 363
Cdd:cd05931 1 RRAAARPDRPAY-----TFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 364 fsVVDPAYPPSRqiiylGVAKPR-GLIMLKGAGTISPTVREFLAQELKIKVEVPGLEVFPdghiVGGLDPVGEDVlrahn 442
Cdd:cd05931 74 --IAVPLPPPTP-----GRHAERlAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPR----LLVVDLLPDTS----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 443 hlGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSkfTMLSGIahdPIQRDM------F 516
Cdd:cd05931 138 --AADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGD--VVVSWL---PLYHDMgligglL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 517 TPLFLGAQLH-VPTADDIGTPGRLAEWMAESEVTVThLTPAMGQLLSAQATR--QIPTL----LNAFFVG------DVLT 583
Cdd:cd05931 211 TPLYSGGPSVlMSPAAFLRRPLRWLRLISRYRATIS-AAPNFAYDLCVRRVRdeDLEGLdlssWRVALNGaepvrpATLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 584 K-----RDC-LRLQA------LAANVRIINMyGTTETQRAVSYFAIPPVSQDSTFLATQKD----IMPAGEGMIDVQLLV 647
Cdd:cd05931 290 RfaeafAPFgFRPEAfrpsygLAEATLFVSG-GPPGTGPVVLRVDRDALAGRAVAVAADDPaareLVSCGRPLPDQEVRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 648 VNRnDRNVPCAVGEVGEIYVRSGGLAEGYL-DQDASAEKFvnnwfavnappRKDTilhpeegfAGPESRYWkgirdrmyR 726
Cdd:cd05931 369 VDP-ETGRELPDGEVGEIWVRGPSVASGYWgRPEATAETF-----------GALA--------ATDEGGWL--------R 420
|
490 500
....*....|....*....|....*..
gi 2234869976 727 SGDLGrYLPDGTVECSGRADDQVKIRG 753
Cdd:cd05931 421 TGDLG-FLHDGELYITGRLKDLIIVRG 446
|
|
| PRK07201 |
PRK07201 |
SDR family oxidoreductase; |
1027-1303 |
5.77e-17 |
|
SDR family oxidoreductase;
Pssm-ID: 235962 [Multi-domain] Cd Length: 657 Bit Score: 86.54 E-value: 5.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1027 TVFLTGATGFLGAFVLYDLLSRtDRVKKVICLVRgktvEQGLERLKEgstdrnvWSDSWvSSGRLEVVTGDLGLDNFGLS 1106
Cdd:PRK07201 2 RYFVTGGTGFIGRRLVSRLLDR-RREATVHVLVR----RQSLSRLEA-------LAAYW-GADRVVPLVGDLTEPGLGLS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1107 QETWNNVANeADVVLHNGALVHWVFPYEKLRSPNVLGTLTAVNLASTGKQKVFVFVSSTSAidtehyvqlseslargSTD 1186
Cdd:PRK07201 69 EADIAELGD-IDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAERLQAATFHHVSSIAV----------------AGD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1187 SKGVPESDDLEGAKSaLKTGYGQSKWVSEKLLFEAGkrGLRGHIVRPGYVVGDSHTAVTNTDDFIWRLVKGCVQLGLVPD 1266
Cdd:PRK07201 132 YEGVFREDDFDEGQG-LPTPYHRTKFEAEKLVREEC--GLPWRVYRPAVVVGDSRTGEMDKIDGPYYFFKVLAKLAKLPS 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2234869976 1267 I-------NNSINMVPVDHVAriTSLAAVSPLPDAPLSVCHVTA 1303
Cdd:PRK07201 209 WlpmvgpdGGRTNIVPVDYVA--DALDHLMHKDGRDGQTFHLTD 250
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
284-960 |
1.33e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 86.38 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 284 RNARQNPDRpcVIQSLPTESPDkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYaHRSVDLVVAVMAVLKAGAt 363
Cdd:PRK05691 17 RRAAQTPDR--LALRFLADDPG---EGVVLSYRDLDLRARTIAAALQARASFGDRAVLLF-PSGPDYVAAFFGCLYAGV- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 364 fsVVDPAYPP--------SRQIIYLGVAKPRglIMLKGAGtisptVREFLAQ-ELKIKVEVPGLEVfpdghiVGGLDPVG 434
Cdd:PRK05691 90 --IAVPAYPPesarrhhqERLLSIIADAEPR--LLLTVAD-----LRDSLLQmEELAAANAPELLC------VDTLDPAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 435 EDVLRAhnhlgetdPNvvLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIahdPIQRD 514
Cdd:PRK05691 155 AEAWQE--------PA--LQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVSWL---PLYHD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 515 M------FTPLFLGaqlhVP-----TADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLN-----AFFV 578
Cdd:PRK05691 222 MgligglLQPIFSG----VPcvlmsPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVSESALERLDlsrwrVAYS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 579 GDVLTKRDCLRLQA--LAA----NVRIINMYGTTETQRAVSY----FAIPPVSQDSTFLATQKD-------IMPAGEGMI 641
Cdd:PRK05691 298 GSEPIRQDSLERFAekFAAcgfdPDSFFASYGLAEATLFVSGgrrgQGIPALELDAEALARNRAepgtgsvLMSCGRSQP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 642 DVQLLVVNRNDRNVpCAVGEVGEIYVRSGGLAEGYL-DQDASAEKFVNNwfavnapprkdtilhpeegfagpESRYWkgi 720
Cdd:PRK05691 378 GHAVLIVDPQSLEV-LGDNRVGEIWASGPSIAHGYWrNPEASAKTFVEH-----------------------DGRTW--- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 721 rdrmYRSGDLGrYLPDGTVECSGRADDQVKIRGFRIELGEIDThlsqhpLVRENVTLVRRDKdeekiLVSYFVPLEGSAL 800
Cdd:PRK05691 431 ----LRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEK------TVEREVEVVRKGR-----VAAFAVNHQGEEG 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 801 EGYASNVpddeddGKGLVKGMKKyRRLIKDIREHLKQKLpkHSVPSLFVPLS--KMPLNPNGKIDKPALP---------- 868
Cdd:PRK05691 495 IGIAAEI------SRSVQKILPP-QALIKSIRQAVAEAC--QEAPSVVLLLNpgALPKTSSGKLQRSACRlrladgslds 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 869 ---FPDTAQASYAAGPSAPGASATEIAmqKIWSTILpnAPQPIPTDESFFDLGGHSILATRLIFEIRKVFVVNAPLGLIF 945
Cdd:PRK05691 566 yalFPALQAVEAAQTAASGDELQARIA--AIWCEQL--KVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLF 641
|
730
....*....|....*
gi 2234869976 946 EKPTIAGLVEAVDAL 960
Cdd:PRK05691 642 EAPTLAAFSAAVARQ 656
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
276-800 |
1.68e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 84.71 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 276 GAITDVFSRNARQNPDRPCVIQslptespdkpQGKVIfSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVM 355
Cdd:PRK06178 33 RPLTEYLRAWARERPQRPAIIF----------YGHVI-TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 356 AVLKAGATFSVVDPAYPPSRQIIYLGVAKPRGLIMLKgagTISPTVREFLAQELKIKVEV----------PGLEVfPDGH 425
Cdd:PRK06178 102 GILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD---QLAPVVEQVRAETSLRHVIVtsladvlpaePTLPL-PDSL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 426 IVGGLDPVGE-DVLRAHNHLGETDPNVVLGPDSIGTLSFTSGSTGIPKG--------------------VRGRHFSLTHF 484
Cdd:PRK06178 178 RAPRLAAAGAiDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGcehtqrdmvytaaaayavavVGGEDSVFLSF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 485 FP--WMS-ERFGLdetskftmlsgiahdpiqrdMFtPLFLGAQLHVptaddigtpgrLAEWMAES--------EVTVTHL 553
Cdd:PRK06178 258 LPefWIAgENFGL--------------------LF-PLFSGATLVL-----------LARWDAVAfmaaveryRVTRTVM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 554 T----------PAMGQ--LLSAQATRQIPtllnafFVGDvLTKRDCLRLQALAANVRIINMYGTTETQRAvsyfaippvs 621
Cdd:PRK06178 306 LvdnavelmdhPRFAEydLSSLRQVRVVS------FVKK-LNPDYRQRWRALTGSVLAEAAWGMTETHTC---------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 622 qDSTFLATQKDIMPAGEGMIDVQLLV------VNRNDRNVPCAVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWFavn 694
Cdd:PRK06178 369 -DTFTAGFQDDDFDLLSQPVFVGLPVpgtefkICDFETGELLPLGAEGEIVVRTPSLLKGYWNKpEATAEALRDGWL--- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 695 apprkdtilhpeegfagpesrywkgirdrmyRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVREN 774
Cdd:PRK06178 445 -------------------------------HTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGS 493
|
570 580
....*....|....*....|....*.
gi 2234869976 775 VTLVRRDKDEEKILVSYFVPLEGSAL 800
Cdd:PRK06178 494 AVVGRPDPDKGQVPVAFVQLKPGADL 519
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
280-867 |
4.93e-16 |
|
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: 82.93 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 280 DVFSRNARQNPDRPCVIQSlptespDKPQGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLK 359
Cdd:cd05970 21 DVVDAMAKEYPDKLALVWC------DDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 360 AGATfSVVDPAYPPSRQIIYLGVAKPRGLIMLKGAGTISPTVREFLAQ----ELKIKVEVPGLEVFPDGHivGGLDPVGE 435
Cdd:cd05970 95 LGAI-AIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKAAPEcpskPKLVWVGDPVPEGWIDFR--KLIKNASP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 436 DVLRAHNhlgetdpNVVLGPDSIGTLSFTSGSTGIPKGVRGRH-FSLTHFFP---WMSER-FGLDETskftmlsgIAHDP 510
Cdd:cd05970 172 DFERPTA-------NSYPCGEDILLVYFSSGTTGMPKMVEHDFtYPLGHIVTakyWQNVReGGLHLT--------VADTG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 511 IQRDMFTPLF----LGAQLHVPTADDIgTPGRLAEWMAESEVTVTHLTPAMGQ-LLSAQATR-QIPTLLNAFFVGDVLTK 584
Cdd:cd05970 237 WGKAVWGKIYgqwiAGAAVFVYDYDKF-DPKALLEKLSKYGVTTFCAPPTIYRfLIREDLSRyDLSSLRYCTTAGEALNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 585 RDCLRLQALAAnVRIINMYGTTETqravsyfaippVSQDSTFLATQKDIMPAGEGMIDVQLLVVNRNDRnvPCAVGEVGE 664
Cdd:cd05970 316 EVFNTFKEKTG-IKLMEGFGQTET-----------TLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGR--SCEAGEEGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 665 IYVRSG-----GLAEGYLDqdaSAEKFVNNWFavnapprkdtilhpeegfagpesrywkgirDRMYRSGDLGRYLPDGTV 739
Cdd:cd05970 382 IVIRTSkgkpvGLFGGYYK---DAEKTAEVWH------------------------------DGYYHTGDAAWMDEDGYL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 740 ECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRE-NVTLVRRdkdeekilvsyfvPLEGSALEgyASNVpddeddgkgLV 818
Cdd:cd05970 429 WFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLEcAVTGVPD-------------PIRGQVVK--ATIV---------LA 484
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2234869976 819 KGMKKYRRLIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05970 485 KGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
316-867 |
8.02e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 82.16 E-value: 8.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 316 GAILRASNVLAHHlimnGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPRglimlkgag 395
Cdd:PRK09088 30 ALVGRLAAVLRRR----GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPR--------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 396 tisptvreflaqelkikvevpgLEVFPDGHIVGGLDPVGEDVLRAHNHLGETDPNVVLGPDSIGTLSFTSGSTGIPKGVr 475
Cdd:PRK09088 97 ----------------------LLLGDDAVAAGRTDVEDLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGV- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 476 grhfslthffpWMSERfGLDETS-KFTMLSGIAHDPI---QRDMFTPLFLGAQLHvPTADDIGT--------PGRLAEWM 543
Cdd:PRK09088 154 -----------MLSER-NLQQTAhNFGVLGRVDAHSSflcDAPMFHIIGLITSVR-PVLAVGGSilvsngfePKRTLGRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 544 AESEVTVTHL--TPAMGQLLSAQATRQIPTL--LNAFFVGDVLTKRDCLRlQALAANVRIINMYGTTEtqrAVSYFAIPp 619
Cdd:PRK09088 221 GDPALGITHYfcVPQMAQAFRAQPGFDAAALrhLTALFTGGAPHAAEDIL-GWLDDGIPMVDGFGMSE---AGTVFGMS- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 620 vsQDSTFLATQKDimPAGEGMIDVQLLVVNRNDRNvpCAVGEVGEIYVRSGGLAEGYL-DQDASAEKFV-NNWFavnapp 697
Cdd:PRK09088 296 --VDCDVIRAKAG--AAGIPTPTVQTRVVDDQGND--CPAGVPGELLLRGPNLSPGYWrRPQATARAFTgDGWF------ 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 698 rkdtilhpeegfagpesrywkgirdrmyRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTL 777
Cdd:PRK09088 364 ----------------------------RTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVV 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 778 VRRDKDEEKIlvsyfvplegsaleGYASNVPDDEDDgkglvkgmkkyrRLIKDIREHLKQKLPKHSVPSLFVPLSKMPLN 857
Cdd:PRK09088 416 GMADAQWGEV--------------GYLAIVPADGAP------------LDLERIRSHLSTRLAKYKVPKHLRLVDALPRT 469
|
570
....*....|
gi 2234869976 858 PNGKIDKPAL 867
Cdd:PRK09088 470 ASGKLQKARL 479
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
460-867 |
1.06e-15 |
|
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: 80.07 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 460 TLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIgtpgrL 539
Cdd:cd17630 4 TVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQA-----L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 540 AEWMAESEVTVTHLTPAM-GQLLSAQATRQIPTLLNAFFVGDVLTKRDcLRLQALAANVRIINMYGTTETQRAVSYFAiP 618
Cdd:cd17630 79 AEDLAPPGVTHVSLVPTQlQRLLDSGQGPAALKSLRAVLLGGAPIPPE-LLERAADRGIPLYTTYGMTETASQVATKR-P 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 619 PVSQDSTflatqkdimpAGEGMIDVQLLVVNRndrnvpcavgevGEIYVRSGGLAEGYLDQDASAEKFVNNWFavnappr 698
Cdd:cd17630 157 DGFGRGG----------VGVLLPGRELRIVED------------GEIWVGGASLAMGYLRGQLVPEFNEDGWF------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 699 kdtilhpeegfagpesrywkgirdrmyRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVREnvtlv 778
Cdd:cd17630 208 ---------------------------TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRD----- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 779 rrdkdeekilvSYFVPlegsalegyasnVPDDEdDGKGLVKGMK-KYRRLIKDIREHLKQKLPKHSVPSLFVPLSKMPLN 857
Cdd:cd17630 256 -----------AFVVG------------VPDEE-LGQRPVAVIVgRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRT 311
|
410
....*....|
gi 2234869976 858 PNGKIDKPAL 867
Cdd:cd17630 312 GGGKVDRRAL 321
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
320-867 |
1.37e-15 |
|
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: 81.01 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 320 RASNVLAHHlimnGIQREDVVMVYAHRSVDLVVAVMAVLKAGAtfsvvdpayppsrqiiylgvakprglimlkgagtisp 399
Cdd:cd05969 12 RFANVLKSL----GVGKGDRVFVLSPRSPELYFSMLGIGKIGA------------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 400 tvreflaqelkikVEVPGLEVFPDGHIVGGLDPVGEDVLRAHNHLGE-TDPNVVLgpdsigTLSFTSGSTGIPKGVRGRH 478
Cdd:cd05969 51 -------------VICPLFSAFGPEAIRDRLENSEAKVLITTEELYErTDPEDPT------LLHYTSGTTGTPKGVLHVH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 479 FSLThfFPWMSER--FGLDETSKF------TMLSGIAHdpiqrDMFTPLFLGAQLHVPTADdiGTPGRLAEWMAESEVTV 550
Cdd:cd05969 112 DAMI--FYYFTGKyvLDLHPDDIYwctadpGWVTGTVY-----GIWAPWLNGVTNVVYEGR--FDAESWYGIIERVKVTV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 551 THLTPA-----MGQLLSAQATRQIPTLLNAFFVGDVLTKrDCLRLQALAANVRIINMYGTTET--QRAVSYFAIPpvsqd 623
Cdd:cd05969 183 WYTAPTairmlMKEGDELARKYDLSSLRFIHSVGEPLNP-EAIRWGMEVFGVPIHDTWWQTETgsIMIANYPCMP----- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 624 stflatqkdIMPAGEGM--IDVQLLVVNRNDRNVPcaVGEVGEIYVRSGglaegyldqdasaekfvnnWfavnaPPRKDT 701
Cdd:cd05969 257 ---------IKPGSMGKplPGVKAAVVDENGNELP--PGTKGILALKPG-------------------W-----PSMFRG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 702 ILHPEEgfagpesRYWKGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRD 781
Cdd:cd05969 302 IWNDEE-------RYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPD 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 782 kdeekilvsyfvPLEGSALEGYASnvpddeddgkgLVKGMKKYRRLIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGK 861
Cdd:cd05969 375 ------------PLRGEIIKAFIS-----------LKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGK 431
|
....*.
gi 2234869976 862 IDKPAL 867
Cdd:cd05969 432 IMRRVL 437
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
463-864 |
2.10e-15 |
|
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: 78.99 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 463 FTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDigtPGRLAEW 542
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFN---PKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 543 MAESEVTVTHLTPAMGQLLsAQATRQIPTLLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETqravSYFaippvsq 622
Cdd:cd17633 84 INQYNATVIYLVPTMLQAL-ARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL----SFI------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 623 dsTFLATQKDIMP--AGEGMIDVQLLVVNRNDrnvpcavGEVGEIYVRSGGLAEGYLDqdasaEKFVNN--WFAVNappr 698
Cdd:cd17633 152 --TYNFNQESRPPnsVGRPFPNVEIEIRNADG-------GEIGKIFVKSEMVFSGYVR-----GGFSNPdgWMSVG---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 699 kdtilhpeegfagpesrywkgirdrmyrsgDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLV 778
Cdd:cd17633 214 ------------------------------DIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 779 RRDKDEEKILVSYFVplegsalegyasnvpddeddGKGLVKgmkkyrrliKDIREHLKQKLPKHSVPSLFVPLSKMPLNP 858
Cdd:cd17633 264 IPDARFGEIAVALYS--------------------GDKLTY---------KQLKRFLKQKLSRYEIPKKIIFVDSLPYTS 314
|
....*.
gi 2234869976 859 NGKIDK 864
Cdd:cd17633 315 SGKIAR 320
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
307-799 |
2.51e-15 |
|
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: 80.63 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 307 PQGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAyppsrqiiylgvAKPR 386
Cdd:cd05923 23 PARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR------------LKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 387 GLIMLKGAGTISPTVREflaqelkikVEVPGLEVFPDGhiVGGLDPVGEDV-LRAHNHLGETDPNVVLGPDSIGTLSFTS 465
Cdd:cd05923 91 ELAELIERGEMTAAVIA---------VDAQVMDAIFQS--GVRVLALSDLVgLGEPESAGPLIEDPPREPEQPAFVFYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 466 GSTGIPKGVRGRHFSLTHFFPWMSE----RFGLDETSKFTMlsgiahdPIQRDM-FTPLFLGA-----QLHVPTADDigt 535
Cdd:cd05923 160 GTTGLPKGAVIPQRAAESRVLFMSTqaglRHGRHNVVLGLM-------PLYHVIgFFAVLVAAlaldgTYVVVEEFD--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 536 PGRLAEWMAESEVTVTHLTPAMGQLL---SAQATRQIPTLLNAFFVGDVLTKRDCLRLQALAANvRIINMYGTTETQRAV 612
Cdd:cd05923 230 PADALKLIEQERVTSLFATPTHLDALaaaAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG-EKVNIYGTTEAMNSL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 613 SYFAIPPVSQDSTFLATQKDIMPAGEGMIdvqllvvnrndrnVPCAVGEVGEIYVRSGGLA--EGYLDQ-DASAEKfvnn 689
Cdd:cd05923 309 YMRDARTGTEMRPGFFSEVRIVRIGGSPD-------------EALANGEEGELIVAAAADAafTGYLNQpEATAKK---- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 690 wfavnapprkdtilhpeegfagpesrywkgIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHP 769
Cdd:cd05923 372 ------------------------------LQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHP 421
|
490 500 510
....*....|....*....|....*....|
gi 2234869976 770 LVRENVTLVRRDKDEEKILVSYFVPLEGSA 799
Cdd:cd05923 422 GVTEVVVIGVADERWGQSVTACVVPREGTL 451
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
281-867 |
3.89e-15 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 80.19 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 281 VFSRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKA 360
Cdd:PRK06155 26 MLARQAERYPDRPLLVF-----------GGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 361 GATFSVVDPAY--PPSRQIiyLGVAKPRGLI----MLKGAGTISPTVrefLAQELKIKVEVPGLEVFPDGHIVGGLDPVG 434
Cdd:PRK06155 95 GAIAVPINTALrgPQLEHI--LRNSGARLLVveaaLLAALEAADPGD---LPLPAVWLLDAPASVSVPAGWSTAPLPPLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 435 EDVlrahnhlgetdPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHfslTHFFPW---MSERFGLDETSK-FTMLSgIAHDP 510
Cdd:PRK06155 170 APA-----------PAAAVQPGDTAAILYTSGTTGPSKGVCCPH---AQFYWWgrnSAEDLEIGADDVlYTTLP-LFHTN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 511 IQRDMFTPLFLGAQLHVptaddigTP----GRLAEWMAESEVTVTHLTPAMGQLLSAQATRQ--------------IPTL 572
Cdd:PRK06155 235 ALNAFFQALLAGATYVL-------EPrfsaSGFWPAVRRHGATVTYLLGAMVSILLSQPAREsdrahrvrvalgpgVPAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 573 LNAFFvgdvlTKRdclrlqalaANVRIINMYGTTETQravSYFAIPPVSQDstflatqkdimPAGEGMI--DVQLLVVNR 650
Cdd:PRK06155 308 LHAAF-----RER---------FGVDLLDGYGSTETN---FVIAVTHGSQR-----------PGSMGRLapGFEARVVDE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 651 NDRNVPcaVGEVGEIYVRS---GGLAEGYldqDASAEKFVNNWfavnapprkdtilhpeegfagpesrywkgiRDRMYRS 727
Cdd:PRK06155 360 HDQELP--DGEPGELLLRAdepFAFATGY---FGMPEKTVEAW------------------------------RNLWFHT 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 728 GDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRE-NVTLVRRDKDEEKILVSyFVPLEGSALEgyasn 806
Cdd:PRK06155 405 GDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAaAVFPVPSELGEDEVMAA-VVLRDGTALE----- 478
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2234869976 807 vPDDeddgkgLVkgmkkyrrlikdirEHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:PRK06155 479 -PVA------LV--------------RHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| AR_FR_like_1_SDR_e |
cd05228 |
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ... |
1028-1287 |
4.77e-15 |
|
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187539 [Multi-domain] Cd Length: 318 Bit Score: 77.71 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1028 VFLTGATGFLGAFVLYDLLSRTDRVKkviCLVRgktveqglerlkegSTDRNVWSDSwvssGRLEVVTGDLgLDNFGLSQ 1107
Cdd:cd05228 1 ILVTGATGFLGSNLVRALLAQGYRVR---ALVR--------------SGSDAVLLDG----LPVEVVEGDL-TDAASLAA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1108 etwnnVANEADVVLHNGALV-----HWvfpyEKLRSPNVLGTLTAVNLASTGKQKVFVFVSSTSAIDTEHYVQLSESLAR 1182
Cdd:cd05228 59 -----AMKGCDRVFHLAAFTslwakDR----KELYRTNVEGTRNVLDAALEAGVRRVVHTSSIAALGGPPDGRIDETTPW 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1183 gstdskgvpesddlegAKSALKTGYGQSKWVSEKLLFEAGKRGLRGHIVRPGYVVGDSHTAVTNTDDFIWRLVKGcvQLG 1262
Cdd:cd05228 130 ----------------NERPFPNDYYRSKLLAELEVLEAAAEGLDVVIVNPSAVFGPGDEGPTSTGLDVLDYLNG--KLP 191
|
250 260
....*....|....*....|....*
gi 2234869976 1263 LVPDinNSINMVPVDHVARITSLAA 1287
Cdd:cd05228 192 AYPP--GGTSFVDVRDVAEGHIAAM 214
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
278-773 |
5.63e-15 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 80.14 E-value: 5.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPDRPCVIQslptespdKPQGK-VIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMA 356
Cdd:COG1022 13 LPDLLRRRAARFPDRVALRE--------KEDGIwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 357 VLKAGAtfsVVDPAYP--PSRQIIY-LGVAKPRGLImlkgAGTisptvREFLAQELKIKVEVPGLEvfpdgHIVGgLDPV 433
Cdd:COG1022 85 ILAAGA---VTVPIYPtsSAEEVAYiLNDSGAKVLF----VED-----QEQLDKLLEVRDELPSLR-----HIVV-LDPR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 434 G----------EDVL---RAHNHLGETDPNVV-LGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSK 499
Cdd:COG1022 147 GlrddprllslDELLalgREVADPAELEARRAaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 500 -----------------FTMLSG--IAHDP----IQRDM--FTPLFLGAqlhVPtaddigtpgRLAEWMAES-EVTVTHL 553
Cdd:COG1022 227 tlsflplahvfertvsyYALAAGatVAFAEspdtLAEDLreVKPTFMLA---VP---------RVWEKVYAGiQAKAEEA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 554 TPAMGQLLSA------------QATRQIPTLLNA-FFVGD--VLTK-RDCL--RLQAL----------------AANVRI 599
Cdd:COG1022 295 GGLKRKLFRWalavgrryararLAGKSPSLLLRLkHALADklVFSKlREALggRLRFAvsggaalgpelarffrALGIPV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 600 INMYGTTETqravsyfaIPPVSqdstflatqkdimpagegmidvqllvVNRNDRNVPCAVG------EV-----GEIYVR 668
Cdd:COG1022 375 LEGYGLTET--------SPVIT--------------------------VNRPGDNRIGTVGpplpgvEVkiaedGEILVR 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 669 SGGLAEGYL-DQDASAEKFVnnwfavnapprkdtilhpEEGFagpesrywkgirdrmYRSGDLGRYLPDGTVECSGRADD 747
Cdd:COG1022 421 GPNVMKGYYkNPEATAEAFD------------------ADGW---------------LHTGDIGELDEDGFLRITGRKKD 467
|
570 580
....*....|....*....|....*..
gi 2234869976 748 QVKIR-GFRIELGEIDTHLSQHPLVRE 773
Cdd:COG1022 468 LIVTSgGKNVAPQPIENALKASPLIEQ 494
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
274-867 |
6.34e-15 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 79.29 E-value: 6.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 274 WKG-AITDVFSRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVV 352
Cdd:cd05920 12 WQDePLGDLLARSAARHPDRIAVVD-----------GDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 353 AVMAVLKAGAtfsVVDPAYPPSRQIIYLGVAKPRGLIMLKGAGTISPTVREFLAQELkikvevpglevfpdghivggldp 432
Cdd:cd05920 81 LFFALLRLGA---VPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAGFDHRALAREL----------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 433 vgedvlrAHNHlgetdPNVVLgpdsigtLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHdpiQ 512
Cdd:cd05920 135 -------AESI-----PEVAL-------FLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH---N 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 513 RDMFTPLFLGAQL---HVPTADDiGTPGRLAEWMAESEVTVTHLTPAMGQL-LSAQATRQI-PTLLNAFFVGDVltkrdc 587
Cdd:cd05920 193 FPLACPGVLGTLLaggRVVLAPD-PSPDAAFPLIEREGVTVTALVPALVSLwLDAAASRRAdLSSLRLLQVGGA------ 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 588 lRLQALAA-------NVRIINMYGTTETqrAVSYFAIPpvSQDSTFLATQ-KDIMPagegmiDVQLLVVNRNDRNVPcaV 659
Cdd:cd05920 266 -RLSPALArrvppvlGCTLQQVFGMAEG--LLNYTRLD--DPDEVIIHTQgRPMSP------DDEIRVVDEEGNPVP--P 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 660 GEVGEIYVRSGGLAEGYLD-QDASAEKFVnnwfavnapprkdtilhpEEGFagpesrywkgirdrmYRSGDLGRYLPDGT 738
Cdd:cd05920 333 GEEGELLTRGPYTIRGYYRaPEHNARAFT------------------PDGF---------------YRTGDLVRRTPDGY 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 739 VECSGRADDQVKIRGFRIELGEIDTHLSQHPLVREnVTLVRRDkDE---EKILVsyFVPLEGSALEgyasnvpddeddgk 815
Cdd:cd05920 380 LVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHD-AAVVAMP-DEllgERSCA--FVVLRDPPPS-------------- 441
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2234869976 816 glvkgmkkyrrlIKDIREHLKQK-LPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05920 442 ------------AAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
278-736 |
9.63e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 76.24 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPDRPCVIQSLPtesPDKPQGKVifSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAV 357
Cdd:PRK12582 51 IPHLLAKWAAEAPDRPWLAQREP---GHGQWRKV--TYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 358 LKAGATFSVVDPAYPPSRQ----IIYL-GVAKPRGLIMLKGAgtisPTVREFLAQELkIKVEVPGLEVFPDGHIVGGLD- 431
Cdd:PRK12582 126 MQAGVPAAPVSPAYSLMSHdhakLKHLfDLVKPRVVFAQSGA----PFARALAALDL-LDVTVVHVTGPGEGIASIAFAd 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 432 ----PVGEDVLRAHNHLGetdpnvvlgPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSK-------- 499
Cdd:PRK12582 201 laatPPTAAVAAAIAAIT---------PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPppvsldwm 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 500 ---FTMLSGIAHDPIqrdmftpLFLGAQLHVptadDIG--TPGRLAEWMA---ESEVTVTHLTPAMGQLLsAQATRQIPT 571
Cdd:PRK12582 272 pwnHTMGGNANFNGL-------LWGGGTLYI----DDGkpLPGMFEETIRnlrEISPTVYGNVPAGYAML-AEAMEKDDA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 572 LLNAFFV--------GDVLTKRDCLRLQALAA-----NVRIINMYGTTETQravsyfaipPVSQdSTFLATQKdimpagE 638
Cdd:PRK12582 340 LRRSFFKnlrlmaygGATLSDDLYERMQALAVrttghRIPFYTGYGATETA---------PTTT-GTHWDTER------V 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 639 GMI-----DVQLLVVnrndrnvpcAVGEVGEIYVRSGGLAEGYL-DQDASAEKFvnnwfavnapprkdtilhPEEGFagp 712
Cdd:PRK12582 404 GLIglplpGVELKLA---------PVGDKYEVRVKGPNVTPGYHkDPELTAAAF------------------DEEGF--- 453
|
490 500
....*....|....*....|....*
gi 2234869976 713 esrywkgirdrmYRSGDLGRYL-PD 736
Cdd:PRK12582 454 ------------YRLGDAARFVdPD 466
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
285-800 |
3.23e-13 |
|
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: 73.81 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 285 NARQNPDRPCVIqslptespDKPQGKVIfSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATF 364
Cdd:cd05904 14 FASAHPSRPALI--------DAATGRAL-TYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 365 SVVDPAYPPS---RQIiylGVAKPRGLImlkgagTISPTVREFLAQELKIKV----EVPGLEVFPDGHIVGGLDPvgedv 437
Cdd:cd05904 85 TTANPLSTPAeiaKQV---KDSGAKLAF------TTAELAEKLASLALPVVLldsaEFDSLSFSDLLFEADEAEP----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 438 lrahnhlgetdPNVVLGPDSIGTLSFTSGSTGIPKGVrgrhfSLTHffpwmseRFGLDETSKFTMLSGIAHDPIQRDMFT 517
Cdd:cd05904 151 -----------PVVVIKQDDVAALLYSSGTTGRSKGV-----MLTH-------RNLIAMVAQFVAGEGSNSDSEDVFLCV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 518 -PLF--------------LGAQLHVPTADDIGTPGRLAEwmaesEVTVTHLtPAmgqllsaqatrqIPTLLNAFFVGDVL 582
Cdd:cd05904 208 lPMFhiyglssfalgllrLGATVVVMPRFDLEELLAAIE-----RYKVTHL-PV------------VPPIVLALVKSPIV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 583 TKRDCLRLQAL---AA---------------NVRIINMYGTTETQravsyfaipPVSqdSTFLATQKDIMPAGE-GMI-- 641
Cdd:cd05904 270 DKYDLSSLRQImsgAAplgkelieafrakfpNVDLGQGYGMTEST---------GVV--AMCFAPEKDRAKYGSvGRLvp 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 642 DVQLLVVNRNDrNVPCAVGEVGEIYVRSGGLAEGYL-DQDASAEkfvnnwfavnapprkdTILhpEEGFagpesrywkgi 720
Cdd:cd05904 339 NVEAKIVDPET-GESLPPNQTGELWIRGPSIMKGYLnNPEATAA----------------TID--KEGW----------- 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 721 rdrmYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSAL 800
Cdd:cd05904 389 ----LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSL 464
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
265-862 |
4.73e-13 |
|
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: 73.77 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 265 PTGDLNWCgwkgaiTDVFSRNARQNPDRPCVIQslptESPDKPQGKVIfSYGAILRASNVLAHHLIMNGIQREDVVMVYA 344
Cdd:cd17634 48 EDATLNLA------ANALDRHLRENGDRTAIIY----EGDDTSQSRTI-SYRELHREVCRFAGTLLDLGVKKGDRVAIYM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 345 HRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPRGLImlkgagTISPTVREFLAQELKIKVEVPGLEVFPDG 424
Cdd:cd17634 117 PMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLI------TADGGVRAGRSVPLKKNVDDALNPNVTSV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 425 HIVGGLDPVGEDV-------LRAHNHLGETDPN---VVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPW-MSERFG 493
Cdd:cd17634 191 EHVIVLKRTGSDIdwqegrdLWWRDLIAKASPEhqpEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATtMKYVFD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 494 L---DETSKFTMLSGIAHDPIQrdMFTPLFLGAQ-LHVPTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQI 569
Cdd:cd17634 271 YgpgDIYWCTADVGWVTGHSYL--LYGPLACGATtLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 570 -----PTLLNAFFVGD------------VLTKRDClrlqalaanvRIINMYGTTETqravSYFAIPPVSQDSTFLATQkd 632
Cdd:cd17634 349 egtdrSSLRILGSVGEpinpeayewywkKIGKEKC----------PVVDTWWQTET----GGFMITPLPGAIELKAGS-- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 633 impAGEGMIDVQLLVVnrNDRNVPCAVGEVGEIYVrsgglaegyldqdasaekfVNNWfavnaPPRKDTILHPEEGFagp 712
Cdd:cd17634 413 ---ATRPVFGVQPAVV--DNEGHPQPGGTEGNLVI-------------------TDPW-----PGQTRTLFGDHERF--- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 713 ESRYWKGIrDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDkdeekilvsyf 792
Cdd:cd17634 461 EQTYFSTF-KGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPH----------- 528
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 793 vPLEGSALEGYASNVPdDEDDGKGLVkgmkkyrrliKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKI 862
Cdd:cd17634 529 -AIKGQAPYAYVVLNH-GVEPSPELY----------AELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
314-826 |
6.81e-13 |
|
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: 72.51 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 314 SYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYppsrqiiylgvaKPRGLimlkg 393
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPML------------KEREL----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 394 agtisptvrEFLAQELKIKVEVPGLEVfpdghivggldpvgedvlrahnhlgetdpnvvlgpDSIGTLSFTSGSTGIPKG 473
Cdd:cd05935 66 ---------EYILNDSGAKVAVVGSEL-----------------------------------DDLALIPYTSGTTGLPKG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 474 VRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDP-IQRDMFTPLFLGAQLHVPTADDIGTpgrLAEWMAESEVTV-T 551
Cdd:cd05935 102 CMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTgFVGSLNTAVYVGGTYVLMARWDRET---ALELIEKYKVTFwT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 552 HLTPAMGQLLSAQ--ATRQIPTLLNAFFVGDVLTKRDCLRLQALAAnVRIINMYGTTETQRAVSyfAIPPVSQDSTFLat 629
Cdd:cd05935 179 NIPTMLVDLLATPefKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG-LRFVEGYGLTETMSQTH--TNPPLRPKLQCL-- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 630 qkdimpaGEGMIDVQLLVVNRNDrNVPCAVGEVGEIYVRSGGLAEGYLDQdasaekfvnnwfavnapprkdtilhPEEGf 709
Cdd:cd05935 254 -------GIP*FGVDARVIDIET-GRELPPNEVGEIVVRGPQIFKGYWNR-------------------------PEET- 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 710 agpESRYWKGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVREnVTLVRRDKDEEKILV 789
Cdd:cd05935 300 ---EESFIEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E-VCVISVPDERVGEEV 375
|
490 500 510
....*....|....*....|....*....|....*...
gi 2234869976 790 SYFVPLEgsalEGYASNVpdDEDDGKGLVKG-MKKYRR 826
Cdd:cd05935 376 KAFIVLR----PEYRGKV--TEEDIIEWAREqMAAYKY 407
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
461-867 |
1.09e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 72.12 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 461 LSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHV-PTAddigTPGRL 539
Cdd:PRK07638 148 MGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLmRKF----IPNQV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 540 AEWMAESEVTVTHLTPAMGQ-LLSAQATRQIPtlLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQrAVSYFaip 618
Cdd:PRK07638 224 LDKLETENISVMYTVPTMLEsLYKENRVIENK--MKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELS-FVTAL--- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 619 pVSQDSTFLATQkdimpAGEGMIDVQLLVvnRNDRNVPCAVGEVGEIYVRSGGLAEGYLDQDASAEKF-VNNWFAVnapp 697
Cdd:PRK07638 298 -VDEESERRPNS-----VGRPFHNVQVRI--CNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELnADGWMTV---- 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 698 rkdtilhpeegfagpesrywkgirdrmyrsGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTL 777
Cdd:PRK07638 366 ------------------------------RDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVI 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 778 VRRDkdeekilvSYFvpleGSALEGYasnvpddeddgkglVKGmkkyRRLIKDIREHLKQKLPKHSVPSLFVPLSKMPLN 857
Cdd:PRK07638 416 GVPD--------SYW----GEKPVAI--------------IKG----SATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYT 465
|
410
....*....|
gi 2234869976 858 PNGKIDKPAL 867
Cdd:PRK07638 466 NSGKIARMEA 475
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
278-867 |
1.56e-12 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 71.84 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPDRPCVIQSlptespdkpQGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAV 357
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVT---------ADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 358 LKAGATFSVVDPAYPPSRQIIYLGVAKPRG-LIMLKGAG-TISPTVREFlaqelKIKVEVPGLEVFPDGHIVGGLDPVGE 435
Cdd:PRK05852 89 SRADLVVVPLDPALPIAEQRVRSQAAGARVvLIDADGPHdRAEPTTRWW-----PLTVNVGGDSGPSGGTLSVHLDAATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 436 DVLRAHNHLGetdpnvvLGPDSiGTLSFTSGSTGIPKGVrgrhfslthffPWMSERFGldeTSKFTMLSGIAHDPiqRD- 514
Cdd:PRK05852 164 PTPATSTPEG-------LRPDD-AMIMFTGGTTGLPKMV-----------PWTHANIA---SSVRAIITGYRLSP--RDa 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 515 --MFTPLFLGAQLHVPTADDIGTPGRL-----------AEWMAESEVTVTHLT--PAMGQLL----SAQATRQIPTLLNa 575
Cdd:PRK05852 220 tvAVMPLYHGHGLIAALLATLASGGAVllpargrfsahTFWDDIKAVGATWYTavPTIHQILleraATEPSGRKPAALR- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 576 fFVGDVLTKRDCLRLQALAAN--VRIINMYGTTETQRAVSYFAIPPVSQDSTFLATQKdimPAGEGMiDVQLLVVNRNDR 653
Cdd:PRK05852 299 -FIRSCSAPLTAETAQALQTEfaAPVVCAFGMTEATHQVTTTQIEGIGQTENPVVSTG---LVGRST-GAQIRIVGSDGL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 654 nvPCAVGEVGEIYVRSGGLAEGYL-DQDASAEKFVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLGR 732
Cdd:PRK05852 374 --PLPAGAVGEVWLRGTTVVRGYLgDPTITAANFTDGWL----------------------------------RTGDLGS 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 733 YLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALEGyasnvpdded 812
Cdd:PRK05852 418 LSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTA---------- 487
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 2234869976 813 dgkglvkgmkkyrrliKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:PRK05852 488 ----------------EELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
14-262 |
3.27e-12 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 70.44 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 14 QNLPSISLPTDYPRPTGANKLIESVhTAQLSEQTSLSLLKLA------LYSededheeeeedvesshkrpsafhLLLAAF 87
Cdd:pfam00668 204 GELPVLQLPKDYARPADRSFKGDRL-SFTLDEDTEELLRKLAkahgttLND-----------------------VLLAAY 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 88 IVLLHRYTGDTDIVVGSSSASAREPLI------------LRLSVDPADPYWAVVRHVQQTEKEAE-ADALPYDVITQALN 154
Cdd:pfam00668 260 GLLLSRYTGQDDIVVGTPGSGRPSPDIermvgmfvntlpLRIDPKGGKTFSELIKRVQEDLLSAEpHQGYPFGDLVNDLR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 155 KgKEDSLDRPLFRVRF----FDETDEPTNNFIGSTSVTSDLTVFITRPPASTRASIAPR---LSLRVLYNSLLFTSARIT 227
Cdd:pfam00668 340 L-PRDLSRHPLFDPMFsfqnYLGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERgggLTIKIDYNTSLFDEETIE 418
|
250 260 270
....*....|....*....|....*....|....*
gi 2234869976 228 SFLDQLSVFLRKVAATPLSPVGSVPLLTPSQKAVL 262
Cdd:pfam00668 419 RFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
455-867 |
1.03e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 68.28 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 455 PDSIGTLSFTSGSTGIPKGVRGRHFSLThFFPWMSERFgLDETSKFTMLSGIAHDPIQRDM---FTPLFLGAQLHVPTAD 531
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEV-YNAWMLALN-SLFDPDDVLLCGLPLFHVNGSVvtlLTPLASGAHVVLAGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 532 DIGTPG------RLAE-WMAESEVTVThltPAMGQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRLQAlAANVRIINMYG 604
Cdd:cd05944 79 GYRNPGlfdnfwKLVErYRITSLSTVP---TVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFED-ATGLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 605 TTETQRAVSyfAIPPvsqdstflATQKDIMPAGEGM--IDVQLLVVNRNDRNV-PCAVGEVGEIYVRSGGLAEGYLDQDA 681
Cdd:cd05944 155 LTEATCLVA--VNPP--------DGPKRPGSVGLRLpyARVRIKVLDGVGRLLrDCAPDEVGEICVAGPGVFGGYLYTEG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 682 SAEKFVNnwfavnapprkdtilhpeegfagpesrywkgirDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEI 761
Cdd:cd05944 225 NKNAFVA---------------------------------DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 762 DTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALEGYAsnvpddeddgkglvkgmkkyrrLIKDIREHLKQKLpk 841
Cdd:cd05944 272 EEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEE----------------------LLAWARDHVPERA-- 327
|
410 420
....*....|....*....|....*.
gi 2234869976 842 hSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05944 328 -AVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
307-862 |
1.06e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 69.15 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 307 PQGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPS--RQIIYLGVAK 384
Cdd:PRK04319 68 ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEavRDRLEDSEAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 385 prGLImlkgagtispTVREFLAQelKIKVEVPGLE-VFpdghIVGGLDPVGEDVLRAHNHLGETDPN---VVLGPDSIGT 460
Cdd:PRK04319 148 --VLI----------TTPALLER--KPADDLPSLKhVL----LVGEDVEEGPGTLDFNALMEQASDEfdiEWTDREDGAI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 461 LSFTSGSTGIPKGVRGRHFS-LTHffpWMSERFGLD--ETSKF---------TMLS-GIahdpiqrdmFTPLFLGAQLHV 527
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHNAmLQH---YQTGKYVLDlhEDDVYwctadpgwvTGTSyGI---------FAPWLNGATNVI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 528 PTADdiGTPGRLAEWMAESEVTVTHLTP-AMGQLLSAqatrqiptllnaffvGDVLTKR---DCLRLQAL---------- 593
Cdd:PRK04319 278 DGGR--FSPERWYRILEDYKVTVWYTAPtAIRMLMGA---------------GDDLVKKydlSSLRHILSvgeplnpevv 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 594 -----AANVRIINMYGTTET--QRAVSYFAIppvsqdstflatqkDIMPA--GEGMIDVQLLVVNRNDRNVPcaVGEVGE 664
Cdd:PRK04319 341 rwgmkVFGLPIHDNWWMTETggIMIANYPAM--------------DIKPGsmGKPLPGIEAAIVDDQGNELP--PNRMGN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 665 IYVRSGglaegyldqdasaekfvnnWfavnaPPRKDTILHPEEgfagpesRYWKGIRDRMYRSGDLGRYLPDGTVECSGR 744
Cdd:PRK04319 405 LAIKKG-------------------W-----PSMMRGIWNNPE-------KYESYFAGDWYVSGDSAYMDEDGYFWFQGR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 745 ADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKIlVSYFVPLEgsalEGYAsnvPDDEddgkglvkgmkky 824
Cdd:PRK04319 454 VDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEI-IKAFVALR----PGYE---PSEE------------- 512
|
570 580 590
....*....|....*....|....*....|....*...
gi 2234869976 825 rrLIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKI 862
Cdd:PRK04319 513 --LKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI 548
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
283-864 |
1.19e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 68.91 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 283 SRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGA 362
Cdd:PRK07470 14 RQAARRFPDRIALVW-----------GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 363 TFSVVDPAYPPSrQIIYLGVAKpRGLIMLKGAGtisptvreFLAQELKIKVEVPGLEvfpdGHIVGGLDPVGEDV---LR 439
Cdd:PRK07470 83 VWVPTNFRQTPD-EVAYLAEAS-GARAMICHAD--------FPEHAAAVRAASPDLT----HVVAIGGARAGLDYealVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 440 AHnhLGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRH----FSLTH----FFPWMSERfglDETSKFTMLS---GIaH 508
Cdd:PRK07470 149 RH--LGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHgqmaFVITNhladLMPGTTEQ---DASLVVAPLShgaGI-H 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 509 DPIQ--RDMFTPLFLGAQLHVPTAddigtpgrlaeWMAESEVTVTHL--TPAMGQLL---SAQATRQIPTLLNAFFVGDV 581
Cdd:PRK07470 223 QLCQvaRGAATVLLPSERFDPAEV-----------WALVERHRVTNLftVPTILKMLvehPAVDRYDHSSLRYVIYAGAP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 582 LTKRDCLRlqALAANVRIInmygttetqraVSYFAIPPVSQDSTFL---------ATQKDIMPAG---EGMiDVQLLvvn 649
Cdd:PRK07470 292 MYRADQKR--ALAKLGKVL-----------VQYFGLGEVTGNITVLppalhdaedGPDARIGTCGferTGM-EVQIQ--- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 650 rNDRNVPCAVGEVGEIYVRSGGLAEGYLD-QDASAEKFVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSG 728
Cdd:PRK07470 355 -DDEGRELPPGETGEICVIGPAVFAGYYNnPEANAKAFRDGWF----------------------------------RTG 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 729 DLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALegyasnvp 808
Cdd:PRK07470 400 DLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPV-------- 471
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2234869976 809 dDEDdgkglvkgmkkyrrlikDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDK 864
Cdd:PRK07470 472 -DEA-----------------ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITK 509
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
286-733 |
1.23e-11 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 69.00 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 286 ARQNPDRPCVIQslptESPDKPQGKVifSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFS 365
Cdd:cd05921 5 ARQAPDRTWLAE----REGNGGWRRV--TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 366 VVDPAYP-PSRQIIYL----GVAKPrGLIMLKGAgtisPTVREFLAQELKIKVEVPGLEVFPDGHIVGGLD-----PVGE 435
Cdd:cd05921 79 PVSPAYSlMSQDLAKLkhlfELLKP-GLVFAQDA----APFARALAAIFPLGTPLVVSRNAVAGRGAISFAelaatPPTA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 436 DVLRAHNhlgetdpnvVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSGI--AHDPIQR 513
Cdd:cd05921 154 AVDAAFA---------AVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVDWLpwNHTFGGN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 514 DMFTP-LFLGAQLHVptadDIG--TPGRLAEWMAE-SEVTVT-HLTPAMGQLLSAQATRQIPTLLNAFF--------VGD 580
Cdd:cd05921 225 HNFNLvLYNGGTLYI----DDGkpMPGGFEETLRNlREISPTvYFNVPAGWEMLVAALEKDEALRRRFFkrlklmfyAGA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 581 VLTKRDCLRLQALAAN-----VRIINMYGTTETQravsyfaipPVSQDSTFLATqkdiMPAGEGM----IDVQLlvvnrn 651
Cdd:cd05921 301 GLSQDVWDRLQALAVAtvgerIPMMAGLGATETA---------PTATFTHWPTE----RSGLIGLpapgTELKL------ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 652 drnVPCavGEVGEIYVRSGGLAEGYLDQ-DASAEKFvnnwfavnapprkdtilhPEEGFagpesrywkgirdrmYRSGDL 730
Cdd:cd05921 362 ---VPS--GGKYEVRVKGPNVTPGYWRQpELTAQAF------------------DEEGF---------------YCLGDA 403
|
...
gi 2234869976 731 GRY 733
Cdd:cd05921 404 AKL 406
|
|
| SDR_e |
cd08946 |
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ... |
1028-1294 |
1.33e-11 |
|
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 212494 [Multi-domain] Cd Length: 200 Bit Score: 65.40 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1028 VFLTGATGFLGAFVLYDLLSRTDRVkkviclvrgktveqglerlkegstdrnvwsdswvssgrlevvtgdLGLDNFglsq 1107
Cdd:cd08946 1 ILVTGGAGFIGSHLVRRLLERGHEV---------------------------------------------VVIDRL---- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1108 etwnnvaneaDVVLHNGALVH----WVFPYEkLRSPNVLGTLTAVNLAS-TGKQKvFVFVSSTSAidtehYvqlseslar 1182
Cdd:cd08946 32 ----------DVVVHLAALVGvpasWDNPDE-DFETNVVGTLNLLEAARkAGVKR-FVYASSASV-----Y--------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1183 GSTDSKGVPESDDLEGaksalKTGYGQSKWVSEKLLFEAGKR-GLRGHIVRPGYVVGDSHTAVTNT--DDFIWRLVKG-C 1258
Cdd:cd08946 86 GSPEGLPEEEETPPRP-----LSPYGVSKLAAEHLLRSYGESyGLPVVILRLANVYGPGQRPRLDGvvNDFIRRALEGkP 160
|
250 260 270
....*....|....*....|....*....|....*.
gi 2234869976 1259 VQLGLvpDINNSINMVPVDHVARITSLAAVSPLPDA 1294
Cdd:cd08946 161 LTVFG--GGNQTRDFIHVDDVVRAILHALENPLEGG 194
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
318-867 |
2.49e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 67.96 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 318 ILRASNVLAHHLimnGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSrQIIYlgvakprgliMLKGAGTI 397
Cdd:PRK06839 37 VSKVAAYLIYEL---NVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN-ELIF----------QLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 398 SPTV-REFLAQELKIK--------VEVPGLEVFPDGHIVGGLDPvgedvlrahnhlGETDPNVVlgpdsigtlSFTSGST 468
Cdd:PRK06839 103 VLFVeKTFQNMALSMQkvsyvqrvISITSLKEIEDRKIDNFVEK------------NESASFII---------CYTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 469 GIPKGVrgrhfSLTH---FFPWMSERFGLDETSK---FTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDigtPGRLAEW 542
Cdd:PRK06839 162 GKPKGA-----VLTQenmFWNALNNTFAIDLTMHdrsIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFE---PTKALSM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 543 MAESEVTVTHLTPAMGQLLSAQATRQIPTL--LNAFFVGDVLTKRDCLRlQALAANVRIINMYGTTETQRAVsyfaippv 620
Cdd:PRK06839 234 IEKHKVTVVMGVPTIHQALINCSKFETTNLqsVRWFYNGGAPCPEELMR-EFIDRGFLFGQGFGMTETSPTV-------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 621 sqdstFLATQKDIM----PAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWFAvna 695
Cdd:PRK06839 305 -----FMLSEEDARrkvgSIGKPVLFCDYELIDENKNKVE--VGEVGELLIRGPNVMKEYWNRpDATEETIQDGWLC--- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 696 pprkdtilhpeegfagpesrywkgirdrmyrSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENV 775
Cdd:PRK06839 375 -------------------------------TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVA 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 776 TLVRRDKDEEKILVSYFVPLEGSALegyasnvpddeddgkglvkgmkkyrrLIKDIREHLKQKLPKHSVPSLFVPLSKMP 855
Cdd:PRK06839 424 VVGRQHVKWGEIPIAFIVKKSSSVL--------------------------IEKDVIEHCRLFLAKYKIPKEIVFLKELP 477
|
570
....*....|..
gi 2234869976 856 LNPNGKIDKPAL 867
Cdd:PRK06839 478 KNATGKIQKAQL 489
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
6-244 |
3.57e-11 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 67.02 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 6 LERVLSRLQNLPSISLPTDYPRPTGANKlIESVHTAQLSEQTSLSLLKLAlysededheeeeedvesSHKRPSAFHLLLA 85
Cdd:cd19539 192 LDFWRRRLRGAEPTALPTDRPRPAGFPY-PGADLRFELDAELVAALRELA-----------------KRARSSLFMVLLA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 86 AFIVLLHRYTGDTDIVVGSSSASAREP------------LILRLSVDPADPYWAVVRHVQQTEKEAEA-DALPYDVITQA 152
Cdd:cd19539 254 AYCVLLRRYTGQTDIVVGTPVAGRNHPrfestvgffvnlLPLRVDVSDCATFRDLIARVRKALVDAQRhQELPFQQLVAE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 153 LNKGKEDSLDrPLFRVrFFDETDEPTNNF------------IGSTSVTSDLTVFITRPPASTRASIAprlslrvlYNSLL 220
Cdd:cd19539 334 LPVDRDAGRH-PLVQI-VFQVTNAPAGELelagglsytegsDIPDGAKFDLNLTVTEEGTGLRGSLG--------YATSL 403
|
250 260
....*....|....*....|....
gi 2234869976 221 FTSARITSFLDQLSVFLRKVAATP 244
Cdd:cd19539 404 FDEETIQGFLADYLQVLRQLLANP 427
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
313-864 |
4.02e-11 |
|
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: 67.16 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 313 FSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSrqiiylgvakprglimlk 392
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 393 gagtisptvreflAQELKIKVEvpglevfpDGHIVggldpvgedVLRAHN-HLGETDPNVVLgpdsigtlsFTSGSTGIP 471
Cdd:cd05973 63 -------------AIEHRLRTS--------GARLV---------VTDAANrHKLDSDPFVMM---------FTSGTTGLP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 472 KGVRGRHFSLTHFFPWMSERFGLDETSKFTMLSgiahDP-----IQRDMFTPLFLGaqlhVPTADDIGTPGRLAEWMAES 546
Cdd:cd05973 104 KGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAA----DPgwaygLYYAITGPLALG----HPTILLEGGFSVESTWRVIE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 547 EVTVTHLT--PAMGQLLSAQ----ATRQIPTLLNAFFVGDVLTKrDCLRLQALAANVRIINMYGTTETQRAVSYFAIP-- 618
Cdd:cd05973 176 RLGVTNLAgsPTAYRLLMAAgaevPARPKGRLRRVSSAGEPLTP-EVIRWFDAALGVPIHDHYGQTELGMVLANHHALeh 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 619 PVSQDStflatqkdimpAGEGMIDVQLLVVNRNDRNVPCAvgevgeiyvRSGGLAegyLDQDASAEKfvnnWFAvnappr 698
Cdd:cd05973 255 PVHAGS-----------AGRAMPGWRVAVLDDDGDELGPG---------EPGRLA---IDIANSPLM----WFR------ 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 699 kdtilhpeeGFAGPESrywKGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLV 778
Cdd:cd05973 302 ---------GYQLPDT---PAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIG 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 779 RRDKDEEKILVSYFVplegsalegyasnvpddeddgkgLVKGMKKYRRLIKDIREHLKQKLPKHSVPSLFVPLSKMPLNP 858
Cdd:cd05973 370 VPDPERTEVVKAFVV-----------------------LRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTP 426
|
....*.
gi 2234869976 859 NGKIDK 864
Cdd:cd05973 427 SGKIQR 432
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
887-962 |
6.49e-11 |
|
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: 59.87 E-value: 6.49e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2234869976 887 SATEIAMQKIWSTILPNAPQPIPTDESFF-DLGGHSILATRLIFEIRKVFVVNAPLGLIFEKPTIAGLVEAVDALRN 962
Cdd:COG0236 4 EELEERLAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
586-870 |
1.56e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 65.40 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 586 DCLRLQALAANvRIINMYGTTETQRAVSYFAIPPVSQDSTflatqkdimpaGEGMIDVQLLVVNRNDRNVPCAVGEVGEI 665
Cdd:PRK07787 257 VFDRLAALTGH-RPVERYGMTETLITLSTRADGERRPGWV-----------GLPLAGVETRLVDEDGGPVPHDGETVGEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 666 YVRSGGLAEGYLDQ-DASAEKFVnnwfavnapprkdtilhpEEGFagpesrywkgirdrmYRSGDLGRYLPDGTVECSGR 744
Cdd:PRK07787 325 QVRGPTLFDGYLNRpDATAAAFT------------------ADGW---------------FRTGDVAVVDPDGMHRIVGR 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 745 -ADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALEgyasnvpddeddgkglvkgmkk 823
Cdd:PRK07787 372 eSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAAD---------------------- 429
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2234869976 824 yrrlikDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALPFP 870
Cdd:PRK07787 430 ------ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
275-867 |
1.91e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 65.18 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 275 KGAITDVFSRNARQNPDRPCVIQSlptespdkPQGKViFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAV 354
Cdd:PRK12583 17 TQTIGDAFDATVARFPDREALVVR--------HQALR-YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 355 MAVLKAGATFSVVDPAYpPSRQIIY-LGVAKPRGLIMLKG---------AGTISPTVREFLAQELKI------------- 411
Cdd:PRK12583 88 FATARIGAILVNINPAY-RASELEYaLGQSGVRWVICADAfktsdyhamLQELLPGLAEGQPGALACerlpelrgvvsla 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 412 KVEVPGLEVFPDghivggLDPVGEDVLRAhnHLGETDPNvvLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSER 491
Cdd:PRK12583 167 PAPPPGFLAWHE------LQARGETVSRE--ALAERQAS--LDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAES 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 492 FGLDETSK----------FTM----LSGIAHdpiqrdmftplflGAQLHVPTadDIGTPGRLAEWMAESEVTVTHLTPAM 557
Cdd:PRK12583 237 LGLTEHDRlcvpvplyhcFGMvlanLGCMTV-------------GACLVYPN--EAFDPLATLQAVEEERCTALYGVPTM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 558 --GQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRL---QALAANVRIinMYGTTETQravsyfaipPVSqdstFLATQKD 632
Cdd:PRK12583 302 fiAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRvmdEMHMAEVQI--AYGMTETS---------PVS----LQTTAAD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 633 IMP-----AGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQDASAEKFVNnwfavnapprKDTILHpee 707
Cdd:PRK12583 367 DLErrvetVGRTQPHLEVKVVDPDGATVP--RGEIGELCTRGYSVMKGYWNNPEATAESID----------EDGWMH--- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 708 gfagpesrywkgirdrmyrSGDLGRYLPDGTVECSGRADDQVkIRGFR-IELGEIDTHLSQHPLVRE-NVTLVRRDKDEE 785
Cdd:PRK12583 432 -------------------TGDLATMDEQGYVRIVGRSKDMI-IRGGEnIYPREIEEFLFTHPAVADvQVFGVPDEKYGE 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 786 KILVsyFVPLE-GSALegyasnvpdDEDdgkglvkgmkkyrrlikDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDK 864
Cdd:PRK12583 492 EIVA--WVRLHpGHAA---------SEE-----------------ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
...
gi 2234869976 865 PAL 867
Cdd:PRK12583 544 FRM 546
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
278-863 |
2.31e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 64.91 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPDRPCVIQslptespdkpqGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAV 357
Cdd:PRK07798 5 IADLFEAVADAVPDRVALVC-----------GDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 358 LKAGATFSVVDPAYPPsRQIIYL-GVAKPRGLIMlkgagtisptVREFLAQELKIKVEVPGLEVF---PDGHIvGGLDPV 433
Cdd:PRK07798 74 FKARAVPVNVNYRYVE-DELRYLlDDSDAVALVY----------EREFAPRVAEVLPRLPKLRTLvvvEDGSG-NDLLPG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 434 GEDVLRAhnhLGETDPNVVLGPDSI--GTLSFTSGSTGIPKGVRGRHfslthffpwmserfgldetskftmlsgiahdpi 511
Cdd:PRK07798 142 AVDYEDA---LAAGSPERDFGERSPddLYLLYTGGTTGMPKGVMWRQ--------------------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 512 qRDMFTPLFLGAQLhvPTADDIGTPGRLAEWMAESEVTVT-------H---LTPAMGQLLSAQAT--------------- 566
Cdd:PRK07798 186 -EDIFRVLLGGRDF--ATGEPIEDEEELAKRAAAGPGMRRfpapplmHgagQWAAFAALFSGQTVvllpdvrfdadevwr 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 567 ---RQIPTLLnaFFVGDVLTK-----------RDCLRLQALAA------------------NVRIINMYGTTETqrAVSY 614
Cdd:PRK07798 263 tieREKVNVI--TIVGDAMARplldaleargpYDLSSLFAIASggalfspsvkeallellpNVVLTDSIGSSET--GFGG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 615 FAIPPVSQDSTFLATQKdimpagegmIDVQLLVVNRNDRNVPCAVGEVGEIyVRSGGLAEGYL-DQDASAEKFvnnwfav 693
Cdd:PRK07798 339 SGTVAKGAVHTGGPRFT---------IGPRTVVLDEDGNPVEPGSGEIGWI-ARRGHIPLGYYkDPEKTAETF------- 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 694 napprkdtilhPEegfagpesrywkgIRDRMYR-SGDLGRYLPDGTVECSGRadDQVKIR--GFRIELGEIDTHLSQHPL 770
Cdd:PRK07798 402 -----------PT-------------IDGVRYAiPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKAHPD 455
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 771 VrENVTLVRRDkDEE--KILVSYFVPLEGSAlegyasnvPDDEddgkglvkgmkkyrrlikDIREHLKQKLPKHSVPSLF 848
Cdd:PRK07798 456 V-ADALVVGVP-DERwgQEVVAVVQLREGAR--------PDLA------------------ELRAHCRSSLAGYKVPRAI 507
|
650
....*....|....*
gi 2234869976 849 VPLSKMPLNPNGKID 863
Cdd:PRK07798 508 WFVDEVQRSPAGKAD 522
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
894-951 |
2.54e-10 |
|
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: 57.57 E-value: 2.54e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2234869976 894 QKIWSTILPNAPQPIPTDESFFDLGGHSILATRLIFEIRKVFVVNAPLGLIFEKPTIA 951
Cdd:pfam00550 4 RELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
285-481 |
3.26e-10 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 64.62 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 285 NARQNPDRPCVIqslptespDKPQGKViFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATF 364
Cdd:PLN02246 32 RLSEFSDRPCLI--------DGATGRV-YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 365 SVVDPAYPPS---RQIIYLGvAKprgLIMLKGAgtISPTVREFlAQELKIKVevpgleVFPDGHIVGGLdPVGEDVLRAH 441
Cdd:PLN02246 103 TTANPFYTPAeiaKQAKASG-AK---LIITQSC--YVDKLKGL-AEDDGVTV------VTIDDPPEGCL-HFSELTQADE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2234869976 442 NHLgetdPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSL 481
Cdd:PLN02246 169 NEL----PEVEISPDDVVALPYSSGTTGLPKGVMLTHKGL 204
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
444-867 |
3.36e-10 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 64.04 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 444 LGETDPNVVL------GPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFP-WMSERFGLDETSKFTMLSGIAHDpIQRD-- 514
Cdd:cd05958 79 LDKARITVALcahaltASDDICILAFTSGTTGAPKATMHFHRDPLASADrYAVNVLRLREDDRFVGSPPLAFT-FGLGgv 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 515 MFTPLFLGAQ-LHVPTAddigTPGRLAEWMAESEVTVTHLTPAMGQLLSA---QATRQIPTLLNAFFVGDVLTKRDCLRL 590
Cdd:cd05958 158 LLFPFGVGASgVLLEEA----TPDLLLSAIARYKPTVLFTAPTAYRAMLAhpdAAGPDLSSLRKCVSAGEALPAALHRAW 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 591 QAlAANVRIINMYGTTETqravsyFAIppvsqdstFL-ATQKDIMPAGEGMI--DVQLLVVNRNDRNVPcaVGEVGEIYV 667
Cdd:cd05958 234 KE-ATGIPIIDGIGSTEM------FHI--------FIsARPGDARPGATGKPvpGYEAKVVDDEGNPVP--DGTIGRLAV 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 668 RsGGLAEGYLDQDASAEKFVNNWFAvnapprkdtilhpeegfagpesrywkgirdrmyrSGDLGRYLPDGTVECSGRADD 747
Cdd:cd05958 297 R-GPTGCRYLADKRQRTYVQGGWNI----------------------------------TGDTYSRDPDGYFRHQGRSDD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 748 QVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGsalegyasnVPDDEDdgkglvkgmkkyrrL 827
Cdd:cd05958 342 MIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPG---------VIPGPV--------------L 398
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2234869976 828 IKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05958 399 ARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
456-862 |
4.39e-10 |
|
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: 63.52 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 456 DSIGTLSFTSGSTGIPKGVR---GRHfslthffpWMS-----ERFGLDETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHV 527
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQqtfGNH--------WWSaigsaLNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 528 PTADDigtPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRlQALAANVRIINMYGTTE 607
Cdd:cd05912 149 VDKFD---AEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILLGGGPAPKPLLE-QCKEKGIPVYQSYGMTE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 608 TqravsyfaippVSQDST--FLATQKDIMPAGEGMIDVQLLVVNRNDRnvpcaVGEVGEIYVRSGGLAEGYLDQ-DASAE 684
Cdd:cd05912 225 T-----------CSQIVTlsPEDALNKIGSAGKPLFPVELKIEDDGQP-----PYEVGEILLKGPNVTKGYLNRpDATEE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 685 KFVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLGrYL-PDGTVECSGRADDQVKIRGFRIELGEIDT 763
Cdd:cd05912 289 SFENGWF----------------------------------KTGDIG-YLdEEGFLYVLDRRSDLIISGGENIYPAEIEE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 764 HLSQHPLVRENVTLVRRDKDEEKILVSYFVplegsalegyaSNVPDDEDdgkglvkgmkkyrrlikDIREHLKQKLPKHS 843
Cdd:cd05912 334 VLLSHPAIKEAGVVGIPDDKWGQVPVAFVV-----------SERPISEE-----------------ELIAYCSEKLAKYK 385
|
410
....*....|....*....
gi 2234869976 844 VPSLFVPLSKMPLNPNGKI 862
Cdd:cd05912 386 VPKKIYFVDELPRTASGKL 404
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
296-883 |
5.41e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 63.61 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 296 IQSLPTESPDK----PQGKVIfSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAY 371
Cdd:PRK06164 16 LDAHARARPDAvaliDEDRPL-SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 372 PpSRQIIY-LGVAKPRGLIMLKG------AGTISPTVREFLAQELKIKVEVPGLEVFPDGHIVGGLDPVGEDVLRAHNHL 444
Cdd:PRK06164 95 R-SHEVAHiLGRGRARWLVVWPGfkgidfAAILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 445 GETDpnvvlGPDSIGTLSFT-SGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSK------------FTMLSGIAHDpi 511
Cdd:PRK06164 174 GERA-----ADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVllaalpfcgvfgFSTLLGALAG-- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 512 qrdmftplflGAQLHVPTADDigtPGRLAEWMAESEVTVTHLT-PAMGQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRL 590
Cdd:PRK06164 247 ----------GAPLVCEPVFD---AARTARALRRHRVTHTFGNdEMLRRILDTAGERADFPSARLFGFASFAPALGELAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 591 QALAANVRIINMYGTTETQravSYFAIPPVSQDstflaTQKDIMPAG---EGMIDVQllVVNRNDRNVpCAVGEVGEIYV 667
Cdd:PRK06164 314 LARARGVPLTGLYGSSEVQ---ALVALQPATDP-----VSVRIEGGGrpaSPEARVR--ARDPQDGAL-LPDGESGEIEI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 668 RSGGLAEGYLD-QDASAEKFVnnwfavnapprkdtilhpeegfagpesrywkgiRDRMYRSGDLGRYLPDGTVECSGRAD 746
Cdd:PRK06164 383 RAPSLMRGYLDnPDATARALT---------------------------------DDGYFRTGDLGYTRGDGQFVYQTRMG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 747 DQVKIRGFRIELGEIDTHLSQHPLVReNVTLVRRDKDEEKILVSYFVPLEGSAlegyasnvPDDEddgkglvkgmkkyrr 826
Cdd:PRK06164 430 DSLRLGGFLVNPAEIEHALEALPGVA-AAQVVGATRDGKTVPVAFVIPTDGAS--------PDEA--------------- 485
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 827 likDIREHLKQKLPKHSVPSLFVPLSKMP--LNPNG-KIDKPALpfPDTAQASYAAGPSA 883
Cdd:PRK06164 486 ---GLMAACREALAGFKVPARVQVVEAFPvtESANGaKIQKHRL--REMAQARLAAERAA 540
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
313-867 |
5.43e-10 |
|
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: 63.38 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 313 FSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGAtfsVVDPAYPpsrqiiylgvakprglimlk 392
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGA---VPVPIYP-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 393 gagTISPTVREFLAQELKIKVevpglevfpdghIVGGldpvgedvlrahnhlgetdpnvvlGPDSIGTLSFTSGSTGIPK 472
Cdd:cd05907 63 ---TSSAEQIAYILNDSEAKA------------LFVE------------------------DPDDLATIIYTSGTTGRPK 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 473 GVRGRHFSLTHFFPWMSERFGLDETSKF-TMLSgIAHDPIQR-DMFTPLFLGAQLHVPTADDIGTPG------------- 537
Cdd:cd05907 104 GVMLSHRNILSNALALAERLPATEGDRHlSFLP-LAHVFERRaGLYVPLLAGARIYFASSAETLLDDlsevrptvflavp 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 538 RLAEWM--AESEVTVTHLTPAMGQLLSAQATR-------QIPTLLNAFFvgdvltkrdclrlqaLAANVRIINMYGTTET 608
Cdd:cd05907 183 RVWEKVyaAIKVKAVPGLKRKLFDLAVGGRLRfaasggaPLPAELLHFF---------------RALGIPVYEGYGLTET 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 609 QRAVSyfaippvsqdstfLATQKDIMPAGEGMidvqllVVNRNDrnvpCAVGEVGEIYVRSGGLAEGYL-DQDASAEKFV 687
Cdd:cd05907 248 SAVVT-------------LNPPGDNRIGTVGK------PLPGVE----VRIADDGEILVRGPNVMLGYYkNPEATAEALD 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 688 -NNWFAvnapprkdtilhpeegfagpesrywkgirdrmyrSGDLGRYLPDGTVECSGRADD-QVKIRGFRIELGEIDTHL 765
Cdd:cd05907 305 aDGWLH----------------------------------TGDLGEIDEDGFLHITGRKKDlIITSGGKNISPEPIENAL 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 766 SQHPLVRENVTLvrrdKDEEKILVSYFVPLEgSALEGYASNVPDDEDDGKGLVKGmKKYRRLIKDIREHLKQKLPKHSVP 845
Cdd:cd05907 351 KASPLISQAVVI----GDGRPFLVALIVPDP-EALEAWAEEHGIAYTDVAELAAN-PAVRAEIEAAVEAANARLSRYEQI 424
|
570 580
....*....|....*....|....*...
gi 2234869976 846 SLFVPLSKMP------LNPNGKIDKPAL 867
Cdd:cd05907 425 KKFLLLPEPFtiengeLTPTLKLKRPVI 452
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
278-668 |
1.29e-09 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 62.61 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPDRPCVIqslpteSPDKPQGKVIFSYGAI-----LRASNVLAHHLIMNGIQRED--VVMVYAhrSVDL 350
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVA------VPGGRGADGKLAYDELsfaelDARSDAIAHGLNAAGIGRGMraVLMVTP--SLEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 351 VVAVMAVLKAGATFSVVDPAyppsrqiiyLGV---------AKPRGLIMLKGAGTISptvREFLAQELKIKVEVPglevf 421
Cdd:PRK09274 80 FALTFALFKAGAVPVLVDPG---------MGIknlkqclaeAQPDAFIGIPKAHLAR---RLFGWGKPSVRRLVT----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 422 pdghiVGGLDPVGEDVLRAHNHLGETD--PNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFgldetsk 499
Cdd:PRK09274 143 -----VGGRLLWGGTTLATLLRDGAAApfPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDY------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 500 ftmlsGIAHDpiQRDMFT-PLF------LGAQLHVP--------TADdigtPGRLAEWMAESEVTVTHLTPA-MGQLLSA 563
Cdd:PRK09274 211 -----GIEPG--EIDLPTfPLFalfgpaLGMTSVIPdmdptrpaTVD----PAKLFAAIERYGVTNLFGSPAlLERLGRY 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 564 QATRQI--PTLLNAFFVGDVLTKRDCLRLQA-LAANVRIINMYGTTEtqravsyfAIPPVSQDS-TFLATQKDIMPAGEG 639
Cdd:PRK09274 280 GEANGIklPSLRRVISAGAPVPIAVIERFRAmLPPDAEILTPYGATE--------ALPISSIESrEILFATRAATDNGAG 351
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2234869976 640 M-----ID-VQLLVVNRNDRNVP-------CAVGEVGEIYVR 668
Cdd:PRK09274 352 IcvgrpVDgVEVRIIAISDAPIPewddalrLATGEIGEIVVA 393
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
415-889 |
1.54e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 62.49 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 415 VPGLEVFpdghIVGGlDPVGEDVLRAHNHLGETDPN---VVLGPDSIGTLSFTSGSTGIPKGVRGRHF-----SLTHFFP 486
Cdd:PRK07786 135 VPLLSTV----VVAG-GSSDDSVLGYEDLLAEAGPAhapVDIPNDSPALIMYTSGTTGRPKGAVLTHAnltgqAMTCLRT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 487 WmserfGLDETSKFTML-SGIAHDPIQRDMFTPLFLGAQ--LHVPTADDigtPGRLAEWMAESEVTVTHLTPAMGQLLSA 563
Cdd:PRK07786 210 N-----GADINSDVGFVgVPLFHIAGIGSMLPGLLLGAPtvIYPLGAFD---PGQLLDVLEAEKVTGIFLVPAQWQAVCA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 564 QATRQIPTLLNAFFVGDVLTKRDCLrLQALAA---NVRIINMYGTTEtqravsyfaIPPVsqdsTFLATQKD----IMPA 636
Cdd:PRK07786 282 EQQARPRDLALRVLSWGAAPASDTL-LRQMAAtfpEAQILAAFGQTE---------MSPV----TCMLLGEDairkLGSV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 637 GEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWFavnapprkdtilhpeegfagpesr 715
Cdd:PRK07786 348 GKVIPTVAARVVDENMNDVP--VGEVGEIVYRAPTLMSGYWNNpEATAEAFAGGWF------------------------ 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 716 ywkgirdrmyRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVsyfvpl 795
Cdd:PRK07786 402 ----------HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPV------ 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 796 egsalegyASNVPDDEDDGKGLvkgmkkyrrliKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALPFPDTAQA 875
Cdd:PRK07786 466 --------AVAAVRNDDAALTL-----------EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGACV 526
|
490
....*....|....
gi 2234869976 876 SYAAGPSAPGASAT 889
Cdd:PRK07786 527 NVERRSASAGFTER 540
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
274-870 |
1.59e-09 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 62.08 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 274 WKGAITDVFSRNARQNPDRPCVIQSLPTespdkpqgkviFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVA 353
Cdd:PRK13382 41 EGMGPTSGFAIAAQRCPDRPGLIDELGT-----------LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 354 VMAVLKAGATFSVVDPAY--PPSRQiiylgVAKPRGLIMLKGAGTISPTVREFLAqelkikvEVPG---LEVFPDGHivg 428
Cdd:PRK13382 110 LLAANRIGADILLLNTSFagPALAE-----VVTREGVDTVIYDEEFSATVDRALA-------DCPQatrIVAWTDED--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 429 glDPVGEDVLRAhNHLGETDPNvvlGPDSIGTLSFTSGSTGIPKGVR-------GRHFSLTHFFPWMSER--------FG 493
Cdd:PRK13382 175 --HDLTVEVLIA-AHAGQRPEP---TGRKGRVILLTSGTTGTPKGARrsgpggiGTLKAILDRTPWRAEEptvivapmFH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 494 LDETSKFTMLSGIAHDPIQRDMFTP---LFLGAQLH------VPTADDigtpgRLAEWMAESevtvthLTPAMGQLL--- 561
Cdd:PRK13382 249 AWGFSQLVLAASLACTIVTRRRFDPeatLDLIDRHRatglavVPVMFD-----RIMDLPAEV------RNRYSGRSLrfa 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 562 SAQATRQIPTLLNAFF--VGDVltkrdclrlqalaanvrIINMYGTTEtqraVSYFAIppvsqdstflATQKDIMP---- 635
Cdd:PRK13382 318 AASGSRMRPDVVIAFMdqFGDV-----------------IYNNYNATE----AGMIAT----------ATPADLRAapdt 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 636 AGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYldqdasaekfvnnwfavnaPPRKDtilhpeegfagpesr 715
Cdd:PRK13382 367 AGRPAEGTEIRILDQDFREVP--TGEVGTIFVRNDTQFDGY-------------------TSGST--------------- 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 716 ywKGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPL 795
Cdd:PRK13382 411 --KDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLK 488
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2234869976 796 EGSALegyasnvpddeddgkglvkgmkkyrrLIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALPFP 870
Cdd:PRK13382 489 PGASA--------------------------TPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
11-244 |
3.78e-09 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 60.51 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 11 SRLQNLPS-ISLPTDYPRPT-----GAnkliesVHTAQLSEQTSLSLLKLAlysededheeeeedvesSHKRPSAFHLLL 84
Cdd:cd19540 197 ETLAGLPEeLELPTDRPRPAvasyrGG------TVEFTIDAELHARLAALA-----------------REHGATLFMVLH 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 85 AAFIVLLHRYTGDTDIVVGSSSA----SAREPLI--------LRLSVDPADPYWAVVRHVQQTEKEAEADA-LPYDVITQ 151
Cdd:cd19540 254 AALAVLLSRLGAGDDIPIGTPVAgrgdEALDDLVgmfvntlvLRTDVSGDPTFAELLARVRETDLAAFAHQdVPFERLVE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 152 ALNkgKEDSLDR-PLFRVRF-FDETDEPTNNF---------IGSTSVTSDLTVFITRPPASTRAsiAPRLSLRVLYNSLL 220
Cdd:cd19540 334 ALN--PPRSTARhPLFQVMLaFQNTAAATLELpgltvepvpVDTGVAKFDLSFTLTERRDADGA--PAGLTGELEYATDL 409
|
250 260
....*....|....*....|....
gi 2234869976 221 FTSARITSFLDQLSVFLRKVAATP 244
Cdd:cd19540 410 FDRSTAERLADRFVRVLEAVVADP 433
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
655-959 |
4.83e-09 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 59.38 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 655 VPCAVGEVGEIYVRSGGLAEGYLDQDASAEKFVNNWFAVNAPPRKDTILHPEEGFAGPESRYWKGIRDRMYRSGDLGRYL 734
Cdd:COG3433 9 APPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 735 PDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVsyfvplegsaLEGYASNVPDDEDDg 814
Cdd:COG3433 89 LRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGL----------LLIVGAVAALDGLA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 815 kglvkgmkkyrrlIKDIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALPFPDTA-QASYAAGPSAPGASATEIAM 893
Cdd:COG3433 158 -------------AAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEaLLAAASPAPALETALTEEEL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2234869976 894 QKIWSTILPNAPQPIPTDESFFDLGGHSILATRLIFEIRKVFvVNAPLGLIFEKPTIAGLVEAVDA 959
Cdd:COG3433 225 RADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAG-LDVSFADLAEHPTLAAWWALLAA 289
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
280-890 |
4.88e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 60.74 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 280 DVFSRNARQNPDRPcVIQSLPTESPDKPQGKVIFS--YGAILRASNVLaHHLimnGIQREDVVMVYAHRSVDLVVAvmav 357
Cdd:PRK07529 29 ELLSRAAARHPDAP-ALSFLLDADPLDRPETWTYAelLADVTRTANLL-HSL---GVGPGDVVAFLLPNLPETHFA---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 358 LKAGATFSVVDPAYP--PSRQII-YLGVAKPRGLIMLKG-AGT-ISPTVREFLAQ--ELKIKVEVPGLEVF--PDGHIVG 428
Cdd:PRK07529 100 LWGGEAAGIANPINPllEPEQIAeLLRAAGAKVLVTLGPfPGTdIWQKVAEVLAAlpELRTVVEVDLARYLpgPKRLAVP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 429 GLDPVGEDVLRAHNHLGETDPNVVL------GPDSIGTLSFTSGSTGIPKGVRGRHFSLThFFPWMSERFgLDETSKFTM 502
Cdd:PRK07529 180 LIRRKAHARILDFDAELARQPGDRLfsgrpiGPDDVAAYFHTGGTTGMPKLAQHTHGNEV-ANAWLGALL-LGLGPGDTV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 503 LSGIahdPiqrdMF----------TPLFLGAQLHVPT---ADDIGTPGRLAEWMAESEVTVTHLTP-AMGQLLsaqatrQ 568
Cdd:PRK07529 258 FCGL---P----LFhvnallvtglAPLARGAHVVLATpqgYRGPGVIANFWKIVERYRINFLSGVPtVYAALL------Q 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 569 IP------TLLNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAVSyfaIPPVSQdstflatqkdimPAGEGMI- 641
Cdd:PRK07529 325 VPvdghdiSSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSS---VNPPDG------------ERRIGSVg 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 642 ------DVQLLVVNRNDRNV-PCAVGEVGEIYVRSGGLAEGYLDqdasaekfvnnwfavnapPRKDTILHPEEGFagpes 714
Cdd:PRK07529 390 lrlpyqRVRVVILDDAGRYLrDCAVDEVGVLCIAGPNVFSGYLE------------------AAHNKGLWLEDGW----- 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 715 rywkgirdrmYRSGDLGRYLPDGTVECSGRADDQVkIR-GFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFV 793
Cdd:PRK07529 447 ----------LNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 794 PLEGSAlegyasnVPDDEddgkglvkgmkkyrrLIKDIREHLKQK--LPKHsvpslFVPLSKMPLNPNGKIDKPALPFPD 871
Cdd:PRK07529 516 LKPGAS-------ATEAE---------------LLAFARDHIAERaaVPKH-----VRILDALPKTAVGKIFKPALRRDA 568
|
650 660
....*....|....*....|...
gi 2234869976 872 TA----QASYAAGPSAPGASATE 890
Cdd:PRK07529 569 IRrvlrAALRDAGVEAEVVDVVE 591
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
463-864 |
4.88e-09 |
|
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: 59.97 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 463 FTSGSTGIPKGVRGRHFSL-THFFPWMSErfGLDETSKFT--MLSGIAHDPIQRDMFTPLFLGAqLHVPTADDIgTPGRL 539
Cdd:cd17635 8 FTSGTTGEPKAVLLANKTFfAVPDILQKE--GLNWVVGDVtyLPLPATHIGGLWWILTCLIHGG-LCVTGGENT-TYKSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 540 AEWMAESEVTVTHLTPAMGQLLSAQATRQIPTL--LNAFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAVSYfai 617
Cdd:cd17635 84 FKILTTNAVTTTCLVPTLLSKLVSELKSANATVpsLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCL--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 618 pPVSQDStflatqKDIMPAGEGMIDVQLLVVNRNDRNVPCavGEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWFavnap 696
Cdd:cd17635 161 -PTDDDS------IEINAVGRPYPGVDVYLAATDGIAGPS--ASFGTIWIKSPANMLGYWNNpERTAEVLIDGWV----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 697 prkdtilhpeegfagpesrywkgirdrmyRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVREnvT 776
Cdd:cd17635 227 -----------------------------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQE--C 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 777 LVRRDKDEEkilvsyfvplegsalegYASNVpddeddGKGLVKGMKKYRRLIKDIREHLKQKLPKHSVPSLFVPLSKMPL 856
Cdd:cd17635 276 ACYEISDEE-----------------FGELV------GLAVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPR 332
|
....*...
gi 2234869976 857 NPNGKIDK 864
Cdd:cd17635 333 TQSGKVKR 340
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
12-244 |
6.09e-09 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 59.97 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 12 RLQNLPS-ISLPTDYPRPTGANKLIESVH---TAQLSEQtslsLLKLAlysededheeeeedvesSHKRPSAFHLLLAAF 87
Cdd:cd19538 198 QLAGLPDeIELPTDYPRPAESSYEGGTLTfeiDSELHQQ----LLQLA-----------------KDNNVTLFMVLQAGF 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 88 IVLLHRYTGDTDIVVGSSSA----SAREPLI------LRLSVDPA-DP-YWAVVRHVQQTEKEA-EADALPYDVITQALN 154
Cdd:cd19538 257 AALLTRLGAGTDIPIGSPVAgrndDSLEDLVgffvntLVLRTDTSgNPsFRELLERVKETNLEAyEHQDIPFERLVEALN 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 155 kgKEDSLDR-PLFRVRF-FDETDEPTNNFIGSTS------VTS---DLTV-FITRPPASTRASIAPRLSlrvlYNSLLFT 222
Cdd:cd19538 337 --PTRSRSRhPLFQIMLaLQNTPQPSLDLPGLEAklelrtVGSakfDLTFeLREQYNDGTPNGIEGFIE----YRTDLFD 410
|
250 260
....*....|....*....|..
gi 2234869976 223 SARITSFLDQLSVFLRKVAATP 244
Cdd:cd19538 411 HETIEALAQRYLLLLESAVENP 432
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
335-966 |
9.05e-09 |
|
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: 60.10 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 335 QREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPRGLIMLKGAGTISPTVREFLAQELKIKVE 414
Cdd:COG3319 23 AAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALALALAAAAAALLLAALAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 415 VPGLEVFPDGHIVGGLDPVGEDVLRAHNHLGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGL 494
Cdd:COG3319 103 LLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVLVLAALLALLLAALLAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 495 DETSKFTMLSGIAHDPIQRDMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLN 574
Cdd:COG3319 183 ALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAALLLLLALALLLLLALL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 575 AFFVGDVLTKRDCLRLQALAANVRIINMYGTTETQRAVSYFAIPPVSQDstflatqkDIMPAGEGMIDVQLLVVNRNDRN 654
Cdd:COG3319 263 LLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGV--------AGALGPIGGGPGLLVLLVLLVLL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 655 VPCAVGEVGEIYVRSGGLAEGYLDQDAsaekfvnnwfavnapprkdtilHPEEGFAGPESRYwkGIRDRMYRSGDLGRYL 734
Cdd:COG3319 335 LPLLLGVGGGGGGGGGGGGAGGLAGRG----------------------LRAAAALRDPAGA--GARGRLRRGGDRGRRL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 735 PDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALEGYAsnvpddeddg 814
Cdd:COG3319 391 GGGLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALL---------- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 815 kglvkgmkkyrrlikdiREHLKQKLPKHSVPSLFVPLSKMPLNPNGKIDKPALPFPDTAqasyAAGPSAPGASATEIAMQ 894
Cdd:COG3319 461 -----------------LLLLLLLLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAA----AAAAAPAPAAALELALA 519
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2234869976 895 KIWSTILpnAPQPIPTDESFFDLGGHSILATRLIFEIRKVFVVNAPLGLIFEKPTIAGLVEAVDALRNADLG 966
Cdd:COG3319 520 LLLLLLL--GLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAAL 589
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
78-237 |
1.14e-08 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 59.20 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 78 SAFHLLLAAFIVLLHRYTGDTDIVV----GSSSASAREPLI--------LRLSVDPADPYWAVVRHVQQTEKEA-EADAL 144
Cdd:cd20483 248 TPFMFLLAAFRAFLYRYTEDEDLTIgmvdGDRPHPDFDDLVgffvnmlpIRCRMDCDMSFDDLLESTKTTCLEAyEHSAV 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 145 PYDVITQALNKGKEDSlDRPLFRVRF----------FDETDEPTNNFIGSTSVT-SDLTVFITRPPASTrasiaprLSLR 213
Cdd:cd20483 328 PFDYIVDALDVPRSTS-HFPIGQIAVnyqvhgkfpeYDTGDFKFTDYDHYDIPTaCDIALEAEEDPDGG-------LDLR 399
|
170 180
....*....|....*....|....
gi 2234869976 214 VLYNSLLFTSARITSFLDQLSVFL 237
Cdd:cd20483 400 LEFSTTLYDSADMERFLDNFVTFL 423
|
|
| AR_SDR_e |
cd05227 |
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ... |
1027-1290 |
1.22e-08 |
|
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187538 [Multi-domain] Cd Length: 301 Bit Score: 58.05 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1027 TVFLTGATGFLGAFVLYDLLSRTDRVKKViclVRGKTVEQGL-ERLKEGStdrnvwsdswvSSGRLEVVTGDLGLDNfgl 1105
Cdd:cd05227 1 LVLVTGATGFIASHIVEQLLKAGYKVRGT---VRSLSKSAKLkALLKAAG-----------YNDRLEFVIVDDLTAP--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1106 sqETWNNVANEADVVLHNGALVHWVFP--YEKLRSPNVLGTLTAVNLAS-TGKQKVFVFVSSTSAIDTEHYvqlseslar 1182
Cdd:cd05227 64 --NAWDEALKGVDYVIHVASPFPFTGPdaEDDVIDPAVEGTLNVLEAAKaAGSVKRVVLTSSVAAVGDPTA--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1183 gSTDSKGVPESD--DLEGAKSALKTGYGQSKWVSEKL---LFEAGKRGLRGHIVRPGYVVGDS--HTAVTNTDDFIWRLV 1255
Cdd:cd05227 133 -EDPGKVFTEEDwnDLTISKSNGLDAYIASKTLAEKAaweFVKENKPKFELITINPGYVLGPSllADELNSSNELINKLL 211
|
250 260 270
....*....|....*....|....*....|....*
gi 2234869976 1256 KGCVqLGLVPDINNsiNMVPVDHVARITSLAAVSP 1290
Cdd:cd05227 212 DGKL-PAIPPNLPF--GYVDVRDVADAHVRALESP 243
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
15-244 |
1.66e-08 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 58.48 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 15 NLPSISLPTDYPRPTgANKLIESVHTAQLSEQTSLSLLKLAlysededheeeeedvESSHKRPSAFhlLLAAFIVLLHRY 94
Cdd:cd20484 198 TLPILELPADRPRSS-APSFEGQTYTRRLPSELSNQIKSFA---------------RSQSINLSTV--FLGIFKLLLHRY 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 95 TGDTDIVVGSSSASAREP------------LILRLSVDPADPYWAVVRHVQQTekeaEADAL-----PYDVITQALNKgK 157
Cdd:cd20484 260 TGQEDIIVGMPTMGRPEErfdsligyfinmLPIRSRILGEETFSDFIRKLQLT----VLDGLdhaayPFPAMVRDLNI-P 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 158 EDSLDRPLFRVRFFDEtdeptnNFIGSTSVTSDLTVFITRPPASTRASI---------------APRLSLRVLYNSLLFT 222
Cdd:cd20484 335 RSQANSPVFQVAFFYQ------NFLQSTSLQQFLAEYQDVLSIEFVEGIhqegeyelvlevyeqEDRFTLNIKYNPDLFD 408
|
250 260
....*....|....*....|..
gi 2234869976 223 SARITSFLDQLSVFLRKVAATP 244
Cdd:cd20484 409 ASTIERMMEHYVKLAEELIANP 430
|
|
| 3b-HSD_HSDB1_like_SDR_e |
cd09811 |
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ... |
1030-1254 |
2.00e-08 |
|
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187671 [Multi-domain] Cd Length: 354 Bit Score: 57.90 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1030 LTGATGFLGAFVLYDLLSRTDRVKKVICLvrGKTVEQGLERLKEGSTDRNvwsdswvssgRLEVVTGDLgldnfgLSQET 1109
Cdd:cd09811 4 VTGGGGFLGQHIIRLLLERKEELKEIRVL--DKAFGPELIEHFEKSQGKT----------YVTDIEGDI------KDLSF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1110 WNNVANEADVVLHNGALVHWVFP--YEKLRSPNVLGTLTAVNLASTGKQKVFVFVSSTSAIDTEHYvqlSESLARGSTDs 1187
Cdd:cd09811 66 LFRACQGVSVVIHTAAIVDVFGPpnYEELEEVNVNGTQAVLEACVQNNVKRLVYTSSIEVAGPNFK---GRPIFNGVED- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2234869976 1188 kgvpesddlEGAKSALKTGYGQSKWVSEKLLFEAGKRGLRGHIV------RPGYVVGDSHTAVTNTDDFIWRL 1254
Cdd:cd09811 142 ---------TPYEDTSTPPYASSKLLAENIVLNANGAPLKQGGYlvtcalRPMYIYGEGSHFLTEIFDFLLTN 205
|
|
| PLN02503 |
PLN02503 |
fatty acyl-CoA reductase 2 |
1029-1289 |
2.41e-08 |
|
fatty acyl-CoA reductase 2
Pssm-ID: 215279 [Multi-domain] Cd Length: 605 Bit Score: 58.72 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1029 FLTGATGFLgAFVLYDLLSRTD-RVKKVICLVRGKTVEQGLERLKEGSTDRNVWS----------DSWVSSgRLEVVTGD 1097
Cdd:PLN02503 123 LITGATGFL-AKVLIEKILRTNpDVGKIYLLIKAKDKEAAIERLKNEVIDAELFKclqethgksyQSFMLS-KLVPVVGN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1098 LGLDNFGLSQETWNNVANEADVVLHNGALVHWVFPYEKLRSPNVLGTLTAVNLASTGKQ-KVFVFVSST----------- 1165
Cdd:PLN02503 201 VCESNLGLEPDLADEIAKEVDVIINSAANTTFDERYDVAIDINTRGPCHLMSFAKKCKKlKLFLQVSTAyvngqrqgrim 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1166 ------------------------SAIDTEHYVQLSESLARGSTDSKGVPESDDLEGAKSALKTGYgQSKWVSEKLLFEA 1221
Cdd:PLN02503 281 ekpfrmgdciarelgisnslphnrPALDIEAEIKLALDSKRHGFQSNSFAQKMKDLGLERAKLYGW-QDTYVFTKAMGEM 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1222 GKRGLRGHIvrPGYVVGDSHTAVTNTDDFI-WR----------LVKGCVQL-GLVPDINNSINMVPVDHVARITsLAAVS 1289
Cdd:PLN02503 360 VINSMRGDI--PVVIIRPSVIESTWKDPFPgWMegnrmmdpivLYYGKGQLtGFLADPNGVLDVVPADMVVNAT-LAAMA 436
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
454-831 |
5.09e-08 |
|
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: 57.37 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 454 GPDSIGTLSFTSGSTGIPKGVRGRHFSLTH-------FFP-------------WMS-ERfgLDETSKFT-----MLSGIA 507
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHANLLHqirslsdIVPpqpgdrflsilpiWHSyER--SAEYFIFAcgcsqAYTSIR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 508 H--DPIQRdmFTPLFLGAqlhVPtaddigtpgRLAEWMAESEVTVTHLTPAMGQ-----LLSAQATRQ-------IPTLL 573
Cdd:cd17640 164 TlkDDLKR--VKPHYIVS---VP---------RLWESLYSGIQKQVSKSSPIKQflflfFLSGGIFKFgisgggaLPPHV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 574 NAFFVgdvltkrdclrlqalAANVRIINMYGTTETQRAVSYFAIPPVSQDStflatqkdimpAGEGMIDVQLLVVNRNDr 653
Cdd:cd17640 230 DTFFE---------------AIGIEVLNGYGLTETSPVVSARRLKCNVRGS-----------VGRPLPGTEIKIVDPEG- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 654 NVPCAVGEVGEIYVRSGGLAEGYLDQDASAEKFVNnwfavnapprkdtilhpEEGFagpesrywkgirdrmYRSGDLGRY 733
Cdd:cd17640 283 NVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLD-----------------SDGW---------------FNTGDLGWL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 734 LPDGTVECSGRADDQVKIR-GFRIELGEIDTHLSQHPLVrENVTLVRRDkdeEKILVSYFVP----LEGsALEGYASNVP 808
Cdd:cd17640 331 TCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFI-EQIMVVGQD---QKRLGALIVPnfeeLEK-WAKESGVKLA 405
|
410 420
....*....|....*....|...
gi 2234869976 809 DDEDDGKGLVKGMKKYRRLIKDI 831
Cdd:cd17640 406 NDRSQLLASKKVLKLYKNEIKDE 428
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
278-478 |
8.24e-08 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 56.81 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPDRPCVIQslptespdkpQGKVIfSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAV 357
Cdd:PRK08279 39 LGDVFEEAAARHPDRPALLF----------EDQSI-SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 358 LKAGAT-----FSVVDPAYPPSrqiiyLGVAKPRGLIMlkGAGTISP--TVREFLAQELKIKVEVPGLEVFPDGHivggl 430
Cdd:PRK08279 108 AKLGAVvallnTQQRGAVLAHS-----LNLVDAKHLIV--GEELVEAfeEARADLARPPRLWVAGGDTLDDPEGY----- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2234869976 431 dpvgEDVLRAHNHLGETDPNV---VLGPDSIgTLSFTSGSTGIPKGVRGRH 478
Cdd:PRK08279 176 ----EDLAAAAAGAPTTNPASrsgVTAKDTA-FYIYTSGTTGLPKAAVMSH 221
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
278-478 |
1.12e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 56.43 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPDRPCViqslpTESPDKPQGKVIfSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAV 357
Cdd:PRK08180 41 LTDRLVHWAQEAPDRVFL-----AERGADGGWRRL-TYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 358 LKAGATFSVVDPAY-----PPSRQIIYLGVAKPrGLIMlkgAGTISPTVREFLAqelkikVEVPGLEVF-----PDGHIV 427
Cdd:PRK08180 115 MYAGVPYAPVSPAYslvsqDFGKLRHVLELLTP-GLVF---ADDGAAFARALAA------VVPADVEVVavrgaVPGRAA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2234869976 428 GGLD-----PVGEDVLRAHNhlgetdpnvVLGPDSIGTLSFTSGSTGIPKGVRGRH 478
Cdd:PRK08180 185 TPFAallatPPTAAVDAAHA---------AVGPDTIAKFLFTSGSTGLPKAVINTH 231
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
598-867 |
1.42e-07 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 56.01 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 598 RIINMYGTTETQRAVSYFA-------IPPVSQDStfLATQKDIMPAGEGMIDVqllVVNRNDRNVPCAVGEVGEIYVRSG 670
Cdd:PLN02479 336 RVTHTYGLSETYGPSTVCAwkpewdsLPPEEQAR--LNARQGVRYIGLEGLDV---VDTKTMKPVPADGKTMGEIVMRGN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 671 GLAEGYL-DQDASAEKFVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLGRYLPDGTVECSGRADDQV 749
Cdd:PLN02479 411 MVMKGYLkNPKANEEAFANGWF----------------------------------HSGDLGVKHPDGYIEIKDRSKDII 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 750 KIRGFRIELGEIDTHLSQHPLVREnVTLVRRDKDEEKILVSYFVPLEGSAlegyasnvpDDEDDgkglvkgmkkyRRLIK 829
Cdd:PLN02479 457 ISGGENISSLEVENVVYTHPAVLE-ASVVARPDERWGESPCAFVTLKPGV---------DKSDE-----------AALAE 515
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2234869976 830 DIREHLKQKLPKHSVPS--LFVPLskmPLNPNGKIDKPAL 867
Cdd:PLN02479 516 DIMKFCRERLPAYWVPKsvVFGPL---PKTATGKIQKHVL 552
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
456-862 |
1.88e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 55.35 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 456 DSIGTLSFTSGSTGIPKGVRGRHFSltHFFPWMSERFGLDETSKFTML--------SGIAHdpiqrdMFTPLFLGAQLHV 527
Cdd:PRK03640 141 DEVATIMYTSGTTGKPKGVIQTYGN--HWWSAVGSALNLGLTEDDCWLaavpifhiSGLSI------LMRSVIYGMRVVL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 528 PTADDigtPGRLAEWMAESEVTVTHLTPAM-GQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRlQALAANVRIINMYGTT 606
Cdd:PRK03640 213 VEKFD---AEKINKLLQTGGVTIISVVSTMlQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLE-QCKEKGIPVYQSYGMT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 607 ETqrAVSYFAIPPvsQDStflatQKDIMPAGEGMIDVQLLVVnrnDRNVPCAVGEVGEIYVRSGGLAEGYLDQ-DASAEK 685
Cdd:PRK03640 289 ET--ASQIVTLSP--EDA-----LTKLGSAGKPLFPCELKIE---KDGVVVPPFEEGEIVVKGPNVTKGYLNReDATRET 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 686 FVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLGrYL-PDGTVECSGRADDQVKIRGFRIELGEIDTH 764
Cdd:PRK03640 357 FQDGWF----------------------------------KTGDIG-YLdEEGFLYVLDRRSDLIISGGENIYPAEIEEV 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 765 LSQHPLVRENVTLVRRDKDEEKILVSYFVplegsalegyaSNVPDDEDdgkglvkgmkkyrrlikDIREHLKQKLPKHSV 844
Cdd:PRK03640 402 LLSHPGVAEAGVVGVPDDKWGQVPVAFVV-----------KSGEVTEE-----------------ELRHFCEEKLAKYKV 453
|
410
....*....|....*...
gi 2234869976 845 PSLFVPLSKMPLNPNGKI 862
Cdd:PRK03640 454 PKRFYFVEELPRNASGKL 471
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
325-864 |
2.04e-07 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 55.58 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 325 LAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGAtfsVVDP-----AYPPSRQIIYLgvAKPrglIMLKGAGTISp 399
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGG---IVAPlnyrwSFEEAKSAMLL--VRP---VMLVTDETCS- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 400 tvreFLAQELKIKvEVP--GLEVFPDGH----IVGGLDPVGEDVLRAHNhLGETDPNVVLGPDSIGTLSFTSGSTGIPKG 473
Cdd:PLN02860 116 ----SWYEELQND-RLPslMWQVFLESPsssvFIFLNSFLTTEMLKQRA-LGTTELDYAWAPDDAVLICFTSGTTGRPKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 474 VRGRHFSLT-------------------HFFPwMSERFGLdeTSKFTML-SGIAHdpiqrdMFTPLFlgaqlHVPTADDI 533
Cdd:PLN02860 190 VTISHSALIvqslakiaivgygeddvylHTAP-LCHIGGL--SSALAMLmVGACH------VLLPKF-----DAKAALQA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 534 gtpgrlaewMAESEVTVTHLTPA-MGQLLSA-------QATRQIPTLLNAffvGDVLTKRDCLRLQALAANVRIINMYGT 605
Cdd:PLN02860 256 ---------IKQHNVTSMITVPAmMADLISLtrksmtwKVFPSVRKILNG---GGSLSSRLLPDAKKLFPNAKLFSAYGM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 606 TETQRAVSYFAIPPVSQDSTFLATQKDIMPAGEGMIDVQLLVVNRNDRNVPCAVG-----EVGEIYVRSGGLAEGYLDQD 680
Cdd:PLN02860 324 TEACSSLTFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIGldessRVGRILTRGPHVMLGYWGQN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 681 -ASAEKFVNN-WFavnapprkDTilhpeegfagpesrywkgirdrmyrsGDLGRYLPDGTVECSGRADDQVKIRGFRIEL 758
Cdd:PLN02860 404 sETASVLSNDgWL--------DT--------------------------GDIGWIDKAGNLWLIGRSNDRIKTGGENVYP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 759 GEIDTHLSQHPLVRENVTLVRRDKDEEKILVSyFVPLEgsalEGYASNVPDDEDDGKGLVKGMkkyrrliKDIREHL-KQ 837
Cdd:PLN02860 450 EEVEAVLSQHPGVASVVVVGVPDSRLTEMVVA-CVRLR----DGWIWSDNEKENAKKNLTLSS-------ETLRHHCrEK 517
|
570 580
....*....|....*....|....*...
gi 2234869976 838 KLPKHSVPSLFVPLSK-MPLNPNGKIDK 864
Cdd:PLN02860 518 NLSRFKIPKLFVQWRKpFPLTTTGKIRR 545
|
|
| UDP_G4E_4_SDR_e |
cd05232 |
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ... |
1027-1238 |
2.06e-07 |
|
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187543 [Multi-domain] Cd Length: 303 Bit Score: 54.28 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1027 TVFLTGATGFLGAFVLYDLLSRTDrvkKVICLVRGKTVEQGLERLKEGstDRNVWSDSWVSSgrlevvtgdlgldnfgls 1106
Cdd:cd05232 1 KVLVTGANGFIGRALVDKLLSRGE---EVRIAVRNAENAEPSVVLAEL--PDIDSFTDLFLG------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1107 qetwnnvaneADVVLHNGALVH-----WVFPYEKLRSPNVLGTLtavNLASTGKQ---KVFVFVSSTSAI--DTEHYvQL 1176
Cdd:cd05232 58 ----------VDAVVHLAARVHvmndqGADPLSDYRKVNTELTR---RLARAAARqgvKRFVFLSSVKVNgeGTVGA-PF 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2234869976 1177 SEslargstDSKGVPESDdlegaksalktgYGQSKWVSEKLLFEAGKR-GLRGHIVRPGYVVG 1238
Cdd:cd05232 124 DE-------TDPPAPQDA------------YGRSKLEAERALLELGASdGMEVVILRPPMVYG 167
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
233-777 |
2.68e-07 |
|
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: 55.19 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 233 LSVFLRKVAATPLSPVGSVPLLTPSQKAVLPNPTGDLNwcgwKGAITDVFSRNARQNPDRPCVIQSLPTeSPDKP----- 307
Cdd:cd05968 9 LEAFLERSAEDNAWFWGEFVKDVGIEWYEPPYQTLDLS----GGKPWAAWFVGGRMNIVEQLLDKWLAD-TRTRPalrwe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 308 --QGKV-IFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAK 384
Cdd:cd05968 84 geDGTSrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 385 PRGLIMLKGAG------TISPTVREFLAQELKI-KVEVPGLEVFPDGHIVGGLDPVGEDVLRAHNHLGETDPnvvlgpDS 457
Cdd:cd05968 164 AKALITADGFTrrgrevNLKEEADKACAQCPTVeKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGAERTES------ED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 458 IGTLSFTSGSTGIPKGVRGRH--FSLTHFFPwMSERFGLDETSKFTMLS--GIAHDPIQrdMFTPLFLGAQLHV-PTADD 532
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVHagFPLKAAQD-MYFQFDLKPGDLLTWFTdlGWMMGPWL--IFGGLILGATMVLyDGAPD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 533 IGTPGRLAEWMAESEvtVTHLTpamgqlLSaqatrqiPTLLNAF--FVGDVLTKRDCLRLQALAA--------------- 595
Cdd:cd05968 315 HPKADRLWRMVEDHE--ITHLG------LS-------PTLIRALkpRGDAPVNAHDLSSLRVLGStgepwnpepwnwlfe 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 596 -----NVRIINMYGTTETQRAV--SYF--AIPPVSQDSTFLATQKDIMpagegmidvqllvvnrNDRNVPcAVGEVGEIY 666
Cdd:cd05968 380 tvgkgRNPIINYSGGTEISGGIlgNVLikPIKPSSFNGPVPGMKADVL----------------DESGKP-ARPEVGELV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 667 VRSG--GLAEGYLDQDasaEKFVNNwfavnapprkdtilhpeegfagpesrYWKGIrDRMYRSGDLGRYLPDGTVECSGR 744
Cdd:cd05968 443 LLAPwpGMTRGFWRDE---DRYLET--------------------------YWSRF-DNVWVHGDFAYYDEEGYFYILGR 492
|
570 580 590
....*....|....*....|....*....|...
gi 2234869976 745 ADDQVKIRGFRIELGEIDTHLSQHPLVRENVTL 777
Cdd:cd05968 493 SDDTINVAGKRVGPAEIESVLNAHPAVLESAAI 525
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
647-862 |
2.83e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 55.01 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 647 VVNRNDRNVPCAVGEVGEIYVRSGGLAEGYLDQ-DASAEKFVNNWFavnapprkdtilhpeegfagpesrywkgirdrmy 725
Cdd:PRK05605 402 IVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRpEETAKSFLDGWF---------------------------------- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 726 RSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVREN--VTLVRRDKDEEkiLVSYFVPLEGSALegy 803
Cdd:PRK05605 448 RTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAavVGLPREDGSEE--VVAAVVLEPGAAL--- 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2234869976 804 asnvpdDEDDgkglvkgmkkyrrlikdIREHLKQKLPKHSVPSLFVPLSKMPLNPNGKI 862
Cdd:PRK05605 523 ------DPEG-----------------LRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
278-680 |
3.68e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 54.62 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 278 ITDVFSRNARQNPdrpcviQSLPTESPDKPqgkVIFSYGAI----LRASNVLAHHlimnGIQREDVVMVYAHRSVDLVVA 353
Cdd:PRK07768 4 FTEKMYANARTSP------RGMVTGEPDAP---VRHTWGEVheraRRIAGGLAAA----GVGPGDAVAVLAGAPVEIAPT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 354 VMAVLKAGATfsvvdpayppsrqiiylgvakprgLIMLKgagtiSPTVREFLAQELKIKVEVPGLeVFPDGHIVGglDPV 433
Cdd:PRK07768 71 AQGLWMRGAS------------------------LTMLH-----QPTPRTDLAVWAEDTLRVIGM-IGAKAVVVG--EPF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 434 GE--DVLRAH-------NHLGETDP--NVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGLDETSKfTM 502
Cdd:PRK07768 119 LAaaPVLEEKgirvltvADLLAADPidPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETD-VM 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 503 LSGIahdPIQRDM------FTPLFLGAQL-HVPTADDIGTPGRLAEWMAESEVTVThLTPA-----MGQLLSAQATRQ-- 568
Cdd:PRK07768 198 VSWL---PLFHDMgmvgflTVPMYFGAELvKVTPMDFLRDPLLWAELISKYRGTMT-AAPNfayalLARRLRRQAKPGaf 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 569 -IPTL---LNAFFVGDVLTKRDCLR------LQALAanvrIINMYGTTETQRAVSyfaIPPVSQ-------DSTFLATQK 631
Cdd:PRK07768 274 dLSSLrfaLNGAEPIDPADVEDLLDagarfgLRPEA----ILPAYGMAEATLAVS---FSPCGAglvvdevDADLLAALR 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 632 DIMPAGEG-----------MIDVQLLVVNRNDRNVPCAvgEVGEIYVRSGGLAEGYLDQD 680
Cdd:PRK07768 347 RAVPATKGntrrlatlgppLPGLEVRVVDEDGQVLPPR--GVGVIELRGESVTPGYLTMD 404
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
454-778 |
4.20e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 54.44 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 454 GPDSIGTLSFTSGSTGIPKGVRGRHFSLT-------HFFP------WMS-----ERFGLDETSKFTMLSGI----AHDPI 511
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLanqraclKFFSpkeddvMMSflppfHAYGFNSCTLFPLLSGVpvvfAYNPL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 512 QrdmftplflgaqlhvptaddigtPGRLAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLNAFFV---GDVLtkRDCL 588
Cdd:PRK06334 261 Y-----------------------PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVvigGDAF--KDSL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 589 RLQALA--ANVRIINMYGTTETQravsyfaipPVSQDSTFLATQKDI---MPAgEGMidvQLLVVNRnDRNVPCAVGEVG 663
Cdd:PRK06334 316 YQEALKtfPHIQLRQGYGTTECS---------PVITINTVNSPKHEScvgMPI-RGM---DVLIVSE-ETKVPVSSGETG 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 664 EIYVRSGGLAEGYLDQDasaekfvnnwfavnapprkdtilhPEEGFAGPESRYWkgirdrmYRSGDLGRYLPDGTVECSG 743
Cdd:PRK06334 382 LVLTRGTSLFSGYLGED------------------------FGQGFVELGGETW-------YVTGDLGYVDRHGELFLKG 430
|
330 340 350
....*....|....*....|....*....|....*...
gi 2234869976 744 RADDQVKIRGFRIELGEIDTHLSQH---PLVRENVTLV 778
Cdd:PRK06334 431 RLSRFVKIGAEMVSLEALESILMEGfgqNAADHAGPLV 468
|
|
| 3b-HSD-like_SDR_e |
cd05241 |
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ... |
1027-1297 |
9.79e-07 |
|
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187552 [Multi-domain] Cd Length: 331 Bit Score: 52.43 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1027 TVFLTGATGFLGAfvlydLLSRTdrvkkviclvrgkTVEQGLERLKegSTDRNVWSDSWVSSGR--LEVVTGDLGLDNFG 1104
Cdd:cd05241 1 SVLVTGGSGFFGE-----RLVKQ-------------LLERGGTYVR--SFDIAPPGEALSAWQHpnIEFLKGDITDRNDV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1105 LSQETwnnvanEADVVLHNGALVHWVFPYEKLRSPNVLGTLTAVNL-ASTGKQKvFVFVSSTSaidtehyVQLSESLARG 1183
Cdd:cd05241 61 EQALS------GADCVFHTAAIVPLAGPRDLYWEVNVGGTQNVLDAcQRCGVQK-FVYTSSSS-------VIFGGQNIHN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1184 STDSKGVPESDdlegaksalKTGYGQSKWVSEKLLFEA-GKRGLRGHIVRPGYVVGdshtavtNTDDFIWRLVKGCVQLG 1262
Cdd:cd05241 127 GDETLPYPPLD---------SDMYAETKAIAEIIVLEAnGRDDLLTCALRPAGIFG-------PGDQGLVPILFEWAEKG 190
|
250 260 270
....*....|....*....|....*....|....*....
gi 2234869976 1263 LVP----DINNSINMVPVDHVARITSLAAVSPLPDAPLS 1297
Cdd:cd05241 191 LVKfvfgRGNNLVDFTYVHNLAHAHILAAAALVKGKTIS 229
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
78-172 |
1.75e-06 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 52.07 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 78 SAFHLLLAAFIVLLHRYTGDTDIVVGSSSASAREP------------LILRLSVDPADPYWAVVRHVQQTEKEA-EADAL 144
Cdd:cd19532 240 TPFHFYLAALQVLLARLLDVDDICIGIADANRTDEdfmetigfflnlLPLRFRRDPSQTFADVLKETRDKAYAAlAHSRV 319
|
90 100 110
....*....|....*....|....*....|...
gi 2234869976 145 PYDVITQALNkgkedsLDR-----PLFRVrFFD 172
Cdd:cd19532 320 PFDVLLDELG------VPRsathsPLFQV-FIN 345
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
293-474 |
1.98e-06 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 52.32 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 293 PCVIQSLPTESPDKPQ--------GKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATF 364
Cdd:PRK05857 14 STVLDRVFEQARQQPEaialrrcdGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 365 SVVDPAYPPSRQIIYLGVAKPRGLIMLKGAGTISPTVREFLAQELKIKVevpglevfpdghivgglDPVGEDVLRAHNhl 444
Cdd:PRK05857 94 VMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAV-----------------DIAAVTRESEHS-- 154
|
170 180 190
....*....|....*....|....*....|...
gi 2234869976 445 GETD---PNVVLGPDSIGTLSFTSGSTGIPKGV 474
Cdd:PRK05857 155 LDAAslaGNADQGSEDPLAMIFTSGTTGEPKAV 187
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
441-862 |
2.21e-06 |
|
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: 52.06 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 441 HNHLGETDPNVVL--GPDSIGTLSFTSGSTGIPKGVrgrhfSLTHFFPWMSERFG-----LDETSKFTMLSGIAHD-PIQ 512
Cdd:cd05914 72 HHILNHSEAKAIFvsDEDDVALINYTSGTTGNSKGV-----MLTYRNIVSNVDGVkevvlLGKGDKILSILPLHHIyPLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 513 RDMFTPLFLGAqlHVPTADDIGTPgrLAEWMAESEVTVTHLTPAMGQLLSAQATRQIPTLLNAFFVG------DVLTKRD 586
Cdd:cd05914 147 FTLLLPLLNGA--HVVFLDKIPSA--KIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPKLTLKKFKFklakkiNNRKIRK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 587 CLR---LQALAANVRIINM-----------------------YGTTETQRAVSYfaIPPvsqDSTFLATQKDIMPAGEGM 640
Cdd:cd05914 223 LAFkkvHEAFGGNIKEFVIggakinpdveeflrtigfpytigYGMTETAPIISY--SPP---NRIRLGSAGKVIDGVEVR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 641 IDvqllvvnrndrnVPCAVGEVGEIYVRSGGLAEGYL-DQDASAEKFV-NNWFavnapprkdtilhpeegfagpesrywk 718
Cdd:cd05914 298 ID------------SPDPATGEGEIIVRGPNVMKGYYkNPEATAEAFDkDGWF--------------------------- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 719 girdrmyRSGDLGRYLPDGTVECSGRADDQ-VKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSyfvpleg 797
Cdd:cd05914 339 -------HTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYID------- 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2234869976 798 salegyasnvPDDEDDGKGLVKgmKKYRRLIKDIREHLKQKLPK----HSVPSLFVPLSKMPLnpnGKI 862
Cdd:cd05914 405 ----------PDFLDVKALKQR--NIIDAIKWEVRDKVNQKVPNykkiSKVKIVKEEFEKTPK---GKI 458
|
|
| Epimerase |
pfam01370 |
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
1028-1238 |
2.40e-06 |
|
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.
Pssm-ID: 396097 [Multi-domain] Cd Length: 238 Bit Score: 50.37 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1028 VFLTGATGFLGAFVLYDLLSRTDRvkkVICLVRGKTveqglerlkegstdrnvwSDSWVSSGRLEVVTGDLgldnfgLSQ 1107
Cdd:pfam01370 1 ILVTGATGFIGSHLVRRLLEKGYE---VIGLDRLTS------------------ASNTARLADLRFVEGDL------TDR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1108 ETWNNVANEA--DVVLHNGALVHW----VFPYEKLRSpNVLGTLTAVNLASTGKQKVFVFVSSTSAIDtehyvqlsesla 1181
Cdd:pfam01370 54 DALEKLLADVrpDAVIHLAAVGGVgasiEDPEDFIEA-NVLGTLNLLEAARKAGVKRFLFASSSEVYG------------ 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2234869976 1182 rgstDSKGVPESDDLEGAKSALKTGYGQSKWVSEKLLFEAGKR-GLRGHIVRPGYVVG 1238
Cdd:pfam01370 121 ----DGAEIPQEETTLTGPLAPNSPYAAAKLAGEWLVLAYAAAyGLRAVILRLFNVYG 174
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
653-867 |
3.19e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 51.56 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 653 RNVPCAVGEVGEIYVRSGGLAEGYL-DQDASAEKFVNNWFavnapprkdtilhpeegfagpesrywkgirdrmyRSGDLG 731
Cdd:PLN03102 383 ESVPRDGKTMGEIVIKGSSIMKGYLkNPKATSEAFKHGWL----------------------------------NTGDVG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 732 RYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVtlvrrdkdeekiLVSYFVPLEGSA------LEGYAS 805
Cdd:PLN03102 429 VIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETA------------VVAMPHPTWGETpcafvvLEKGET 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2234869976 806 NVPDDEDdgkglvKGMKKYRRLIKDIREHlkqkLPKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:PLN03102 497 TKEDRVD------KLVTRERDLIEYCREN----LPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
78-244 |
3.74e-06 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 51.26 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 78 SAFHLLLAAFIVLLHRYTGDTDIVVGSSSASaRE---------------PLILRLSVDPADPYWAVvrHVQQTEKEA-EA 141
Cdd:cd19066 245 TPTQLLLAAFALALKRLTASIDVVIGLTFLN-RPdeavedtiglflnllPLRIDTSPDATFPELLK--RTKEQSREAiEH 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 142 DALPYDVITQALnkGKEDSLDR-PLFRVRF-FDETDEPTNNFIGSTSVTSDLTVFITRPPAST-RASIAPR--LSLRVLY 216
Cdd:cd19066 322 QRVPFIELVRHL--GVVPEAPKhPLFEPVFtFKNNQQQLGKTGGFIFTTPVYTSSEGTVFDLDlEASEDPDgdLLLRLEY 399
|
170 180
....*....|....*....|....*...
gi 2234869976 217 NSLLFTSARITSFLDQLSVFLRKVAATP 244
Cdd:cd19066 400 SRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
725-773 |
4.80e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 51.28 E-value: 4.80e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2234869976 725 YRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRE 773
Cdd:PTZ00237 494 YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
265-841 |
5.51e-06 |
|
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: 50.78 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 265 PTGDLNWCgwKGAItDVFSRNARqnPDRPCVIQslptESPDKPQGKViFSYGAILRASNVLAHHLIMNGIQREDVVMVYA 344
Cdd:cd05967 45 VGGRLNTC--YNAL-DRHVEAGR--GDQIALIY----DSPVTGTERT-YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 345 HRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPRgLIMLKGAGTISPTVREF---------LAQELKIKVEV 415
Cdd:cd05967 115 PMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPK-LIVTASCGIEPGKVVPYkplldkaleLSGHKPHHVLV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 416 PGLEVFPDGHIVGGLDPVGEDVLRAHnhlGETDPNVVLGPDSIGTLsFTSGSTGIPKGV---RGRHFSLTHffpW-MSER 491
Cdd:cd05967 194 LNRPQVPADLTKPGRDLDWSELLAKA---EPVDCVPVAATDPLYIL-YTSGTTGKPKGVvrdNGGHAVALN---WsMRNI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 492 FGLDETSKFTMLSGIA----HDPIqrdMFTPLFLGAQLHVPTADDIGTPGRLAEWMAESEVTVTHLTPAMGQLlsaQATR 567
Cdd:cd05967 267 YGIKPGDVWWAASDVGwvvgHSYI---VYGPLLHGATTVLYEGKPVGTPDPGAFWRVIEKYQVNALFTAPTAI---RAIR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 568 QIPTllnaffVGDVLTKRDCLRLQAL-----------------AANVRIINMYGTTETQRAVsyfAIPPVSQDstflatQ 630
Cdd:cd05967 341 KEDP------DGKYIKKYDLSSLRTLflagerldpptlewaenTLGVPVIDHWWQTETGWPI---TANPVGLE------P 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 631 KDIMP--AGEGMIDVQLLVVNRNDRnvPCAVGEVGEIYVR----SGGLAEGYLDQdasaEKFVNNWFAvNAPPrkdtilh 704
Cdd:cd05967 406 LPIKAgsPGKPVPGYQVQVLDEDGE--PVGPNELGNIVIKlplpPGCLLTLWKND----ERFKKLYLS-KFPG------- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 705 peegfagpesrywkgirdrMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDE 784
Cdd:cd05967 472 -------------------YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELK 532
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2234869976 785 EKILVSYFVPLEGsalegyasnVPDDEDDgkgLVKGmkkyrrLIKDIRE-----------HLKQKLPK 841
Cdd:cd05967 533 GQVPLGLVVLKEG---------VKITAEE---LEKE------LVALVREqigpvaafrlvIFVKRLPK 582
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
310-769 |
6.34e-06 |
|
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: 50.60 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 310 KVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATFSVVDPAYPPSRQIIYLGVAKPR--- 386
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTivf 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 387 ----GLIMLKGAGTISPTVREFLAQELKIKV-EVPGLEVFPDGHivgglDPVGEDVlrahnhlGETDPNVVLGPDSIGTL 461
Cdd:cd17642 122 cskkGLQKVLNVQKKLKIIKTIIILDSKEDYkGYQCLYTFITQN-----LPPGFNE-------YDFKPPSFDRDEQVALI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 462 SFTSGSTGIPKGVRGRHFSL-THFFPWMSERFGLDETSKFTMLSGIahdPIQR--DMFTPL---FLGAQLHVPTAddigt 535
Cdd:cd17642 190 MNSSGSTGLPKGVQLTHKNIvARFSHARDPIFGNQIIPDTAILTVI---PFHHgfGMFTTLgylICGFRVVLMYK----- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 536 pgrlaewmAESEVTVTHLtpamgQLLSAQATRQIPTLLNAFFVGDVLTKRDCLRLQALAANVRIInmygTTETQRAVS-Y 614
Cdd:cd17642 262 --------FEEELFLRSL-----QDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPL----SKEVGEAVAkR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 615 FAIPPVSQ--------DSTFLATQKDIMPAGEGMIDVQLLV-VNRNDRNVPCAVGEVGEIYVRSGGLAEGYldqdasaek 685
Cdd:cd17642 325 FKLPGIRQgygltettSAILITPEGDDKPGAVGKVVPFFYAkVVDLDTGKTLGPNERGELCVKGPMIMKGY--------- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 686 fVNNWFAVNAPPRKDTILHpeegfagpesrywkgirdrmyrSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHL 765
Cdd:cd17642 396 -VNNPEATKALIDKDGWLH----------------------SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESIL 452
|
....
gi 2234869976 766 SQHP 769
Cdd:cd17642 453 LQHP 456
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
284-473 |
8.99e-06 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 49.87 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 284 RNARQNPDRPCViqslptESPDkpqGKVIfSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGAT 363
Cdd:PRK07514 10 RAAFADRDAPFI------ETPD---GLRY-TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 364 FSVVDPAYPPSRQIIYLGVAKPRGLImlkgagtISPTVREFLAqelKIKVEVPGLEVFPdghivggLDPVGE-DVLRAHN 442
Cdd:PRK07514 80 FLPLNTAYTLAELDYFIGDAEPALVV-------CDPANFAWLS---KIAAAAGAPHVET-------LDADGTgSLLEAAA 142
|
170 180 190
....*....|....*....|....*....|.
gi 2234869976 443 HLGETDPNVVLGPDSIGTLSFTSGSTGIPKG 473
Cdd:PRK07514 143 AAPDDFETVPRGADDLAAILYTSGTTGRSKG 173
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
904-959 |
1.23e-05 |
|
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: 44.93 E-value: 1.23e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2234869976 904 APQPIPTDESFFDLGGHSILATRLIFEIRKVFVVNAPLGLIFEKPTIAGLVEAVDA 959
Cdd:smart00823 29 AAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
284-474 |
1.45e-05 |
|
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: 49.48 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 284 RNARQNPDRPCVIQSlptesPDKPQGKVIFSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGAT 363
Cdd:cd05966 61 RHLKERGDKVAIIWE-----GDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 364 FSVVDPAYPPS--RQIIYLGVAK--------PRG--LIMLKG----AGTISPTVREFLAqelkikVEVPGLEVfpdgHIV 427
Cdd:cd05966 136 HSVVFAGFSAEslADRINDAQCKlvitadggYRGgkVIPLKEivdeALEKCPSVEKVLV------VKRTGGEV----PMT 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2234869976 428 GGLDPVGEDVLRahNHLGETDPNVVLGPDSIGTLsFTSGSTGIPKGV 474
Cdd:cd05966 206 EGRDLWWHDLMA--KQSPECEPEWMDSEDPLFIL-YTSGSTGKPKGV 249
|
|
| 3Beta_HSD |
pfam01073 |
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ... |
1031-1297 |
2.04e-05 |
|
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.
Pssm-ID: 366449 [Multi-domain] Cd Length: 279 Bit Score: 48.13 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1031 TGATGFLGAFVLYDLLSRtDRVKKVICL-VRgktveqglerlkegstDRNVWSDSWVSSGRLEVVTGDLgldnfgLSQET 1109
Cdd:pfam01073 3 TGGGGFLGRHIIKLLVRE-GELKEVRVFdLR----------------ESPELLEDFSKSNVIKYIQGDV------TDKDD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1110 WNNVANEADVVLHNGAL--VHWVFPYEKLRSPNVLGTLTAVNLASTGKQKVFVFVSSTSAIDTEHYvqlSESLARGStds 1187
Cdd:pfam01073 60 LDNALEGVDVVIHTASAvdVFGKYTFDEIMKVNVKGTQNVLEACVKAGVRVLVYTSSAEVVGPNSY---GQPILNGD--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1188 kgvpESDDLEgakSALKTGYGQSKWVSEKLLFEAGKRGLRGH------IVRPGYVVGDShtavtntDDFIWRLVKGCVQL 1261
Cdd:pfam01073 134 ----EETPYE---STHQDAYPRSKAIAEKLVLKANGRPLKNGgrlytcALRPAGIYGEG-------DRLLVPFIVNLAKL 199
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2234869976 1262 GL----VPDINNSINMVPVDHVARITSLAA---VSPLPDAPLS 1297
Cdd:pfam01073 200 GLakfkTGDDNNLSDRVYVGNVAWAHILAAralQDPKKMSSIA 242
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
708-773 |
2.81e-05 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 48.33 E-value: 2.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2234869976 708 GFAGPESRYWKGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRE 773
Cdd:cd05974 293 GYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAE 358
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
460-867 |
6.22e-05 |
|
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: 47.46 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 460 TLSFTSGSTGIPKGVRGRHFSLTHFFPwMSERFGLDETSKFTML----SGIAHDPIQrDMFTPLFLGAQL---HVPTADd 532
Cdd:cd05928 178 AIYFTSGTTGSPKMAEHSHSSLGLGLK-VNGRYWLDLTASDIMWntsdTGWIKSAWS-SLFEPWIQGACVfvhHLPRFD- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 533 igtPGRLAEWMAESEVTVTHLTPAMGQLLSAQ--ATRQIPTLLNAFFVGDVLTKRDCLRLQALAAnVRIINMYGTTETqr 610
Cdd:cd05928 255 ---PLVILKTLSSYPITTFCGAPTVYRMLVQQdlSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTG-LDIYEGYGQTET-- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 611 avsyfaippvsqdSTFLATQK--DIMPA--GEGMI--DVQllVVNRNDRNVPcaVGEVGEIYVRSG-----GLAEGYLDQ 679
Cdd:cd05928 329 -------------GLICANFKgmKIKPGsmGKASPpyDVQ--IIDDNGNVLP--PGTEGDIGIRVKpirpfGLFSGYVDN 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 680 dasaekfvnnwfavnapprkdtilhpeegfagPEsRYWKGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELG 759
Cdd:cd05928 392 --------------------------------PE-KTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPF 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 760 EIDTHLSQHPLVRENVTLVRRDKDEEKIlVSYFVPLEGSalegYASNVPDdeddgkglvkgmkkyrRLIKDIREHLKQKL 839
Cdd:cd05928 439 EVESALIEHPAVVESAVVSSPDPIRGEV-VKAFVVLAPQ----FLSHDPE----------------QLTKELQQHVKSVT 497
|
410 420
....*....|....*....|....*...
gi 2234869976 840 PKHSVPSLFVPLSKMPLNPNGKIDKPAL 867
Cdd:cd05928 498 APYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
13-166 |
6.73e-05 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 47.18 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 13 LQNLPsislPTDYPRPTGANKLIESVHTAQLSEQTSLSLLKLALysededheeeeedvessHKRPSAFHLLLAAFIVLLH 92
Cdd:cd19537 169 LSGLP----LLNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFST-----------------SSGITLHQLALAAVALALQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 93 RYTGDTDIVVGS-----SSASAR-------EPLILRLSVDPADPYWA--VVRHVQQTEKEAEADALPYDVITQALNKgKE 158
Cdd:cd19537 228 DLSDRTDIVLGApylnrTSEEDMetvglflEPLPIRIRFPSSSDASAadFLRAVRRSSQAALAHAIPWHQLLEHLGL-PP 306
|
....*...
gi 2234869976 159 DSLDRPLF 166
Cdd:cd19537 307 DSPNHPLF 314
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
413-771 |
6.82e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 47.33 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 413 VEVPGLEVFpdghIVGglDPVGEDVLRAHnhlGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERF 492
Cdd:PRK13388 116 LDLPGVRVL----DVD--TPAYAELVAAA---GALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 493 GLdetskftmlsgIAHDPIQRDMftPLFLGAQLHVPTADDIGTPGRLAEWMAES---------EVTVTHLT---PAMGQL 560
Cdd:PRK13388 187 GL-----------TRDDVCYVSM--PLFHSNAVMAGWAPAVASGAAVALPAKFSasgflddvrRYGATYFNyvgKPLAYI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 561 LsaqATRQIP-----TLLNAFfvGDVLTKRDCLRLQALAAnVRIINMYGTTETqrAVSyfaippvsqdstflATQKDIMP 635
Cdd:PRK13388 254 L---ATPERPddadnPLRVAF--GNEASPRDIAEFSRRFG-CQVEDGYGSSEG--AVI--------------VVREPGTP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 636 AGE-GMIDVQLLVVNrNDRNVPCAVGE-------------VGEIYVRSG-GLAEGYL-DQDASAEKfvnnwfavnapprk 699
Cdd:PRK13388 312 PGSiGRGAPGVAIYN-PETLTECAVARfdahgallnadeaIGELVNTAGaGFFEGYYnNPEATAER-------------- 376
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2234869976 700 dtilhpeegfagpesrywkgIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLV 771
Cdd:PRK13388 377 --------------------MRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAI 428
|
|
| SDR_a1 |
cd05265 |
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ... |
1032-1316 |
8.04e-05 |
|
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187575 [Multi-domain] Cd Length: 250 Bit Score: 45.74 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1032 GATGFLGAFVLYDLLSRTDRVKkviCLVRGKTVEQGLERLKEGSTDRNVWSDswvssgrLEVVTGDlgldnfglsqETWn 1111
Cdd:cd05265 7 GGTRFIGKALVEELLAAGHDVT---VFNRGRTKPDLPEGVEHIVGDRNDRDA-------LEELLGG----------EDF- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1112 nvaneaDVVLHNGAlvhwvfpyeklRSPNVLGTLTAVnLASTGKQkvFVFVSSTSAidtehYvqlsESLARGSTDS--KG 1189
Cdd:cd05265 66 ------DVVVDTIA-----------YTPRQVERALDA-FKGRVKQ--YIFISSASV-----Y----LKPGRVITEStpLR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1190 VPESDDLEGAKSalktgYGQSKWVSEKLLFEAGkrGLRGHIVRPGYVVGdshtAVTNTDD---FIWRLVKGcvqlG--LV 1264
Cdd:cd05265 117 EPDAVGLSDPWD-----YGRGKRAAEDVLIEAA--AFPYTIVRPPYIYG----PGDYTGRlayFFDRLARG----RpiLV 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2234869976 1265 PDINNSI-NMVPVDHVARITSLAAVSplPDAPLSVCHVTARPLPTFNGMLSSL 1316
Cdd:cd05265 182 PGDGHSLvQFIHVKDLARALLGAAGN--PKAIGGIFNITGDEAVTWDELLEAC 232
|
|
| PLN02996 |
PLN02996 |
fatty acyl-CoA reductase |
1027-1164 |
1.24e-04 |
|
fatty acyl-CoA reductase
Pssm-ID: 215538 [Multi-domain] Cd Length: 491 Bit Score: 46.24 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1027 TVFLTGATGFLGAFVLYDLLSRTDRVKKVICLVRGKTVEQGLERLKEGSTD-------RNVWSDSWVS--SGRLEVVTGD 1097
Cdd:PLN02996 13 TILVTGATGFLAKIFVEKILRVQPNVKKLYLLLRASDAKSATQRLHDEVIGkdlfkvlREKLGENLNSliSEKVTPVPGD 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2234869976 1098 -----LGLDNFGLSQETWnnvaNEADVVLHNGALVHWVFPYEKLRSPNVLGTLTAVNLAS-TGKQKVFVFVSS 1164
Cdd:PLN02996 93 isyddLGVKDSNLREEMW----KEIDIVVNLAATTNFDERYDVALGINTLGALNVLNFAKkCVKVKMLLHVST 161
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
314-772 |
1.47e-04 |
|
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: 45.91 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 314 SYGAILRASNVLAHHLIMNGIQR--EDVVMVYAhrSVDLVVAVMAVLKAGATFSVVDPAyppsrqiiyLGVAKprgliml 391
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRgmRAVLMVPP--GPDFFALTFALFKAGAVPVLIDPG---------MGRKN------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 392 kgagtisptvrefLAQELKikvevpglEVFPDGHIvgGLDPVGEDVLrahnhlgetdpnvvlgpdsigtLSFTSGSTGIP 471
Cdd:cd05910 66 -------------LKQCLQ--------EAEPDAFI--GIPKADEPAA----------------------ILFTSGSTGTP 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 472 KGVRGRHFSLTHFFPWMSERFgldetskftmlsGIAHDpiQRDMFT-PLF--LGAQLHV--------PTADDIGTPGRLA 540
Cdd:cd05910 101 KGVVYRHGTFAAQIDALRQLY------------GIRPG--EVDLATfPLFalFGPALGLtsvipdmdPTRPARADPQKLV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 541 EWMAESEVTVTHLTPAMGQLLS---AQATRQIPTLLNAFFVGDVLTKRDCLRL-QALAANVRIINMYGTTEtqravsyfA 616
Cdd:cd05910 167 GAIRQYGVSIVFGSPALLERVArycAQHGITLPSLRRVLSAGAPVPIALAARLrKMLSDEAEILTPYGATE--------A 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 617 IPPVS-QDSTFLATQKDIMPAGEGM--------IDVQLLVVN-------RNDRNVPcaVGEVGEIYVRSGGLAEGYL--- 677
Cdd:cd05910 239 LPVSSiGSRELLATTTAATSGGAGTcvgrpipgVRVRIIEIDdepiaewDDTLELP--RGEIGEITVTGPTVTPTYVnrp 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 678 DQDASAEkfvnnwfavnapprkdtILHPEEGFagpesrywkgirdrMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIE 757
Cdd:cd05910 317 VATALAK-----------------IDDNSEGF--------------WHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLY 365
|
490
....*....|....*
gi 2234869976 758 LGEIDTHLSQHPLVR 772
Cdd:cd05910 366 TEPVERVFNTHPGVR 380
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
610-744 |
1.92e-04 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 45.80 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 610 RAVSYFAIPPVSQDStflATQKDIMPAGEGMIDVQLLVVNRNDRNvPCAVGEVGEIYVRSGGLAEGY--LDQDASAEKFV 687
Cdd:cd05905 340 RALRHGVVRLDERDK---PNSLPLQDSGKVLPGAQVAIVNPETKG-LCKDGEIGEIWVNSPANASGYflLDGETNDTFKV 415
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 688 NNWFAVNAPPRKDTILHPEE-GFAGPESRYWKGI--RDRMYRSGDLgrylpDGTVECSGR 744
Cdd:cd05905 416 FPSTRLSTGITNNSYARTGLlGFLRPTKCTDLNVeeHDLLFVVGSI-----DETLEVRGL 470
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
536-775 |
2.40e-04 |
|
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: 44.95 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 536 PGRLAEWMAESEVTV-THLTPAMGQLLSAQAT--RQIPTLLNaffVGDVLTKRDCLRLQALAaNVRIINMYGTTETQRAV 612
Cdd:cd17637 77 PAEALELIEEEKVTLmGSFPPILSNLLDAAEKsgVDLSSLRH---VLGLDAPETIQRFEETT-GATFWSLYGQTETSGLV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 613 SYfaiPPVSQDSTflatqkdimPAGEGMIDVQLLVVNRNDRNVPcaVGEVGEIYVRSGGLAEGYLDQD-ASAEKFVNNWf 691
Cdd:cd17637 153 TL---SPYRERPG---------SAGRPGPLVRVRIVDDNDRPVP--AGETGEIVVRGPLVFQGYWNLPeLTAYTFRNGW- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 692 avnapprkdtilhpeegfagpesrywkgirdrmYRSGDLGRYLPDGTVECSGR--ADDQVKIRGFRIELGEIDTHLSQHP 769
Cdd:cd17637 218 ---------------------------------HHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHP 264
|
....*.
gi 2234869976 770 LVRENV 775
Cdd:cd17637 265 AIAEVC 270
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
720-789 |
3.90e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 44.75 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 720 IRdrmYRSGDLGRYLPDgtvECS------------GRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTL-VRRDKDEEK 786
Cdd:COG1541 295 IR---YRTGDLTRLLPE---PCPcgrthprigrilGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIvVDREGGLDE 368
|
...
gi 2234869976 787 ILV 789
Cdd:COG1541 369 LTV 371
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
313-868 |
5.21e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 44.22 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 313 FSYGAILRASNVLAHHLIMNGIQREDVVMVYAHRSVDLVVAVMAVLKAGATfsvvdpayppsrqiiylgvakprglimlk 392
Cdd:PRK13383 61 LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGAD----------------------------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 393 gagtISPTVREFLAQELKIKVEVPGLE-VFPDGHIVGGLDPVGEDVLrahnhlgETDPNVVLGPDSIG---------TLS 462
Cdd:PRK13383 112 ----VVPISTEFRSDALAAALRAHHIStVVADNEFAERIAGADDAVA-------VIDPATAGAEESGGrpavaapgrIVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 463 FTSGSTGIPKGVRGRHFSLTHFFPWMS--ERFGLDETSKFTMLsgiahdpiqrdmfTPLF--LGAQLHVPTADDIGTPGR 538
Cdd:PRK13383 181 LTSGTTGKPKGVPRAPQLRSAVGVWVTilDRTRLRTGSRISVA-------------MPMFhgLGLGMLMLTIALGGTVLT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 539 LAEWMAESEVTVTHLTPA---------MGQLLS----AQATRQIPTLLNAFFVGDVLTKRDCLRLQALAANVrIINMYGT 605
Cdd:PRK13383 248 HRHFDAEAALAQASLHRAdaftavpvvLARILElpprVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 606 TETqrAVSYFAIPPVSQDSTflatqkdiMPAGEGMIDVQLLVVNRNDRNVPCAVgeVGEIYVRSGGLAEGYLDQDAsaek 685
Cdd:PRK13383 327 TEV--GIGALATPADLRDAP--------ETVGKPVAGCPVRILDRNNRPVGPRV--TGRIFVGGELAGTRYTDGGG---- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 686 fvnnwfavnapprkdtilhpeegfagpesrywKGIRDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHL 765
Cdd:PRK13383 391 --------------------------------KAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENAL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 766 SQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALEGYAsnvpddeddgkglvkgmkkyrrlikdIREHLKQKLPKHSVP 845
Cdd:PRK13383 439 AAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQ--------------------------LRDYLKDRVSRFEQP 492
|
570 580
....*....|....*....|...
gi 2234869976 846 SLFVPLSKMPLNPNGKIDKPALP 868
Cdd:PRK13383 493 RDINIVSSIPRNPTGKVLRKELP 515
|
|
| UDP_G4E_5_SDR_e |
cd05264 |
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ... |
1028-1257 |
1.02e-03 |
|
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187574 [Multi-domain] Cd Length: 300 Bit Score: 42.69 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1028 VFLTGATGFLG-AFVLYdllsrtdrvkkviCLVRGKTVEqglerlkegSTDRNVWSDSwVSSGRLEVVTGDLGlDNFGLS 1106
Cdd:cd05264 2 VLIVGGNGFIGsHLVDA-------------LLEEGPQVR---------VFDRSIPPYE-LPLGGVDYIKGDYE-NRADLE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1107 QETwnnvaNEADVVLHngaLVHWVFPYEKLRSP------NVLGTLTAVN-LASTGKQKvFVFVSSTSAIdtehYvqlses 1179
Cdd:cd05264 58 SAL-----VGIDTVIH---LASTTNPATSNKNPildiqtNVAPTVQLLEaCAAAGIGK-IIFASSGGTV----Y------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1180 larGSTDSKGVPESDDLEGAKSalktgYGQSKWVSEKLL-FEAGKRGLRGHIVRPG--YVVGDSHT---AVTNTddFIWR 1253
Cdd:cd05264 119 ---GVPEQLPISESDPTLPISS-----YGISKLAIEKYLrLYQYLYGLDYTVLRISnpYGPGQRPDgkqGVIPI--ALNK 188
|
....
gi 2234869976 1254 LVKG 1257
Cdd:cd05264 189 ILRG 192
|
|
| AR_like_SDR_e |
cd05193 |
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ... |
1028-1245 |
1.39e-03 |
|
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This subgroup contains aldehyde reductase and flavonoid reductase of the extended SDR-type and related proteins. Proteins in this subgroup have a complete SDR-type active site tetrad and a close match to the canonical extended SDR NADP-binding motif. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187536 [Multi-domain] Cd Length: 295 Bit Score: 42.60 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1028 VFLTGATGFLGAFVLYDLLSRTDRVKKvicLVRGKT---VEQGLERLKEGSTDRNVW-SDSWVSSGRLEVVTGdlgldnf 1103
Cdd:cd05193 1 VLVTGASGFVASHVVEQLLERGYKVRA---TVRDPSkvkKVNHLLDLDAKPGRLELAvADLTDEQSFDEVIKG------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1104 glsqetwnnvaneADVVLHNGALVHWV--FPYEKLRsPNVLGTLTAVNLAS-TGKQKVFVFVSSTSAIdtehyvqlseSL 1180
Cdd:cd05193 71 -------------CAGVFHVATPVSFSskDPNEVIK-PAIGGTLNALKAAAaAKSVKRFVLTSSAGSV----------LI 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1181 ARGSTDSKGVPES--DDLEGAKSALKT--GYGQSKWVSEKLLFE-AGKRGLRGHIVRPGYVVGDSHTAVT 1245
Cdd:cd05193 127 PKPNVEGIVLDEKswNLEEFDSDPKKSawVYAASKTLAEKAAWKfADENNIDLITVIPTLTIGTIFDSET 196
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
78-244 |
1.68e-03 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 42.74 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 78 SAFHLLLAAFIVLLHRYTGDTDIVVG------SSSASAREP------LILRLSVDPADPYWAVVRHVqqteKEAEADAL- 144
Cdd:cd19533 241 SWPSFFIALVAAYLHRLTGANDVVLGvpvmgrLGAAARQTPgmvantLPLRLTVDPQQTFAELVAQV----SRELRSLLr 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 145 ----PYDVITQALnkgKEDSLDRPLFRV-----RF-----FDETDEPTNNFigSTSVTSDLTVFIT-RPPASTrasiapr 209
Cdd:cd19533 317 hqryRYEDLRRDL---GLTGELHPLFGPtvnymPFdygldFGGVVGLTHNL--SSGPTNDLSIFVYdRDDESG------- 384
|
170 180 190
....*....|....*....|....*....|....*
gi 2234869976 210 LSLRVLYNSLLFTSARITSFLDQLSVFLRKVAATP 244
Cdd:cd19533 385 LRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| YbjT |
COG0702 |
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ... |
1027-1290 |
2.11e-03 |
|
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];
Pssm-ID: 440466 [Multi-domain] Cd Length: 215 Bit Score: 41.37 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1027 TVFLTGATGFLGAFVLYDLLsrtDRVKKVICLVRGKTVEQGLERlkegstdrnvwsdswvssGRLEVVTGDLgldnfgLS 1106
Cdd:COG0702 1 KILVTGATGFIGRRVVRALL---ARGHPVRALVRDPEKAAALAA------------------AGVEVVQGDL------DD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1107 QETWNNVANEADVVLHngaLVHwvfpyeklrspnvlgtltavnlaSTGKQKVFVFVSSTSAI-------DTEHYVQLSes 1179
Cdd:COG0702 54 PESLAAALAGVDAVFL---LVP-----------------------SGPGGDFAVDVEGARNLadaakaaGVKRIVYLS-- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1180 lARGSTDSKGVPesddlegaksalktgYGQSKWVSEKLLFEAgkrGLRGHIVRPGYVVGdshtavtNTDDFIWRLVKGCV 1259
Cdd:COG0702 106 -ALGADRDSPSP---------------YLRAKAAVEEALRAS---GLPYTILRPGWFMG-------NLLGFFERLRERGV 159
|
250 260 270
....*....|....*....|....*....|.
gi 2234869976 1260 qlGLVPDINNSINMVPVDHVARITSLAAVSP 1290
Cdd:COG0702 160 --LPLPAGDGRVQPIAVRDVAEAAAAALTDP 188
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
658-864 |
3.16e-03 |
|
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: 41.33 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 658 AVGEVGEIYVRSGGLAEGYLDQDASAEKfvnnwfAVNApprkDTILHpeegfagpesrywkgirdrmyrSGDLGRYLPDG 737
Cdd:cd17638 182 RIADDGEVLVRGYNVMQGYLDDPEATAE------AIDA----DGWLH----------------------TGDVGELDERG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 738 TVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEKILVSYFVPLEGSALegyasnvpdDEDDgkgl 817
Cdd:cd17638 230 YLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTL---------TEED---- 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2234869976 818 vkgmkkyrrLIKDIREHLKQklpkHSVPSLFVPLSKMPLNPNGKIDK 864
Cdd:cd17638 297 ---------VIAWCRERLAN----YKVPRFVRFLDELPRNASGKVMK 330
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
642-853 |
3.28e-03 |
|
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: 41.57 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 642 DVQLLVVNRNDRNVPCAVGEVGEIYVRSGGLA--EGYLDQDASAEKFVNNWFAvnapprkdtilhpeegfagpesrywKG 719
Cdd:cd05940 267 ESGEPIRDAEGRCIKVPRGEPGLLISRINPLEpfDGYTDPAATEKKILRDVFK-------------------------KG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 720 irDRMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTlvrrdkdeekilvsYFVPLEGsa 799
Cdd:cd05940 322 --DAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANV--------------YGVQVPG-- 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2234869976 800 LEGYAS----NVPDDED-DGKGLVKgmkkyrrlikdireHLKQKLPKHSVPsLFVPLSK 853
Cdd:cd05940 384 TDGRAGmaaiVLQPNEEfDLSALAA--------------HLEKNLPGYARP-LFLRLQP 427
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
716-862 |
4.13e-03 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 41.39 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 716 YWKGIRDrMYRSGDLGRYLPDGTVECSGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVtlvrrdkdeekiLVSYFVPL 795
Cdd:cd05966 463 YFSKFPG-YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAA------------VVGRPHDI 529
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2234869976 796 EGSALegYASNVPDDeddgkglvkGMKKYRRLIKDIREHLKQKLPKHSVPS--LFVPlsKMPLNPNGKI 862
Cdd:cd05966 530 KGEAI--YAFVTLKD---------GEEPSDELRKELRKHVRKEIGPIATPDkiQFVP--GLPKTRSGKI 585
|
|
| UDP_G4E_3_SDR_e |
cd05240 |
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ... |
1028-1257 |
4.38e-03 |
|
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187551 [Multi-domain] Cd Length: 306 Bit Score: 40.81 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1028 VFLTGATGFLGAFVLyDLLSRTDRVKKVICLvrgktveqglerlkegstDRNVWSDSWvssGRLEVVTGDL----GLDNF 1103
Cdd:cd05240 1 ILVTGAAGGLGRLLA-RRLAASPRVIGVDGL------------------DRRRPPGSP---PKVEYVRLDIrdpaAADVF 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1104 GLsqetwnnvaNEADVVLHNGALVHWVFPYEKLRSPNVLGTLTAVNLASTGKQKVFVFVSSTSAidtehYVQLSESLARG 1183
Cdd:cd05240 59 RE---------READAVVHLAFILDPPRDGAERHRINVDGTQNVLDACAAAGVPRVVVTSSVAV-----YGAHPDNPAPL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2234869976 1184 STDS--KGVPESddlegaksalktGYGQSKWVSEKLLFEAGKR--GLRGHIVRPGYVVGdSHTAVTNTDDFIWRLVKG 1257
Cdd:cd05240 125 TEDAplRGSPEF------------AYSRDKAEVEQLLAEFRRRhpELNVTVLRPATILG-PGTRNTTRDFLSPRRLPV 189
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
723-807 |
5.37e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 41.26 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 723 RMYRSGDLGRYLPDGTVECSGRADDQVKIR-GFRIELGEIDTHLSQHPLVrENVtLVRRDKdeekiLVSYFVPL---EGS 798
Cdd:PLN02387 535 RWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYV-DNI-MVHADP-----FHSYCVALvvpSQQ 607
|
....*....
gi 2234869976 799 ALEGYASNV 807
Cdd:PLN02387 608 ALEKWAKKA 616
|
|
| SDR_a7 |
cd05262 |
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ... |
1028-1243 |
7.26e-03 |
|
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187572 [Multi-domain] Cd Length: 291 Bit Score: 40.02 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1028 VFLTGATGFLGAFVLYDLLSRTDRvkkVICLVRGktvEQGLERLkegstdrnvwsdswvSSGRLEVVTGDLGldnfglSQ 1107
Cdd:cd05262 3 VFVTGATGFIGSAVVRELVAAGHE---VVGLARS---DAGAAKL---------------EAAGAQVHRGDLE------DL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1108 ETWNNVANEADVVLHNGAlVHWVFPYE---KLRSPNVLGTLTAvnLASTGKQkvFVFVSSTSAIdtehyvqlseslarGS 1184
Cdd:cd05262 56 DILRKAAAEADAVIHLAF-THDFDNFAqacEVDRRAIEALGEA--LRGTGKP--LIYTSGIWLL--------------GP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1185 TDSKGVPESDDLEGAKSALKTgygqskwVSEKLLFEAGKRGLRGHIVR-PGYVVGDSHTA 1243
Cdd:cd05262 117 TGGQEEDEEAPDDPPTPAARA-------VSEAAALELAERGVRASVVRlPPVVHGRGDHG 169
|
|
| CDP_TE_SDR_e |
cd05258 |
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that ... |
1027-1244 |
8.59e-03 |
|
CDP-tyvelose 2-epimerase, extended (e) SDRs; CDP-tyvelose 2-epimerase is a tetrameric SDR that catalyzes the conversion of CDP-D-paratose to CDP-D-tyvelose, the last step in tyvelose biosynthesis. This subgroup is a member of the extended SDR subfamily, with a characteristic active site tetrad and NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187568 [Multi-domain] Cd Length: 337 Bit Score: 39.97 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1027 TVFLTGATGFLGAfVLYDLLSRTDrvKKVIC---LVRgKTVEQGLERLKEGSTDRNVwsdswvssgrlEVVTGDlgLDNf 1103
Cdd:cd05258 2 RVLITGGAGFIGS-NLARFFLKQG--WEVIGfdnLMR-RGSFGNLAWLKANREDGGV-----------RFVHGD--IRN- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 1104 glsQETWNNVANEADVVLHNGA--LVHWvfpyeKLRSP------NVLGTLTAVNLA-STGKQKVFVFvSSTSAI--DTEH 1172
Cdd:cd05258 64 ---RNDLEDLFEDIDLIIHTAAqpSVTT-----SASSPrldfetNALGTLNVLEAArQHAPNAPFIF-TSTNKVygDLPN 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2234869976 1173 YVQLSE-----SLARGSTDSKGVPESDDLEGAKSAlktgYGQSKWVSEKLLFEAGKR-GLRGHIVRPGYVVGDSHTAV 1244
Cdd:cd05258 135 YLPLEEletryELAPEGWSPAGISESFPLDFSHSL----YGASKGAADQYVQEYGRIfGLKTVVFRCGCLTGPRQFGT 208
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
455-536 |
8.88e-03 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 40.55 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2234869976 455 PDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFpwMSERFGLDETSKFTMLSGIahdPIQRDM------FTPLFLGA-QLHV 527
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNM--FAILNSTEWKTKDRILSWM---PLTHDMgliafhLAPLIAGMnQYLM 179
|
....*....
gi 2234869976 528 PTADDIGTP 536
Cdd:cd05908 180 PTRLFIRRP 188
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
455-483 |
8.91e-03 |
|
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: 40.28 E-value: 8.91e-03
10 20
....*....|....*....|....*....
gi 2234869976 455 PDSIGTLSFTSGSTGIPKGVrgrhfSLTH 483
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGV-----MLTH 136
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
443-502 |
9.29e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 40.43 E-value: 9.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2234869976 443 HLGETDPNVVLGPDSIGTLSFTSGSTGIPKGVRGRHFSLTHFFPWMSERFGL--DETSKFTM 502
Cdd:PRK07867 139 HRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLgpDDVCYVSM 200
|
|
| |
