|
Name |
Accession |
Description |
Interval |
E-value |
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
23-1424 |
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: 2024.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 23 RWSERLSALPSLALPTDYPRPSPAKLVESFQTLPIPpsltpallrltleySTLYPSSPLPTPYHLLLTSFSILLFRYTPD 102
Cdd:TIGR03443 1 RWSERLDNPTLSVLPHDYLRPANNRLVEATYSLQLP--------------SAEVTAGGGSTPFIILLAAFAALVYRLTGD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 103 PSLVLYptvaVNSTPSTHPLLLKMELSPEMSFFEILHQVLTQ-EIIATQDSVPLSTLVDHLK------PEGPLFRVRFFD 175
Cdd:TIGR03443 67 EDIVLG----TSSNKSGRPFVLRLNITPELSFLQLYAKVSEEeKEGASDIGVPFDELSEHIQaakkleRTPPLFRLAFQD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 176 STTLEMDpttslttdltLYLLAQPTETPI-TRTSIPSLYLRLVYNSLLFTQNRITSLLESLLQLLTSASEKSfNHPIGSL 254
Cdd:TIGR03443 143 APDNQQT----------TYSTGSTTDLTVfLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNP-DEPIGKV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 255 PIRTISQEKILPDPTSDLNWCDFVGAIPDIFSANAKKYPDKLCVIQSEQtngiMEGPSKGRKTFTYGQIDKASNVIAHCL 334
Cdd:TIGR03443 212 SLITPSQKSLLPDPTKDLDWSGFRGAIHDIFADNAEKHPDRTCVVETPS----FLDPSSKTRSFTYKQINEASNILAHYL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 335 IQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLVIEKAGELAKIVKDFIKDKL 414
Cdd:TIGR03443 288 LKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEKAGTLDQLVRDYIDKEL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 415 DLKILIPSISLSSNG-------KEEYQDILEKYQNLSQTPTGIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWM 487
Cdd:TIGR03443 368 ELRTEIPALALQDDGslvggslEGGETDVLAPYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWM 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 488 SKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQ 567
Cdd:TIGR03443 448 AKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAQATTP 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 568 IPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAVSYFAIPSVNEDSTFLSTQKDLISAGQGMIDVQLLVV 647
Cdd:TIGR03443 528 IPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMYGTTETQRAVSYFEIPSRSSDSTFLKNLKDVMPAGKGMKNVQLLVV 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 648 NRTDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFGQDLKREDTLIG---PAREHWFGIRDRMYRSGDLGR 723
Cdd:TIGR03443 608 NRNDRTQTCGVGEVGEIYVRAGGLAEGYLGlPELNAEKFVNNWFVDPSHWIDLDKEnnkPEREFWLGPRDRLYRTGDLGR 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 724 YLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIN--DNLEGLISESDNPQ 801
Cdd:TIGR03443 688 YLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDksDELEEFKSEVDDEE 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 802 DDEEveeeeenekdlkmeMLRGVRRYRRLIKDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKLPFPDTSLVPTV 881
Cdd:TIGR03443 768 SSDP--------------VVKGLIKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAV 833
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 882 -----PTTDSTMLTPTQKTIHDIWLKLLPSPPNTIGMEEIFFDMGGHSILATRLIFEIRKTFVVNAPLGLVFDKPTIGGQ 956
Cdd:TIGR03443 834 aknrsASAADEEFTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGF 913
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 957 AREVDSLRN-EELTPAFDTVTPSRPTTKPRSYSDDLPELVSLLP-TFSPLPSDYNTKPLTVFLTGATGFLGGFILNDLLT 1034
Cdd:TIGR03443 914 AKEVDRLKKgEELADEGDSEIEEEETVLELDYAKDAKTLVDSLPkSYPSRKELDASTPITVFLTGATGFLGSFILRDLLT 993
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1035 NRSSRIKKVICLVRSSSLEKGQERLINSCTLLGIWNPSWLseNKLEIIIGDLSKPQFDLSSKSWDYLSKETDAILHNGAI 1114
Cdd:TIGR03443 994 RRSNSNFKVFAHVRAKSEEAGLERLRKTGTTYGIWDEEWA--SRIEVVLGDLSKEKFGLSDEKWSDLTNEVDVIIHNGAL 1071
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1115 VHWVYPYEKLKPTNVLSTLECLKLCCQgGKMKSFTFVSSTSVLDTEGFIKKSDEELQNGNDGLREDDDLEQGKKGLVTGY 1194
Cdd:TIGR03443 1072 VHWVYPYSKLRDANVIGTINVLNLCAE-GKAKQFSFVSSTSALDTEYYVNLSDELVQAGGAGIPESDDLMGSSKGLGTGY 1150
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1195 GQSKWVAEKLIMMAQNNGLRGWIVRPGYVMGDSKSAVTNTDDFIWRMVKGCLQLGLIPDINNSINLVPVDHVSLLCSLSL 1274
Cdd:TIGR03443 1151 GQSKWVAEYIIREAGKRGLRGCIVRPGYVTGDSKTGATNTDDFLLRMLKGCIQLGLIPNINNTVNMVPVDHVARVVVAAA 1230
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1275 LSPppppspppppsssssspltspsseKPTSGPYVIHVTGHPRIRFNDLLSFLPFYGYKVEKVEYVIWRSKLEQHVLET- 1353
Cdd:TIGR03443 1231 LNP------------------------PKESELAVAHVTGHPRIRFNDFLGTLKTYGYDVEIVDYVHWRKSLERFVIERs 1286
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589279984 1354 QDNALFPLLHFVLDDLPTSTKSAELDDTNARTL----AKQAGE--KEGAGVGEEEVGKYLSWLIRAGFLDEPDGKGK 1424
Cdd:TIGR03443 1287 EDNALFPLLHFVLDDLPQSTKAPELDDTNAATSlkadAAWTGVdvSSGAGVTEEQIGIYIAYLVKVGFLPAPTKTGA 1363
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
292-873 |
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: 821.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 292 YPDKLCVIQSEQTNgimegpSKGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSV 371
Cdd:cd17647 1 FPERTCVVETPSLN------SSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 372 VDPAYPPNRQIVYLEVSNPKGLLVIEKAGelakivkdfikdkldlkilipsislssngkeeyqdilekyqnlsqtptgII 451
Cdd:cd17647 75 IDPAYPPARQNIYLGVAKPRGLIVIRAAG-------------------------------------------------VV 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 452 LGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDD 531
Cdd:cd17647 106 VGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 532 IGTPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAV 611
Cdd:cd17647 186 IGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQRAV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 612 SYFAIPSVNEDSTFLSTQKDLISAGQGMIDVQLLVVNRTDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWF 690
Cdd:cd17647 266 SYFEVPSRSSDPTFLKNLKDVMPAGRGMLNVQLLVVNRNDRTQICGIGEVGEIYVRAGGLAEGYRGlPELNKEKFVNNWF 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 691 -------GQDLKREDtligPAREHWFGIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVR 763
Cdd:cd17647 346 vepdhwnYLDKDNNE----PWRQFWLGPRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVR 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 764 ENVTLVRRDKDEEKVLVSYFVPindnlegliseSDNPQDDEEVEEEEENEKDLKMEMLRGVRRYRRLIKDIREYLRKKLP 843
Cdd:cd17647 422 ENITLVRRDKDEEPTLVSYIVP-----------RFDKPDDESFAQEDVPKEVSTDPIVKGLIGYRKLIKDIREFLKKRLA 490
|
570 580 590
....*....|....*....|....*....|
gi 589279984 844 SYAVPSVYFPLSKLPLNPNGKVDKPKLPFP 873
Cdd:cd17647 491 SYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
314-870 |
8.89e-137 |
|
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: 427.71 E-value: 8.89e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 314 GRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGL 393
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 394 LViekagelakivkdfikdkldlkilipsislssngkeeyqdilekyqnlsqtptgiilGPDSPATLSFTSGSTGIPKGV 473
Cdd:cd05930 89 LT---------------------------------------------------------DPDDLAYVIYTSGSTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 474 KGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRLAEWMDDCQVSVTHLT 553
Cdd:cd05930 112 MVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 554 PAM-GQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAVSYFAIPSVNEDStflstqkDL 632
Cdd:cd05930 192 PSLlRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEED-------GR 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 633 ISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPSATAEKFVMNWFGQdlkredtligparehwfgi 711
Cdd:cd05930 265 VPIGRPIPNTRVYVLDENLRPVP--PGVPGELYIGGAGLARGYLnRPELTAERFVPNPFGP------------------- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 712 RDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPindnle 791
Cdd:cd05930 324 GERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVP------ 397
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589279984 792 glisESDNPQDdeeveeeeenekdlkmemlrgvrryrrlIKDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd05930 398 ----DEGGELD----------------------------EEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
13-1008 |
4.20e-135 |
|
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: 450.46 E-value: 4.20e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 13 PASELKAKLDRWSERL-SALPSLALPTDYPRPSPAKLVESFQTLPIPPSLTPALLRLTLEYSTlypssplpTPYHLLLTS 91
Cdd:COG1020 200 QGEELARQLAYWRQQLaGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGV--------TLFMVLLAA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 92 FSILLFRYT--PDpslvlyptVAVNSTPS--THP------------LLLKMELSPEMSFFEILHQVLTQ--EIIATQDsV 153
Cdd:COG1020 272 FALLLARYSgqDD--------VVVGTPVAgrPRPeleglvgffvntLPLRVDLSGDPSFAELLARVRETllAAYAHQD-L 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 154 PLSTLVDHLKPE-----GPLFRVRF----FDSTTLEMDpttsLTTDLTLYLLAQPTETPITRTSIPS---LYLRLVYNSL 221
Cdd:COG1020 343 PFERLVEELQPErdlsrNPLFQVMFvlqnAPADELELP----GLTLEPLELDSGTAKFDLTLTVVETgdgLRLTLEYNTD 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 222 LFTQNRItsllesllqlltsasEKSFNH--------------PIGSLPIRTIS-QEKIL----------PDPTSdlnwcd 276
Cdd:COG1020 419 LFDAATI---------------ERMAGHlvtllealaadpdqPLGDLPLLTAAeRQQLLaewnataapyPADAT------ 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 277 fvgaIPDIFSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMV 356
Cdd:COG1020 478 ----LHELFEAQAARTPDAVAVVFGDQS-------------LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMV 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 357 VCVMGILKAGGVFSVVDPAYPPNRqIVY-LEVSNPKgLLVIEKAgelakivkdfIKDKLDlKILIPSISLSSNGKEEYqd 435
Cdd:COG1020 541 VALLAVLKAGAAYVPLDPAYPAER-LAYmLEDAGAR-LVLTQSA----------LAARLP-ELGVPVLALDALALAAE-- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 436 ilekyqnlSQTPTGIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMF 515
Cdd:COG1020 606 --------PATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIF 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 516 TPLFLGAELYVPTSDDIGTPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKN 595
Cdd:COG1020 678 GALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPG 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 596 VCIINMYGTTETQRAVSYFAIPSVNEDStflstqkDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGY 675
Cdd:COG1020 758 ARLVNLYGPTETTVDSTYYEVTPPDADG-------GSVPIGRPIANTRVYVLDAHLQPVP--VGVPGELYIGGAGLARGY 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 676 L-DPSATAEKFVMNWFGQDlkredtligparehwfGirDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDT 754
Cdd:COG1020 829 LnRPELTAERFVADPFGFP----------------G--ARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEA 890
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 755 HLSRHPLVRENVTLVRRDKDEEKVLVSYFVPindnlegliseSDNPQDDEEVeeeeenekdlkmemlrgvrryrrlikdI 834
Cdd:COG1020 891 ALLQHPGVREAVVVAREDAPGDKRLVAYVVP-----------EAGAAAAAAL---------------------------L 932
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 835 REYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKLPFPDTSLVPTVPTTDSTMLTPTQKTIHDIWLKLLpsppntIGME 914
Cdd:COG1020 933 RLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVV------VGDD 1006
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 915 EIFFDMGGHSILATRLIFEIRKTFVVNAPLGLVFDKPTIGGQAREVDSLRNEELTPAFDTVTPSRPTTKPRSYSDDLPEL 994
Cdd:COG1020 1007 DFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLAL 1086
|
1050
....*....|....
gi 589279984 995 VSLLPTFSPLPSDY 1008
Cdd:COG1020 1087 LLLLALLALLALLL 1100
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
319-766 |
2.25e-122 |
|
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: 387.78 E-value: 2.25e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 319 TYGQIDKASNVIAHCLIQN-GLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLVIE 397
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 398 KAGELAkivkdfikDKLDLKILIPSISlssngkeeyqDILEKYQNLSQTPTGIILGPDSPATLSFTSGSTGIPKGVKGRH 477
Cdd:TIGR01733 81 ALASRL--------AGLVLPVILLDPL----------ELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 478 YSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRL-AEWMDDCQVSVTHLTPAM 556
Cdd:TIGR01733 143 RSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALlAALIAEHPVTVLNLTPSL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 557 GQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAVSYFAIPSVNEDSTFLstqkdlISAG 636
Cdd:TIGR01733 223 LALLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESP------VPIG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 637 QGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPSATAEKFVMNWFGQdlkredtligparehwfGIRDRM 715
Cdd:TIGR01733 297 RPLANTRLYVLDDDLRPVP--VGVVGELYIGGPGVARGYLnRPELTAERFVPDPFAG-----------------GDGARL 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 589279984 716 YRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENV 766
Cdd:TIGR01733 358 YRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAV 408
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
14-988 |
3.38e-109 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 384.13 E-value: 3.38e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 14 ASELKAKLDRWSERLSA-LPSLALPTDYPRPSpaklVESFQ----TLPIPPSLTPALLRLTLEYSTlypssplpTPYHLL 88
Cdd:PRK12467 233 AGERERQLAYWQEQLGGeHTVLELPTDRPRPA----VPSYRgarlRVDLPQALSAGLKALAQREGV--------TLFMVL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 89 LTSFSILLFRYTPDPSLVLYPTVAVNSTPSTHPLL--------LKMELSPEMSFFEILHQV--LTQEIIATQDsVPLSTL 158
Cdd:PRK12467 301 LASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIgffvntqvLKAEVDPQASFLELLQQVkrTALGAQAHQD-LPFEQL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 159 VDHLKPE-----GPLFRVRFFDSTTLEMD--------PTTSLTTDLTLYLLAQPTETPITRTSIPSLYLRLVYNSLLFTQ 225
Cdd:PRK12467 380 VEALQPErslshSPLFQVMFNHQNTATGGrdregaqlPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEA 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 226 NRITSLLESLLQLLTSASEKsFNHPIGSLPIrtiSQEKILPDPTSDLNWCDFV---GAIPDIFSANAKKYPDKLCVIQSE 302
Cdd:PRK12467 460 TTIERLATHWRNLLEAIVAE-PRRRLGELPL---LDAEERARELVRWNAPATEyapDCVHQLIEAQARQHPERPALVFGE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 303 QTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQI 382
Cdd:PRK12467 536 QV-------------LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 383 VYLEVSNPKGLLVIEkagELAKivkdfikdKLDLKILIPSISLSSNGkeeyqDILEKYQNLSQTPTgiiLGPDSPATLSF 462
Cdd:PRK12467 603 YMLDDSGVRLLLTQS---HLLA--------QLPVPAGLRSLCLDEPA-----DLLCGYSGHNPEVA---LDPDNLAYVIY 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 463 TSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRLAEWM 542
Cdd:PRK12467 664 TSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALM 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 543 DDCQVSVTHLTPAMGQ-LLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAVSYFAIPSVNE 621
Cdd:PRK12467 744 ADQGVTVLKIVPSHLQaLLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEER 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 622 DStflstqkDLISAGQGMIDVQLLVVNRTdrLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFGQDlkredtl 700
Cdd:PRK12467 824 DF-------GNVPIGQPLANLGLYILDHY--LNPVPVGVVGELYIGGAGLARGYHRrPALTAERFVPDPFGAD------- 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 701 igparehwfgiRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVrRDKDEEKVLV 780
Cdd:PRK12467 888 -----------GGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLV 955
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 781 SYFVPindnleGLISESDNPQDdeeveeeeenekdlkmemlrgvrryrrLIKDIREYLRKKLPSYAVPSVYFPLSKLPLN 860
Cdd:PRK12467 956 AYLVP------AAVADGAEHQA---------------------------TRDELKAQLRQVLPDYMVPAHLLLLDSLPLT 1002
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 861 PNGKVDKPKLPFPDTSlvpTVPTTDSTMLTPTQKTIHDIWLKLLPSPPntIGMEEIFFDMGGHSILATRLIFEIRKTFVV 940
Cdd:PRK12467 1003 PNGKLDRKALPKPDAS---AVQATFVAPQTELEKRLAAIWADVLKVER--VGLTDNFFELGGHSLLATQVISRVRQRLGI 1077
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*...
gi 589279984 941 NAPLGLVFDKPTIGGQAREVDSLRNEELTPAFDTvtpSRPTTKPRSYS 988
Cdd:PRK12467 1078 QVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDV---DRDQPLPLSYA 1122
|
|
| SDR_e1 |
cd05235 |
extended (e) SDRs, subgroup 1; This family consists of an SDR module of multidomain proteins ... |
1014-1342 |
6.00e-105 |
|
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: 335.39 E-value: 6.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1014 TVFLTGATGFLGGFILNDLLtnRSSRIKKVICLVRSSSLEKGQERLINSCTLLGIWNPSWLSENKLEIIIGDLSKPQFDL 1093
Cdd:cd05235 1 TVLLTGATGFLGAYLLRELL--KRKNVSKIYCLVRAKDEEAALERLIDNLKEYGLNLWDELELSRIKVVVGDLSKPNLGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1094 SSKSWDYLSKETDAILHNGAIVHWVYPYEKLKPTNVLSTLECLKLCCQgGKMKSFTFVSSTSVLDTEgfikksdeelQNG 1173
Cdd:cd05235 79 SDDDYQELAEEVDVIIHNGANVNWVYPYEELKPANVLGTKELLKLAAT-GKLKPLHFVSTLSVFSAE----------EYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1174 NDGLREDDDLEQGKKGLVTGYGQSKWVAEKLIMMAQNNGLRGWIVRPGYVMGDSKSAVTNTDDFIWRMVKGCLQLGLIPD 1253
Cdd:cd05235 148 ALDDEESDDMLESQNGLPNGYIQSKWVAEKLLREAANRGLPVAIIRPGNIFGDSETGIGNTDDFFWRLLKGCLQLGIYPI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1254 INNSINLVPVDHVSLLCSLSLLspppppspppppsssssspltspsseKPTSGPYVIHVTGHPRIRFNDLLSFLPFYGYK 1333
Cdd:cd05235 228 SGAPLDLSPVDWVARAIVKLAL--------------------------NESNEFSIYHLLNPPLISLNDLLDALEEKGYS 281
|
....*....
gi 589279984 1334 VEKVEYVIW 1342
Cdd:cd05235 282 IKEVSYEEW 290
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
14-957 |
3.83e-97 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 347.15 E-value: 3.83e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 14 ASELKAKLDRWSERL-SALPSLALPTDYPRPSPAKLVESFQTLPIPPSLTPALLRLT-LEYSTLYpssplptpyHLLLTS 91
Cdd:PRK12467 1298 AGERARQLAYWKAQLgGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALArREGVTLF---------MLLLAS 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 92 FSILLFRYTPDPSLVLYPTVAVNSTPSTHPLL--------LKMELSPEMSFFEILHQVLTQEIIAT--QDsVPLSTLVDH 161
Cdd:PRK12467 1369 FQTLLHRYSGQDDIRVGVPIANRNRAETEGLIgffvntqvLRAEVDGQASFQQLLQQVKQAALEAQahQD-LPFEQLVEA 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 162 LKPE-----GPLFRVRFFDSTTLEMD----PTTSLTTDLTLYLLAQPTETPITRTSIPSLYLRLVYNSLLF---TQNRIT 229
Cdd:PRK12467 1448 LQPErslshSPLFQVMFNHQRDDHQAqaqlPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFeasTIERLA 1527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 230 SLLESLLQLLTSASEKsfnhPIGSLPIRT-ISQEKILpdptsdLNW----CDFVGA--IPDIFSANAKKYPDKLCVIQSE 302
Cdd:PRK12467 1528 GHWLNLLQGLVADPER----RLGELDLLDeAERRQIL------EGWnathTGYPLArlVHQLIEDQAAATPEAVALVFGE 1597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 303 QTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQI 382
Cdd:PRK12467 1598 QE-------------LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLA 1664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 383 VYLEVSNpKGLLVIEKAgelakivkdfIKDKLDLKILIPSISLssngkEEYQDILEKYqnlSQTPTGIILGPDSPATLSF 462
Cdd:PRK12467 1665 YMIEDSG-IELLLTQSH----------LQARLPLPDGLRSLVL-----DQEDDWLEGY---SDSNPAVNLAPQNLAYVIY 1725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 463 TSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRLAEWM 542
Cdd:PRK12467 1726 TSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLI 1805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 543 DDCQVSVTHLTPAMGQLLsAQATRQI---PSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAVSYFAIPSV 619
Cdd:PRK12467 1806 ERQQVTTLHFVPSMLQQL-LQMDEQVehpLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRK 1884
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 620 NEdstflsTQKDLISAGQGMIDVQLLVVNRTdrLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFGQdlkred 698
Cdd:PRK12467 1885 DL------EGRDSVPIGQPIANLSTYILDAS--LNPVPIGVAGELYLGGVGLARGYLNrPALTAERFVADPFGT------ 1950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 699 tligparehwfgIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVrRDKDEEKV 778
Cdd:PRK12467 1951 ------------VGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQ 2017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 779 LVSYFVPindNLEGLISESDNPQddeeveeeeenekdlkmemlrgvrRYRRLIKDireYLRKKLPSYAVPSVYFPLSKLP 858
Cdd:PRK12467 2018 LVAYVVP---TDPGLVDDDEAQV------------------------ALRAILKN---HLKASLPEYMVPAHLVFLARMP 2067
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 859 LNPNGKVDKPKLPFPDTSLVPTV---PTTDstmltpTQKTIHDIWLKLLPSPpnTIGMEEIFFDMGGHSILATRLIFEIR 935
Cdd:PRK12467 2068 LTPNGKLDRKALPAPDASELQQAyvaPQSE------LEQRLAAIWQDVLGLE--QVGLHDNFFELGGDSIISIQVVSRAR 2139
|
970 980
....*....|....*....|..
gi 589279984 936 KTFVVNAPLGLvFDKPTIGGQA 957
Cdd:PRK12467 2140 QAGIRFTPKDL-FQHQTVQSLA 2160
|
|
| Thioester-redct |
TIGR01746 |
thioester reductase domain; This model includes the terminal domain from the fungal alpha ... |
1014-1415 |
4.78e-97 |
|
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: 316.66 E-value: 4.78e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1014 TVFLTGATGFLGGFILNDLLTNRSSRikKVICLVRSSSLEKGQERLINSCTLLGIWNPSWLSEnKLEIIIGDLSKPQFDL 1093
Cdd:TIGR01746 1 TVLLTGATGFLGAYLLEELLRRSTRA--KVICLVRADSEEHAMERLREALRSYRLWHENLAME-RIEVVAGDLSKPRLGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1094 SSKSWDYLSKETDAILHNGAIVHWVYPYEKLKPTNVLSTLECLKLCCQGgKMKSFTFVSSTSVLDTEgfikksdeelqNG 1173
Cdd:TIGR01746 78 SDAEWERLAENVDTIVHNGALVNHVYPYSELRGANVLGTVEVLRLAASG-RAKPLHYVSTISVGAAI-----------DL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1174 NDGLREDDDLEQGKKGLVTGYGQSKWVAEKLIMMAQNNGLRGWIVRPGYVMGDSKSAVTNTDDFIWRMVKGCLQLGLIPD 1253
Cdd:TIGR01746 146 STGVTEDDATVTPYPGLAGGYTQSKWVAELLVREASDRGLPVTIVRPGRILGDSYTGAWNSSDILWRMVKGCLALGAYPQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1254 IN-NSINLVPVDHVSLLCSLSLLSPPpppspppppsssssspltspssekPTSGPYVIHVTGHPRIRFNDLLSFLPFYGY 1332
Cdd:TIGR01746 226 SPeLTEDLTPVDFVARAIVALSSRPA------------------------ASAGGIVFHVVNPNPVPLDEFLEWLERAGY 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1333 KVEKVEYVIWRSKLEQHVLETQD---NALFPLLHFVLD-DLPTSTKSAELDDTNARTLAKQAGEKEgAGVGEEEVGKYLS 1408
Cdd:TIGR01746 282 NLRLVSFDEWLQRLEDSDTAKRDsrrYPLLPLLHFTGDaFESDETDTRNLDSRSTAEALEGDGIRE-PSITAPLLHLYLQ 360
|
....*..
gi 589279984 1409 WLIRAGF 1415
Cdd:TIGR01746 361 YLKEIGF 367
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
285-874 |
2.22e-96 |
|
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: 319.27 E-value: 2.22e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 285 FSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILK 364
Cdd:cd17655 3 FEEQAEKTPDHTAVVFEDQT-------------LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 365 AGGVFSVVDPAYPPNRqIVY-LEVSNPKGLLviekagelakivkdfIKDKLDLKIlipsISLSSNGKEEYQDILEKyqnl 443
Cdd:cd17655 70 AGGAYLPIDPDYPEER-IQYiLEDSGADILL---------------TQSHLQPPI----AFIGLIDLLDEDTIYHE---- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 444 SQTPTGIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAE 523
Cdd:cd17655 126 ESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 524 LYVPTSDDIGTPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHL-AKNVCIINMY 602
Cdd:cd17655 206 LYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELfGTNPTITNAY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 603 GTTETQRAVSYFAIPSVNedstflsTQKDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYLD-PSAT 681
Cdd:cd17655 286 GPTETTVDASIYQYEPET-------DQQVSVPIGKPLGNTRIYILDQYGRPQP--VGVAGELYIGGEGVARGYLNrPELT 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 682 AEKFVmnwfgqdlkredtligparEHWFGIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPL 761
Cdd:cd17655 357 AEKFV-------------------DDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPD 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 762 VRENVTLVRRDKDEEKVLVSYFVpindnlegliseSDNPQDdeeveeeeenekdlkmemlrgvrryrrlIKDIREYLRKK 841
Cdd:cd17655 418 IKEAVVIARKDEQGQNYLCAYIV------------SEKELP----------------------------VAQLREFLARE 457
|
570 580 590
....*....|....*....|....*....|...
gi 589279984 842 LPSYAVPSVYFPLSKLPLNPNGKVDKPKLPFPD 874
Cdd:cd17655 458 LPDYMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
14-958 |
2.91e-96 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 344.63 E-value: 2.91e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 14 ASELKAKLDRWSERL-SALPSLALPTDYPRPSPAKLVESFQTLPIPPSLTPALlRLTLEYSTLypssplpTPYHLLLTSF 92
Cdd:PRK12316 233 AGEQERQLEYWRAQLgEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEAL-RGTARRQGL-------TLFMLLLGAF 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 93 SILLFRYTPDPSLVLYPTVAVNSTPSTHPLL--------LKMELSPEMSFFEILHQV--LTQEIIATQDsVPLSTLVDHL 162
Cdd:PRK12316 305 NVLLHRYSGQTDIRVGVPIANRNRAEVEGLIgffvntqvLRSVFDGRTRVATLLAGVkdTVLGAQAHQD-LPFERLVEAL 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 163 KPE-----GPLFRVRF------FDSTTLEMDPTTSLTTDLTLYLLAQPTETPITRTSIPSLYLRLVYNSLLF---TQNRI 228
Cdd:PRK12316 384 KVErslshSPLFQVMYnhqplvADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFearTVERM 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 229 TSLLESLLQLLTSASEKSfnhpIGSLPIRTISQEKILPDptsdlNWcdfvgaipdifSANAKKYPDKLCVIQ--SEQTNG 306
Cdd:PRK12316 464 ARHWQNLLRGMVENPQAR----VDELPMLDAEERGQLVE-----GW-----------NATAAEYPLQRGVHRlfEEQVER 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 307 IMEGPSK--GRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVY 384
Cdd:PRK12316 524 TPEAPALafGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYM 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 385 LEVSNpKGLLVIEKagelakivkdFIKDKLDLKILIPSISLSSNGKEeyqdiLEKYqnlSQTPTGIILGPDSPATLSFTS 464
Cdd:PRK12316 604 LEDSG-VQLLLSQS----------HLGRKLPLAAGVQVLDLDRPAAW-----LEGY---SEENPGTELNPENLAYVIYTS 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 465 GSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRLAEWMDD 544
Cdd:PRK12316 665 GSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINR 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 545 CQVSVTHLTPAMGQ-LLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAVSYFaipsvneds 623
Cdd:PRK12316 745 EGVDTLHFVPSMLQaFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHW--------- 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 624 TFLSTQKDLISAGQGMIDVQLLVVNRTdrLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFGQDlkredtlig 702
Cdd:PRK12316 816 TCVEEGGDSVPIGRPIANLACYILDAN--LEPVPVGVLGELYLAGRGLARGYHGrPGLTAERFVPSPFVAG--------- 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 703 parehwfgirDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRrdkdEEKVLVSY 782
Cdd:PRK12316 885 ----------ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQLVGY 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 783 FVPindnleglisesdnpqddeeveeeeenekdlkmEMLRGVRRyrrliKDIREYLRKKLPSYAVPSVYFPLSKLPLNPN 862
Cdd:PRK12316 951 VVL---------------------------------ESEGGDWR-----EALKAHLAASLPEYMVPAQWLALERLPLTPN 992
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 863 GKVDKPKLPFPDTSLVPTV---PTTDstmltpTQKTIHDIWLKLLPSPPntIGMEEIFFDMGGHSILATRLIFEIRKTFV 939
Cdd:PRK12316 993 GKLDRKALPAPEASVAQQGyvaPRNA------LERTLAAIWQDVLGVER--VGLDDNFFELGGDSIVSIQVVSRARQAGI 1064
|
970
....*....|....*....
gi 589279984 940 VNAPLGLvFDKPTIGGQAR 958
Cdd:PRK12316 1065 QLSPRDL-FQHQTIRSLAL 1082
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
282-870 |
4.21e-96 |
|
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: 318.45 E-value: 4.21e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 282 PDIFSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMG 361
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRT-------------LTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 362 ILKAGGVFSVVDPAYPPNRQIVYLEVSNPKglLVIEKAGELAKIVKDfikdkLDLKILIPSISLSsngkeeyqdilekyq 441
Cdd:cd17646 68 VLKAGAAYLPLDPGYPADRLAYMLADAGPA--VVLTTADLAARLPAG-----GDVALLGDEALAA--------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 442 nLSQTPTGIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLG 521
Cdd:cd17646 126 -PPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 522 AELYVPTSDDIGTPGRLAEWMDDCQVSVTHLTPAM-GQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLqHLAKNVCIIN 600
Cdd:cd17646 205 ARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMlRVFLAEPAAGSCASLRRVFCSGEALPPELAARF-LALPGAELHN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 601 MYGTTETQRAVSYFAIPSVNEDSTflstqkdlISAGQGMIDVQLLVVnrTDRLVPCAVGEMGEIYVRSGGLAEGYLD-PS 679
Cdd:cd17646 284 LYGPTEAAIDVTHWPVRGPAETPS--------VPIGRPVPNTRLYVL--DDALRPVPVGVPGELYLGGVQLARGYLGrPA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 680 ATAEKFVMNWFGQDlkredtligparehwfgirDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRH 759
Cdd:cd17646 354 LTAERFVPDPFGPG-------------------SRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAH 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 760 PLVRENVTLVRRDKDEEKVLVSYFVPINDNLEGLISEsdnpqddeeveeeeenekdlkmemlrgvrryrrlikdIREYLR 839
Cdd:cd17646 415 PAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAA-------------------------------------LRAHLA 457
|
570 580 590
....*....|....*....|....*....|.
gi 589279984 840 KKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd17646 458 ERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
283-870 |
5.46e-95 |
|
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: 315.29 E-value: 5.46e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 283 DIFSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGI 362
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRS-------------LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 363 LKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLVIEKAGELAkivkdfikdkldlkilipsislssngkEEYQDILEKYQN 442
Cdd:cd12117 68 LKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDRSLAGRA---------------------------GGLEVAVVIDEA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 443 LSQTPTG---IILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFF---PWMSkrfgLNEKSKFTMLSGIAHDPIQRDMFT 516
Cdd:cd12117 121 LDAGPAGnpaVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVkntNYVT----LGPDDRVLQTSPLAFDASTFEIWG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 517 PLFLGAELYVPTSDDIGTPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNV 596
Cdd:cd12117 197 ALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 597 CIINMYGTTETQRAVSYFAIPSVNEDStflstqkDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL 676
Cdd:cd12117 277 RLVNGYGPTENTTFTTSHVVTELDEVA-------GSIPIGRPIANTRVYVLDEDGRPVP--PGVPGELYVGGDGLALGYL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 677 -DPSATAEKFVmnwfgqdlkredtligparEHWFGIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTH 755
Cdd:cd12117 348 nRPALTAERFV-------------------ADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAA 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 756 LSRHPLVRENVTLVRRDKDEEKVLVSYFVPindnlEGLISESdnpqddeeveeeeenekdlkmemlrgvrryrrlikDIR 835
Cdd:cd12117 409 LRAHPGVREAVVVVREDAGGDKRLVAYVVA-----EGALDAA-----------------------------------ELR 448
|
570 580 590
....*....|....*....|....*....|....*
gi 589279984 836 EYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd12117 449 AFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
285-871 |
2.52e-90 |
|
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: 302.34 E-value: 2.52e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 285 FSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILK 364
Cdd:cd17651 1 FERQAARTPDAPALVAEGRR-------------LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 365 AGGVFSVVDPAYPPNRQIVYLEVSNPKGLLVIEKAGELAKIVKDFIkdkldlkilipsislssngkeeYQDILEKYQNLS 444
Cdd:cd17651 68 AGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPALAGELAVELVAV----------------------TLLDQPGAAAGA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 445 QTPTGIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAEL 524
Cdd:cd17651 126 DAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 525 YVPTsDDIGT-PGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQI--PSLLNAFFVG------DVLTKRDCTRLQHLAkn 595
Cdd:cd17651 206 VLPP-EEVRTdPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGvrLAALRYLLTGgeqlvlTEDLREFCAGLPGLR-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 596 vcIINMYGTTETQRAVSYfaipsvnEDSTFLSTQKDLISAGQGMIDVQLLVVNRTDRlvPCAVGEMGEIYVRSGGLAEGY 675
Cdd:cd17651 283 --LHNHYGPTETHVVTAL-------SLPGDPAAWPAPPPIGRPIDNTRVYVLDAALR--PVPPGVPGELYIGGAGLARGY 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 676 L-DPSATAEKFVmnwfgqdlkredtligparEHWFGIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDT 754
Cdd:cd17651 352 LnRPELTAERFV-------------------PDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEA 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 755 HLSRHPLVRENVTLVRRDKDEEKVLVSYFVPindnleglisesdnpqddeeveeeeenekdlkmemlrgVRRYRRLIKDI 834
Cdd:cd17651 413 ALARHPGVREAVVLAREDRPGEKRLVAYVVG--------------------------------------DPEAPVDAAEL 454
|
570 580 590
....*....|....*....|....*....|....*..
gi 589279984 835 REYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKLP 871
Cdd:cd17651 455 RAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-958 |
2.02e-89 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 323.06 E-value: 2.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 2 AESALVNGTTTPASELKAKLDRWSERL-SALPSLALPTDYPRPSPAKLVESFQTLPIPPSLTPALLRLTLEYSTlypssp 80
Cdd:PRK12316 2770 ADYAAWQRAWMDSGEGARQLDYWRERLgGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGV------ 2843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 81 lpTPYHLLLTSFSILLFRYTPDPSLVLYPTVAVNSTPSTHPLL--------LKMELSPEMSFFEILHQVLTQ--EIIATQ 150
Cdd:PRK12316 2844 --TLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIgffvntqvLRAQVDAQLAFRDLLGQVKEQalGAQAHQ 2921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 151 DsVPLSTLVDHLKPE-----GPLFRVRFFDSTTLEMDPTTSLTTDLTLYLLAQPTETPITRT---SIPSLYLRLVYNSLL 222
Cdd:PRK12316 2922 D-LPFEQLVEALQPErslshSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDtweSAEGLGASLTYATDL 3000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 223 FTQNRITSLLESLLQLLTSASEKSfNHPIGSLPIRTISQEkilpdptsdlnwcdfvGAIPDIFSANAKKYPDKLCVIQ-- 300
Cdd:PRK12316 3001 FDARTVERLARHWQNLLRGMVENP-QRSVDELAMLDAEER----------------GQLLEAWNATAAEYPLERGVHRlf 3063
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 301 SEQTNGIMEGPSK--GRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPP 378
Cdd:PRK12316 3064 EEQVERTPDAVALafGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPE 3143
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 379 NRQIVYLEVSnpkgllviekagelakivkdfikdKLDLKILIPSISLSSNGKEEYQDILEKYQNLSQTPTGIILGPDSPA 458
Cdd:PRK12316 3144 ERLAYMLEDS------------------------GAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLA 3199
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 459 TLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRL 538
Cdd:PRK12316 3200 YVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALL 3279
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 539 AEWMDDCQVSVTHLTPAMGQLLSAQATRQIPSLLNAFFVGDVLTKRDCtrLQHLAKNVCIINMYGTTETQRAVSYFAIPS 618
Cdd:PRK12316 3280 VELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADL--QQQVFAGLPLYNLYGPTEATITVTHWQCVE 3357
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 619 VNEDSTFLstqkdlisaGQGMIDVQLLVVNrtDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFGQDlkre 697
Cdd:PRK12316 3358 EGKDAVPI---------GRPIANRACYILD--GSLEPVPVGALGELYLGGEGLARGYHNrPGLTAERFVPDPFVPG---- 3422
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 698 dtligparehwfgirDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLvrrdKDEEK 777
Cdd:PRK12316 3423 ---------------ERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGR 3483
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 778 VLVSYFVPindnleglisesDNPQDDeeveeeeenekdlkmemLRGVrryrrlikdIREYLRKKLPSYAVPSVYFPLSKL 857
Cdd:PRK12316 3484 QLVAYVVP------------EDEAGD-----------------LREA---------LKAHLKASLPEYMVPAHLLFLERM 3525
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 858 PLNPNGKVDKPKLPFPDTSLVPT---VPTtdstmlTPTQKTIHDIWLKLLPSPpnTIGMEEIFFDMGGHSILATRLIFEI 934
Cdd:PRK12316 3526 PLTPNGKLDRKALPRPDAALLQQdyvAPV------NELERRLAAIWADVLKLE--QVGLTDNFFELGGDSIISLQVVSRA 3597
|
970 980
....*....|....*....|....
gi 589279984 935 RKTFVVNAPLGLvFDKPTIGGQAR 958
Cdd:PRK12316 3598 RQAGIRFTPKDL-FQHQTIQGLAR 3620
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
24-954 |
5.73e-89 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 321.52 E-value: 5.73e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 24 WSERLSALPS---LALPTDYPRPSPAKLVESFQTLpIPPSLTPALLRLTLEYSTlypssPLPTpyhLLLTSFSILLFRYT 100
Cdd:PRK12316 4285 WREQLAALDEptrLAQAIARADLRSANGYGEHVRE-LDATATARLREFARTQRV-----TLNT---LVQAAWLLLLQRYT 4355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 101 PDPSLVLYPTVA----------------VNSTPsthpllLKMELSPEMSFFEILHQVLTQEIIATQ-------------- 150
Cdd:PRK12316 4356 GQDTVAFGATVAgrpaelpgiegqiglfINTLP------VIATPRAQQSVVEWLQQVQRQNLALREhehtplyeiqrwag 4429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 151 -------DSV------PLSTLVDHLKPEGplfrVRFFDSTTLEMdpttslttdltlyllaqpTETPITrTSI---PSLYL 214
Cdd:PRK12316 4430 qggealfDSLlvfenyPVSEALQQGAPGG----LRFGEVTNHEQ------------------TNYPLT-LAVglgETLSL 4486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 215 RLVYNSLLF---TQNRITSLLESLLQLLTSASEKsfnhPIGSLP-IRTISQEKILPDptsdlnWCDFVGAIPD------I 284
Cdd:PRK12316 4487 QFSYDRGHFdaaTIERLARHLTNLLEAMAEDPQR----RLGELQlLEKAEQQRIVAL------WNRTDAGYPAtrcvhqL 4556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 285 FSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILK 364
Cdd:PRK12316 4557 VAERARMTPDAVAVVFDEEK-------------LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLK 4623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 365 AGGVFSVVDPAYPPNRQIVYLEVSNPKGLLViekagelakivKDFIKDKLDLKILIPSISLssngkeeyqDILEKYQNLS 444
Cdd:PRK12316 4624 AGGAYVPLDPEYPRERLAYMMEDSGAALLLT-----------QSHLLQRLPIPDGLASLAL---------DRDEDWEGFP 4683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 445 QTPTGIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAEL 524
Cdd:PRK12316 4684 AHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASV 4763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 525 YVPtSDDIGTPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQ--IPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMY 602
Cdd:PRK12316 4764 VIR-DDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDgePPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGY 4842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 603 GTTETQRAVSYFAIPsvnedstflstqkDLISAGQGMIDVQLLVVNRT-----DRLVPCAVGEMGEIYVRSGGLAEGYLD 677
Cdd:PRK12316 4843 GPTETTVTVLLWKAR-------------DGDACGAAYMPIGTPLGNRSgyvldGQLNPLPVGVAGELYLGGEGVARGYLE 4909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 678 -PSATAEKFVMNWFGQDlkredtligparehwfgiRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHL 756
Cdd:PRK12316 4910 rPALTAERFVPDPFGAP------------------GGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARL 4971
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 757 SRHPLVRENVtLVRRDKDEEKVLVSYFVPINDNLegliSESDNPQDDeeveeeeenekdlkmemLRGVrryrrlikdIRE 836
Cdd:PRK12316 4972 REHPAVREAV-VIAQEGAVGKQLVGYVVPQDPAL----ADADEAQAE-----------------LRDE---------LKA 5020
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 837 YLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKLPFPDTSLVPTVPTTDSTMLtptQKTIHDIWLKLLPSPpnTIGMEEI 916
Cdd:PRK12316 5021 ALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSEL---EQQVAAIWAEVLQLE--RVGLDDN 5095
|
970 980 990
....*....|....*....|....*....|....*...
gi 589279984 917 FFDMGGHSILATRLIFEIRKTFVVNAPLGLVFDKPTIG 954
Cdd:PRK12316 5096 FFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLA 5133
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
317-870 |
1.58e-87 |
|
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: 293.06 E-value: 1.58e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 317 TFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRqivylevsnpkgllvi 396
Cdd:cd17643 12 RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER---------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 397 ekageLAKIVKDfikdkldlkilipsislssngkeeyqdilekyqnlSQtPTGIILGPDSPATLSFTSGSTGIPKGVKGR 476
Cdd:cd17643 76 -----IAFILAD-----------------------------------SG-PSLLLTDPDDLAYVIYTSGSTGRPKGVVVS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 477 HYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRLAEWMDDCQVSVTHLTP-A 555
Cdd:cd17643 115 HANVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPsA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 556 MGQLLSA--QATRQIPSLLNAFFVGDVLTKRdctRLQHLAKNVC-----IINMYGTTETQRAVSYFAIpsvnedstflsT 628
Cdd:cd17643 195 FYQLVEAadRDGRDPLALRYVIFGGEALEAA---MLRPWAGRFGldrpqLVNMYGITETTVHVTFRPL-----------D 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 629 QKDLISAGQGMI-----DVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFGqdlkredtlig 702
Cdd:cd17643 261 AADLPAAAASPIgrplpGLRVYVLDADGRPVP--PGVVGELYVSGAGVARGYLGrPELTAERFVANPFG----------- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 703 parehwfGIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSY 782
Cdd:cd17643 328 -------GPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAY 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 783 FVPiNDNLEGLISEsdnpqddeeveeeeenekdlkmemlrgvrryrrlikdIREYLRKKLPSYAVPSVYFPLSKLPLNPN 862
Cdd:cd17643 401 VVA-DDGAAADIAE-------------------------------------LRALLKELLPDYMVPARYVPLDALPLTVN 442
|
....*...
gi 589279984 863 GKVDKPKL 870
Cdd:cd17643 443 GKLDRAAL 450
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
281-870 |
7.89e-87 |
|
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: 292.14 E-value: 7.89e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGS-------------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAML 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPPNRqivylevsnpkgllviekageLAKIVKDfikdkldlkiLIPSISLSSNgkeeyqdileky 440
Cdd:cd05918 68 AVLKAGGAFVPLDPSHPLQR---------------------LQEILQD----------TGAKVVLTSS------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 441 qnlsqtptgiilgPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFL 520
Cdd:cd05918 105 -------------PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 521 GAELYVPTSDDIgtPGRLAEWMDDCQVSVTHLTPAMGQLLSAQatrQIPSLLNAFFVGDVLTKRDCTRLqhlAKNVCIIN 600
Cdd:cd05918 172 GGCLCIPSEEDR--LNDLAGFINRLRVTWAFLTPSVARLLDPE---DVPSLRTLVLGGEALTQSDVDTW---ADRVRLIN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 601 MYGTTETQRAVSYFAIPSvNEDSTFLstqkdlisaGQGmIDVQLLVVN--RTDRLVPcaVGEMGEIYVRSGGLAEGYL-D 677
Cdd:cd05918 244 AYGPAECTIAATVSPVVP-STDPRNI---------GRP-LGATCWVVDpdNHDRLVP--IGAVGELLIEGPILARGYLnD 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 678 PSATAEKFVMNWFgqdlkredtligPAREHWFGIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLS 757
Cdd:cd05918 311 PEKTAAAFIEDPA------------WLKQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLR 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 758 RHPLVRENVT---LVRRDKDEEKVLVSYFVPINDNLEGLISESDNPQDDeeveeeeenekdlkmemlrgvRRYRRLIKDI 834
Cdd:cd05918 379 QSLPGAKEVVvevVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPS---------------------DEFRALVAEL 437
|
570 580 590
....*....|....*....|....*....|....*.
gi 589279984 835 REYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd05918 438 RSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
287-1019 |
3.09e-86 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 312.87 E-value: 3.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 287 ANAKKYPDKLCVIQ--SEQTNGIMEGPSK--GRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGI 362
Cdd:PRK12467 3086 ATAAAYPSERLVHQliEAQVARTPEAPALvfGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAV 3165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 363 LKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLL----VIEKAGELAkIVKDFIKDKLDLKILIPSislssngkeeyqdile 438
Cdd:PRK12467 3166 LKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLtqahLLEQLPAPA-GDTALTLDRLDLNGYSEN---------------- 3228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 439 kyqnlsqTPTGIILGpDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPL 518
Cdd:PRK12467 3229 -------NPSTRVMG-ENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTL 3300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 519 FLGAELYVpTSDDIGTPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQ-IPSLLNAFFVGDVLTKRDCTRLQHLAKNVC 597
Cdd:PRK12467 3301 ICGGCLVV-RDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGAdCASLDIYVFGGEAVPPAAFEQVKRKLKPRG 3379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 598 IINMYGTTETQRAVSYFAIPSvneDSTFLSTQkdlISAGQGMIDVQLLVVNrtDRLVPCAVGEMGEIYVRSGGLAEGYLD 677
Cdd:PRK12467 3380 LTNGYGPTEAVVTVTLWKCGG---DAVCEAPY---APIGRPVAGRSIYVLD--GQLNPVPVGVAGELYIGGVGLARGYHQ 3451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 678 -PSATAEKFVMNWFGqdlkredtligparehwfGIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHL 756
Cdd:PRK12467 3452 rPSLTAERFVADPFS------------------GSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARL 3513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 757 SRHPLVRENVTLVrRDKDEEKVLVSYFVPindnleglisesDNPQDDeeveeeeenekdlkmemlrgvrryrrLIKDIRE 836
Cdd:PRK12467 3514 LQHPSVREAVVLA-RDGAGGKQLVAYVVP------------ADPQGD--------------------------WRETLRD 3554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 837 YLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKLPFPDTSLVPT--VPTTDstmltpTQKTIHDIWLKLLPSPpnTIGME 914
Cdd:PRK12467 3555 HLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREyvAPRSE------VEQQLAAIWADVLGVE--QVGVT 3626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 915 EIFFDMGGHSILATRLIFEIRKTFVVNAPLGLVFDKPTIGGQAREVdslrneeltPAFDtvTPSRPTTKPRSYSDDLPEL 994
Cdd:PRK12467 3627 DNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS---------PLGD--VPVNLLLDLNRLETGFPAL 3695
|
730 740
....*....|....*....|....*
gi 589279984 995 VSLLPTFSplpSDYNTKPLTVFLTG 1019
Cdd:PRK12467 3696 FCRHEGLG---TVFDYEPLAVILEG 3717
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
314-984 |
1.95e-83 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 300.42 E-value: 1.95e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 314 GRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKgl 393
Cdd:PRK10252 480 ARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPS-- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 394 LVIEKAGELAKIVkdfikDKLDLKILipsislssngkeeyqdileKYQNLSQTPTGIILG---PDSPATLSFTSGSTGIP 470
Cdd:PRK10252 558 LLITTADQLPRFA-----DVPDLTSL-------------------CYNAPLAPQGAAPLQlsqPHHTAYIIFTSGSTGRP 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 471 KGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRLAEWMDDCQVSVT 550
Cdd:PRK10252 614 KGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTT 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 551 HLTPAM-----GQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAkNVCIINMYGTTETQRAVSYFaiPSVNEDSTF 625
Cdd:PRK10252 694 HFVPSMlaafvASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLT-GAPLHNLYGPTEAAVDVSWY--PAFGEELAA 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 626 LSTqkDLISAGQGMIDVQLLVVNrtDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFGQDlkredtligpa 704
Cdd:PRK10252 771 VRG--SSVPIGYPVWNTGLRILD--ARMRPVPPGVAGDLYLTGIQLAQGYLGrPDLTASRFIADPFAPG----------- 835
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 705 rehwfgirDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVR------RDKDEEKV 778
Cdd:PRK10252 836 --------ERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQ 907
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 779 LVSYfvpindnlegLISESDNPQDdeeveeeeenekdlkMEMLrgvrryrrlikdiREYLRKKLPSYAVPSVYFPLSKLP 858
Cdd:PRK10252 908 LVGY----------LVSQSGLPLD---------------TSAL-------------QAQLRERLPPHMVPVVLLQLDQLP 949
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 859 LNPNGKVDKPKLPFPDTslvpTVPTTDSTMLTPTQKTIHDIWLKLLPSPPNtiGMEEIFFDMGGHSILATRLIFEIRKTF 938
Cdd:PRK10252 950 LSANGKLDRKALPLPEL----KAQVPGRAPKTGTETIIAAAFSSLLGCDVV--DADADFFALGGHSLLAMKLAAQLSRQF 1023
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 589279984 939 VVNAPLGLVFDKPTIGGQAREVDSLRNEELTPAFDTVTPSRPTTKP 984
Cdd:PRK10252 1024 ARQVTPGQVMVASTVAKLATLLDAEEDESRRLGFGTILPLREGDGP 1069
|
|
| Lys2b |
COG3320 |
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ... |
1014-1266 |
3.50e-83 |
|
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: 273.62 E-value: 3.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1014 TVFLTGATGFLGGFILNDLLTNRSSRIkkvICLVRSSSLEKGQERLINSCTLLGIWNPSWLSenKLEIIIGDLSKPQFDL 1093
Cdd:COG3320 2 TVLLTGATGFLGAHLLRELLRRTDARV---YCLVRASDEAAARERLEALLERYGLWLELDAS--RVVVVAGDLTQPRLGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1094 SSKSWDYLSKETDAILHNGAIVHWVYPYEKLKPTNVLSTLECLKLCCQGGKmKSFTFVSSTSVLDtegfikksdeelQNG 1173
Cdd:COG3320 77 SEAEFQELAEEVDAIVHLAALVNLVAPYSELRAVNVLGTREVLRLAATGRL-KPFHYVSTIAVAG------------PAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1174 NDGLREDDDLEQGKkGLVTGYGQSKWVAEKLIMMAQNNGLRGWIVRPGYVMGDSKSAVTNTDDFIWRMVKGCLQLGLIPD 1253
Cdd:COG3320 144 RSGVFEEDDLDEGQ-GFANGYEQSKWVAEKLVREARERGLPVTIYRPGIVVGDSRTGETNKDDGFYRLLKGLLRLGAAPG 222
|
250
....*....|....
gi 589279984 1254 INNS-INLVPVDHV 1266
Cdd:COG3320 223 LGDArLNLVPVDYV 236
|
|
| NAD_binding_4 |
pfam07993 |
Male sterility protein; This family represents the C-terminal region of the male sterility ... |
1017-1266 |
6.05e-83 |
|
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: 272.56 E-value: 6.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1017 LTGATGFLGGFILNDLLTnRSSRIKKVICLVRSSSLEKGQERLINSCTLLGIWNPSWLSE-NKLEIIIGDLSKPQFDLSS 1095
Cdd:pfam07993 1 LTGATGFLGKVLLEKLLR-STPDVKKIYLLVRAKDGESALERLRQELEKYPLFDALLKEAlERIVPVAGDLSEPNLGLSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1096 KSWDYLSKETDAILHNGAIVHWVYPYEKLKPTNVLSTLECLKLCCQGGKMKSFTFVSsTSVLDTEGFIKKSDEELQNGND 1175
Cdd:pfam07993 80 EDFQELAEEVDVIIHSAATVNFVEPYDDARAVNVLGTREVLRLAKQGKQLKPFHHVS-TAYVNGERGGLVEEKPYPEGED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1176 GLREDDDLEQGKKGLVTGYGQSKWVAEKLIMMAQNNGLRGWIVRPGYVMGDSKSAVTNTDDFIWRMVKGCLQLGLIPDIN 1255
Cdd:pfam07993 159 DMLLDEDEPALLGGLPNGYTQTKWLAEQLVREAARRGLPVVIYRPSIITGEPKTGWINNFDFGPRGLLGGIGKGVLPSIL 238
|
250
....*....|....*
gi 589279984 1256 NS----INLVPVDHV 1266
Cdd:pfam07993 239 GDpdavLDLVPVDYV 253
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
317-871 |
4.16e-80 |
|
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: 271.43 E-value: 4.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 317 TFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPkGLLVI 396
Cdd:cd17652 12 TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARP-ALLLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 397 EkagelakivkdfikdkldlkilipsislssngkeeyqdilekyqnlsqtptgiilgPDSPATLSFTSGSTGIPKGVKGR 476
Cdd:cd17652 91 T--------------------------------------------------------PDNLAYVIYTSGSTGRPKGVVVT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 477 HYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRLAEWMDDCQVSVTHLTPAm 556
Cdd:cd17652 115 HRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPA- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 557 gqLLSAQATRQIPSLLNAFFVGDVltkrdCTR--LQHLAKNVCIINMYGTTETqravsyfaipsvnedsTFLSTQKDLIS 634
Cdd:cd17652 194 --ALAALPPDDLPDLRTLVVAGEA-----CPAelVDRWAPGRRMINAYGPTET----------------TVCATMAGPLP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 635 AGQG------MIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFGqdlkredtliGPAreh 707
Cdd:cd17652 251 GGGVppigrpVPGTRVYVLDARLRPVP--PGVPGELYIAGAGLARGYLNrPGLTAERFVADPFG----------APG--- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 708 wfgirDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPin 787
Cdd:cd17652 316 -----SRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVP-- 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 788 dnlegliseSDNPQDDEeveeeeenekdlkmemlrgvrryrrliKDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDK 867
Cdd:cd17652 389 ---------APGAAPTA---------------------------AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432
|
....
gi 589279984 868 PKLP 871
Cdd:cd17652 433 RALP 436
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
293-871 |
1.64e-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: 267.31 E-value: 1.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 293 PDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVV 372
Cdd:cd17649 1 PDAVALVFGDQS-------------LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 373 DPAYPPNRqIVYLevsnpkgllvIEKAGelAKIVkdfikdkldlkilipsislssngkeeyqdilekyqnLSQTPtgiil 452
Cdd:cd17649 68 DPEYPAER-LRYM----------LEDSG--AGLL------------------------------------LTHHP----- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 453 gpDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDI 532
Cdd:cd17649 94 --RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELW 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 533 GTPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQI----PSLLNAFFVGDVLTKRDCTRLQHLAknVCIINMYGTTETQ 608
Cdd:cd17649 172 ASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGdgrpPSLRLYIFGGEALSPELLRRWLKAP--VRLFNAYGPTEAT 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 609 RAVSYFAIPSVNEDstflstQKDLISAGQGMIDVQLLVVNrtDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVM 687
Cdd:cd17649 250 VTPLVWKCEAGAAR------AGASMPIGRPLGGRSAYILD--ADLNPVPVGVTGELYIGGEGLARGYLGrPELTAERFVP 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 688 NWFGqdlkredtliGPArehwfgirDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVREnVT 767
Cdd:cd17649 322 DPFG----------APG--------SRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVRE-AA 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 768 LVRRDKDEEKVLVSYFVPINDNLEGLISESdnpqddeeveeeeenekdlkmemlrgvrryrrlikdIREYLRKKLPSYAV 847
Cdd:cd17649 383 VVALDGAGGKQLVAYVVLRAAAAQPELRAQ------------------------------------LRTALRASLPDYMV 426
|
570 580
....*....|....*....|....
gi 589279984 848 PSVYFPLSKLPLNPNGKVDKPKLP 871
Cdd:cd17649 427 PAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
285-980 |
2.15e-78 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 288.01 E-value: 2.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 285 FSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILK 364
Cdd:PRK12316 2009 IAEQAARAPEAIAVVFGDQH-------------LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLK 2075
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 365 AGGVFSVVDPAYPPNRqIVYLEVSNPKGLLVIEKAgelakivkdfIKDKLDLKILIPSISLssngkeeyqDILEKYQNLS 444
Cdd:PRK12316 2076 AGGAYVPLDPNYPAER-LAYMLEDSGAALLLTQRH----------LLERLPLPAGVARLPL---------DRDAEWADYP 2135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 445 QTPTGIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAEL 524
Cdd:PRK12316 2136 DTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV 2215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 525 YVpTSDDIGTPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQ--IPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMY 602
Cdd:PRK12316 2216 LI-RDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDgrPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGY 2294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 603 GTTETQRAVSYF-AIPSVNEDSTFlstqkdlISAGQGMIDVQLLVVNRTdrLVPCAVGEMGEIYVRSGGLAEGYLD-PSA 680
Cdd:PRK12316 2295 GPTEAVVTPLLWkCRPQDPCGAAY-------VPIGRALGNRRAYILDAD--LNLLAPGMAGELYLGGEGLARGYLNrPGL 2365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 681 TAEKFVMNWFGqdlkredtligparehwfGIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHP 760
Cdd:PRK12316 2366 TAERFVPDPFS------------------ASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHP 2427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 761 LVRENVtLVRRDKDEEKVLVSYFVPindnleglisesDNPQDDeeveeeeenekdlkmemlrgvrryrrLIKDIREYLRK 840
Cdd:PRK12316 2428 AVREAV-VVAQDGASGKQLVAYVVP------------DDAAED--------------------------LLAELRAWLAA 2468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 841 KLPSYAVPSVYFPLSKLPLNPNGKVDKPKLPFPDTSLVPTVPTTDSTMLtptQKTIHDIWLKLLPSppNTIGMEEIFFDM 920
Cdd:PRK12316 2469 RLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGL---EQRLAAIWQAVLKV--EQVGLDDHFFEL 2543
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 921 GGHSILATRLIFEIRKTFVVNAPLGLVFDKPTIGGQAREVDSLRNEElTPAFDTVTPSRP 980
Cdd:PRK12316 2544 GGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSR-APVLQKVTRVQP 2602
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
289-870 |
3.07e-78 |
|
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: 266.42 E-value: 3.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 289 AKKYPDKLCViqseqtngiMEGPskgrKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGV 368
Cdd:cd05945 1 AAANPDRPAV---------VEGG----RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 369 FSVVDPAYPPNRQivylevsnpkgLLVIEKAGelakivkdfikdkldlkilipsislssngkeeyqdilekyqnlsqtPT 448
Cdd:cd05945 68 YVPLDASSPAERI-----------REILDAAK----------------------------------------------PA 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 449 GIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPT 528
Cdd:cd05945 91 LLIADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 529 SDDIGTPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATR---QIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTT 605
Cdd:cd05945 171 RDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFtpeSLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 606 ETQRAVSYFAIPsvNEDSTflstQKDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPSATAEK 684
Cdd:cd05945 251 EATVAVTYIEVT--PEVLD----GYDRLPIGYAKPGAKLVILDEDGRPVP--PGEKGELVISGPSVSKGYLnNPEKTAAA 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 685 FVMNWfGQdlkredtligparehwfgirdRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE 764
Cdd:cd05945 323 FFPDE-GQ---------------------RAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKE 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 765 NVTLVRRDKDEEKVLVSYFVPindnlegliSESDNPQddeeveeeeenekdlkmemlrgvrryrrLIKDIREYLRKKLPS 844
Cdd:cd05945 381 AVVVPKYKGEKVTELIAFVVP---------KPGAEAG----------------------------LTKAIKAELAERLPP 423
|
570 580
....*....|....*....|....*.
gi 589279984 845 YAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd05945 424 YMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
317-870 |
1.60e-77 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 264.92 E-value: 1.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 317 TFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPkGLLVI 396
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEP-ALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 397 EKAGElakivkdfikDKLDLKILIPSISLssngkeeyQDILEKYQNLSQTPTgiilgPDSPATLSFTSGSTGIPKGVKGR 476
Cdd:cd12116 91 DDALP----------DRLPAGLPVLLLAL--------AAAAAAPAAPRTPVS-----PDDLAYVIYTSGSTGRPKGVVVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 477 HYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRLAEWMDDCQVSVTHLTPAM 556
Cdd:cd12116 148 HRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPAT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 557 GQLLSAQATRQIPSLlNAFFVGDVLTKRDCTRLqhLAKNVCIINMYGTTETqravsyfaipsvnedsTFLSTQKDlISAG 636
Cdd:cd12116 228 WRMLLDAGWQGRAGL-TALCGGEALPPDLAARL--LSRVGSLWNLYGPTET----------------TIWSTAAR-VTAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 637 QGMIDV-------QLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFGQDlkredtligparehw 708
Cdd:cd12116 288 AGPIPIgrplantQVYVLDAALRPVP--PGVPGELYIGGDGVAQGYLGrPALTAERFVPDPFAGP--------------- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 709 fgiRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDkDEEKVLVSYFVPind 788
Cdd:cd12116 351 ---GSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVVL--- 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 789 nleglisESDNPQDdeeveeeeenekdlkmemlrgvrryrrlIKDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKP 868
Cdd:cd12116 424 -------KAGAAPD----------------------------AAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRK 468
|
..
gi 589279984 869 KL 870
Cdd:cd12116 469 AL 470
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
281-871 |
2.65e-76 |
|
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: 261.60 E-value: 2.65e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQ-------------LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPPNRqivylevsnpkgllviekageLAKIVKDfikdkldlkiliPSISLssngkeeyqdileky 440
Cdd:cd17644 69 AILKAGGAYVPLDPNYPQER---------------------LTYILED------------AQISV--------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 441 qnlsqtptgIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFL 520
Cdd:cd17644 101 ---------LLTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLS 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 521 GAELYVPTSDDIGTPGRLAEWMDDCQVSVTHLTPAMGQLLS---AQATRQIPSLLNAFFVG--DVLTKRDCTRLQHLAKN 595
Cdd:cd17644 172 GATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVlelLLSTIDLPSSLRLVIVGgeAVQPELVRQWQKNVGNF 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 596 VCIINMYGTTETQRAVSYFAIPSVNEDstflstQKDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGY 675
Cdd:cd17644 252 IQLINVYGPTEATIAATVCRLTQLTER------NITSVPIGRPIANTQVYILDENLQPVP--VGVPGELHIGGVGLARGY 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 676 LD-PSATAEKFVMNWFGQDLKredtligparehwfgirDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDT 754
Cdd:cd17644 324 LNrPELTAEKFISHPFNSSES-----------------ERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEA 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 755 HLSRHPLVRENVTLVRRDKDEEKVLVSYFVPiNDNLEGLISEsdnpqddeeveeeeenekdlkmemlrgvrryrrlikdI 834
Cdd:cd17644 387 VLSQHNDVKTAVVIVREDQPGNKRLVAYIVP-HYEESPSTVE-------------------------------------L 428
|
570 580 590
....*....|....*....|....*....|....*..
gi 589279984 835 REYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKLP 871
Cdd:cd17644 429 RQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
319-870 |
1.04e-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: 258.94 E-value: 1.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 319 TYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKgLLVIEk 398
Cdd:cd17650 14 TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAK-LLLTQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 399 agelakivkdfikdkldlkilipsislssngkeeyqdilekyqnlsqtptgiilgPDSPATLSFTSGSTGIPKGVKGRHY 478
Cdd:cd17650 92 -------------------------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 479 SLTH-FFPWmSKRFGLNEKS-KFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRLAEWMDDCQVSVTHLTPAM 556
Cdd:cd17650 117 NVAHaAHAW-RREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPAL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 557 GQLLSAQATRQ--IPSLLNAFFVG-DVLTKRD-CTRLQHLAKNVCIINMYGTTETQRAVSYFaipsvnEDSTFLSTQKDL 632
Cdd:cd17650 196 IRPVMAYVYRNglDLSAMRLLIVGsDGCKAQDfKTLAARFGQGMRIINSYGVTEATIDSTYY------EEGRDPLGDSAN 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 633 ISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPSATAEKFVMNWFGQDlkredtligparehwfgi 711
Cdd:cd17650 270 VPIGRPLPNTAMYVLDERLQPQP--VGVAGELYIGGAGVARGYLnRPELTAERFVENPFAPG------------------ 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 712 rDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPindnle 791
Cdd:cd17650 330 -ERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVA------ 402
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589279984 792 gliSESDNpqddeeveeeeenekdlkmemlrgvrryrrlIKDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd17650 403 ---AATLN-------------------------------TAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
16-988 |
3.96e-74 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 274.35 E-value: 3.96e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 16 ELKAKLDRWSERLS-ALPSLALPTDYPRPSPAKLVESFQTLPIPPSLTPALLRLTLEYSTlypssplpTPYHLLLTSFSI 94
Cdd:PRK05691 861 EAARQLAYWKAQLGdEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQA--------TLFMVLLAAFQA 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 95 LLFRYTPDPSLVLYPTVAVNSTPSTHPLL--------LKMELSPEMSFFEILHQV--LTQEIIATQDsVPLSTLVDHL-- 162
Cdd:PRK05691 933 LLHRYSGQGDIRIGVPNANRPRLETQGLVgffintqvLRAQLDGRLPFTALLAQVrqATLGAQAHQD-LPFEQLVEALpq 1011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 163 KPEGPLFRVRF----FDSTTLEMDPTTSLTTDLTLYLLA------QPTETPITRtsipsLYLRLVYNSLLFTQNRITSLL 232
Cdd:PRK05691 1012 AREQGLFQVMFnhqqRDLSALRRLPGLLAEELPWHSREAkfdlqlHSEEDRNGR-----LTLSFDYAAELFDAATIERLA 1086
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 233 ESLLQLLTSASEKSfNHPIGSLPIRTISQEKILpdptsdLNWCDFVGA-----IPDIFSANAKKYPDKLCVIqseqtngi 307
Cdd:PRK05691 1087 EHFLALLEQVCEDP-QRALGDVQLLDAAERAQL------AQWGQAPCApaqawLPELLNEQARQTPERIALV-------- 1151
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 308 MEGPSKGrktftYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRqIVYLEV 387
Cdd:PRK05691 1152 WDGGSLD-----YAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER-LAYMLA 1225
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 388 SNPKGLLVIEKAgelakivkdfIKDKLDLKILIPSISLssngkeeyqDILEkYQNLSQTPTGIILGPDSPATLSFTSGST 467
Cdd:PRK05691 1226 DSGVELLLTQSH----------LLERLPQAEGVSAIAL---------DSLH-LDSWPSQAPGLHLHGDNLAYVIYTSGST 1285
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 468 GIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRLAEWMDDCQV 547
Cdd:PRK05691 1286 GQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGV 1365
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 548 SVTHLTPAMGQL-----LSAQATrqipSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAVSYFAIPSvnED 622
Cdd:PRK05691 1366 TTLHFVPPLLQLfidepLAAACT----SLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQA--ED 1439
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 623 STFLSTQKDLisagqGMIDVQLLvvnrTDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFGQDlkredtli 701
Cdd:PRK05691 1440 GERSPIGRPL-----GNVLCRVL----DAELNLLPPGVAGELCIGGAGLARGYLGrPALTAERFVPDPLGED-------- 1502
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 702 gparehwfgiRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKvLVS 781
Cdd:PRK05691 1503 ----------GARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQ-LVG 1571
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 782 YFVpindnlegliseSDNPQDDEEVeeeeenekdlkmemlrgvrryrrlikDIREYLRKKLPSYAVPSVYFPLSKLPLNP 861
Cdd:PRK05691 1572 YYT------------GEAGQEAEAE--------------------------RLKAALAAELPEYMVPAQLIRLDQMPLGP 1613
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 862 NGKVDKPKLPFPDTSLVPTVPTTdstmlTPTQKTIHDIWLKLLPSPpnTIGMEEIFFDMGGHSILATRLIFEIRKTFVVN 941
Cdd:PRK05691 1614 SGKLDRRALPEPVWQQREHVEPR-----TELQQQIAAIWREVLGLP--RVGLRDDFFALGGHSLLATQIVSRTRQACDVE 1686
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|
gi 589279984 942 APLGLVFDKPTIGGQAREVDSLRNE---ELTPAFDTVTPSRPTtkPRSYS 988
Cdd:PRK05691 1687 LPLRALFEASELGAFAEQVARIQAAgerNSQGAIARVDRSQPV--PLSYS 1734
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
283-870 |
3.02e-73 |
|
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: 251.85 E-value: 3.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 283 DIFSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGI 362
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDES-------------LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 363 LKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLViekagelakivkdfikdkldlkilipsislssngkeeyqdilekyqn 442
Cdd:cd12115 70 LKAGAAYVPLDPAYPPERLRFILEDAQARLVLT----------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 443 lsqtptgiilGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEkskftmLSGI-AHDPIQRD-----MFT 516
Cdd:cd12115 103 ----------DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEE------LAGVlASTSICFDlsvfeLFG 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 517 PLFLGAELyVPTSDDIGTPGRLAEwmddCQVSVTHLTP-AMGQLLSAQATRQIPSLLNafFVGDVLTKRDCTRLQHLAKN 595
Cdd:cd12115 167 PLATGGKV-VLADNVLALPDLPAA----AEVTLINTVPsAAAELLRHDALPASVRVVN--LAGEPLPRDLVQRLYARLQV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 596 VCIINMYGTTETQRAVSYFAIPSVNEDStflstqkdlISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGY 675
Cdd:cd12115 240 ERVVNLYGPSEDTTYSTVAPVPPGASGE---------VSIGRPLANTQAYVLDRALQPVP--LGVPGELYIGGAGVARGY 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 676 L-DPSATAEKFVMNWFGQDLkredtligparehwfgirdRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDT 754
Cdd:cd12115 309 LgRPGLTAERFLPDPFGPGA-------------------RLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEA 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 755 HLSRHPLVRENVTLVRRDKDEEKVLVSYFVPinDNLEGLisesdnpqddeeveeeeenekdlkmemlrgvrryrrLIKDI 834
Cdd:cd12115 370 ALRSIPGVREAVVVAIGDAAGERRLVAYIVA--EPGAAG------------------------------------LVEDL 411
|
570 580 590
....*....|....*....|....*....|....*.
gi 589279984 835 REYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd12115 412 RRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
285-743 |
5.48e-73 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 250.31 E-value: 5.48e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 285 FSANAKKYPDKLCVIQSEQTngimegpskgrkTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILK 364
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGR------------RLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 365 AGGVFSVVDPAYPPNRQIVYLEVSNPKgLLVIEKAGELAKIVKdfIKDKLDLKILIPSISLSSNGKEEYQDILEKYQNLS 444
Cdd:pfam00501 69 AGAVYVPLNPRLPAEELAYILEDSGAK-VLITDDALKLEELLE--ALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 445 QTPTgIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSK----RFGLNEKSKFTMLSGIAHD-PIQRDMFTPLF 519
Cdd:pfam00501 146 PPPP-PPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDfGLSLGLLGPLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 520 LGAELYVPTSDDIGTPGRLAEWMDDCQVSVTHLTPAMGQLL---SAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNV 596
Cdd:pfam00501 225 AGATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLleaGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 597 cIINMYGTTETqravsyfaIPSVNEDSTFLSTQKDLISAGQGMIDVQLLVVNrTDRLVPCAVGEMGEIYVRSGGLAEGYL 676
Cdd:pfam00501 305 -LVNGYGLTET--------TGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVD-DETGEPVPPGEPGELCVRGPGVMKGYL 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589279984 677 -DPSATAEKFvmnwfgqdlkredtligparehwfgIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIR 743
Cdd:pfam00501 375 nDPELTAEAF-------------------------DEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
281-870 |
1.30e-70 |
|
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: 244.33 E-value: 1.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIQseqtngimegpskGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF-------------GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPPnRQIVY-LEVSNPKGLLViekagelakivkdfikdkldlkilipsislssngkeeyqdilek 439
Cdd:COG0318 68 AALRAGAVVVPLNPRLTA-EELAYiLEDSGARALVT-------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 440 yqnlsqtptgiilgpdspATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHD-PIQRDMFTPL 518
Cdd:COG0318 103 ------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 519 FLGAELYVPTSDDigtPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQ---IPSLLNAFFVGDVLTKRDCTRLQHLAkN 595
Cdd:COG0318 165 LAGATLVLLPRFD---PERVLELIERERVTVLFGVPTMLARLLRHPEFArydLSSLRLVVSGGAPLPPELLERFEERF-G 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 596 VCIINMYGTTETQRAVSYfaipsvnedSTFLSTQKDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGY 675
Cdd:COG0318 241 VRIVEGYGLTETSPVVTV---------NPEDPGERRPGSVGRPLPGVEVRIVDEDGRELP--PGEVGEIVVRGPNVMKGY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 676 L-DPSATAEKFvmnwfgqdlkredtligparehwfgiRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDT 754
Cdd:COG0318 310 WnDPEATAEAF--------------------------RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEE 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 755 HLSRHPLVRE-NVTLVRRDKDEEKVLVsYFVPindnlegliseSDNPQDDEeveeeeenekdlkmemlrgvrryrrliKD 833
Cdd:COG0318 364 VLAAHPGVAEaAVVGVPDEKWGERVVA-FVVL-----------RPGAELDA---------------------------EE 404
|
570 580 590
....*....|....*....|....*....|....*..
gi 589279984 834 IREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:COG0318 405 LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
317-871 |
1.04e-68 |
|
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: 240.07 E-value: 1.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 317 TFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKglLVI 396
Cdd:cd17656 13 KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVR--VVL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 397 EKAGELAKIVKDFIKDKLDLkiliPSISlssngKEEYQDILEKYQNlsqtptgiilgpDSPATLSFTSGSTGIPKGVKGR 476
Cdd:cd17656 91 TQRHLKSKLSFNKSTILLED----PSIS-----QEDTSNIDYINNS------------DDLLYIIYTSGTTGKPKGVQLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 477 HYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDIGTPGRLAEWMDDCQVSVTHLTPAM 556
Cdd:cd17656 150 HKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 557 GQLLSA--QATRQIPSLL-NAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAVSYFAIPSVNedstflstQKDLI 633
Cdd:cd17656 230 LKFIFSerEFINRFPTCVkHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTTYTINPEAE--------IPELP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 634 SAGQGMIDVQLLVVNRTDRLVPCavGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFGQDlkredtligparehwfgir 712
Cdd:cd17656 302 PIGKPISNTWIYILDQEQQLQPQ--GIVGELYISGASVARGYLNrQELTAEKFFPDPFDPN------------------- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 713 DRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPINdnleg 792
Cdd:cd17656 361 ERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQ----- 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589279984 793 lisesdnpqddeeveeeeenekdlkmemlrgvrryRRLIKDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKLP 871
Cdd:cd17656 436 -----------------------------------ELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
293-867 |
2.72e-68 |
|
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: 238.71 E-value: 2.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 293 PDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVV 372
Cdd:cd12114 1 PDATAVICGDGT-------------LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 373 DPAYPPNRQIVYLEVSNPKGLLVIEKAGELAKIVKDFIKDKLDLkilipsislssngkeeyqdilekyQNLSQTPTGIIL 452
Cdd:cd12114 68 DIDQPAARREAILADAGARLVLTDGPDAQLDVAVFDVLILDLDA------------------------LAAPAPPPPVDV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 453 GPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDI 532
Cdd:cd12114 124 APDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 533 GTPGRLAEWMDDCQVSVTHLTPAMGQLL---SAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQR 609
Cdd:cd12114 204 RDPAHWAELIERHGVTLWNSVPALLEMLldvLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 610 AVSYFAIPSVNED--StflstqkdlISAGQGMIDVQLLVVNRTDRlvPCAVGEMGEIYVRSGGLAEGYL-DPSATAEKFV 686
Cdd:cd12114 284 WSIYHPIDEVPPDwrS---------IPYGRPLANQRYRVLDPRGR--DCPDWVPGELWIGGRGVALGYLgDPELTAARFV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 687 mnwfgQDLKREdtligparehwfgirdRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENV 766
Cdd:cd12114 353 -----THPDGE----------------RLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAV 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 767 TLVRRDkDEEKVLVSYFVPINDNlEGLISESdnpqddeeveeeeenekdlkmemlrgvrryrrlikdIREYLRKKLPSYA 846
Cdd:cd12114 412 VVVLGD-PGGKRLAAFVVPDNDG-TPIAPDA------------------------------------LRAFLAQTLPAYM 453
|
570 580
....*....|....*....|.
gi 589279984 847 VPSVYFPLSKLPLNPNGKVDK 867
Cdd:cd12114 454 IPSRVIALEALPLTANGKVDR 474
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
284-871 |
3.16e-66 |
|
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: 231.29 E-value: 3.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 284 IFSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGIL 363
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQS-------------LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 364 KAGGVFSVVDPAYPPNRQIVYLEVSNPKglLVIEKAGELAKIVkdfikdkldlkilipsislssngkeeyqdilekyqnl 443
Cdd:cd17645 70 KAGGAYVPIDPDYPGERIAYMLADSSAK--ILLTNPDDLAYVI------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 444 sqtptgiilgpdspatlsFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAE 523
Cdd:cd17645 111 ------------------YTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 524 LYVPTSDDIGTPGRLAEWMDDCQVSVTHL-TPAMGQLLSAQATrqipSLLNAFFVGDVLTKRDctrlqhlAKNVCIINMY 602
Cdd:cd17645 173 LHVVPSERRLDLDALNDYFNQEGITISFLpTGAAEQFMQLDNQ----SLRVLLTGGDKLKKIE-------RKGYKLVNNY 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 603 GTTETQRAVSYFAIpsvneDSTFLStqkdlISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYLD-PSAT 681
Cdd:cd17645 242 GPTENTVVATSFEI-----DKPYAN-----IPIGKPIDNTRVYILDEALQLQP--IGVAGELCIAGEGLARGYLNrPELT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 682 AEKFVMNWFGQDlkredtligparehwfgirDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPL 761
Cdd:cd17645 310 AEKFIVHPFVPG-------------------ERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPL 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 762 VRENVTLVRRDKDEEKVLVSYFVPindnleglisESDNPqddeeveeeeenekdlkmemlrgvrryrrlIKDIREYLRKK 841
Cdd:cd17645 371 IELAAVLAKEDADGRKYLVAYVTA----------PEEIP------------------------------HEELREWLKND 410
|
570 580 590
....*....|....*....|....*....|
gi 589279984 842 LPSYAVPSVYFPLSKLPLNPNGKVDKPKLP 871
Cdd:cd17645 411 LPDYMIPTYFVHLKALPLTANGKVDRKALP 440
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
283-870 |
2.07e-65 |
|
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: 228.73 E-value: 2.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 283 DIFSANAKKYPDKLCViqseqtngimEGPSKgrkTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGI 362
Cdd:cd17653 1 DAFERIAAAHPDAVAV----------ESLGG---SLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 363 LKAGGVFSVVDPAYPPNRQIVYLEVSNPKgllviekagelakivkdfikdkldlkILIPSISlssngkeeyqdilekyqn 442
Cdd:cd17653 68 LKAGAAYVPLDAKLPSARIQAILRTSGAT--------------------------LLLTTDS------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 443 lsqtptgiilgPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGA 522
Cdd:cd17653 104 -----------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGG 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 523 ELYVPTSDDigtpgrlaEWMDDCQ-VSVTHLTPAMGQLLSAQatrQIPSLLNAFFVGDVLTKrdcTRLQHLAKNVCIINM 601
Cdd:cd17653 173 TLVLADPSD--------PFAHVARtVDALMSTPSILSTLSPQ---DFPNLKTIFLGGEAVPP---SLLDRWSPGRRLYNA 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 602 YGTTETQRAVSYFAI-PSVNedstflstqkdlISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPS 679
Cdd:cd17653 239 YGPTECTISSTMTELlPGQP------------VTIGKPIPNSTCYILDADLQPVP--EGVVGEICISGVQVARGYLgNPA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 680 ATAEKFVMNWFgqdlkredtligparehWFGirDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEI-DTHLSR 758
Cdd:cd17653 305 LTASKFVPDPF-----------------WPG--SRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIeEVVLQS 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 759 HPLVRENVTLVRRDkdeekVLVSYFVPINDNLEGLisesdnpqddeeveeeeenekdlkmemlrgvrryrrlikdiREYL 838
Cdd:cd17653 366 QPEVTQAAAIVVNG-----RLVAFVTPETVDVDGL-----------------------------------------RSEL 399
|
570 580 590
....*....|....*....|....*....|..
gi 589279984 839 RKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd17653 400 AKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
293-871 |
9.83e-65 |
|
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: 227.67 E-value: 9.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 293 PDKLCVIQseqtngimegpskGRKTFTYGQIDKASNVIAHCLIQNG-LKKEEVVMVYAARSVEMVVCVMGILKAGGVFSV 371
Cdd:cd17648 1 PDRVAVVY-------------GDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 372 VDPAYPPNRqiVYLEVSNPKGLLVIEKAGELAKIVkdfikdkldlkilipsislssngkeeyqdilekyqnlsqtptgii 451
Cdd:cd17648 68 IDPSYPDER--IQFILEDTGARVVITNSTDLAYAI--------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 452 lgpdspatlsFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGL--NEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTS 529
Cdd:cd17648 101 ----------YTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGrdNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPD 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 530 DDIGTPGRLAEWMDDCQVSVTHLTPAmgqLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNVcIINMYGTTETqr 609
Cdd:cd17648 171 EMRFDPDRFYAYINREKVTYLSGTPS---VLQQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGL-IINAYGPTET-- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 610 avsyfAIPSVNedSTFLSTQKDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMN 688
Cdd:cd17648 245 -----TVTNHK--RFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVP--VGAVGELYLGGDGVARGYLNrPELTAERFLPN 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 689 WFGQDLKREDtligparehwfGIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTL 768
Cdd:cd17648 316 PFQTEQERAR-----------GRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVV 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 769 VRRDKD-----EEKVLVSYFVPIndnlEGLISESdnpqddeeveeeeenekdlkmemlrgvrryrrlikDIREYLRKKLP 843
Cdd:cd17648 385 AKEDASqaqsrIQKYLVGYYLPE----PGHVPES-----------------------------------DLLSFLRAKLP 425
|
570 580
....*....|....*....|....*...
gi 589279984 844 SYAVPSVYFPLSKLPLNPNGKVDKPKLP 871
Cdd:cd17648 426 RYMVPARLVRLEGIPVTINGKLDVRALP 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
14-936 |
3.35e-62 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 235.83 E-value: 3.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 14 ASELKAKLDRWSERL-SALPSLALPTDYPRPSpaklVESFQ----TLPIPPSLTPALLRLTLEYSTlypssplpTPYHLL 88
Cdd:PRK05691 1912 SGERQRQLDYWKAQLgNEHPLLELPADRPRPP----VQSHRgelyRFDLSPELAARVRAFNAQRGL--------TLFMTM 1979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 89 LTSFSILLFRYTPDPSLVLYPTVAVNSTPSTHPLL--------LKMELSPEMSFFEILHQVlTQEIIATQ--DSVPLSTL 158
Cdd:PRK05691 1980 TATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIgaflntqvLRCQLDGQMSVSELLEQV-RQTVIEGQshQDLPFDHL 2058
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 159 VDHLKPE-----GPLFRV-------RFFDSTTLemdpttslttdltlyllAQPTETPIT---RTSIPSLYLR-------- 215
Cdd:PRK05691 2059 VEALQPPrsaayNPLFQVmcnvqrwEFQQSRQL-----------------AGMTVEYLVndaRATKFDLNLEvtdldgrl 2121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 216 ---LVYNSLLFTQNRITSLLESLLQLLtsasEKSFNHP---IGSLPIRTISQEKILPDPTS------DLNWCdfvgaIPD 283
Cdd:PRK05691 2122 gccLTYSRDLFDEPRIARMAEHWQNLL----EALLGDPqqrLAELPLLAAAEQQQLLDSLAgeageaRLDQT-----LHG 2192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 284 IFSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGIL 363
Cdd:PRK05691 2193 LFAAQAARTPQAPALTFAGQT-------------LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAIL 2259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 364 KAGGVFSVVDPAYPPNRQIVYLEVSNpKGLLVIEKA-----GELAKIVKDFikdkldlkilipsiSLssngkEEYQDILE 438
Cdd:PRK05691 2260 KAGGAYVPLDPEYPLERLHYMIEDSG-IGLLLSDRAlfealGELPAGVARW--------------CL-----EDDAAALA 2319
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 439 KYqnlSQTPTGIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPL 518
Cdd:PRK05691 2320 AY---SDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPL 2396
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 519 FLGAELYVPTSDDIGTPgRLAEWMDDCQVSVTHLTPAMG----QLLSAQAtRQIPSLLnAFFVGDVLTKRDCTRLQHLAK 594
Cdd:PRK05691 2397 LCGARVVLRAQGQWGAE-EICQLIREQQVSILGFTPSYGsqlaQWLAGQG-EQLPVRM-CITGGEALTGEHLQRIRQAFA 2473
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 595 NVCIINMYGTTETqrAVSYFAIPSvnedstflstqKDLISAGQGMIDVQLLVVNRT-----DRLVPCAVGEMGEIYVRSG 669
Cdd:PRK05691 2474 PQLFFNAYGPTET--VVMPLACLA-----------PEQLEEGAASVPIGRVVGARVayildADLALVPQGATGELYVGGA 2540
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 670 GLAEGYLD-PSATAEKFVMNWFGQDlkredtligparehwfgiRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIE 748
Cdd:PRK05691 2541 GLAQGYHDrPGLTAERFVADPFAAD------------------GGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIE 2602
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 749 LGEIDTHLSRHPLVRENVTLVRrDKDEEKVLVSYFVpindnleGLISESDNPQDDeeveeeeenekdlkmemlrgvrryr 828
Cdd:PRK05691 2603 LGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLV-------SAVAGQDDEAQA------------------------- 2649
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 829 RLIKDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKLPFPDTSLVPTVPTTDSTMLtptQKTIHDIWLKLLPSpp 908
Cdd:PRK05691 2650 ALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSEL---EQQLAQIWREVLNV-- 2724
|
970 980
....*....|....*....|....*...
gi 589279984 909 NTIGMEEIFFDMGGHSILATRLIFEIRK 936
Cdd:PRK05691 2725 ERVGLGDNFFELGGDSILSIQVVSRARQ 2752
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
318-969 |
1.46e-59 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 227.36 E-value: 1.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 318 FTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLVIE 397
Cdd:PRK05691 3746 WSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSA 3825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 398 KAGELAKIVKDFIKDKLDLKILIpsislssngKEEYQdilekYQNLSQTPTGIILGPDSPATLSFTSGSTGIPKGVkgrh 477
Cdd:PRK05691 3826 ACREQARALLDELGCANRPRLLV---------WEEVQ-----AGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGV---- 3887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 478 yslthffpwMSKRFGL--NEKSKFTMLSGIAHDPIQR------DMFTPLFLGAELY------VPtsDDIG-TPGRLAEWM 542
Cdd:PRK05691 3888 ---------MVEQRGMlnNQLSKVPYLALSEADVIAQtasqsfDISVWQFLAAPLFgarveiVP--NAIAhDPQGLLAHV 3956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 543 DDCQVSVTHLTPAMGQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAVSYFAIPSVned 622
Cdd:PRK05691 3957 QAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLA--- 4033
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 623 stflSTQKDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPSATAEKFVMNWFGqdlkredtli 701
Cdd:PRK05691 4034 ----STRGSYLPIGSPTDNNRLYLLDEALELVP--LGAVGELCVAGTGVGRGYVgDPLRTALAFVPHPFG---------- 4097
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 702 gparehwfGIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVrRDKDEEKVLVS 781
Cdd:PRK05691 4098 --------APGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAV-QEGVNGKHLVG 4168
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 782 YFVPindnlegliseSDNPQDDEEveeeeenekdlkmemlrgvrryrrLIKDIREYLRKKLPSYAVPSVYFPLSKLPLNP 861
Cdd:PRK05691 4169 YLVP-----------HQTVLAQGA------------------------LLERIKQRLRAELPDYMVPLHWLWLDRLPLNA 4213
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 862 NGKVDKPKLPFPDTSLVptvptTDSTMLTPT---QKTIHDIWLKLLPSppNTIGMEEIFFDMGGHSILATRLIFEIRKTF 938
Cdd:PRK05691 4214 NGKLDRKALPALDIGQL-----QSQAYLAPRnelEQTLATIWADVLKV--ERVGVHDNFFELGGHSLLATQIASRVQKAL 4286
|
650 660 670
....*....|....*....|....*....|.
gi 589279984 939 VVNAPLGLVFDKPTIGGQAREVDSLRNEELT 969
Cdd:PRK05691 4287 QRNVPLRAMFECSTVEELAEYIEGLAGSAID 4317
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
289-870 |
2.79e-50 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 186.64 E-value: 2.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 289 AKKYPDKLCVIQSEQTNgimegpskgrktfTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGV 368
Cdd:PRK04813 12 AQTQPDFPAYDYLGEKL-------------TYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 369 FSVVDPAYPPNRQIVYLEVSNPKGLLVIEkagelakivkDFIKDKLDLKILIPsislssngkEEYQDILEKyqNLSQTPT 448
Cdd:PRK04813 79 YIPVDVSSPAERIEMIIEVAKPSLIIATE----------ELPLEILGIPVITL---------DELKDIFAT--GNPYDFD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 449 GIILGPDSPATLsFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFtmlsgIAHDPIQRDM-----FTPLFLGAE 523
Cdd:PRK04813 138 HAVKGDDNYYII-FTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQF-----LNQAPYSFDLsvmdlYPTLASGGT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 524 LYVPTSDDIGTPGRLAEWMDDCQVSVTHLTPA---MGQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIIN 600
Cdd:PRK04813 212 LVALPKDMTANFKQLFETLPQLPINVWVSTPSfadMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 601 MYGTTETQRAVSyfAIPSVNEdstfLSTQKDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPS 679
Cdd:PRK04813 292 TYGPTEATVAVT--SIEITDE----MLDQYKRLPIGYAKPDSPLLIIDEEGTKLP--DGEQGEIVISGPSVSKGYLnNPE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 680 ATAEKFVMnwfgqdlkrEDTLigparehwfgirdRMYRSGDLGrYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRH 759
Cdd:PRK04813 364 KTAEAFFT---------FDGQ-------------PAYHTGDAG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQS 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 760 PLVRENVTlVRRDKDeEKV--LVSYFVPINDNLEglisesdnpqddeeveeeeeneKDLKmemlrgvrryrrLIKDIREY 837
Cdd:PRK04813 421 SYVESAVV-VPYNKD-HKVqyLIAYVVPKEEDFE----------------------REFE------------LTKAIKKE 464
|
570 580 590
....*....|....*....|....*....|...
gi 589279984 838 LRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:PRK04813 465 LKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
457-866 |
8.90e-49 |
|
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: 177.48 E-value: 8.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 457 PATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDigtPG 536
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFD---PE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 537 RLAEWMDDCQVSVTHLTPAMGQLL---SAQATRQIPSLLNAFFVGDVLTKRDCTRLqHLAKNVCIINMYGTTETQRAVSY 613
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLlkaPESAGYDLSSLRALVSGGAPLPPELLERF-EEAPGIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 614 FAIPSVNEDSTflstqkdliSAGQGMIDVQLLVVNRTDRlvPCAVGEMGEIYVRSGGLAEGYLDPSATAEKFvmnwfgqd 693
Cdd:cd04433 158 GPPDDDARKPG---------SVGRPVPGVEVRIVDPDGG--ELPPGEIGELVVRGPSVMKGYWNNPEATAAV-------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 694 lkredtligparehwfgIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDK 773
Cdd:cd04433 219 -----------------DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 774 DEEKVLVSYFVPinDNLEGLISEsdnpqddeeveeeeenekdlkmemlrgvrryrrlikDIREYLRKKLPSYAVPSVYFP 853
Cdd:cd04433 282 EWGERVVAVVVL--RPGADLDAE------------------------------------ELRAHVRERLAPYKVPRRVVF 323
|
410
....*....|...
gi 589279984 854 LSKLPLNPNGKVD 866
Cdd:cd04433 324 VDALPRTASGKID 336
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
316-865 |
7.06e-41 |
|
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: 158.53 E-value: 7.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 316 KTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPnRQIVY-LEVSNPKGLL 394
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTA-DELAHqLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 395 V----IEKAGELAKIVKDFIK-----DKLDLKILIPSISLSSNGKEEYQDILEKyqnlsqtptgiILGPDSPATLSFTSG 465
Cdd:cd05911 88 TdpdgLEKVKEAAKELGPKDKiivldDKPDGVLSIEDLLSPTLGEEDEDLPPPL-----------KDGKDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 466 STGIPKGVKGRHYSLT--HFFPWMSkrFGLNEKSKFTMLsgiahdpiqrdMFTPLF-------------LGAELYVPTSD 530
Cdd:cd05911 157 TTGLPKGVCLSHRNLIanLSQVQTF--LYGNDGSNDVIL-----------GFLPLYhiyglfttlasllNGATVIIMPKF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 531 DIgtpgrlAEWMDDCQ---VSVTHLTPAMGQLL--SAQATR-QIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGT 604
Cdd:cd05911 224 DS------ELFLDLIEkykITFLYLVPPIAAALakSPLLDKyDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 605 TETQRAVSYfaIPSVNEDSTflstqkdliSAGQGMIDVQLLVVNRTDRLVpCAVGEMGEIYVRSGGLAEGYL-DPSATAE 683
Cdd:cd05911 298 TETGGILTV--NPDGDDKPG---------SVGRLLPNVEAKIVDDDGKDS-LGPNEPGEICVRGPQVMKGYYnNPEATKE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 684 KFvmnwfgqdlkredtligpAREHWFgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVR 763
Cdd:cd05911 366 TF------------------DEDGWL-------HTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVA 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 764 EnvtlvrrdkdeekVLVsyfVPINDNLEG-----LISESDNPQDDEeveeeeenekdlkmemlrgvrryrrliKDIREYL 838
Cdd:cd05911 421 D-------------AAV---IGIPDEVSGelpraYVVRKPGEKLTE---------------------------KEVKDYV 457
|
570 580
....*....|....*....|....*....
gi 589279984 839 RKKLPSYA--VPSVYFpLSKLPLNPNGKV 865
Cdd:cd05911 458 AKKVASYKqlRGGVVF-VDEIPKSASGKI 485
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
281-870 |
2.34e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 151.88 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCViqseqtngimegpSKGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:PRK06187 8 IGRILRHGARKHPDKEAV-------------YFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPPNrQIVY-LEVSNPKGLLViekAGELAKIVKDfIKDKLDL--KILI---PSISLSSNGKEEYQ 434
Cdd:PRK06187 75 AVPKIGAVLHPINIRLKPE-EIAYiLNDAEDRVVLV---DSEFVPLLAA-ILPQLPTvrTVIVegdGPAAPLAPEVGEYE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 435 DILEkyqNLSQTPTGIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKF--------TMLSGIa 506
Cdd:PRK06187 150 ELLA---AASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYlvivpmfhVHAWGL- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 507 hdpiqrdMFTPLFLGAELYVPTSDDigtPGRLAEWMDDCQVSVTHLTPAMGQ-LLSAQATRQI----------------P 569
Cdd:PRK06187 226 -------PYLALMAGAKQVIPRRFD---PENLLDLIETERVTFFFAVPTIWQmLLKAPRAYFVdfsslrlviyggaalpP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 570 SLLNAFfvgdvLTKRDCTrlqhlaknvcIINMYGTTETQRAVSyFAIPsvnEDSTFLSTQKdLISAGQGMIDVQLLVVNR 649
Cdd:PRK06187 296 ALLREF-----KEKFGID----------LVQGYGMTETSPVVS-VLPP---EDQLPGQWTK-RRSAGRPLPGVEARIVDD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 650 TDRLVPCAVGEMGEIYVRSGGLAEGYL-DPSATAEKFVMNWfgqdlkredtligparehwfgirdrmYRSGDLGRYLPDG 728
Cdd:PRK06187 356 DGDELPPDGGEVGEIIVRGPWLMQGYWnRPEATAETIDGGW--------------------------LHTGDVGYIDEDG 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 729 NVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVREN-VTLVRRDKDEEKVLVsyFVPINDNLEglISEsdnpqddeeve 807
Cdd:PRK06187 410 YLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVaVIGVPDEKWGERPVA--VVVLKPGAT--LDA----------- 474
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589279984 808 eeeenekdlkmemlrgvrryrrliKDIREYLRKKLPSYAVP-SVYFpLSKLPLNPNGKVDKPKL 870
Cdd:PRK06187 475 ------------------------KELRAFLRGRLAKFKLPkRIAF-VDELPRTSVGKILKRVL 513
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
272-865 |
5.07e-36 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 145.64 E-value: 5.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 272 LNWCDfvgaipDIFSANAKKYPDKLCVIqseqtngiMEGPSKGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAAR 351
Cdd:COG0365 8 LNIAY------NCLDRHAEGRGDKVALI--------WEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 352 SVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPK------GLLVIEKAGELAKIVKDFIKD--KLDLKILIP-- 421
Cdd:COG0365 74 IPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKvlitadGGLRGGKVIDLKEKVDEALEElpSLEHVIVVGrt 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 422 SISLSSNGKEEYQDILEkyqNLSQTPTGIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKR-FGLNEKSKF- 499
Cdd:COG0365 154 GADVPMEGDLDWDELLA---AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFw 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 500 --------TMLSGIahdpiqrdMFTPLFLGAE--LY--VPTSDDigtPGRLAEWMDDCQVSVTHLTPAMgqllsaqatrq 567
Cdd:COG0365 231 ctadigwaTGHSYI--------VYGPLLNGATvvLYegRPDFPD---PGRLWELIEKYGVTVFFTAPTA----------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 568 IPSLLNAffVGDVLTKRDCTRLQHL-----------------AKNVCIINMYGTTETqraVSYFAIPSVNEDSTFLSTQK 630
Cdd:COG0365 289 IRALMKA--GDEPLKKYDLSSLRLLgsageplnpevwewwyeAVGVPIVDGWGQTET---GGIFISNLPGLPVKPGSMGK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 631 dlisAGQGMiDVQllVVNRTDRlvPCAVGEMGEIYVRSG--GLAEGYL-DPSATAEKFvmnwfgqdlkredtligpareh 707
Cdd:COG0365 364 ----PVPGY-DVA--VVDEDGN--PVPPGEEGELVIKGPwpGMFRGYWnDPERYRETY---------------------- 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 708 wFGIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVREnvtlvrrdkdeekVLVsyfVPIN 787
Cdd:COG0365 413 -FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAE-------------AAV---VGVP 475
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 788 DnleglisesdnpqddeeveeeeenekDLKMEM------LR-GVRRYRRLIKDIREYLRKKLPSYAVPSVYFPLSKLPLN 860
Cdd:COG0365 476 D--------------------------EIRGQVvkafvvLKpGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKT 529
|
....*
gi 589279984 861 PNGKV 865
Cdd:COG0365 530 RSGKI 534
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
288-867 |
1.60e-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: 132.35 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 288 NAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGG 367
Cdd:cd17631 4 RARRHPDRTALVFGGRS-------------LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 368 VFSvvdpayPPNRQIvylevsnpkgllvieKAGELAKIVKDFikdklDLKILIpsislssngkeeyqdilekyqnlsqtp 447
Cdd:cd17631 71 VFV------PLNFRL---------------TPPEVAYILADS-----GAKVLF--------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 448 tgiilgpDSPATLSFTSGSTGIPKGVKGRHYSLThffpWMSKR----FGLNEKSKFTMLSGIAHDPiQRDMFTP--LFLG 521
Cdd:cd17631 98 -------DDLALLMYTSGTTGRPKGAMLTHRNLL----WNAVNalaaLDLGPDDVLLVVAPLFHIG-GLGVFTLptLLRG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 522 AELYVPTSDDigtPGRLAEWMDDCQVSVTHLTPAMGQLLSA--QATRQIPSLLNAFFVGD----VLTKRDCtrlqhLAKN 595
Cdd:cd17631 166 GTVVILRKFD---PETVLDLIERHRVTSFFLVPTMIQALLQhpRFATTDLSSLRAVIYGGapmpERLLRAL-----QARG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 596 VCIINMYGTTETQRAVsyfaipsvnedsTFLS---TQKDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLA 672
Cdd:cd17631 238 VKFVQGYGMTETSPGV------------TFLSpedHRRKLGSAGRPVFFVEVRIVDPDGREVP--PGEVGEIVVRGPHVM 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 673 EGYLD-PSATAEKFVMNWFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGE 751
Cdd:cd17631 304 AGYWNrPEATAAAFRDGWF--------------------------HTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAE 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 752 IDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPindnleglisESDNPQDDeeveeeeenekdlkmemlrgvrryrrli 831
Cdd:cd17631 358 VEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVP----------RPGAELDE---------------------------- 399
|
570 580 590
....*....|....*....|....*....|....*.
gi 589279984 832 KDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDK 867
Cdd:cd17631 400 DELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| MupV_like_SDR_e |
cd05263 |
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ... |
1015-1266 |
3.42e-30 |
|
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: 122.09 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1015 VFLTGATGFLGGFILNDLLtnrsSRIKKVICLVRSSSLEKGQERLinscTLLGIWNPswlsenKLEIIIGDLSKPQFDLS 1094
Cdd:cd05263 1 VFVTGGTGFLGRHLVKRLL----ENGFKVLVLVRSESLGEAHERI----EEAGLEAD------RVRVLEGDLTQPNLGLS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1095 SKSWDYLSKETDAILHNGAIVHWVYPYEKLKPTNVLSTLECLKLCCQGGKmKSFTFVSSTSVldtegfikksdeelqngn 1174
Cdd:cd05263 67 AAASRELAGKVDHVIHCAASYDFQAPNEDAWRTNIDGTEHVLELAARLDI-QRFHYVSTAYV------------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1175 DGLRED----DDLEQGkKGLVTGYGQSKWVAEKLIMMAQNNgLRGWIVRPGYVMGDSKSAVTNTDDFIWRMVKGCLQLGL 1250
Cdd:cd05263 128 AGNREGnireTELNPG-QNFKNPYEQSKAEAEQLVRAAATQ-IPLTVYRPSIVVGDSKTGRIEKIDGLYELLNLLAKLGR 205
|
250 260
....*....|....*....|
gi 589279984 1251 IP----DINNSINLVPVDHV 1266
Cdd:cd05263 206 WLpmpgNKGARLNLVPVDYV 225
|
|
| FAR-N_SDR_e |
cd05236 |
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ... |
1014-1266 |
5.74e-26 |
|
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: 110.47 E-value: 5.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1014 TVFLTGATGFLGGFILNDLLTNrSSRIKKVICLVRSSSLEKGQERL---INSCTLLGIWNPSWLSENKLEIIIGDLSKPQ 1090
Cdd:cd05236 2 SVLITGATGFLGKVLLEKLLRS-CPDIGKIYLLIRGKSGQSAEERLrelLKDKLFDRGRNLNPLFESKIVPIEGDLSEPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1091 FDLSSKSWDYLSKETDAILHNGAIVHWVYPYEKLKPTNVLSTLECLKLCCQGGKMKSFTFVSSTSVldtEGFIKKSDEEL 1170
Cdd:cd05236 81 LGLSDEDLQTLIEEVNIIIHCAATVTFDERLDEALSINVLGTLRLLELAKRCKKLKAFVHVSTAYV---NGDRQLIEEKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1171 QNGNDGLRED-------DDLEQGKKGLVTGYGQ------SKWVAEkLIMMAQNNGLRGWIVRPGYVMGDSKSAVTNTDDF 1237
Cdd:cd05236 158 YPPPADPEKLidilelmDDLELERATPKLLGGHpntytfTKALAE-RLVLKERGNLPLVIVRPSIVGATLKEPFPGWIDN 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 589279984 1238 iWRMVKG---CLQLGLIPDINNSIN----LVPVDHV 1266
Cdd:cd05236 237 -FNGPDGlflAYGKGILRTMNADPNavadIIPVDVV 271
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
266-795 |
3.02e-25 |
|
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: 111.99 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 266 PDPTSDLNWcdfvGAIPDIFSANAKKYPDKLCViqSEQTNGIMEgpskgrkTFTYGQ-IDKASNvIAHCLIQNGLKKEEV 344
Cdd:cd05906 1 PLHRPEGAP----RTLLELLLRAAERGPTKGIT--YIDADGSEE-------FQSYQDlLEDARR-LAAGLRQLGLRPGDS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 345 VMVYAARSVEMVVCVMGILKAGGV--FSVVDPAYP-PNRQIVYLE-----VSNPKGLLVIEKAGELAKIVKDFikdkldl 416
Cdd:cd05906 67 VILQFDDNEDFIPAFWACVLAGFVpaPLTVPPTYDePNARLRKLRhiwqlLGSPVVLTDAELVAEFAGLETLS------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 417 kiLIPSISLSSngkeeyQDILEKYQNLSQTPtgiILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEK 496
Cdd:cd05906 140 --GLPGIRVLS------IEELLDTAADHDLP---QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 497 SKFtmLS--------GIAHDPIQrdmftPLFLGAE-LYVPTSDDIGTPGRLAEWMDDCQVSVThLTPAMGQLLSAQATRQ 567
Cdd:cd05906 209 DVF--LNwvpldhvgGLVELHLR-----AVYLGCQqVHVPTEEILADPLRWLDLIDRYRVTIT-WAPNFAFALLNDLLEE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 568 IPS----------LLNAFFVGDVLTKRDCTRL--QHLAKNVCIINMYGTTETQRAVSY---FAIPSVNEDSTFLSTqkdl 632
Cdd:cd05906 281 IEDgtwdlsslryLVNAGEAVVAKTIRRLLRLlePYGLPPDAIRPAFGMTETCSGVIYsrsFPTYDHSQALEFVSL---- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 633 isaGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPSATAEKFvmnwfgqdlkREDTligparehWFgi 711
Cdd:cd05906 357 ---GRPIPGVSMRIVDDEGQLLP--EGEVGRLQVRGPVVTKGYYnNPEANAEAF----------TEDG--------WF-- 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 712 rdrmyRSGDLGrYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTL---VRRDKDEEKVLVSYFVPIND 788
Cdd:cd05906 412 -----RTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAafaVRDPGAETEELAIFFVPEYD 485
|
....*..
gi 589279984 789 NLEGLIS 795
Cdd:cd05906 486 LQDALSE 492
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
318-871 |
7.25e-24 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 106.22 E-value: 7.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 318 FTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYppnrqivylevsnpkgllvie 397
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTAL--------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 398 KAGELAKIVkdfikDKLDLKILIPSislssngkeeyqdilekyqnlsqtptgiilgpdsPATLSFTSGSTGIPKGVKGRH 477
Cdd:cd05934 63 RGDELAYII-----DHSGAQLVVVD----------------------------------PASILYTSGTTGPPKGVVITH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 478 YSLTHFFPWMSKRFGLNEKskftmlsgiahDPIQRDMftPLFLGAELYVPTSDDIGTPGRLA--------EWMDDCQ--- 546
Cdd:cd05934 104 ANLTFAGYYSARRFGLGED-----------DVYLTVL--PLFHINAQAVSVLAALSVGATLVllprfsasRFWSDVRryg 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 547 VSVTHLTPAMGQLLSAQAT----RQIPSLLNAFFVGDVLTKRD-CTRLqhlakNVCIINMYGTTETQRAVsyfAIPSVNE 621
Cdd:cd05934 171 ATVTNYLGAMLSYLLAQPPspddRAHRLRAAYGAPNPPELHEEfEERF-----GVRLLEGYGMTETIVGV---IGPRDEP 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 622 DSTFlstqkdliSAGQGMIDVQLLVVNRTDRlvPCAVGEMGEIYVRSG---GLAEGYL-DPSATAEKFvmnwfgqdlkre 697
Cdd:cd05934 243 RRPG--------SIGRPAPGYEVRIVDDDGQ--ELPAGEPGELVIRGLrgwGFFKGYYnMPEATAEAM------------ 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 698 dtligpaREHWFgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE-NVTLVRRDKDEE 776
Cdd:cd05934 301 -------RNGWF-------HTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREaAVVAVPDEVGED 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 777 KVLVsyFVPINDnlegliSESDNPQddeeveeeeenekdlkmemlrgvrryrrlikDIREYLRKKLPSYAVPSVYFPLSK 856
Cdd:cd05934 367 EVKA--VVVLRP------GETLDPE-------------------------------ELFAFCEGQLAYFKVPRYIRFVDD 407
|
570
....*....|....*
gi 589279984 857 LPLNPNGKVDKPKLP 871
Cdd:cd05934 408 LPKTPTEKVAKAQLR 422
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
281-870 |
9.34e-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: 103.41 E-value: 9.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIqseqtngimegpSKGRKtFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:cd05936 1 LADLLEEAARRFPDKTALI------------FMGRK-LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPPNrqivylevsnpkgllviekagELAKIVKDFikdklDLKILIPSISLssngkeeyQDILEKY 440
Cdd:cd05936 68 GALKAGAVVVPLNPLYTPR---------------------ELEHILNDS-----GAKALIVAVSF--------TDLLAAG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 441 QNLSQTPTgiiLGPDSPATLSFTSGSTGIPKGVKGRHYSLT--------HFFPWMSKR------------FGLnekskfT 500
Cdd:cd05936 114 APLGERVA---LTPEDVAVLQYTSGTTGVPKGAMLTHRNLVanalqikaWLEDLLEGDdvvlaalplfhvFGL------T 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 501 MlsgiahdpiqrDMFTPLFLGAELY-VPTSDDIGTpgrlaewMDDCQVS-VTHLT--PAMGQLLSAQAT---RQIPSLLN 573
Cdd:cd05936 185 V-----------ALLLPLALGATIVlIPRFRPIGV-------LKEIRKHrVTIFPgvPTMYIALLNAPEfkkRDFSSLRL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 574 AFFVGDVLTKRDCTRLQHLAkNVCIINMYGTTETQRAVSyfaipsVNedstFLSTQKDLISAGQGMIDVQLLVVNRTDRL 653
Cdd:cd05936 247 CISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVA------VN----PLDGPRKPGSIGIPLPGTEVKIVDDDGEE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 654 VPCavGEMGEIYVRSGGLAEGYL-DPSATAEKFVMNWFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDGNVEC 732
Cdd:cd05936 316 LPP--GEVGELWVRGPQVMKGYWnRPEETAEAFVDGWL--------------------------RTGDIGYMDEDGYFFI 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 733 TGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPINDnleGLISEsdnpqddeeveeeeen 812
Cdd:cd05936 368 VDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEG---ASLTE---------------- 428
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 589279984 813 ekdlkmemlrgvrryrrliKDIREYLRKKLPSYAVP-SVYFpLSKLPLNPNGKVDKPKL 870
Cdd:cd05936 429 -------------------EEIIAFCREQLAGYKVPrQVEF-RDELPKSAVGKILRREL 467
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
283-870 |
2.12e-22 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 103.29 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 283 DIFSANAKKYPDKLCVIQSEQTngimegpskgrkTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGI 362
Cdd:PRK06087 27 DYWQQTARAMPDKIAVVDNHGA------------SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLAC 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 363 LKAGGVFSVVDPAYPpNRQIVY-LEVSNPKGLLVIEKageLAKI--VKDFIKDKLDLKILIPSISLSSNGKE----EYQD 435
Cdd:PRK06087 95 LKVGAVSVPLLPSWR-EAELVWvLNKCQAKMFFAPTL---FKQTrpVDLILPLQNQLPQLQQIVGVDKLAPAtsslSLSQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 436 ILEKYQNLSQTPTgiiLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDP-IQRDM 514
Cdd:PRK06087 171 IIADYEPLTTAIT---THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATgFLHGV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 515 FTPLFLGAELYVptsDDIGTPGRLAEWMDDCQVSVTH-LTPAMGQLLSA--QATRQIPSLlnAFFV--GDVLTK---RDC 586
Cdd:PRK06087 248 TAPFLIGARSVL---LDIFTPDACLALLEQQRCTCMLgATPFIYDLLNLleKQPADLSAL--RFFLcgGTTIPKkvaREC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 587 trLQHlakNVCIINMYGTTETqravsyfaIPS--VNEDStflSTQKDLISAGQGMIDVQLLVVNRTDRLVPCavGEMGEI 664
Cdd:PRK06087 323 --QQR---GIKLLSVYGSTES--------SPHavVNLDD---PLSRFMHTDGYAAAGVEIKVVDEARKTLPP--GCEGEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 665 YVRSGGLAEGYLD-PSATAEKFvmnwfgqdlkredtligpAREHWFgirdrmYrSGDLGRYLPDGNVECTGRADDqIKIR 743
Cdd:PRK06087 385 ASRGPNVFMGYLDePELTARAL------------------DEEGWY------Y-SGDLCRMDEAGYIKITGRKKD-IIVR 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 744 GFR-IELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPindnleglisesdnpqddeeveeeeenekdlkmemlr 822
Cdd:PRK06087 439 GGEnISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVL------------------------------------- 481
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 589279984 823 gVRRYRRL-IKDIREYL-RKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:PRK06087 482 -KAPHHSLtLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
319-785 |
3.52e-21 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 99.12 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 319 TYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNrQIVYLevsnpkgllvIEK 398
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA-ELAEL----------IER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 399 aGELAKIVKDFIKDKLDlKILIPSISLSSNGKEEYQDILEKYQNLSQTPTGiilGPDSPATLSFTSGSTGIPKGVKGRHY 478
Cdd:cd05923 99 -GEMTAAVIAVDAQVMD-AIFQSGVRVLALSDLVGLGEPESAGPLIEDPPR---EPEQPAFVFYTSGTTGLPKGAVIPQR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 479 SLTHFFPWMSK----RFGLNEKSKFTMlsgiahdPIQRDM-FTPLFLGA-----ELYVPTSDDigtPGRLAEWMDDCQVS 548
Cdd:cd05923 174 AAESRVLFMSTqaglRHGRHNVVLGLM-------PLYHVIgFFAVLVAAlaldgTYVVVEEFD---PADALKLIEQERVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 549 VTHLTPAMGQLL---SAQATRQIPSLLNAFFVGDVLTKRDCTRLqHLAKNVCIINMYGTTETQravsyfaipsvneDSTF 625
Cdd:cd05923 244 SLFATPTHLDALaaaAEFAGLKLSSLRHVTFAGATMPDAVLERV-NQHLPGEKVNIYGTTEAM-------------NSLY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 626 LSTQKdlisAGQGM-----IDVQLL-VVNRTDRLVPcaVGEMGEIYVRSGGLA--EGYLD-PSATAEKfvmnwfgqdlkr 696
Cdd:cd05923 310 MRDAR----TGTEMrpgffSEVRIVrIGGSPDEALA--NGEEGELIVAAAADAafTGYLNqPEATAKK------------ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 697 edtligparehwfgIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEE 776
Cdd:cd05923 372 --------------LQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWG 437
|
....*....
gi 589279984 777 KVLVSYFVP 785
Cdd:cd05923 438 QSVTACVVP 446
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
308-744 |
2.07e-20 |
|
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: 96.92 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 308 MEGPSKGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAArSVEMVVCVMGILKAGGVfsVVdPAYPPNRQ------ 381
Cdd:cd05931 15 LDDEGGREETLTYAELDRRARAIAARLQAVGKPGDRVLLLAPP-GLDFVAAFLGCLYAGAI--AV-PLPPPTPGrhaerl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 382 --IvyLEVSNPKGLLVIekAGELAKIVKDFIKDKLDLKILIPSIslssngkeeyqDILEKyqNLSQTPTGIILGPDSPAT 459
Cdd:cd05931 91 aaI--LADAGPRVVLTT--AAALAAVRAFAASRPAAGTPRLLVV-----------DLLPD--TSAADWPPPSPDPDDIAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 460 LSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSkfTMLSGIahdPIQRDM------FTPLFLGAELY-VPTSDDI 532
Cdd:cd05931 154 LQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGD--VVVSWL---PLYHDMgligglLTPLYSGGPSVlMSPAAFL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 533 GTPGRLAEWMDDCQVSVThLTPAMGQLLSAQATR--QIPSL----LNAFFVG------DVLT-----------KRDCTRL 589
Cdd:cd05931 229 RRPLRWLRLISRYRATIS-AAPNFAYDLCVRRVRdeDLEGLdlssWRVALNGaepvrpATLRrfaeafapfgfRPEAFRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 590 QH-LAKNVCIINMyGTTETQRAVSYFAIPSVNEDSTFLSTQKD----LISAGQGMIDVQLLVVNrTDRLVPCAVGEMGEI 664
Cdd:cd05931 308 SYgLAEATLFVSG-GPPGTGPVVLRVDRDALAGRAVAVAADDPaareLVSCGRPLPDQEVRIVD-PETGRELPDGEVGEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 665 YVRSGGLAEGYL-DPSATAEKFvmnwfgqdlkreDTLIGPAREHWFgirdrmyRSGDLGrYLPDGNVECTGRADDQIKIR 743
Cdd:cd05931 386 WVRGPSVASGYWgRPEATAETF------------GALAATDEGGWL-------RTGDLG-FLHDGELYITGRLKDLIIVR 445
|
.
gi 589279984 744 G 744
Cdd:cd05931 446 G 446
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
317-764 |
3.23e-20 |
|
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: 95.53 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 317 TFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVfsvvdpayppnrqivylevSNPkgLLVI 396
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV-------------------TNP--ILPF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 397 EKAGELAkivkdFIKDKLDLKIL-IPSislsSNGKEEYQDIlekyqnlsqtptgiilgPDSPATLSFTSGSTGIPKGVKG 475
Cdd:cd05903 60 FREHELA-----FILRRAKAKVFvVPE----RFRQFDPAAM-----------------PDAVALLLFTSGTTGEPKGVMH 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 476 RHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDP-IQRDMFTPLFLGAELYVptsDDIGTPGRLAEWMDdcQVSVTHL-- 552
Cdd:cd05903 114 SHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTgFVYGFTLPLLLGAPVVL---QDIWDPDKALALMR--EHGVTFMmg 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 553 -TPAMGQLLSA-QATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAVSyfAIPSVNEDstflstqK 630
Cdd:cd05903 189 aTPFLTDLLNAvEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVT--SITPAPED-------R 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 631 DLISAGQGMIDVQLLVVNrtDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFgqdlkredtligparehwf 709
Cdd:cd05903 260 RLYTDGRPLPGVEIKVVD--DTGATLAPGVEGELLSRGPSVFLGYLDrPDLTADAAPEGWF------------------- 318
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 589279984 710 girdrmyRSGDLGRYLPDGNVECTGRADDQIkIR-GFRIELGEIDTHLSRHPLVRE 764
Cdd:cd05903 319 -------RTGDLARLDEDGYLRITGRSKDII-IRgGENIPVLEVEDLLLGHPGVIE 366
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
317-870 |
3.60e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 96.26 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 317 TFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLVI 396
Cdd:PRK06178 58 VITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 397 EKAGELAKIVK--------------DFIKDKLDLKiLIPSISLSSNGKEEYQDILEKYQNLSQTPTGIILGPDSPATLSF 462
Cdd:PRK06178 138 DQLAPVVEQVRaetslrhvivtslaDVLPAEPTLP-LPDSLRAPRLAAAGAIDLLPALRACTAPVPLPPPALDALAALNY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 463 TSGSTGIPKGVKGRH----------YSLTH----------FFP--WMS-KRFGLnekskftmlsgiahdpiqrdMFtPLF 519
Cdd:PRK06178 217 TGGTTGMPKGCEHTQrdmvytaaaaYAVAVvggedsvflsFLPefWIAgENFGL--------------------LF-PLF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 520 LGAELYVPTSDDigtPGRLAEWMDDCQVSVTHLT----------PAMGQ--LLSAQATRQIPsllnafFVGDvLTKRDCT 587
Cdd:PRK06178 276 SGATLVLLARWD---AVAFMAAVERYRVTRTVMLvdnavelmdhPRFAEydLSSLRQVRVVS------FVKK-LNPDYRQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 588 RLQHLAKNVCIINMYGTTETQRAvsyfaipsvneDSTFLSTQK---DLISA----GQGMIDVQLLVVN-RTDRLVPcaVG 659
Cdd:PRK06178 346 RWRALTGSVLAEAAWGMTETHTC-----------DTFTAGFQDddfDLLSQpvfvGLPVPGTEFKICDfETGELLP--LG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 660 EMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDGNVECTGRADD 738
Cdd:PRK06178 413 AEGEIVVRTPSLLKGYWNkPEATAEALRDGWL--------------------------HTGDIGKIDEQGFLHYLGRRKE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 739 QIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVpindnlegLISESDNPQDdeeveeeeenekdlkm 818
Cdd:PRK06178 467 MLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQ--------LKPGADLTAA---------------- 522
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 589279984 819 emlrgvrryrrlikDIREYLRKKLPSYAVPSVYFpLSKLPLNPNGKVDKPKL 870
Cdd:PRK06178 523 --------------ALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
317-870 |
3.74e-20 |
|
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: 95.23 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 317 TFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQivylevsnpkgLLVI 396
Cdd:cd17654 16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS-----------LTVM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 397 EKAGelakiVKDFIKDKLDLkilipSISLSSNGKEEYQDILEKYqnlsqtptgiilgpdSPATLSFTSGSTGIPKGVKGR 476
Cdd:cd17654 85 KKCH-----VSYLLQNKELD-----NAPLSFTPEHRHFNIRTDE---------------CLAYVIHTSGTTGTPKIVAVP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 477 HYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAEL-YVPTSDDIgTPGRLAEWMDDCQ-VSVTHLTP 554
Cdd:cd17654 140 HKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLlIVPTSVKV-LPSKLADILFKRHrITVLQATP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 555 AM----------GQLLSAQATRQIPSLLNAFFVGDVLTKrdcTRLQHLAKnVCIINMYGTTETQRAVSYFAIPSvnEDST 624
Cdd:cd17654 219 TLfrrfgsqsikSTVLSATSSLRVLALGGEPFPSLVILS---SWRGKGNR-TRIFNIYGITEVSCWALAYKVPE--EDSP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 625 flstqkdlISAGQGMIDvqlLVVNRTDRlvpCAVGEMGEIYVrsGGLAEGYLdpsataekfvmnwfgqdLKREDTligpa 704
Cdd:cd17654 293 --------VQLGSPLLG---TVIEVRDQ---NGSEGTGQVFL--GGLNRVCI-----------------LDDEVT----- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 705 rehwfGIRDRMYRSGDLGRyLPDGNVECTGRADDQIKIRGFRIELGEID-THLSRHPLVRENVTLvrrdKDEEKVLVSYF 783
Cdd:cd17654 335 -----VPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQqVIESCLGVESCAVTL----SDQQRLIAFIV 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 784 VPINDNLeglisesdnpqddeeveeeeenekdlkmemlrgvrryrrlikdIREYLRK-KLPSYAVPSVYFPLSKLPLNPN 862
Cdd:cd17654 405 GESSSSR-------------------------------------------IHKELQLtLLSSHAIPDTFVQIDKLPLTSH 441
|
....*...
gi 589279984 863 GKVDKPKL 870
Cdd:cd17654 442 GKVDKSEL 449
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
280-764 |
1.14e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 94.61 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 280 AIPDIFSANAKKYPDKLCVIQseqtngimegpskGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCV 359
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVF-------------GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 360 MGILKAGGVFSVVDPAYPPNrQIVY-LEVSNPKGLLVIEKAGELAKIVKDfiKDKLDLKILIPSISLSSNGkEEYQDILE 438
Cdd:PRK08316 79 LACARAGAVHVPVNFMLTGE-ELAYiLDHSGARAFLVDPALAPTAEAALA--LLPVDTLILSLVLGGREAP-GGWLDFAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 439 KYQNLSQTPTGIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHffPWMSKRFGLNEKSKFTMLSGIahdPI----QRDM 514
Cdd:PRK08316 155 WAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIA--EYVSCIVAGDMSADDIPLHAL---PLyhcaQLDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 515 F--TPLFLGAELYVPTSDDigtPGRLAEWMDDCQVSVTHLTPA--MGQLLSAQ-ATRQIPSLLNAFFVGDVLTKRDCTRL 589
Cdd:PRK08316 230 FlgPYLYVGATNVILDAPD---PELILRTIEAERITSFFAPPTvwISLLRHPDfDTRDLSSLRKGYYGASIMPVEVLKEL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 590 QHLAKNVCIINMYGTTEtqravsyfaIPSVnedSTFLSTQKDLI---SAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYV 666
Cdd:PRK08316 307 RERLPGLRFYNCYGQTE---------IAPL---ATVLGPEEHLRrpgSAGRPVLNVETRVVDDDGNDVA--PGEVGEIVH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 667 RSGGLAEGYLD-PSATAEKFVMNWFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRGF 745
Cdd:PRK08316 373 RSPQLMLGYWDdPEKTAEAFRGGWF--------------------------HSGDLGVMDEEGYITVVDRKKDMIKTGGE 426
|
490
....*....|....*....
gi 589279984 746 RIELGEIDTHLSRHPLVRE 764
Cdd:PRK08316 427 NVASREVEEALYTHPAVAE 445
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
279-870 |
1.78e-19 |
|
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: 93.97 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 279 GAIPDIFSANAKKYPDKLCVIqseqtngimegpsKGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVC 358
Cdd:cd05959 4 NAATLVDLNLNEGRGDKTAFI-------------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 359 VMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLViekAGELAKIVKDFI-KDKLDLKILIpsislSSNGKEEY---- 433
Cdd:cd05959 71 FLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV---SGELAPVLAAALtKSEHTLVVLI-----VSGGAGPEagal 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 434 ---QDILEKYQNLSQTPTGiilgPDSPATLSFTSGSTGIPKGVKGRHYSLThffpWMSKRFGLNekskftmLSGIAHDpi 510
Cdd:cd05959 143 llaELVAAEAEQLKPAATH----ADDPAFWLYSSGSTGRPKGVVHLHADIY----WTAELYARN-------VLGIRED-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 511 qrDMF---TPLF----LGAELYVPTSddIG----------TPGRLAEWMDDCQVSVTHltpamgqllsaqatrQIPSLLN 573
Cdd:cd05959 206 --DVCfsaAKLFfaygLGNSLTFPLS--VGattvlmperpTPAAVFKRIRRYRPTVFF---------------GVPTLYA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 574 AFFVGDVLTKRDCTRLQ-----------HLAKN------VCIINMYGTTETQRavsyfaipsvnedsTFLSTQKDLI--- 633
Cdd:cd05959 267 AMLAAPNLPSRDLSSLRlcvsagealpaEVGERwkarfgLDILDGIGSTEMLH--------------IFLSNRPGRVryg 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 634 SAGQGMIDVQLLVVNrtDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWfgqdlkredtligparehwfgir 712
Cdd:cd05959 333 TTGKPVPGYEVELRD--EDGGDVADGEPGELYVRGPSSATMYWNnRDKTRDTFQGEW----------------------- 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 713 drmYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPindnleg 792
Cdd:cd05959 388 ---TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVL------- 457
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589279984 793 lisesdnpqddeeveeeeenekdlkmemLRGVRRYRRLIKDIREYLRKKLPSYAVP-SVYFpLSKLPLNPNGKVDKPKL 870
Cdd:cd05959 458 ----------------------------RPGYEDSEALEEELKEFVKDRLAPYKYPrWIVF-VDELPKTATGKIQRFKL 507
|
|
| WcaG |
COG0451 |
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
1014-1264 |
1.92e-19 |
|
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 90.42 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1014 TVFLTGATGFLGGFILNDLLtnrsSRIKKVICLVRSSSlekGQERLINSctllgiwnpswlseNKLEIIIGDLSKPQfdl 1093
Cdd:COG0451 1 RILVTGGAGFIGSHLARRLL----ARGHEVVGLDRSPP---GAANLAAL--------------PGVEFVRGDLRDPE--- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1094 sskSWDYLSKETDAILHNGAIVH-WVYPYEKLKPTNVLSTLECLKLCCQGGkMKSFTFVSSTSVLDtegfikksdeelqN 1172
Cdd:COG0451 57 ---ALAAALAGVDAVVHLAAPAGvGEEDPDETLEVNVEGTLNLLEAARAAG-VKRFVYASSSSVYG-------------D 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1173 GNDGLREDDDLeqgkkGLVTGYGQSKWVAEKLIM-MAQNNGLRGWIVRPGYVMGDSKSAVTNtdDFIWRMVKGcLQLGLI 1251
Cdd:COG0451 120 GEGPIDEDTPL-----RPVSPYGASKLAAELLARaYARRYGLPVTILRPGNVYGPGDRGVLP--RLIRRALAG-EPVPVF 191
|
250
....*....|...
gi 589279984 1252 PDINNSINLVPVD 1264
Cdd:COG0451 192 GDGDQRRDFIHVD 204
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
281-764 |
2.46e-19 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 94.01 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKlcVIQSEQTNGImegpskgRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:COG1022 13 LPDLLRRRAARFPDR--VALREKEDGI-------WQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVfSVvdPAYP--PNRQIVY-LEVSNPKgLLVIEKAGELAKIVKdfIKDKL-DLKILI---PSISLSSNGKEEY 433
Cdd:COG1022 84 AILAAGAV-TV--PIYPtsSAEEVAYiLNDSGAK-VLFVEDQEQLDKLLE--VRDELpSLRHIVvldPRGLRDDPRLLSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 434 QDILEKYQNLsQTPTGII-----LGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSK---------- 498
Cdd:COG1022 158 DELLALGREV-ADPAELEarraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRtlsflplahv 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 499 -------FTMLSG--IAHDP----IQRDM--FTPLFLGAelyVPtsddigtpgRLAE-WMDDCQVSVTHLTPAMGQLLSA 562
Cdd:COG1022 237 fertvsyYALAAGatVAFAEspdtLAEDLreVKPTFMLA---VP---------RVWEkVYAGIQAKAEEAGGLKRKLFRW 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 563 ------------QATRQIPSLLNA-FFVGD--VLTK-RDCT--RLQH-------LAKNVC---------IINMYGTTETq 608
Cdd:COG1022 305 alavgrryararLAGKSPSLLLRLkHALADklVFSKlREALggRLRFavsggaaLGPELArffralgipVLEGYGLTET- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 609 ravsyFAIPSVNEDSTFlstqkDLISAGQGMIDVQLlvvnrtdrlvpcAVGEMGEIYVRSGGLAEGYL-DPSATAEKFvm 687
Cdd:COG1022 384 -----SPVITVNRPGDN-----RIGTVGPPLPGVEV------------KIAEDGEILVRGPNVMKGYYkNPEATAEAF-- 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589279984 688 nwfgqdlkredtligpAREHWFgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIR-GFRIELGEIDTHLSRHPLVRE 764
Cdd:COG1022 440 ----------------DADGWL-------HTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQ 494
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
314-870 |
3.91e-19 |
|
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: 92.76 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 314 GRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKgl 393
Cdd:cd05926 11 STPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 394 LVIEKAGELAKIVKDFIKDK---LDLKILIPSISLSSNGKEEYQDILEKYQNLSQTPTGiilgPDSPATLSFTSGSTGIP 470
Cdd:cd05926 89 LVLTPKGELGPASRAASKLGlaiLELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPL----PDDLALILHTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 471 KGVKGRHYSLTHFFPWMSKRFGLNEKSKfTML-------SGIAhdpiqRDMFTPLFLGAELYVPtsddigtPGRLAE--W 541
Cdd:cd05926 165 KGVPLTHRNLAASATNITNTYKLTPDDR-TLVvmplfhvHGLV-----ASLLSTLAAGGSVVLP-------PRFSAStfW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 542 MDDCQVSVTHLT--PAMGQLL---SAQATRQIPSLLNafFVgdvltkRDCTR---LQHLAK-----NVCIINMYGTTETQ 608
Cdd:cd05926 232 PDVRDYNATWYTavPTIHQILlnrPEPNPESPPPKLR--FI------RSCSAslpPAVLEAleatfGAPVLEAYGMTEAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 609 RAVSYFAIPSvnedstflsTQKDLISAGQGmIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPSATAEKFVm 687
Cdd:cd05926 304 HQMTSNPLPP---------GPRKPGSVGKP-VGVEVRILDEDGEILP--PGVVGEICLRGPNVTRGYLnNPEANAEAAF- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 688 nwfgqdlkredtligpaREHWFgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVT 767
Cdd:cd05926 371 -----------------KDGWF-------RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 768 L-VRRDKDEEKVlVSYFVPindnleglisesdnpqddeeveeeeenekDLKMEMLRgvrryrrliKDIREYLRKKLPSYA 846
Cdd:cd05926 427 FgVPDEKYGEEV-AAAVVL-----------------------------REGASVTE---------EELRAFCRKHLAAFK 467
|
570 580
....*....|....*....|....*
gi 589279984 847 VPS-VYFpLSKLPLNPNGKVDKPKL 870
Cdd:cd05926 468 VPKkVYF-VDELPKTATGKIQRRKV 491
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
318-870 |
4.04e-19 |
|
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: 92.01 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 318 FTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFsvvdpayppnrqivylevsnpkgllvie 397
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVY---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 398 kagelakivkdfikdkldlkilIPsisLSSNGKEEyqDILEKYQNLSqtPTGIILGPDSPATLSFTSGSTGIPKGVKGRH 477
Cdd:cd05972 53 ----------------------VP---LTTLLGPK--DIEYRLEAAG--AKAIVTDAEDPALIYFTSGTTGLPKGVLHTH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 478 -YSLTHfFPWMSKRFGLNEKSKFTMLSgiahDP-----IQRDMFTPLFLGAELYVPTSDDIgTPGRLAEWMDDCQVSVTH 551
Cdd:cd05972 104 sYPLGH-IPTAAYWLGLRPDDIHWNIA----DPgwakgAWSSFFGPWLLGATVFVYEGPRF-DAERILELLERYGVTSFC 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 552 LTPAMGQLLSAQ--ATRQIPSLLNAFFVGDVLTK------RDCTRLQhlaknvcIINMYGTTETQRAVsyfaipsvnedS 623
Cdd:cd05972 178 GPPTAYRMLIKQdlSSYKFSHLRLVVSAGEPLNPeviewwRAATGLP-------IRDGYGQTETGLTV-----------G 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 624 TFLSTQKDLISAGQGMIDVQLLVVNRTDRlvPCAVGEMGEIYVRSG--GLAEGYL-DPSATAEKFVMNWfgqdlkredtl 700
Cdd:cd05972 240 NFPDMPVKPGSMGRPTPGYDVAIIDDDGR--ELPPGEEGDIAIKLPppGLFLGYVgDPEKTEASIRGDY----------- 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 701 igparehwfgirdrmYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVREnVTLVRRDKDEEKVLV 780
Cdd:cd05972 307 ---------------YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAE-AAVVGSPDPVRGEVV 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 781 SYFVPINDNLEglisesdnPQDdeeveeeeenekdlkmemlrgvrryrRLIKDIREYLRKKLPSYAVPSVYFPLSKLPLN 860
Cdd:cd05972 371 KAFVVLTSGYE--------PSE--------------------------ELAEELQGHVKKVLAPYKYPREIEFVEELPKT 416
|
570
....*....|
gi 589279984 861 PNGKVDKPKL 870
Cdd:cd05972 417 ISGKIRRVEL 426
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
316-870 |
5.76e-19 |
|
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: 91.58 E-value: 5.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 316 KTFTYGQIDKASNVIAHCLIQNG-LKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKglL 394
Cdd:cd05941 10 DSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPS--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 395 VIEkagelakivkdfikdkldlkilipsislssngkeeyqdilekyqnlsqtptgiilgpdsPATLSFTSGSTGIPKGVK 474
Cdd:cd05941 88 VLD-----------------------------------------------------------PALILYTSGTTGRPKGVV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 475 GRHYSLTHffpwMSKrfGLNEKSKFTMLSGIAHD-PIQR------DMFTPLFLGAELYVPTSDDigtPGRLAEWMDDCQV 547
Cdd:cd05941 109 LTHANLAA----NVR--ALVDAWRWTEDDVLLHVlPLHHvhglvnALLCPLFAGASVEFLPKFD---PKEVAISRLMPSI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 548 SVTHLTPAMGQLLSAQATRQIPSLLNAffvgdvltKRDCTRlqHLAKNVC--------------------IINMYGTTET 607
Cdd:cd05941 180 TVFMGVPTIYTRLLQYYEAHFTDPQFA--------RAAAAE--RLRLMVSgsaalpvptleeweaitghtLLERYGMTEI 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 608 QRAVSyfaipsvnedsTFLSTQKDLISAGQGMIDVQLLVVNRtDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFV 686
Cdd:cd05941 250 GMALS-----------NPLDGERRPGTVGMPLPGVQARIVDE-ETGEPLPRGEVGEIQVRGPSVFKEYWNkPEATKEEFT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 687 -MNWFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDGNVECTGR-ADDQIKIRGFRIELGEIDTHLSRHPLVRE 764
Cdd:cd05941 318 dDGWF--------------------------KTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSE 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 765 NVTLVRRDKDEEKVLVSYFVPindnleglisESDNPQDDeeveeeeenekdlkmemlrgvrryrrlIKDIREYLRKKLPS 844
Cdd:cd05941 372 CAVIGVPDPDWGERVVAVVVL----------RAGAAALS---------------------------LEELKEWAKQRLAP 414
|
570 580
....*....|....*....|....*.
gi 589279984 845 YAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd05941 415 YKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
315-865 |
7.90e-19 |
|
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: 90.95 E-value: 7.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 315 RKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGvfsvvdpayppnrqivylevsnpkgll 394
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGA--------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 395 viekagelakivkdfikdkldlkILIPSISLSSNGKEEYQdilekyqnLSQTPTGIIL--GPDSPATLSFTSGSTGIPKG 472
Cdd:cd05971 57 -----------------------IAVPLFALFGPEALEYR--------LSNSGASALVtdGSDDPALIIYTSGTTGPPKG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 473 VKGRH---------YSLTH-FFP-------------WMSKRFGLNEKSKFTMLSGIAHDPIQRDmftplflgaelyvpts 529
Cdd:cd05971 106 ALHAHrvllghlpgVQFPFnLFPrdgdlywtpadwaWIGGLLDVLLPSLYFGVPVLAHRMTKFD---------------- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 530 ddigtPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQIPSLLN--AFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTET 607
Cdd:cd05971 170 -----PKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKlrAIATGGESLGEELLGWAREQFGVEVNEFYGQTEC 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 608 QRAVSyfaipsvneDSTFLSTQKDLiSAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVR---SGGLAEGYLDPSATAEK 684
Cdd:cd05971 245 NLVIG---------NCSALFPIKPG-SMGKPIPGHRVAIVDDNGTPLP--PGEVGEIAVElpdPVAFLGYWNNPSATEKK 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 685 FVMNWFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRe 764
Cdd:cd05971 313 MAGDWL--------------------------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVL- 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 765 NVTLVRRDKDEEKVLVSYFVPINdnleglisESDNPQDDeeveeeeenekdlkmemlrgvrryrrLIKDIREYLRKKLPS 844
Cdd:cd05971 366 MAAVVGIPDPIRGEIVKAFVVLN--------PGETPSDA--------------------------LAREIQELVKTRLAA 411
|
570 580
....*....|....*....|..
gi 589279984 845 YAVP-SVYFPlSKLPLNPNGKV 865
Cdd:cd05971 412 HEYPrEIEFV-NELPRTATGKI 432
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
326-870 |
1.36e-18 |
|
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: 90.58 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 326 ASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGG----VFSVVDPAYPPNrQIVYLeVSNPKGLLVIEKAGe 401
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKES-VLRYL-VADAGGRIVLADAG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 402 lakivkdfIKDKLDLKIL---IPSISLSSNGKEEYQDILEkyqnlsqtptGIILGPDSPATLSFTSGSTGIPKGVKGRHY 478
Cdd:cd05922 79 --------AADRLRDALPaspDPGTVLDADGIRAARASAP----------AHEVSHEDLALLLYTSGSTGSPKLVRLSHQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 479 SLTHFFPWMSKRFGLNEKSK-FTMLsgiahdPIQRD-----MFTPLFLGAELYVPTSddiGTPGRlaEWMDDCQVS-VTH 551
Cdd:cd05922 141 NLLANARSIAEYLGITADDRaLTVL------PLSYDyglsvLNTHLLRGATLVLTND---GVLDD--AFWEDLREHgATG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 552 LT--PAMGQLLS--AQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAVSYFAIPSVNEDSTfls 627
Cdd:cd05922 210 LAgvPSTYAMLTrlGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPG--- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 628 tqkdliSAGQGMIDVQLLVVNRTDRlvPCAVGEMGEIYVRSGGLAEGYLDPSAtaekfvmnwfgqdlkredtliGPAREH 707
Cdd:cd05922 287 ------SIGLAIPGGEFEILDDDGT--PTPPGEPGEIVHRGPNVMKGYWNDPP---------------------YRRKEG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 708 WFGirDRMYrSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVsyFVpin 787
Cdd:cd05922 338 RGG--GVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLAL--FV--- 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 788 dnleglisESDNPQDDeeveeeeenekdlkmemlrgvrryrrliKDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDK 867
Cdd:cd05922 410 --------TAPDKIDP----------------------------KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDY 453
|
...
gi 589279984 868 PKL 870
Cdd:cd05922 454 AAL 456
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
281-870 |
1.47e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 91.12 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIQseqtngimegpskGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:PRK07656 7 LPELLARAARRFGDKEAYVF-------------GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPPnRQIVY-LEVSNPKGLLVIEKAGELAKIVKDFIKDkLDLKILIPSISLSSNGKEE--YQDIL 437
Cdd:PRK07656 74 GALKAGAVVVPLNTRYTA-DEAAYiLARGDAKALFVLGLFLGVDYSATTRLPA-LEHVVICETEEDDPHTEKMktFTDFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 438 EKYQNLSQTPTgiiLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFtmlsgIAHDPiqrdMF-- 515
Cdd:PRK07656 152 AAGDPAERAPE---VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRY-----LAANP----FFhv 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 516 --------TPLFLGAELY-VPTSDdigtPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQIPSL--LNAFFVGD----- 579
Cdd:PRK07656 220 fgykagvnAPLMRGATILpLPVFD----PDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLssLRLAVTGAasmpv 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 580 VLTKRDCTRLqhlakNVCII-NMYGTTEtqravsyfAIPSVnedsTF--LSTQKDLI--SAGQGMIDVQLLVVNRTDRLV 654
Cdd:PRK07656 296 ALLERFESEL-----GVDIVlTGYGLSE--------ASGVT----TFnrLDDDRKTVagTIGTAIAGVENKIVNELGEEV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 655 PcaVGEMGEIYVRSGGLAEGYL-DPSATAEKfvmnwfgqdLKREDTLigparehwfgirdrmyRSGDLGRYLPDGNVECT 733
Cdd:PRK07656 359 P--VGEVGELLVRGPNVMKGYYdDPEATAAA---------IDADGWL----------------HTGDLGRLDEEGYLYIV 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 734 GRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPindNLEGLISEsdnpqddeeveeeeene 813
Cdd:PRK07656 412 DRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVL---KPGAELTE----------------- 471
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 589279984 814 kdlkmemlrgvrryrrliKDIREYLRKKLPSYAVP-SVYFpLSKLPLNPNGKVDKPKL 870
Cdd:PRK07656 472 ------------------EELIAYCREHLAKYKVPrSIEF-LDELPKNATGKVLKRAL 510
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
315-870 |
1.92e-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: 89.83 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 315 RKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPnrqivylevsnpkgll 394
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHP---------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 395 viekagelakivkdfikdkldlkilipsislssngkEEYQDILEKYQnlsqtPTGIILGPDSPATLSFTSGSTGIPKGVK 474
Cdd:cd05919 72 ------------------------------------DDYAYIARDCE-----ARLVVTSADDIAYLLYSSGTTGPPKGVM 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 475 GRHYSLTHFFP-WMSKRFGLNEK------SKFTMLSGIAHDpiqrdMFTPLFLGAELYVptSDDIGTPGRLAEWMDDCQV 547
Cdd:cd05919 111 HAHRDPLLFADaMAREALGLTPGdrvfssAKMFFGYGLGNS-----LWFPLAVGASAVL--NPGWPTAERVLATLARFRP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 548 SVTHLTPAMGQLLSAQAT---RQIPSLLNAFFVGDVLTKRDCTRLQHlAKNVCIINMYGTTETQRavsyfaipsvnedsT 624
Cdd:cd05919 184 TVLYGVPTFYANLLDSCAgspDALRSLRLCVSAGEALPRGLGERWME-HFGGPILDGIGATEVGH--------------I 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 625 FLSTQKDLI---SAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYldpsataekfvmnWfgqdlKREDTLI 701
Cdd:cd05919 249 FLSNRPGAWrlgSTGRPVPGYEIRLVDEEGHTIP--PGEEGDLLVRGPSAAVGY-------------W-----NNPEKSR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 702 GPAREHWfgirdrmYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVS 781
Cdd:cd05919 309 ATFNGGW-------YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTA 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 782 YFVpindnlegLISESDNPQddeeveeeeenekdlkmemlrgvrryrRLIKDIREYLRKKLPSYAVPSVYFPLSKLPLNP 861
Cdd:cd05919 382 FVV--------LKSPAAPQE---------------------------SLARDIHRHLLERLSAHKVPRRIAFVDELPRTA 426
|
....*....
gi 589279984 862 NGKVDKPKL 870
Cdd:cd05919 427 TGKLQRFKL 435
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
318-870 |
4.10e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 89.61 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 318 FTYGQIDKASNVIAHCLIQNGLKKEEVVMVYA---ARSVEMVVCVMGIlkaGGVFSVVDPAYPPNrQIVY-LEVSNPKGL 393
Cdd:cd12119 26 YTYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLELYYAVPGM---GAVLHTINPRLFPE-QIAYiINHAEDRVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 394 LV-------IEKAGELAKIVKDFIKDKLDLKILIPSIslssNGKEEYQDILEkyqnlSQTPTGIIlgPD----SPATLSF 462
Cdd:cd12119 102 FVdrdflplLEAIAPRLPTVEHVVVMTDDAAMPEPAG----VGVLAYEELLA-----AESPEYDW--PDfdenTAAAICY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 463 TSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLsgiahdPIqrdmfTPLF-------------LGAELYVPTS 529
Cdd:cd12119 171 TSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSESDVVL------PV-----VPMFhvnawglpyaaamVGAKLVLPGP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 530 DDigTPGRLAEWMDDCQVSVTHLTPAMGQ-LLSAQAT--RQIPSLLNAFFVGDVLTKRDCTRLqhLAKNVCIINMYGTTE 606
Cdd:cd12119 240 YL--DPASLAELIEREGVTFAAGVPTVWQgLLDHLEAngRDLSSLRRVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 607 TQrAVSYFAIPSVNEDSTFLSTQKDL-ISAGQGMIDVQLLVVNRTDRLVPCAVGEMGEIYVRSGGLAEGYLDPSATAEKF 685
Cdd:cd12119 316 TS-PLGTVARPPSEHSNLSEDEQLALrAKQGRPVPGVELRIVDDDGRELPWDGKAVGELQVRGPWVTKSYYKNDEESEAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 686 vmnwfgqdlkredtligpAREHWFgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVREN 765
Cdd:cd12119 395 ------------------TEDGWL-------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 766 VTLVRRDK--DEEKVLVsyfvpindnleglISESDNPQDDEeveeeeenekdlkmemlrgvrryrrliKDIREYLRKKLP 843
Cdd:cd12119 450 AVIGVPHPkwGERPLAV-------------VVLKEGATVTA---------------------------EELLEFLADKVA 489
|
570 580
....*....|....*....|....*..
gi 589279984 844 SYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd12119 490 KWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
286-871 |
7.10e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 88.83 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 286 SANAKKYPDKLCVIQSeqtngimegpskgRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKA 365
Cdd:PRK07788 56 AHAARRAPDRAALIDE-------------RGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 366 GGVFSVVDPAYPPnRQIVylEVSNPKGLLVIEKAGELAKIVKDFIKDKLDLKILIPS---ISLSSNGKEEYQDILEKyqn 442
Cdd:PRK07788 123 GARIILLNTGFSG-PQLA--EVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNpddDEPSGSTDETLDDLIAG--- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 443 lsqTPTGIILGPDSPATLS-FTSGSTGIPKGVKGRHYSLthffpwmskrfglnekskFTMLSGI-AHDPIQRDMFT---- 516
Cdd:PRK07788 197 ---SSTAPLPKPPKPGGIViLTSGTTGTPKGAPRPEPSP------------------LAPLAGLlSRVPFRAGETTllpa 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 517 PLFLGAELYVPTsddIGTPGRlaewmddCQVsVTH--LTPAmgQLLSAQATRQI------PSLLNAFF--VGDVLTKRDC 586
Cdd:PRK07788 256 PMFHATGWAHLT---LAMALG-------STV-VLRrrFDPE--ATLEDIAKHKAtalvvvPVMLSRILdlGPEVLAKYDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 587 TRLQ-----------HLAKNV------CIINMYGTTEtqraVSYFAIpsvnedstflSTQKDLI----SAGQGMIDVQLL 645
Cdd:PRK07788 323 SSLKiifvsgsalspELATRAleafgpVLYNLYGSTE----VAFATI----------ATPEDLAeapgTVGRPPKGVTVK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 646 VVNRTDRLVPcaVGEMGEIYVRSGGLAEGYLDpsataekfvmnwfGQDLKREDTLIgparehwfgirdrmyRSGDLGRYL 725
Cdd:PRK07788 389 ILDENGNEVP--RGVVGRIFVGNGFPFEGYTD-------------GRDKQIIDGLL---------------SSGDVGYFD 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 726 PDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPindnleglisESDNPQDDee 805
Cdd:PRK07788 439 EDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVK----------APGAALDE-- 506
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589279984 806 veeeeenekdlkmemlrgvrryrrliKDIREYLRKKLPSYAVP-SVYFpLSKLPLNPNGKVDKPKLP 871
Cdd:PRK07788 507 --------------------------DAIKDYVRDNLARYKVPrDVVF-LDELPRNPTGKVLKRELR 546
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
281-870 |
1.02e-17 |
|
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: 88.28 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERR-------------LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVfsvvdP--AYPPNRQ--IVYL-EVSNPKGLLVIEKAGE--LAKIVKDFIKDKLDLKILI------PSISLSS 427
Cdd:COG1021 94 ALFRAGAI-----PvfALPAHRRaeISHFaEQSEAVAYIIPDRHRGfdYRALARELQAEVPSLRHVLvvgdagEFTSLDA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 428 ngkeeyqdilekyqnLSQTPTGIIL---GPDSPATLSFTSGSTGIPKGVKGRH----YSLTHffpwMSKRFGLNEKSKFT 500
Cdd:COG1021 169 ---------------LLAAPADLSEprpDPDDVAFFQLSGGTTGLPKLIPRTHddylYSVRA----SAEICGLDADTVYL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 501 MLSGIAHDpiqrdmFT---PLFLGAeLYV-------PTSDdigtPGRLAEWMDDCQVSVTHLTPAM-------------- 556
Cdd:COG1021 230 AALPAAHN------FPlssPGVLGV-LYAggtvvlaPDPS----PDTAFPLIERERVTVTALVPPLallwldaaersryd 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 557 ----------GQLLSAQATRQIPSLLNAffvgdvltkrdctRLQhlaknvciiNMYGTTETqravsyfaipSVN----ED 622
Cdd:COG1021 299 lsslrvlqvgGAKLSPELARRVRPALGC-------------TLQ---------QVFGMAEG----------LVNytrlDD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 623 S--TFLSTQKDLISAGqgmiDvQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFgqdlkredt 699
Cdd:COG1021 347 PeeVILTTQGRPISPD----D-EVRIVDEDGNPVP--PGEVGELLTRGPYTIRGYYRaPEHNARAFTPDGF--------- 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 700 ligparehwfgirdrmYRSGDLGRYLPDGNVECTGRADDQIkIRGfrielGE------IDTHLSRHPLVReNVTLVRRDk 773
Cdd:COG1021 411 ----------------YRTGDLVRRTPDGYLVVEGRAKDQI-NRG-----GEkiaaeeVENLLLAHPAVH-DAAVVAMP- 466
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 774 DE---EKVlVSYFVPINDNLEglisesdnpqddeeveeeeenekdlkmemlrgvrryrrlIKDIREYLR-KKLPSYAVPS 849
Cdd:COG1021 467 DEylgERS-CAFVVPRGEPLT---------------------------------------LAELRRFLReRGLAAFKLPD 506
|
650 660
....*....|....*....|.
gi 589279984 850 VYFPLSKLPLNPNGKVDKPKL 870
Cdd:COG1021 507 RLEFVDALPLTAVGKIDKKAL 527
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
283-870 |
1.61e-17 |
|
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: 87.38 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 283 DIFSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGI 362
Cdd:cd05920 19 DLLARSAARHPDRIAVVDGDRR-------------LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 363 LKAGGVfsvvdP--AYPPNRQivyLEVSNpkgllVIEKAGELAKIVKDFIKDkldlkilipsislsSNGKEEYQDILEKy 440
Cdd:cd05920 86 LRLGAV-----PvlALPSHRR---SELSA-----FCAHAEAVAYIVPDRHAG--------------FDHRALARELAES- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 441 qnlsqtptgiilGPDsPATLSFTSGSTGIPKGVKGRH----YSLTHFFPWMskrfGLNEKSKFTMLSGIAHdpiQRDMFT 516
Cdd:cd05920 138 ------------IPE-VALFLLSGGTTGTPKLIPRTHndyaYNVRASAEVC----GLDQDTVYLAVLPAAH---NFPLAC 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 517 PLFLGAELY----VPTSDdiGTPGRLAEWMDDCQVSVTHLTPAMGQL-LSAQATRQI-PSLLNAFFVGDVLTKRDCTRLQ 590
Cdd:cd05920 198 PGVLGTLLAggrvVLAPD--PSPDAAFPLIEREGVTVTALVPALVSLwLDAAASRRAdLSSLRLLQVGGARLSPALARRV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 591 HLAKNVCIINMYGTTETqrAVSYfaipsvnedsTFLSTQKDLISAGQGM---IDVQLLVVNRTDRLVPcaVGEMGEIYVR 667
Cdd:cd05920 276 PPVLGCTLQQVFGMAEG--LLNY----------TRLDDPDEVIIHTQGRpmsPDDEIRVVDEEGNPVP--PGEEGELLTR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 668 SGGLAEGYLD-PSATAEKFVMNWFgqdlkredtligparehwfgirdrmYRSGDLGRYLPDGNVECTGRADDQIKIRGFR 746
Cdd:cd05920 342 GPYTIRGYYRaPEHNARAFTPDGF-------------------------YRTGDLVRRTPDGYLVVEGRIKDQINRGGEK 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 747 IELGEIDTHLSRHPLVREnVTLVRRDkDE---EKVLVsYFVPINDNLEglisesdnpqddeeveeeeenekdlkmemLRG 823
Cdd:cd05920 397 IAAEEVENLLLRHPAVHD-AAVVAMP-DEllgERSCA-FVVLRDPPPS-----------------------------AAQ 444
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 589279984 824 VRRYRRlikdireylRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd05920 445 LRRFLR---------ERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
281-764 |
7.24e-17 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 85.88 E-value: 7.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIQSEQTNGIMEgpskgrkTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:PRK13295 26 INDDLDACVASCPDKTAVTAVRLGTGAPR-------RFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPpNRQIVY-LEVSNPKGLLViekagelAKIVKDFIKDKL--DLKILIPSIS----LSSNGKEEY 433
Cdd:PRK13295 99 ACSRIGAVLNPLMPIFR-ERELSFmLKHAESKVLVV-------PKTFRGFDHAAMarRLRPELPALRhvvvVGGDGADSF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 434 QDIL-----EKYQNLSQTPTGIILGPDSPATLSFTSGSTGIPKGVkgRHYSLTHF---FPWmSKRFGLNEKSKFTMLSGI 505
Cdd:PRK13295 171 EALLitpawEQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGV--MHTANTLManiVPY-AERLGLGADDVILMASPM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 506 AHDP-IQRDMFTPLFLGAELYVptsDDIGTPGRLAEWMDDCQVSVTHL-TPAMGQLLSAQATRQIP-SLLNAFFVGDVLT 582
Cdd:PRK13295 248 AHQTgFMYGLMMPVMLGATAVL---QDIWDPARAAELIRTEGVTFTMAsTPFLTDLTRAVKESGRPvSSLRTFLCAGAPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 583 KRDCTRLQHLAKNVCIINMYGTTETQrAVSyfaipsvnedSTFLSTQKDLISAGQG--MIDVQLLVVNRTDRLVPcaVGE 660
Cdd:PRK13295 325 PGALVERARAALGAKIVSAWGMTENG-AVT----------LTKLDDPDERASTTDGcpLPGVEVRVVDADGAPLP--AGQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 661 MGEIYVRSGGLAEGYLdpsataekfvmnwfgqdlKREDtLIGPAREHWFGirdrmyrSGDLGRYLPDGNVECTGRADDQI 740
Cdd:PRK13295 392 IGRLQVRGCSNFGGYL------------------KRPQ-LNGTDADGWFD-------TGDLARIDADGYIRISGRSKDVI 445
|
490 500
....*....|....*....|....*
gi 589279984 741 kIRGFR-IELGEIDTHLSRHPLVRE 764
Cdd:PRK13295 446 -IRGGEnIPVVEIEALLYRHPAIAQ 469
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
456-868 |
9.53e-17 |
|
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: 83.15 E-value: 9.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 456 SPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNekskftmlsgiahDPIQRDMFTPLF-------------LGA 522
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFG-------------GGDSWLLSLPLYhvgglailvrsllAGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 523 ELYVPTsddigtpGRLAEWMDDCQVSVTH--LTPAM-GQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRlQHLAKNVCII 599
Cdd:cd17630 68 ELVLLE-------RNQALAEDLAPPGVTHvsLVPTQlQRLLDSGQGPAALKSLRAVLLGGAPIPPELLE-RAADRGIPLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 600 NMYGTTETQRAVSyfaipsvnedSTFLSTQKDLiSAGQGMIDVQLLVVNRtdrlvpcavgemGEIYVRSGGLAEGYLDPS 679
Cdd:cd17630 140 TTYGMTETASQVA----------TKRPDGFGRG-GVGVLLPGRELRIVED------------GEIWVGGASLAMGYLRGQ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 680 ATAEKFVMNWFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRH 759
Cdd:cd17630 197 LVPEFNEDGWF--------------------------TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAH 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 760 PLVREnvtlvrrdkdeekVLVsyfVPINDNLEGlisesdnpqddeeveeeeenekdlkmEMLRGVRRYR--RLIKDIREY 837
Cdd:cd17630 251 PAVRD-------------AFV---VGVPDEELG--------------------------QRPVAVIVGRgpADPAELRAW 288
|
410 420 430
....*....|....*....|....*....|.
gi 589279984 838 LRKKLPSYAVPSVYFPLSKLPLNPNGKVDKP 868
Cdd:cd17630 289 LKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
318-764 |
2.62e-16 |
|
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: 83.32 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 318 FTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLVIE 397
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 398 KagelakivkdfIKDKLDlkilipsislssngkeeyqdilekyqnlsqtptgiilgPDSPATLSFTSGSTGIPKGVKGRH 477
Cdd:cd05969 81 E-----------LYERTD--------------------------------------PEDPTLLHYTSGTTGTPKGVLHVH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 478 YSLThfFPWMSKR--FGLNEKSKF------TMLSGIAHDpiqrdMFTPLFLGAELYVptSDDIGTPGRLAEWMDDCQVSV 549
Cdd:cd05969 112 DAMI--FYYFTGKyvLDLHPDDIYwctadpGWVTGTVYG-----IWAPWLNGVTNVV--YEGRFDAESWYGIIERVKVTV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 550 THLTPA-----MGQLLSAQATRQIPSLLNAFFVGDVLTKrDCTRLQHLAKNVCIINMYGTTETQravsyfAIPSVNedst 624
Cdd:cd05969 183 WYTAPTairmlMKEGDELARKYDLSSLRFIHSVGEPLNP-EAIRWGMEVFGVPIHDTWWQTETG------SIMIAN---- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 625 FLSTQKDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSG--GLAEGYL-DPSATAEKFVMNWfgqdlkredtli 701
Cdd:cd05969 252 YPCMPIKPGSMGKPLPGVKAAVVDENGNELP--PGTKGILALKPGwpSMFRGIWnDEERYKNSFIDGW------------ 317
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 589279984 702 gparehwfgirdrmYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE 764
Cdd:cd05969 318 --------------YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAE 366
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
16-173 |
3.14e-16 |
|
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: 82.79 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 16 ELKAKLDRWSERLS-ALPSLALPTDYPRPSpaklVESFQ----TLPIPPSLTPALLRLTLEYSTlypssplpTPYHLLLT 90
Cdd:cd19531 187 VLERQLAYWREQLAgAPPVLELPTDRPRPA----VQSFRgarvRFTLPAELTAALRALARREGA--------TLFMTLLA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 91 SFSILLFRYT--PDpslvlyptVAVnSTPS---THP------------LLLKMELSPEMSFFEILHQV--LTQEIIATQD 151
Cdd:cd19531 255 AFQVLLHRYSgqDD--------IVV-GTPVagrNRAelegligffvntLVLRTDLSGDPTFRELLARVreTALEAYAHQD 325
|
170 180
....*....|....*....|....*..
gi 589279984 152 sVPLSTLVDHLKPEG-----PLFRVRF 173
Cdd:cd19531 326 -LPFEKLVEALQPERdlsrsPLFQVMF 351
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
283-764 |
9.55e-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: 82.16 E-value: 9.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 283 DIFSANAKKYPDKLCVIQ-SEQTNgimegpskgRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMG 361
Cdd:cd05970 21 DVVDAMAKEYPDKLALVWcDDAGE---------ERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 362 ILKAGGVfSVVDPAYPPNRQIVY-LEVSNPKGLLVIEKagelaKIVKDFIKDKL-DLKILIPSISLSSNGKEEYQDILEK 439
Cdd:cd05970 92 LHKLGAI-AIPATHQLTAKDIVYrIESADIKMIVAIAE-----DNIPEEIEKAApECPSKPKLVWVGDPVPEGWIDFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 440 YQNLS---QTPTG-IILGPDSPATLSFTSGSTGIPKGVKGRH-YSLTHFfpwMSKRFGLNEKSKFTMLSgIAHDPIQRDM 514
Cdd:cd05970 166 IKNASpdfERPTAnSYPCGEDILLVYFSSGTTGMPKMVEHDFtYPLGHI---VTAKYWQNVREGGLHLT-VADTGWGKAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 515 FTPLFlgaelyvptsddigtpgrlAEWMDDCQVSV---THLTPAmgQLLSAQATRQI-----PSLLNAFFVGDVLTKRDC 586
Cdd:cd05970 242 WGKIY-------------------GQWIAGAAVFVydyDKFDPK--ALLEKLSKYGVttfcaPPTIYRFLIREDLSRYDL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 587 TRLQHLAKNVCIINM-----------------YGTTETQRAVsyfaipsvnedSTFLSTQKDLISAGQGMIDVQLLVVNR 649
Cdd:cd05970 301 SSLRYCTTAGEALNPevfntfkektgiklmegFGQTETTLTI-----------ATFPWMEPKPGSMGKPAPGYEIDLIDR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 650 TDRlvPCAVGEMGEIYVRSG-----GLAEGYL-DPSATAEKFvmnwfgqdlkredtligparehwfgiRDRMYRSGDLGR 723
Cdd:cd05970 370 EGR--SCEAGEEGEIVIRTSkgkpvGLFGGYYkDAEKTAEVW--------------------------HDGYYHTGDAAW 421
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 589279984 724 YLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE 764
Cdd:cd05970 422 MDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLE 462
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
288-762 |
1.34e-15 |
|
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: 81.51 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 288 NAKKYPDKLCVIQSeqtngimegpSKGRkTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGG 367
Cdd:cd05904 14 FASAHPSRPALIDA----------ATGR-ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 368 VFSVVDPAYPPN---RQIvylEVSNPKGLLViekAGELAKIVKDFikdklDLKILIPSiSLSSNGKEEYQDILEkyQNLS 444
Cdd:cd05904 83 VVTTANPLSTPAeiaKQV---KDSGAKLAFT---TAELAEKLASL-----ALPVVLLD-SAEFDSLSFSDLLFE--ADEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 445 QTPTGIIlGPDSPATLSFTSGSTGIPKGVkgrhySLTHffpwmskRFGLNEKSKFTMLSGIAHDPIQRDMFT-PLF---- 519
Cdd:cd05904 149 EPPVVVI-KQDDVAALLYSSGTTGRSKGV-----MLTH-------RNLIAMVAQFVAGEGSNSDSEDVFLCVlPMFhiyg 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 520 ----------LGAELYVPTSDDIGTPGRLAEwmddcQVSVTHLT--P---------AMGQLLSAQATRQIPS-------- 570
Cdd:cd05904 216 lssfalgllrLGATVVVMPRFDLEELLAAIE-----RYKVTHLPvvPpivlalvksPIVDKYDLSSLRQIMSgaaplgke 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 571 LLNAFfvgdvltkrdctrlqhLAK--NVCIINMYGTTETQRAVSYFaipsvnedSTFLSTQKDLISAGQGMIDVQLLVVN 648
Cdd:cd05904 291 LIEAF----------------RAKfpNVDLGQGYGMTESTGVVAMC--------FAPEKDRAKYGSVGRLVPNVEAKIVD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 649 -RTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPSATAEKFVmnwfgqdlkredtligpaREHWFgirdrmyRSGDLGRYLP 726
Cdd:cd05904 347 pETGESLP--PNQTGELWIRGPSIMKGYLnNPEATAATID------------------KEGWL-------HTGDLCYIDE 399
|
490 500 510
....*....|....*....|....*....|....*.
gi 589279984 727 DGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLV 762
Cdd:cd05904 400 DGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEI 435
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
454-762 |
5.39e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 79.64 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 454 PDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHdpIQRDMFTP-LFLGAELYVPTSDDi 532
Cdd:PRK06188 167 PPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH--AGGAFFLPtLLRGGTVIVLAKFD- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 533 gtPGRLAEWMDDCQVSVTHLTPAMGQLL---SAQATRQIPSLLNAFFVGDVLTKrdcTRLQHLAKNVCII--NMYGTTET 607
Cdd:PRK06188 244 --PAEVLRAIEEQRITATFLVPTMIYALldhPDLRTRDLSSLETVYYGASPMSP---VRLAEAIERFGPIfaQYYGQTEA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 608 QRAVSYFAipsvnEDSTFLSTQKDLISAGQGM--IDVQLLvvnrTDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEK 684
Cdd:PRK06188 319 PMVITYLR-----KRDHDPDDPKRLTSCGRPTpgLRVALL----DEDGREVAQGEVGEICVRGPLVMDGYWNrPEETAEA 389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589279984 685 FVMNWFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLV 762
Cdd:PRK06188 390 FRDGWL--------------------------HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAV 441
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
289-725 |
7.32e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 79.56 E-value: 7.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 289 AKKYPDKLCVIqsEQtNGIMEGPSKGRKTFTYGQIDKASNVIAHCLIQNGLKK--EEVVMVYAarSVEMVVCVMGILKAG 366
Cdd:PRK09274 16 AQERPDQLAVA--VP-GGRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRgmRAVLMVTP--SLEFFALTFALFKAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 367 GVFSVVDPAYPPNRQIVYLEVSNPKGLLVIEKAgELAKIVkdFIKDKLDLKILIP-SISLSSNGKEeYQDILEKYQNLSq 445
Cdd:PRK09274 91 AVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPKA-HLARRL--FGWGKPSVRRLVTvGGRLLWGGTT-LATLLRDGAAAP- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 446 tPTGIILGPDSPATLSFTSGSTGIPKGVKGRH-------YSLTHFFpwmskrfglnekskftmlsGIAHDpiQRDMFT-P 517
Cdd:PRK09274 166 -FPMADLAPDDMAAILFTSGSTGTPKGVVYTHgmfeaqiEALREDY-------------------GIEPG--EIDLPTfP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 518 LF------LGAELYVPTSD-------DigtPGRLAEWMDDCQVSVTHLTPA-MGQLLSAQATRQI--PSLLNAFFVGDVL 581
Cdd:PRK09274 224 LFalfgpaLGMTSVIPDMDptrpatvD---PAKLFAAIERYGVTNLFGSPAlLERLGRYGEANGIklPSLRRVISAGAPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 582 TKRDCTRLQH-LAKNVCIINMYGTTEtqravsyfAIP-SVNEDSTFLSTQKDLISAGQGM-----ID-VQLLVVNRTDRL 653
Cdd:PRK09274 301 PIAVIERFRAmLPPDAEILTPYGATE--------ALPiSSIESREILFATRAATDNGAGIcvgrpVDgVEVRIIAISDAP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 654 VP-------CAVGEMGEIYVRSGGLAEGYLD-PSATAE-KfvmnwfgqdlkredtLIGPAREHWfgirdrmYRSGDLGrY 724
Cdd:PRK09274 373 IPewddalrLATGEIGEIVVAGPMVTRSYYNrPEATRLaK---------------IPDGQGDVW-------HRMGDLG-Y 429
|
.
gi 589279984 725 L 725
Cdd:PRK09274 430 L 430
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
293-784 |
8.31e-15 |
|
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: 79.54 E-value: 8.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 293 PDKLCVI-QSEQTNGImegpskgrKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSV 371
Cdd:cd17634 67 GDRTAIIyEGDDTSQS--------RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 372 VDPAYPPNRQIVYLEVSNPKGLLVIEKAGELAKIV--KDFIKDKLDLKILIPS--ISLSSNGKE---------EYQDILE 438
Cdd:cd17634 139 IFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSVplKKNVDDALNPNVTSVEhvIVLKRTGSDidwqegrdlWWRDLIA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 439 KYQNLSQTptgIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPW-MSKRFGLNEKSKFTMLSGI----AHDPIqrd 513
Cdd:cd17634 219 KASPEHQP---EAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATtMKYVFDYGPGDIYWCTADVgwvtGHSYL--- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 514 MFTPLFLGAE--LY--VPtsdDIGTPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQI-----PSLLNAFFVGDVL--- 581
Cdd:cd17634 293 LYGPLACGATtlLYegVP---NWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIegtdrSSLRILGSVGEPInpe 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 582 TKRDCTRlqHLAKNVC-IINMYGTTETqravSYFAIPSVNEDSTFLSTqkdliSAGQGMIDVQLLVVNRTDRLVPCAvge 660
Cdd:cd17634 370 AYEWYWK--KIGKEKCpVVDTWWQTET----GGFMITPLPGAIELKAG-----SATRPVFGVQPAVVDNEGHPQPGG--- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 661 mgeiyvrsgglAEGYLDPSATAEKFVMNWFGQDLKREDTligparehWFGIRDRMYRSGDLGRYLPDGNVECTGRADDQI 740
Cdd:cd17634 436 -----------TEGNLVITDPWPGQTRTLFGDHERFEQT--------YFSTFKGMYFSGDGARRDEDGYYWITGRSDDVI 496
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 589279984 741 KIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFV 784
Cdd:cd17634 497 NVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVV 540
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
316-764 |
1.25e-14 |
|
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: 78.02 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 316 KTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVfSVvdPAYPpnrqivylevsnpkgllv 395
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAV-PV--PIYP------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 396 iekagelakivkdfikdkldlkilipsislsSNGKEEYQDILEKyqnlSQTPTGIILGPDSPATLSFTSGSTGIPKGVKG 475
Cdd:cd05907 63 -------------------------------TSSAEQIAYILND----SEAKALFVEDPDDLATIIYTSGTTGRPKGVML 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 476 RHYSLTHFFPWMSKRFGLNEKSKF-TMLSgIAHDPIQR-DMFTPLFLGAELYVPTSDDIGTPG-------------RLAE 540
Cdd:cd05907 108 SHRNILSNALALAERLPATEGDRHlSFLP-LAHVFERRaGLYVPLLAGARIYFASSAETLLDDlsevrptvflavpRVWE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 541 WMDDC--QVSVTHLTPAMGQLLSAQATRQIPS-------LLNAFFvgdvltkrdctrlqhLAKNVCIINMYGTTETQRAV 611
Cdd:cd05907 187 KVYAAikVKAVPGLKRKLFDLAVGGRLRFAASggaplpaELLHFF---------------RALGIPVYEGYGLTETSAVV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 612 SyfaipsVNEDSTFlstqkDLISAGQGMIDVQllvvnrtdrlvpCAVGEMGEIYVRSGGLAEGYL-DPSATAEKFVmnwf 690
Cdd:cd05907 252 T------LNPPGDN-----RIGTVGKPLPGVE------------VRIADDGEILVRGPNVMLGYYkNPEATAEALD---- 304
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 589279984 691 gqdlkredtligparehwfgiRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFR-IELGEIDTHLSRHPLVRE 764
Cdd:cd05907 305 ---------------------ADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKnISPEPIENALKASPLISQ 358
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
314-870 |
2.76e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 77.31 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 314 GRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVfsvvdpayppnrqIVYLEV--SNPK 391
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV-------------AVLLNTrlSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 392 GLLVIEKAGELAKIVKDFIKDKLDLKIlipSISLSSNGKEEYQDI-LEKYQNLSQTptgiilgpdspATLSFTSGSTGIP 470
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEAKLIPGI---SVKFAELMNGPKEEAeIQEEFDLDEV-----------ATIMYTSGTTGKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 471 KGVK---GRHyslthffpWMSKR-----FGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDigtPGRLAEWM 542
Cdd:PRK03640 157 KGVIqtyGNH--------WWSAVgsalnLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKFD---AEKINKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 543 DDCQVSVTHLTPAM-GQLLSAQATRQIPSLLNAFFVG----DVLTKRDCTRlqhlaKNVCIINMYGTTETqrAVSYFAIP 617
Cdd:PRK03640 226 QTGGVTIISVVSTMlQRLLERLGEGTYPSSFRCMLLGggpaPKPLLEQCKE-----KGIPVYQSYGMTET--ASQIVTLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 618 SvnEDStflstQKDLISAGQGMIDVQLLVVnrtDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFgqdlkr 696
Cdd:PRK03640 299 P--EDA-----LTKLGSAGKPLFPCELKIE---KDGVVVPPFEEGEIVVKGPNVTKGYLNrEDATRETFQDGWF------ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 697 edtligparehwfgirdrmyRSGDLGrYL-PDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDE 775
Cdd:PRK03640 363 --------------------KTGDIG-YLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKW 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 776 EKVLVSYFVpindnLEGLISESdnpqddeeveeeeenekdlkmemlrgvrryrrlikDIREYLRKKLPSYAVPSVYFPLS 855
Cdd:PRK03640 422 GQVPVAFVV-----KSGEVTEE-----------------------------------ELRHFCEEKLAKYKVPKRFYFVE 461
|
570
....*....|....*
gi 589279984 856 KLPLNPNGKVDKPKL 870
Cdd:PRK03640 462 ELPRNASGKLLRHEL 476
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
281-867 |
4.20e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 73.66 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIQSEqtngimegpskgrKTFTYGQIDKASNVIAHCLIQNGlKKEEVVMVYAARSVEMVVCVM 360
Cdd:PRK07638 3 ITKEYKKHASLQPNKIAIKEND-------------RVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPPNRQIVYLEVSNPkGLLVIEkagelakivkDFIKDKLDlKILIPSISLssngkEEYQDILEKY 440
Cdd:PRK07638 69 GAAMAGWTCVPLDIKWKQDELKERLAISNA-DMIVTE----------RYKLNDLP-DEEGRVIEI-----DEWKRMIEKY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 441 qnlSQTPTGIILGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFL 520
Cdd:PRK07638 132 ---LPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 521 GAELYV-PTSddigTPGRLAEWMDDCQVSVTHLTPAMGQ-LLSAQATRQIPslLNAFFVGDVLTKRDCTRLQHLAKNVCI 598
Cdd:PRK07638 209 GQTVHLmRKF----IPNQVLDKLETENISVMYTVPTMLEsLYKENRVIENK--MKIISSGAKWEAEAKEKIKNIFPYAKL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 599 INMYGTTETQravsyFAIPSVNEDSTFLSTqkdliSAGQGMIDVQLLVVNRTDrlVPCAVGEMGEIYVRSGGLAEGYLDP 678
Cdd:PRK07638 283 YEFYGASELS-----FVTALVDEESERRPN-----SVGRPFHNVQVRICNEAG--EEVQKGEIGTVYVKSPQFFMGYIIG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 679 SATAEKfvmnwfgqdlkredtligPAREHWFGIRdrmyrsgDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSR 758
Cdd:PRK07638 351 GVLARE------------------LNADGWMTVR-------DVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHE 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 759 HPLVRENVTlvrrdkdeekvlvsyfVPINDNLEGLISESdnpqddeeveeeeenekdlkmeMLRGvrryRRLIKDIREYL 838
Cdd:PRK07638 406 HPAVDEIVV----------------IGVPDSYWGEKPVA----------------------IIKG----SATKQQLKSFC 443
|
570 580
....*....|....*....|....*....
gi 589279984 839 RKKLPSYAVPSVYFPLSKLPLNPNGKVDK 867
Cdd:PRK07638 444 LQRLSSFKIPKEWHFVDEIPYTNSGKIAR 472
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
281-867 |
7.49e-13 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 73.00 E-value: 7.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIQSEQtngimegpskgRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVTAD-----------RIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLV-IEKAGELAKIVKDFikdkLDLKILIPSISLSSNGK-EEYQDILE 438
Cdd:PRK05852 87 AASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIdADGPHDRAEPTTRW----WPLTVNVGGDSGPSGGTlSVHLDAAT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 439 KYQNLSQTPTGiiLGPDSpATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAH-DPIQRDMFTP 517
Cdd:PRK05852 163 EPTPATSTPEG--LRPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHgHGLIAALLAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 518 LFLGAELYVPTSddigtpGRLAE---WMDDCQVSVTHLT--PAMGQ-LLSAQATRQIPSLLNAF-FVGDV---LTKRDCT 587
Cdd:PRK05852 240 LASGGAVLLPAR------GRFSAhtfWDDIKAVGATWYTavPTIHQiLLERAATEPSGRKPAALrFIRSCsapLTAETAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 588 RLQH--LAKNVCiinMYGTTETQRAVSYFAIPSVNEDSTFLSTQkDLISAGQGmidVQLLVVnRTDRLvPCAVGEMGEIY 665
Cdd:PRK05852 314 ALQTefAAPVVC---AFGMTEATHQVTTTQIEGIGQTENPVVST-GLVGRSTG---AQIRIV-GSDGL-PLPAGAVGEVW 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 666 VRSGGLAEGYL-DPSATAEKFVMNWFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRG 744
Cdd:PRK05852 385 LRGTTVVRGYLgDPTITAANFTDGWL--------------------------RTGDLGSLSAAGDLSIRGRIKELINRGG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 745 FRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPindnlegliSESDNPQDDeeveeeeenekdlkmemlrgv 824
Cdd:PRK05852 439 EKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVP---------RESAPPTAE--------------------- 488
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 589279984 825 rryrrlikDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDK 867
Cdd:PRK05852 489 --------ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
318-867 |
1.11e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 71.78 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 318 FTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKglLVIE 397
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGAR--LVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 398 KAGELAKIVKDfikdkldlkilipsislssngkeeyqdilekyqnlsqtptgiilgpdsPATLSFTSGSTGIPKGVKGRH 477
Cdd:cd05973 79 DAANRHKLDSD------------------------------------------------PFVMMFTSGTTGLPKGVPVPL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 478 YSLTHFFPWMSKRFGLNEKSKFTMLSgiahDP-----IQRDMFTPLFLGaelyVPTSDDIGTPGRLAEWMDDCQVSVTHL 552
Cdd:cd05973 111 RALAAFGAYLRDAVDLRPEDSFWNAA----DPgwaygLYYAITGPLALG----HPTILLEGGFSVESTWRVIERLGVTNL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 553 T--PAMGQLLSAQ----ATRQIPSLLNAFFVGDVLTKrDCTRLQHLAKNVCIINMYGTTEtqravsyFAIPSVNEDStfL 626
Cdd:cd05973 183 AgsPTAYRLLMAAgaevPARPKGRLRRVSSAGEPLTP-EVIRWFDAALGVPIHDHYGQTE-------LGMVLANHHA--L 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 627 STQKDLISAGQGMIDVQLLVVN-RTDRLVPcavGEMGEIYvrsgglaegyLDPSATAekfvMNWF-GQDLKREDTLIGpa 704
Cdd:cd05973 253 EHPVHAGSAGRAMPGWRVAVLDdDGDELGP---GEPGRLA----------IDIANSP----LMWFrGYQLPDTPAIDG-- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 705 reHWfgirdrmYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDkDEEKVLVSYFV 784
Cdd:cd05973 314 --GY-------YLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPD-PERTEVVKAFV 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 785 PINDNLEGlisesdNPQddeeveeeeenekdlkmemlrgvrryrrLIKDIREYLRKKLPSYAVP-SVYFpLSKLPLNPNG 863
Cdd:cd05973 384 VLRGGHEG------TPA----------------------------LADELQLHVKKRLSAHAYPrTIHF-VDELPKTPSG 428
|
....
gi 589279984 864 KVDK 867
Cdd:cd05973 429 KIQR 432
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
454-762 |
1.49e-12 |
|
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: 70.97 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 454 PDSPATLSFTSGSTGIPKGVKGRHYSLThFFPWMSKRFGLNeKSKFTMLSGI------AHDPIqrdMFTPLFLGAELYVP 527
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEV-YNAWMLALNSLF-DPDDVLLCGLplfhvnGSVVT---LLTPLASGAHVVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 528 TSDDIGTPGRLAE-WMDDCQVSVTHLT---PAMGQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKnVCIINMYG 603
Cdd:cd05944 76 GPAGYRNPGLFDNfWKLVERYRITSLStvpTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATG-LPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 604 TTETQRAVSyfaipsVNedstFLSTQKDLISAGQGM--IDVQLLVVNRTDRLV-PCAVGEMGEIYVRSGGLAEGYLDpsa 680
Cdd:cd05944 155 LTEATCLVA------VN----PPDGPKRPGSVGLRLpyARVRIKVLDGVGRLLrDCAPDEVGEICVAGPGVFGGYLY--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 681 taekfvmnwfgQDLKREdtligpareHWfgIRDRMYRSGDLGRYLPDGNVECTGRADDQIkIR-GFRIELGEIDTHLSRH 759
Cdd:cd05944 222 -----------TEGNKN---------AF--VADGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRH 278
|
...
gi 589279984 760 PLV 762
Cdd:cd05944 279 PAV 281
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
281-762 |
1.59e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 71.84 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIQseqtngimegpskGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:PRK07798 5 IADLFEAVADAVPDRVALVC-------------GDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAML 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPPNrQIVYL-EVSNPKGLLViekAGELAKIVKDfIKDKLD-LKILI----PSISLSSNGKEEYQ 434
Cdd:PRK07798 72 GAFKARAVPVNVNYRYVED-ELRYLlDDSDAVALVY---EREFAPRVAE-VLPRLPkLRTLVvvedGSGNDLLPGAVDYE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 435 DILEkyqnlsQTPTGIILGPDSPATLSF--TSGSTGIPKGVKGRHyslthffpwmskrfglnekskftmlsgiahdpiqR 512
Cdd:PRK07798 147 DALA------AGSPERDFGERSPDDLYLlyTGGTTGMPKGVMWRQ----------------------------------E 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 513 DMFTPLFLGAELYvpTSDDIGTPGRLAEWMDDCQVSVT-------H---LTPAMGQLLSAQATRQIPSL-LNA------- 574
Cdd:PRK07798 187 DIFRVLLGGRDFA--TGEPIEDEEELAKRAAAGPGMRRfpapplmHgagQWAAFAALFSGQTVVLLPDVrFDAdevwrti 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 575 --------FFVGDVLTK-----------RDCTRLQHLA------------------KNVCIINMYGTTETqrAVSYFAIP 617
Cdd:PRK07798 265 erekvnviTIVGDAMARplldaleargpYDLSSLFAIAsggalfspsvkeallellPNVVLTDSIGSSET--GFGGSGTV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 618 SVNEDSTFLSTQKdlisagqgmIDVQLLVVNRTDRLVPCAVGEMGEIyVRSGGLAEGYL-DPSATAEKFvmnwfgqdlkR 696
Cdd:PRK07798 343 AKGAVHTGGPRFT---------IGPRTVVLDEDGNPVEPGSGEIGWI-ARRGHIPLGYYkDPEKTAETF----------P 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589279984 697 EdtligparehwfgIRDRMYR-SGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLV 762
Cdd:PRK07798 403 T-------------IDGVRYAiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDV 456
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
313-870 |
2.43e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 71.35 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 313 KGRKTfTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVfsvvdpAYPPNRQIVYLEVS---N 389
Cdd:PRK07786 39 LGNTT-TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI------AVPVNFRLTPPEIAflvS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 390 PKGLLVIEKAGELAKIVKDFIKDKLDLKILIPSISLSSNGKEEYQDILEKyqnLSQTPTGIILGPDSPATLSFTSGSTGI 469
Cdd:PRK07786 112 DCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAE---AGPAHAPVDIPNDSPALIMYTSGTTGR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 470 PKGVKGRH-----YSLTHFFPWmskRFGLNEKSKFtMLSGIAHDPIQRDMFTPLFLGAE--LYVPTSDDigtPGRLAEWM 542
Cdd:PRK07786 189 PKGAVLTHanltgQAMTCLRTN---GADINSDVGF-VGVPLFHIAGIGSMLPGLLLGAPtvIYPLGAFD---PGQLLDVL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 543 DDCQVSVTHLTPAMGQLLSAQATRQiPSLLNAFFVGDVLTKRDCTRLQHLAK---NVCIINMYGTTEtqraVSYFAIPSV 619
Cdd:PRK07786 262 EAEKVTGIFLVPAQWQAVCAEQQAR-PRDLALRVLSWGAAPASDTLLRQMAAtfpEAQILAAFGQTE----MSPVTCMLL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 620 NEDSTflstqKDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPSATAEKFVMNWFgqdlkred 698
Cdd:PRK07786 337 GEDAI-----RKLGSVGKVIPTVAARVVDENMNDVP--VGEVGEIVYRAPTLMSGYWnNPEATAEAFAGGWF-------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 699 tligparehwfgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKV 778
Cdd:PRK07786 402 ------------------HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 779 LVSYFVPINDNleglisesdnpqddeeveeeeeneKDLKMEmlrgvrryrrlikDIREYLRKKLPSYAVPSVYFPLSKLP 858
Cdd:PRK07786 464 PVAVAAVRNDD------------------------AALTLE-------------DLAEFLTDRLARYKHPKALEIVDALP 506
|
570
....*....|..
gi 589279984 859 LNPNGKVDKPKL 870
Cdd:PRK07786 507 RNPAGKVLKTEL 518
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
454-870 |
5.43e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 68.84 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 454 PDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSK----------FTMLSGI---------------AHD 508
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRlcipvplfhcFGSVLGVlaclthgatmvfpspSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 509 P------IQRDMFTPLFlGaelyVPTS--DDIGTPgrlaewmDDCQVSVTHL-TPAM-GQLLSAQATRQIPSLLNAffvg 578
Cdd:cd05917 81 PlavleaIEKEKCTALH-G----VPTMfiAELEHP-------DFDKFDLSSLrTGIMaGAPCPPELMKRVIEVMNM---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 579 dvltkrdctrlqhlaKNVCIInmYGTTETQrAVSYFAIPsvnEDSTFlstqKDLISAGQGMIDVQLLVVNRTDRLVPcAV 658
Cdd:cd05917 145 ---------------KDVTIA--YGMTETS-PVSTQTRT---DDSIE----KRVNTVGRIMPHTEAKIVDPEGGIVP-PV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 659 GEMGEIYVRSGGLAEGYL-DPSATAEKfvmnwfgqdlkredtlIGparehwfgiRDRMYRSGDLGRYLPDGNVECTGRAD 737
Cdd:cd05917 199 GVPGELCIRGYSVMKGYWnDPEKTAEA----------------ID---------GDGWLHTGDLAVMDEDGYCRIVGRIK 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 738 DQIkIRGFR-IELGEIDTHLSRHPLVRE-NVTLVRRDKDEEKVLVsyFVPINDNLEglISESdnpqddeeveeeeenekd 815
Cdd:cd05917 254 DMI-IRGGEnIYPREIEEFLHTHPKVSDvQVVGVPDERYGEEVCA--WIRLKEGAE--LTEE------------------ 310
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 589279984 816 lkmemlrgvrryrrlikDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd05917 311 -----------------DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
642-788 |
7.05e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 69.63 E-value: 7.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 642 VQLLVVNRTDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFvmnwfgqdlkREDTligparehWFgirdrmyRSGD 720
Cdd:PRK07787 302 VETRLVDEDGGPVPHDGETVGELQVRGPTLFDGYLNrPDATAAAF----------TADG--------WF-------RTGD 356
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589279984 721 LGRYLPDGNVECTGR-ADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIND 788
Cdd:PRK07787 357 VAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD 425
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
456-867 |
9.82e-12 |
|
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: 67.82 E-value: 9.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 456 SPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYVPTSDDigtP 535
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFN---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 536 GRLAEWMDDCQVSVTHLTPAMGQLLsAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTEtQRAVSYfa 615
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQAL-ARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSE-LSFITY-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 616 ipSVNEDStflstqKDLISAGQGMIDVQLLVVNRTDrlvpcavGEMGEIYVRSGGLAEGYLDPSATAEkfvmnwfgqdlk 695
Cdd:cd17633 154 --NFNQES------RPPNSVGRPFPNVEIEIRNADG-------GEIGKIFVKSEMVFSGYVRGGFSNP------------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 696 redtligparehwfgirDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTlvrrdkde 775
Cdd:cd17633 207 -----------------DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIV-------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 776 ekvlvsyfVPINDNLEG----LISESDNPQDdeeveeeeenekdlkmemlrgvrryrrliKDIREYLRKKLPSYAVPSVY 851
Cdd:cd17633 262 --------VGIPDARFGeiavALYSGDKLTY-----------------------------KQLKRFLKQKLSRYEIPKKI 304
|
410
....*....|....*.
gi 589279984 852 FPLSKLPLNPNGKVDK 867
Cdd:cd17633 305 IFVDSLPYTSSGKIAR 320
|
|
| PRK07201 |
PRK07201 |
SDR family oxidoreductase; |
1014-1266 |
1.08e-11 |
|
SDR family oxidoreductase;
Pssm-ID: 235962 [Multi-domain] Cd Length: 657 Bit Score: 69.59 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1014 TVFLTGATGFLGGFILNDLLTNRssRIKKVICLVRSSSLEKGQErlinsctLLGIWNpswlsENKLEIIIGDLSKPQFDL 1093
Cdd:PRK07201 2 RYFVTGGTGFIGRRLVSRLLDRR--REATVHVLVRRQSLSRLEA-------LAAYWG-----ADRVVPLVGDLTEPGLGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1094 SSKSWDYLSKeTDAILHNGAIVHWVYPYEKLKPTNVLSTLECLKLC--CQGGkmkSFTFVSSTSVLdtegfikksdeelq 1171
Cdd:PRK07201 68 SEADIAELGD-IDHVVHLAAIYDLTADEEAQRAANVDGTRNVVELAerLQAA---TFHHVSSIAVA-------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1172 nGN-DGLREDDDLEQGkKGLVTGYGQSKWVAEKLIMmaQNNGLRGWIVRPGYVMGDSKSAVTNTDDFIWRMVKGCLQLGL 1250
Cdd:PRK07201 130 -GDyEGVFREDDFDEG-QGLPTPYHRTKFEAEKLVR--EECGLPWRVYRPAVVVGDSRTGEMDKIDGPYYFFKVLAKLAK 205
|
250 260
....*....|....*....|...
gi 589279984 1251 IPDI-------NNSINLVPVDHV 1266
Cdd:PRK07201 206 LPSWlpmvgpdGGRTNIVPVDYV 228
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
287-870 |
1.14e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 69.12 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 287 ANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQI-DKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKA 365
Cdd:PRK06839 10 KRAYLHPDRIAIITEEEE-------------MTYKQLhEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 366 GGVFSVVDPAYPPNRQIVYLEVSnpkGLLVIEKAGELAKIVKDfIKDKLDLKILIPSISLSSNGKEEYQDILEKyqnlsq 445
Cdd:PRK06839 77 ECIAVPLNIRLTENELIFQLKDS---GTTVLFVEKTFQNMALS-MQKVSYVQRVISITSLKEIEDRKIDNFVEK------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 446 tptgiilGPDSPATLSFTSGSTGIPKGVKGRHYSLthFFPWMSKRFGLN---EKSKFTMLSGIAHDPIQRDMFTPLFLGA 522
Cdd:PRK06839 147 -------NESASFIICYTSGTTGKPKGAVLTQENM--FWNALNNTFAIDltmHDRSIVLLPLFHIGGIGLFAFPTLFAGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 523 ELYVPTSDDigtPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQIPSL--LNAFFVGDVLTKRDCTRlQHLAKNVCIIN 600
Cdd:PRK06839 218 VIIVPRKFE---PTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLqsVRWFYNGGAPCPEELMR-EFIDRGFLFGQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 601 MYGTTETQRAVSYFAipsvNEDStflstQKDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYLD-PS 679
Cdd:PRK06839 294 GFGMTETSPTVFMLS----EEDA-----RRKVGSIGKPVLFCDYELIDENKNKVE--VGEVGELLIRGPNVMKEYWNrPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 680 ATAEKfvmnwfgqdlkredtligparehwfgIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRH 759
Cdd:PRK06839 363 ATEET--------------------------IQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 760 PLVRENVTLVRRDKDEEKVLVSYFVPINDnleGLISEsdnpqddeeveeeeenekdlkmemlrgvrryrrliKDIREYLR 839
Cdd:PRK06839 417 SDVYEVAVVGRQHVKWGEIPIAFIVKKSS---SVLIE-----------------------------------KDVIEHCR 458
|
570 580 590
....*....|....*....|....*....|.
gi 589279984 840 KKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:PRK06839 459 LFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
455-870 |
1.36e-11 |
|
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: 68.14 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 455 DSPATLSFTSGSTGIPKGVK---GRHyslthffpWMSKR-----FGLNEKSKFTMLSGIAHDPIQRDMFTPLFLGAELYV 526
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQqtfGNH--------WWSAIgsalnLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 527 PTSDDigtPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQIPSLLNAFFVGDvlTKRDCTRL-QHLAKNVCIINMYGTT 605
Cdd:cd05912 149 VDKFD---AEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILLGG--GPAPKPLLeQCKEKGIPVYQSYGMT 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 606 ETQRAVSYFAIpsvnEDStflstQKDLISAGQGMIDVQLLVVNRTDRLvpcavGEMGEIYVRSGGLAEGYLD-PSATAEK 684
Cdd:cd05912 224 ETCSQIVTLSP----EDA-----LNKIGSAGKPLFPVELKIEDDGQPP-----YEVGEILLKGPNVTKGYLNrPDATEES 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 685 FVMNWFgqdlkredtligparehwfgirdrmyRSGDLGrYL-PDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVR 763
Cdd:cd05912 290 FENGWF--------------------------KTGDIG-YLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 764 ENVTLVRRDKDEEKVLVSYFVpindnLEGLISESdnpqddeeveeeeenekdlkmemlrgvrryrrlikDIREYLRKKLP 843
Cdd:cd05912 343 EAGVVGIPDDKWGQVPVAFVV-----SERPISEE-----------------------------------ELIAYCSEKLA 382
|
410 420
....*....|....*....|....*..
gi 589279984 844 SYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:cd05912 383 KYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| AR_SDR_e |
cd05227 |
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ... |
1014-1246 |
1.96e-11 |
|
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: 66.52 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1014 TVFLTGATGFLGGFILNDLLTNrssrIKKVICLVRSSSLEKGQERLInsctllgiwnPSWLSENKLEI-IIGDLSKPQfd 1092
Cdd:cd05227 1 LVLVTGATGFIASHIVEQLLKA----GYKVRGTVRSLSKSAKLKALL----------KAAGYNDRLEFvIVDDLTAPN-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1093 lsskSWDYLSKETDAILHNGAIVHWV---YPYEKLKPTnVLSTLECLKLCCQGGKMKSFTFVSST-SVLDTEGFIKKsde 1168
Cdd:cd05227 65 ----AWDEALKGVDYVIHVASPFPFTgpdAEDDVIDPA-VEGTLNVLEAAKAAGSVKRVVLTSSVaAVGDPTAEDPG--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1169 elqngnDGLREDD--DLEQGKKGLVTGYGQSKWVAEKLI--MMAQNNGlrGW---IVRPGYVMGDSKSA--VTNTDDFIW 1239
Cdd:cd05227 137 ------KVFTEEDwnDLTISKSNGLDAYIASKTLAEKAAweFVKENKP--KFeliTINPGYVLGPSLLAdeLNSSNELIN 208
|
....*..
gi 589279984 1240 RMVKGCL 1246
Cdd:cd05227 209 KLLDGKL 215
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
281-685 |
2.25e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 68.53 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIQSEQTNGIMEGpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:PRK12582 51 IPHLLAKWAAEAPDRPWLAQREPGHGQWRK-------VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPPNRQ----IVYL-EVSNPkGLLVIEKAGELAKIVKdfIKDKLDLKILIPSISLSSNGKEEYQD 435
Cdd:PRK12582 124 AAMQAGVPAAPVSPAYSLMSHdhakLKHLfDLVKP-RVVFAQSGAPFARALA--ALDLLDVTVVHVTGPGEGIASIAFAD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 436 IlekyqnLSQTPTGII------LGPDSPATLSFTSGSTGIPKGVKGRHYSLT----------------------HFFPWm 487
Cdd:PRK12582 201 L------AATPPTAAVaaaiaaITPDTVAKYLFTSGSTGMPKAVINTQRMMCaniamqeqlrprepdppppvslDWMPW- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 488 skrfglneksKFTMLSGIAHDPIqrdmftpLFLGAELYVptsdDIG--TPGRLAEWMDDC-QVSVTHL--TPAMGQLLsA 562
Cdd:PRK12582 274 ----------NHTMGGNANFNGL-------LWGGGTLYI----DDGkpLPGMFEETIRNLrEISPTVYgnVPAGYAML-A 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 563 QATRQIPSLLNAFFV--------GDVLTKRDCTRLQHLA-----KNVCIINMYGTTETQRAVSyfaipsvnedSTFLSTQ 629
Cdd:PRK12582 332 EAMEKDDALRRSFFKnlrlmaygGATLSDDLYERMQALAvrttgHRIPFYTGYGATETAPTTT----------GTHWDTE 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 589279984 630 KDLIsAGQGMIDVQLlvvnrtdRLVPcaVGEMGEIYVRSGGLAEGYL-DPSATAEKF 685
Cdd:PRK12582 402 RVGL-IGLPLPGVEL-------KLAP--VGDKYEVRVKGPNVTPGYHkDPELTAAAF 448
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
643-870 |
2.63e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 67.95 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 643 QLLVVN-RTDRLVPCAVGEMGEIYVRSGGLAEGYL-DPSATAEKFVMNWFgqdlkredtligparehwfgirdrmyRSGD 720
Cdd:PLN02479 383 GLDVVDtKTMKPVPADGKTMGEIVMRGNMVMKGYLkNPKANEEAFANGWF--------------------------HSGD 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 721 LGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVREnVTLVRRDKDEEKVLVSYFVPINDNLEGliseSDNP 800
Cdd:PLN02479 437 LGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLE-ASVVARPDERWGESPCAFVTLKPGVDK----SDEA 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 589279984 801 qddeeveeeeenekdlkmemlrgvrryrRLIKDIREYLRKKLPSYAVP-SVYFplSKLPLNPNGKVDKPKL 870
Cdd:PLN02479 512 ----------------------------ALAEDIMKFCRERLPAYWVPkSVVF--GPLPKTATGKIQKHVL 552
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
318-762 |
4.42e-11 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 67.11 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 318 FTYGQI-DKASNVIAHcLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVfSVvdPAYP---PNRQIVYLEVSNPKGL 393
Cdd:cd05932 7 FTWGEVaDKARRLAAA-LRALGLEPGSKIALISKNCAEWFITDLAIWMAGHI-SV--PLYPtlnPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 394 LViekaGELA--KIVKDFIKDKLDLKILIPSISLssNGKEEYQDILEKYQNLSQTPTGiilGPDSPATLSFTSGSTGIPK 471
Cdd:cd05932 83 FV----GKLDdwKAMAPGVPEGLISISLPPPSAA--NCQYQWDDLIAQHPPLEERPTR---FPEQLATLIYTSGTTGQPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 472 GVKGRHYSLTHFFPWMSKRFGLNEKSKftMLS--GIAHdpIQRDMF---TPLFLGAELYVPTSDDigtpgrlaEWMDDCQ 546
Cdd:cd05932 154 GVMLTFGSFAWAAQAGIEHIGTEENDR--MLSylPLAH--VTERVFvegGSLYGGVLVAFAESLD--------TFVEDVQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 547 VSVTHL---TPAMGQLLSAQATRQIPS-----LLNAFFVGDVLTKR-------DCTRL----------------QHLAKN 595
Cdd:cd05932 222 RARPTLffsVPRLWTKFQQGVQDKIPQqklnlLLKIPVVNSLVKRKvlkglglDQCRLagcgsapvppallewyRSLGLN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 596 VCiiNMYGTTETQrAVSYFAIPSVNEDSTflstqkdlisAGQGMIDVQLlvvnrtdrlvpcAVGEMGEIYVRSGGLAEG- 674
Cdd:cd05932 302 IL--EAYGMTENF-AYSHLNYPGRDKIGT----------VGNAGPGVEV------------RISEDGEILVRSPALMMGy 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 675 YLDPSATAEKFVmnwfgqdlkredtligparehwfgiRDRMYRSGDLGRYLPDGNVECTGRADDQIKI-RGFRIELGEID 753
Cdd:cd05932 357 YKDPEATAEAFT-------------------------ADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIE 411
|
....*....
gi 589279984 754 THLSRHPLV 762
Cdd:cd05932 412 NKLAEHDRV 420
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
453-762 |
4.73e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 67.29 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 453 GPDSPATLSFTSGSTGIPKGVKGRHYSLThFFPWMSKRFgLNEKSKFTMLSGIahdPiqrdMF----------TPLFLGA 522
Cdd:PRK07529 211 GPDDVAAYFHTGGTTGMPKLAQHTHGNEV-ANAWLGALL-LGLGPGDTVFCGL---P----LFhvnallvtglAPLARGA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 523 ELYVPTSD---DIGTPGRLAEWMDDCQVSVTHLTP-AMGQLLsaqatrQIP------SLLNAFFVG------DVLTkrdc 586
Cdd:PRK07529 282 HVVLATPQgyrGPGVIANFWKIVERYRINFLSGVPtVYAALL------QVPvdghdiSSLRYALCGaaplpvEVFR---- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 587 tRLQHlAKNVCIINMYGTTETQRAVSyfaipsVNedstFLSTQKDLISAGQGMIDVQLLVVNRTD---RLVPCAVGEMGE 663
Cdd:PRK07529 352 -RFEA-ATGVRIVEGYGLTEATCVSS------VN----PPDGERRIGSVGLRLPYQRVRVVILDDagrYLRDCAVDEVGV 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 664 IYVRSGGLAEGYLDPSataekfvmnwfgQDlkredtligpaREHWFGirDRMYRSGDLGRYLPDGNVECTGRADDQIkIR 743
Cdd:PRK07529 420 LCIAGPNVFSGYLEAA------------HN-----------KGLWLE--DGWLNTGDLGRIDADGYFWLTGRAKDLI-IR 473
|
330 340
....*....|....*....|
gi 589279984 744 -GFRIELGEIDTHLSRHPLV 762
Cdd:PRK07529 474 gGHNIDPAAIEEALLRHPAV 493
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
281-870 |
4.99e-11 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 67.09 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIQSEQTngimegpskgrktFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLVFGGTR-------------WTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAY--PPNRQIvyLEVSNPKgLLVIEKAGeLAKIvkdfikDKLDLKIL-IPSISLSSNGKEEYQDIL 437
Cdd:PRK06155 90 GCAWLGAIAVPINTALrgPQLEHI--LRNSGAR-LLVVEAAL-LAAL------EAADPGDLpLPAVWLLDAPASVSVPAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 438 EKYQNLSQTPTGII---LGPDSPATLSFTSGSTGIPKGVKGRHyslTHFFPW---MSKRFGLNEKSK-FTMLSgIAHDPI 510
Cdd:PRK06155 160 WSTAPLPPLDAPAPaaaVQPGDTAAILYTSGTTGPSKGVCCPH---AQFYWWgrnSAEDLEIGADDVlYTTLP-LFHTNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 511 QRDMFTPLFLGAELYV-PTSDDIGTPGRLAEwmddCQVSVTHLTPAMGQLLSAQATRQ---------------IPSLLNA 574
Cdd:PRK06155 236 LNAFFQALLAGATYVLePRFSASGFWPAVRR----HGATVTYLLGAMVSILLSQPAREsdrahrvrvalgpgvPAALHAA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 575 FFvgdvltkrdcTRLqhlakNVCIINMYGTTETQrAVSYFAIPSVNEDStflstqkdlisAGQGMIDVQLLVVNRTDRLV 654
Cdd:PRK06155 312 FR----------ERF-----GVDLLDGYGSTETN-FVIAVTHGSQRPGS-----------MGRLAPGFEARVVDEHDQEL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 655 PcaVGEMGEIYVRS---GGLAEGYL-DPSATAEKfvmnWfgQDLkredtligparehWFGIRDRMYRSgdlgrylPDGNV 730
Cdd:PRK06155 365 P--DGEPGELLLRAdepFAFATGYFgMPEKTVEA----W--RNL-------------WFHTGDRVVRD-------ADGWF 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 731 ECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE-NVTLVRRDKDEEKVLVSYFVPindnlEGlisESDNPQddeeveee 809
Cdd:PRK06155 417 RFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAaAVFPVPSELGEDEVMAAVVLR-----DG---TALEPV-------- 480
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 589279984 810 eenekdlkmemlrgvrryrrlikDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:PRK06155 481 -----------------------ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
317-493 |
5.39e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 67.23 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 317 TFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLVI 396
Cdd:PRK04319 73 KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 397 EKAgeLAKIVkdfiKDKL-DLK-ILIPSISLSSNGKeeYQDILEKYQNLSQTPTGIILGPDSPATLSFTSGSTGIPKGVK 474
Cdd:PRK04319 153 PAL--LERKP----ADDLpSLKhVLLVGEDVEEGPG--TLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVL 224
|
170 180
....*....|....*....|
gi 589279984 475 GRHYS-LTHffpWMSKRFGL 493
Cdd:PRK04319 225 HVHNAmLQH---YQTGKYVL 241
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
279-870 |
5.45e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 67.11 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 279 GAIPDIFSANAKKYPDKLCVIQSEQTngimegpskgrKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVC 358
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRHQA-----------LRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 359 VMGILKAGGVFSVVDPAYpPNRQIVY-LEVSNPKGLLVI---------EKAGELAKIVKDFIKDKL---DLKILIPSISL 425
Cdd:PRK12583 87 QFATARIGAILVNINPAY-RASELEYaLGQSGVRWVICAdafktsdyhAMLQELLPGLAEGQPGALaceRLPELRGVVSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 426 SSN---GKEEYQDILEKYQNLSQTPTGII---LGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSK- 498
Cdd:PRK12583 166 APApppGFLAWHELQARGETVSREALAERqasLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 499 ---------FTM----LSGIAHdpiqrdmftplflGAELYVPTS--DDIGTPGRLAEwmDDCqvSVTHLTPAM--GQLLS 561
Cdd:PRK12583 246 cvpvplyhcFGMvlanLGCMTV-------------GACLVYPNEafDPLATLQAVEE--ERC--TALYGVPTMfiAELDH 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 562 AQATR-QIPSLLNAFFVGDV----LTKRDCTRLqHLAKnvcIINMYGTTETQravsyfaiPSVNEDSTFLSTQKDLISAG 636
Cdd:PRK12583 309 PQRGNfDLSSLRTGIMAGAPcpieVMRRVMDEM-HMAE---VQIAYGMTETS--------PVSLQTTAADDLERRVETVG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 637 QGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPSATAEkfvmnwfgqdlkredtliGPAREHWfgirdrM 715
Cdd:PRK12583 377 RTQPHLEVKVVDPDGATVP--RGEIGELCTRGYSVMKGYWnNPEATAE------------------SIDEDGW------M 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 716 YrSGDLGRYLPDGNVECTGRADDQIkIRGFR-IELGEIDTHLSRHPLVRE-NVTLVRRDKDEEKVLVsyFVPINdnlEGL 793
Cdd:PRK12583 431 H-TGDLATMDEQGYVRIVGRSKDMI-IRGGEnIYPREIEEFLFTHPAVADvQVFGVPDEKYGEEIVA--WVRLH---PGH 503
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589279984 794 ISESDnpqddeeveeeeenekdlkmemlrgvrryrrlikDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:PRK12583 504 AASEE----------------------------------ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRM 546
|
|
| AR_FR_like_1_SDR_e |
cd05228 |
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ... |
1015-1266 |
7.10e-11 |
|
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: 65.38 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1015 VFLTGATGFLGGFILNDLLTnRSSRIKkviCLVRSSSlekgqerlinsctllgiwNPSWLSENKLEIIIGDLSKPQfdls 1094
Cdd:cd05228 1 ILVTGATGFLGSNLVRALLA-QGYRVR---ALVRSGS------------------DAVLLDGLPVEVVEGDLTDAA---- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1095 skSWDYLSKETDAILHNGAIVHWVYPYEK-LKPTNVLSTLECLKLCCQGGkMKSFTFVSSTSVLdtegfikksdeelqNG 1173
Cdd:cd05228 55 --SLAAAMKGCDRVFHLAAFTSLWAKDRKeLYRTNVEGTRNVLDAALEAG-VRRVVHTSSIAAL--------------GG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1174 NDGLREDDDLEQGKKGLVTGYGQSKWVAEKLIMMAQNNGLRGWIVRPGYVMGDSKSAVTNTDDFIWRMVKGCLQlGLIPD 1253
Cdd:cd05228 118 PPDGRIDETTPWNERPFPNDYYRSKLLAELEVLEAAAEGLDVVIVNPSAVFGPGDEGPTSTGLDVLDYLNGKLP-AYPPG 196
|
250
....*....|...
gi 589279984 1254 innSINLVPVDHV 1266
Cdd:cd05228 197 ---GTSFVDVRDV 206
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
309-768 |
1.06e-10 |
|
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: 66.36 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 309 EGPSKGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVS 388
Cdd:cd05968 83 EGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 389 NPKGLLVIEKAGELAKIVKdfIKDKLDL---------KILIPSISLSSNGKEEYQDILEKYQNLSQTPTGIILGPDSPAT 459
Cdd:cd05968 163 EAKALITADGFTRRGREVN--LKEEADKacaqcptveKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGAERTESEDPLM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 460 LSFTSGSTGIPKGVKGRHYSlthfFPW-----MSKRFGLNEKSKFTMLS--GIAHDPIQrdMFTPLFLGAE--LY--VPT 528
Cdd:cd05968 241 IIYTSGTTGKPKGTVHVHAG----FPLkaaqdMYFQFDLKPGDLLTWFTdlGWMMGPWL--IFGGLILGATmvLYdgAPD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 529 SDDigtPGRLAEWMDDCQvsVTHLTpamgqlLSaqatrqiPSLLNAF--FVGDVLTKRDCTRLQHLAK------------ 594
Cdd:cd05968 315 HPK---ADRLWRMVEDHE--ITHLG------LS-------PTLIRALkpRGDAPVNAHDLSSLRVLGStgepwnpepwnw 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 595 --------NVCIINMYGTTETQRAV--SYFAIP----SVNedstflstqkdliSAGQGMIDVqllVVNRTDRLVPcavGE 660
Cdd:cd05968 377 lfetvgkgRNPIINYSGGTEISGGIlgNVLIKPikpsSFN-------------GPVPGMKAD---VLDESGKPAR---PE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 661 MGEIYVRSG--GLAEGyldpsataekfvmnwFGQDLKRedtligpAREHWFGIRDRMYRSGDLGRYLPDGNVECTGRADD 738
Cdd:cd05968 438 VGELVLLAPwpGMTRG---------------FWRDEDR-------YLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDD 495
|
490 500 510
....*....|....*....|....*....|
gi 589279984 739 QIKIRGFRIELGEIDTHLSRHPLVRENVTL 768
Cdd:cd05968 496 TINVAGKRVGPAEIESVLNAHPAVLESAAI 525
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
281-480 |
1.17e-10 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 65.77 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIqsEQTNGimegpskgrKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:PLN02330 30 LPDFVLQDAELYADKVAFV--EAVTG---------KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPPNRQIVYLEVSNPKglLVIEKAGELAKIvkdfikDKLDLKILIPSiSLSSNGKEEYQDILEKY 440
Cdd:PLN02330 99 GIMAAGGVFSGANPTALESEIKKQAEAAGAK--LIVTNDTNYGKV------KGLGLPVIVLG-EEKIEGAVNWKELLEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 589279984 441 QNLSQTPTG-IILGPDSPAtLSFTSGSTGIPKGVKGRHYSL 480
Cdd:PLN02330 170 DRAGDTSDNeEILQTDLCA-LPFSSGTTGISKGVMLTHRNL 209
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
277-480 |
1.41e-10 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 65.77 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 277 FVGAIPDIFSAN-----------AKKYPDKLCVIqseqtngimEGPSkGRkTFTYGQIDKASNVIAHCLIQNGLKKEEVV 345
Cdd:PLN02246 10 FRSKLPDIYIPNhlplhdycferLSEFSDRPCLI---------DGAT-GR-VYTYADVELLSRRVAAGLHKLGIRQGDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 346 MVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKglLVIEKAGELAKiVKDFIKDKlDLKILipSISL 425
Cdd:PLN02246 79 MLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAK--LIITQSCYVDK-LKGLAEDD-GVTVV--TIDD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 589279984 426 SSNGKEEYQDILEkyQNLSQTPTgIILGPDSPATLSFTSGSTGIPKGVKGRHYSL 480
Cdd:PLN02246 153 PPEGCLHFSELTQ--ADENELPE-VEISPDDVVALPYSSGTTGLPKGVMLTHKGL 204
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
281-478 |
2.66e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 64.90 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIQseqtngimegpskGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:PRK08279 39 LGDVFEEAAARHPDRPALLF-------------EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVdpayppNRQIV------YLEVSNPKGLLVIEKAGELAKIVKDFIKDKLDLKILIPSISLSSNGKEEYQ 434
Cdd:PRK08279 106 GLAKLGAVVALL------NTQQRgavlahSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 589279984 435 DILEKYQNLSQTPTGIILGPDsPATLSFTSGSTGIPKGVKGRHY 478
Cdd:PRK08279 180 AAAAGAPTTNPASRSGVTAKD-TAFYIYTSGTTGLPKAAVMSHM 222
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
313-797 |
2.84e-10 |
|
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: 64.30 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 313 KGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVfsvvdpayppnrqivylevSNPKG 392
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV-------------------DVVRG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 393 llviekagelakivkdfikdkldlkilipsislSSNGKEEYQDILEkyqnlSQTPTGIIL--GPDSPATLSFTSGSTGIP 470
Cdd:cd17640 62 ---------------------------------SDSSVEELLYILN-----HSESVALVVenDSDDLATIIYTSGTTGNP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 471 KGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHDpIQRDMFTPLFL--GAELYVptsddigTPGRLAEWMDDCQ-- 546
Cdd:cd17640 104 KGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHS-YERSAEYFIFAcgCSQAYT-------SIRTLKDDLKRVKph 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 547 --VSVTHLTPAM-----GQLLSAQATRQIpsLLNAFFVGDVLTKRDC---TRLQHL-----AKNVCIINMYGTTETQrav 611
Cdd:cd17640 176 yiVSVPRLWESLysgiqKQVSKSSPIKQF--LFLFFLSGGIFKFGISgggALPPHVdtffeAIGIEVLNGYGLTETS--- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 612 syfAIPSVNEdstflsTQKDLI-SAGQGMIDVQLLVVNRTDRlVPCAVGEMGEIYVRSGGLAEGYL-DPSATAEkfVMNW 689
Cdd:cd17640 251 ---PVVSARR------LKCNVRgSVGRPLPGTEIKIVDPEGN-VVLPPGEKGIVWVRGPQVMKGYYkNPEATSK--VLDS 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 690 FGqdlkredtligparehWFgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIR-GFRIELGEIDTHLSRHPLVrENVTL 768
Cdd:cd17640 319 DG----------------WF-------NTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFI-EQIMV 374
|
490 500
....*....|....*....|....*....
gi 589279984 769 VRRDkdeEKVLVSYFVPINDNLEGLISES 797
Cdd:cd17640 375 VGQD---QKRLGALIVPNFEELEKWAKES 400
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
319-993 |
3.46e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 319 TYGQIDKASNVIAHCLIQNGLKKEEVVMVYAArSVEMVVCVMGILKAGgVFSVvdPAYPPN--------RQIVYLEVSNP 390
Cdd:PRK05691 42 SYRDLDLRARTIAAALQARASFGDRAVLLFPS-GPDYVAAFFGCLYAG-VIAV--PAYPPEsarrhhqeRLLSIIADAEP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 391 KGLLVIEK-AGELAKIvkdfikDKL---DLKILIPSISLSSNGKEEYQDilekyqnlsqtPTgiiLGPDSPATLSFTSGS 466
Cdd:PRK05691 118 RLLLTVADlRDSLLQM------EELaaaNAPELLCVDTLDPALAEAWQE-----------PA---LQPDDIAFLQYTSGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 467 TGIPKGVKGRHYSLTHFfPWMSKR-FGLNEKSKFTMLSGIahdPIQRDM------FTPLFLGaelyVPTSddIGTPG--- 536
Cdd:PRK05691 178 TALPKGVQVSHGNLVAN-EQLIRHgFGIDLNPDDVIVSWL---PLYHDMgligglLQPIFSG----VPCV--LMSPAyfl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 537 -RLAEWMDdcQVSVTHLTPAMG-----QLLSAQATRQIPSLLN-----AFFVGDVLTKRDCTRLQHLAKNVCIIN----- 600
Cdd:PRK05691 248 eRPLRWLE--AISEYGGTISGGpdfayRLCSERVSESALERLDlsrwrVAYSGSEPIRQDSLERFAEKFAACGFDpdsff 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 601 -MYGTTETQRAVSY----FAIPSVNEDSTFLS-------TQKDLISAGQGMIDVQLLVVNrTDRLVPCAVGEMGEIYVRS 668
Cdd:PRK05691 326 aSYGLAEATLFVSGgrrgQGIPALELDAEALArnraepgTGSVLMSCGRSQPGHAVLIVD-PQSLEVLGDNRVGEIWASG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 669 GGLAEGYL-DPSATAEKFVmNWFGQDlkredtligparehWFgirdrmyRSGDLGrYLPDGNVECTGRADDQIKIRGFRI 747
Cdd:PRK05691 405 PSIAHGYWrNPEASAKTFV-EHDGRT--------------WL-------RTGDLG-FLRDGELFVTGRLKDMLIVRGHNL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 748 ELGEIDThlsrhpLVRENVTLVRRDKdeekvlVSYFVPINDNLEGLisesdnpqddeeveeeeenekDLKMEMLRGVRRY 827
Cdd:PRK05691 462 YPQDIEK------TVEREVEVVRKGR------VAAFAVNHQGEEGI---------------------GIAAEISRSVQKI 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 828 ---RRLIKDIREYLRKKLPSyaVPSVYFPLS--KLPLNPNGKVDKP--KLPFPDTSLVP---------TVPTTDSTMLTP 891
Cdd:PRK05691 509 lppQALIKSIRQAVAEACQE--APSVVLLLNpgALPKTSSGKLQRSacRLRLADGSLDSyalfpalqaVEAAQTAASGDE 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 892 TQKTIHDIWLKLLPSppNTIGMEEIFFDMGGHSILATRLIFEIRKTFVVNAPLGLVFDKPTIGGQAREVDSLRNEeltpa 971
Cdd:PRK05691 587 LQARIAAIWCEQLKV--EQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAG----- 659
|
730 740
....*....|....*....|..
gi 589279984 972 fDTVTPSRPTTKPRsySDDLPE 993
Cdd:PRK05691 660 -GGAAQAAIARLPR--GQALPQ 678
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
314-870 |
4.36e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 64.27 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 314 GRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGL 393
Cdd:PLN03102 36 GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 394 LVIEKAGELAKIVKDFI---KDKLDLK-ILIPSISLSSNGKEEYQDilekYQNLSQ----TPTGI-----ILGPDSPATL 460
Cdd:PLN03102 116 FVDRSFEPLAREVLHLLsseDSNLNLPvIFIHEIDFPKRPSSEELD----YECLIQrgepTPSLVarmfrIQDEHDPISL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 461 SFTSGSTGIPKGV----KGRHYSLTH--------FFP---WMSKRFGLNeksKFTMLSGIAH----DPIQRDMFTP-LFL 520
Cdd:PLN03102 192 NYTSGTTADPKGVvishRGAYLSTLSaiigwemgTCPvylWTLPMFHCN---GWTFTWGTAArggtSVCMRHVTAPeIYK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 521 GAELY-------VPTSDDIGTPGrlaewmddcqvSVTHLTPAMGQLLSAQATRQIPSLLnaffvgdvltkrdCTRLQHLA 593
Cdd:PLN03102 269 NIEMHnvthmccVPTVFNILLKG-----------NSLDLSPRSGPVHVLTGGSPPPAAL-------------VKKVQRLG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 594 KNVciINMYGTTETQRAVSYFAIPsvNEDSTFLSTQKDLISAGQGMIDVQLLVVN----RTDRLVPCAVGEMGEIYVRSG 669
Cdd:PLN03102 325 FQV--MHAYGLTEATGPVLFCEWQ--DEWNRLPENQQMELKARQGVSILGLADVDvknkETQESVPRDGKTMGEIVIKGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 670 GLAEGYL-DPSATAEKFVMNWFGqdlkredtligparehwfgirdrmyrSGDLGRYLPDGNVECTGRADDQIKIRGFRIE 748
Cdd:PLN03102 401 SIMKGYLkNPKATSEAFKHGWLN--------------------------TGDVGVIHPDGHVEIKDRSKDIIISGGENIS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 749 LGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVpindnLEGliSESDNPQDDEEVeeeeenekdlkmemlrgVRRYR 828
Cdd:PLN03102 455 SVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVV-----LEK--GETTKEDRVDKL-----------------VTRER 510
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 589279984 829 RLIkdirEYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKL 870
Cdd:PLN03102 511 DLI----EYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
319-865 |
4.53e-10 |
|
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: 63.65 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 319 TYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYppnrqivylevsnpkgllvieK 398
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPML---------------------K 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 399 AGELAKIVKDfikdkLDLKILIPSISLssngkeeyqdilekyqnlsqtptgiilgpDSPATLSFTSGSTGIPKGVKGRHY 478
Cdd:cd05935 62 ERELEYILND-----SGAKVAVVGSEL-----------------------------DDLALIPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 479 SLthFFPWMSKRFGLNEKSKFTMLSGIA--HDP-IQRDMFTPLFLGAELYVPTSDDIGTpgrLAEWMDDCQVSV-THLTP 554
Cdd:cd05935 108 SA--AANALQSAVWTGLTPSDVILACLPlfHVTgFVGSLNTAVYVGGTYVLMARWDRET---ALELIEKYKVTFwTNIPT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 555 AMGQLLSAQ--ATRQIPSLLNAFFVGDVLTKRDCTRLQHLAkNVCIINMYGTTETQRAVSyfAIPSVNEDSTFLstqkdl 632
Cdd:cd05935 183 MLVDLLATPefKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMSQTH--TNPPLRPKLQCL------ 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 633 isaGQGMIDVQLLVVNRTDrLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVmnwfgqdlkredTLIGparehwfgi 711
Cdd:cd05935 254 ---GIP*FGVDARVIDIET-GRELPPNEVGEIVVRGPQIFKGYWNrPEETEESFI------------EIKG--------- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 712 rDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVREnVTLVRRDKDEEKVLVSYFVPINDNLE 791
Cdd:cd05935 309 -RRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E-VCVISVPDERVGEEVKAFIVLRPEYR 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589279984 792 GLISEsdnpqddeeveeeeenekdlkmemlrgvrryrrliKDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKV 865
Cdd:cd05935 387 GKVTE-----------------------------------EDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
284-764 |
5.33e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 63.91 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 284 IFSANAKKYPDKLCVIQseqtngimegpskGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGIL 363
Cdd:PRK07470 12 FLRQAARRFPDRIALVW-------------GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 364 KAGGVFSvvdpayPPN-RQ----IVYL-EVSNPKGLLVIEKAGELAKIVKDFIKDkLDLKILIPSislsSNGKEEYQDIL 437
Cdd:PRK07470 79 RLGAVWV------PTNfRQtpdeVAYLaEASGARAMICHADFPEHAAAVRAASPD-LTHVVAIGG----ARAGLDYEALV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 438 EKyqNLSQTPTGIILGPDSPATLSFTSGSTGIPKGVkgrhySLTH-------------FFPwmskrfGLNEKSKFTMLSG 504
Cdd:PRK07470 148 AR--HLGARVANAAVDHDDPCWFFFTSGTTGRPKAA-----VLTHgqmafvitnhladLMP------GTTEQDASLVVAP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 505 IAHDP-IQRdmFTPLFLGAELYVPTSD--DIGTPGRLAEwmddcQVSVTHL--TPAMGQLL---SAQATRQIPSLLNAFF 576
Cdd:PRK07470 215 LSHGAgIHQ--LCQVARGAATVLLPSErfDPAEVWALVE-----RHRVTNLftVPTILKMLvehPAVDRYDHSSLRYVIY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 577 VGDVLTKRDCTR-LQHLAKNVciinmygttetqraVSYFAIPSVNEDSTFL---------STQKDLISAG---QGMiDVQ 643
Cdd:PRK07470 288 AGAPMYRADQKRaLAKLGKVL--------------VQYFGLGEVTGNITVLppalhdaedGPDARIGTCGferTGM-EVQ 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 644 LLvvnrTDRLVPCAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVMNWFgqdlkredtligparehwfgirdrmyRSGDLG 722
Cdd:PRK07470 353 IQ----DDEGRELPPGETGEICVIGPAVFAGYYNnPEANAKAFRDGWF--------------------------RTGDLG 402
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 589279984 723 RYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE 764
Cdd:PRK07470 403 HLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSE 444
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
457-867 |
1.17e-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: 61.89 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 457 PATLSFTSGSTGIPKGVKGRHYSLThFFPWMSKRFGLNEKSKFT--MLSGIAHDPIQRDMFTPLFLGAeLYVPTSDDIgT 534
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFF-AVPDILQKEGLNWVVGDVtyLPLPATHIGGLWWILTCLIHGG-LCVTGGENT-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 535 PGRLAEWMDDCQVSVTHLTP-AMGQLLS--AQATRQIPSLlNAFFVGDVLTKRDCTRLQHLAKNVCIINMYGTTETQRAv 611
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVPtLLSKLVSelKSANATVPSL-RLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 612 syfaipsvnedsTFLSTQKDLI---SAGQGMIDVQLLVVNRTDRLVPCavGEMGEIYVRSGGLAEGYLD-PSATAEKFVM 687
Cdd:cd17635 158 ------------LCLPTDDDSIeinAVGRPYPGVDVYLAATDGIAGPS--ASFGTIWIKSPANMLGYWNnPERTAEVLID 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 688 NWFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVT 767
Cdd:cd17635 224 GWV--------------------------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECAC 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 768 LVRRDKDEEKVLVSYFVpindnleglISESDNpqddeeveeeeenekdlkmemlrgvrryRRLIKDIREYLRKKLPSYAV 847
Cdd:cd17635 278 YEISDEEFGELVGLAVV---------ASAELD----------------------------ENAIRALKHTIRRELEPYAR 320
|
410 420
....*....|....*....|
gi 589279984 848 PSVYFPLSKLPLNPNGKVDK 867
Cdd:cd17635 321 PSTIVIVTDIPRTQSGKVKR 340
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
300-788 |
1.29e-09 |
|
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: 62.72 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 300 QSEQTNGIMEGPSKGRK-TFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPP 378
Cdd:cd05967 64 RGDQIALIYDSPVTGTErTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 379 NRQIVYLEVSNPKgLLVIEKAG-ELAKIV--KDFIKDKLDL------KILI---PSISLSSNGKE---EYQDILEKYQNL 443
Cdd:cd05967 144 KELASRIDDAKPK-LIVTASCGiEPGKVVpyKPLLDKALELsghkphHVLVlnrPQVPADLTKPGrdlDWSELLAKAEPV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 444 SQTPtgiILGPDsPATLSFTSGSTGIPKGV---KGRH-----YSlthffpwMSKRFGLNEKSKFTMLSGIA----HDPIq 511
Cdd:cd05967 223 DCVP---VAATD-PLYILYTSGTTGKPKGVvrdNGGHavalnWS-------MRNIYGIKPGDVWWAASDVGwvvgHSYI- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 512 rdMFTPLFLGAELYVPTSDDIGTPGRLAEW--MDDCQVSVTHLTPAmgqllSAQATRQIPSllnaffVGDVLTKRDCTRL 589
Cdd:cd05967 291 --VYGPLLHGATTVLYEGKPVGTPDPGAFWrvIEKYQVNALFTAPT-----AIRAIRKEDP------DGKYIKKYDLSSL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 590 QHL-----------------AKNVCIINMYGTTETQRAVSyfAIPSVNEDstfLSTQKDliSAGQGMIDVQLLVVNRTDR 652
Cdd:cd05967 358 RTLflagerldpptlewaenTLGVPVIDHWWQTETGWPIT--ANPVGLEP---LPIKAG--SPGKPVPGYQVQVLDEDGE 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 653 lvPCAVGEMGEIYVR----SGGLAEGYLDPsataEKFVMNWFGQDlkredtligparehwfgirDRMYRSGDLGRYLPDG 728
Cdd:cd05967 431 --PVGPNELGNIVIKlplpPGCLLTLWKND----ERFKKLYLSKF-------------------PGYYDTGDAGYKDEDG 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 729 NVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFVPIND 788
Cdd:cd05967 486 YLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG 545
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
289-870 |
1.34e-09 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 62.32 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 289 AKKYPDKLCVIQseqtngimegpskGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGV 368
Cdd:cd12118 14 AAVYPDRTSIVY-------------GDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 369 FSVVdpayppNRQIvylevsnpkgllvieKAGELAkivkdFIKDKLDLKILIPSISLssngkeEYQDILEkyqnlSQTPT 448
Cdd:cd12118 81 LNAL------NTRL---------------DAEEIA-----FILRHSEAKVLFVDREF------EYEDLLA-----EGDPD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 449 GIILGPDS---PATLSFTSGSTGIPKGVKGRH-----------------------YSLTHF------FPWMSKRFG---- 492
Cdd:cd12118 124 FEWIPPADewdPIALNYTSGTTGRPKGVVYHHrgaylnalanilewemkqhpvylWTLPMFhcngwcFPWTVAAVGgtnv 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 493 ----LNEKSKFTMLS--GIAHdpiqrdmftplFLGAelyvPTSDDIgtpgrLAEWMDDCQVSVTHLTpamgQLLSAQATR 566
Cdd:cd12118 204 clrkVDAKAIYDLIEkhKVTH-----------FCGA----PTVLNM-----LANAPPSDARPLPHRV----HVMTAGAPP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 567 QiPSLLNaffvgdvltkrdctRLQHLAKNVCIInmYGTTETQRAVSyFAIPSVNEDSTFLSTQKDLIsAGQGMIDV---Q 643
Cdd:cd12118 260 P-AAVLA--------------KMEELGFDVTHV--YGLTETYGPAT-VCAWKPEWDELPTEERARLK-ARQGVRYVgleE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 644 LLVVN-RTDRLVPCAVGEMGEIYVRSGGLAEGYL-DPSATAEKFVMNWFgqdlkredtligparehwfgirdrmyRSGDL 721
Cdd:cd12118 321 VDVLDpETMKPVPRDGKTIGEIVFRGNIVMKGYLkNPEATAEAFRGGWF--------------------------HSGDL 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 722 GRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSyFVPINDNleglisesdnpq 801
Cdd:cd12118 375 AVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCA-FVELKEG------------ 441
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 802 ddeeveeeeeneKDLKMEmlrgvrryrrlikDIREYLRKKLPSYAVP-SVYFplSKLPLNPNGKVDKPKL 870
Cdd:cd12118 442 ------------AKVTEE-------------EIIAFCREHLAGFMVPkTVVF--GELPKTSTGKIQKFVL 484
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
894-954 |
4.03e-09 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 54.11 E-value: 4.03e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 589279984 894 KTIHDIWLKLLPSPPNTIGMEEIFFDMGGHSILATRLIFEIRKTFVVNAPLGLVFDKPTIG 954
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
656-785 |
4.29e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 60.91 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 656 CAVGEMGEIYVRSGGLAEGYLD-PSATAEKFVmnwfgqdlkredtligparehwfgiRDRMYRSGDLGRYLPDGNVECTG 734
Cdd:PRK06164 372 LPDGESGEIEIRAPSLMRGYLDnPDATARALT-------------------------DDGYFRTGDLGYTRGDGQFVYQT 426
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 589279984 735 RADDQIKIRGFRIELGEIDTHLSRHPLVReNVTLVRRDKDEEKVLVSYFVP 785
Cdd:PRK06164 427 RMGDSLRLGGFLVNPAEIEHALEALPGVA-AAQVVGATRDGKTVPVAFVIP 476
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
890-965 |
6.89e-09 |
|
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: 54.09 E-value: 6.89e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589279984 890 TPTQKTIHDIWLKLLPSPPNTIGMEEIFF-DMGGHSILATRLIFEIRKTFVVNAPLGLVFDKPTIGGQAREVDSLRN 965
Cdd:COG0236 4 EELEERLAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
317-773 |
7.65e-09 |
|
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: 59.76 E-value: 7.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 317 TFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLlvi 396
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 397 ekagelakivkdFIKDKLDLKILIpsislssngkeeyqdilekyqnlsqtptgiilgpdspatlsFTSGSTGIPKGVKgr 476
Cdd:cd05914 84 ------------FVSDEDDVALIN-----------------------------------------YTSGTTGNSKGVM-- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 477 hysLTHFFPWMSKRFG-----LNEKSKFTMLSGIAHD-PIQRDMFTPLFLGAELYVPTSddigTPGRLAEWMDDCQVSVT 550
Cdd:cd05914 109 ---LTYRNIVSNVDGVkevvlLGKGDKILSILPLHHIyPLTFTLLLPLLNGAHVVFLDK----IPSAKIIALAFAQVTPT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 551 HLTPAMGQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLAK--------------------------------NVCI 598
Cdd:cd05914 182 LGVPVPLVIEKIFKMDIIPKLTLKKFKFKLAKKINNRKIRKLAFkkvheafggnikefviggakinpdveeflrtiGFPY 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 599 INMYGTTETQRAVSYfaipsvNEDSTFLSTqkdliSAGQGMIDVQLlvvnRTDRLVPCAvgEMGEIYVRSGGLAEGYL-D 677
Cdd:cd05914 262 TIGYGMTETAPIISY------SPPNRIRLG-----SAGKVIDGVEV----RIDSPDPAT--GEGEIIVRGPNVMKGYYkN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 678 PSATAEKFVMN-WFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDGNVECTGRADDQIKI-RGFRIELGEIDTH 755
Cdd:cd05914 325 PEATAEAFDKDgWF--------------------------HTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAK 378
|
490
....*....|....*...
gi 589279984 756 LSRHPLVRENVTLVRRDK 773
Cdd:cd05914 379 INNMPFVLESLVVVQEKK 396
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
319-763 |
1.75e-08 |
|
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: 58.63 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 319 TYGQIDKASNVIAHCLIQNGLKK--EEVVMVYAarSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLVI 396
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRgmRAVLMVPP--GPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 397 EKAGElakivkdfikdkldlkilipsislssngkeeyqdilekyqnlsqtptgiilgpdsPATLSFTSGSTGIPKGVKGR 476
Cdd:cd05910 82 PKADE-------------------------------------------------------PAAILFTSGSTGTPKGVVYR 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 477 HYSLTHFFPWMSKRFglnekskftmlsGIAHDpiQRDMFT-PLF------LGAELYVPTSDDI----GTPGRLAEWMDDC 545
Cdd:cd05910 107 HGTFAAQIDALRQLY------------GIRPG--EVDLATfPLFalfgpaLGLTSVIPDMDPTrparADPQKLVGAIRQY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 546 QVSVTHLTPAMGQLLS---AQATRQIPSLLNAFFVGDVLTKRDCTRLQH-LAKNVCIINMYGTTEtqravsyfAIP-SVN 620
Cdd:cd05910 173 GVSIVFGSPALLERVArycAQHGITLPSLRRVLSAGAPVPIALAARLRKmLSDEAEILTPYGATE--------ALPvSSI 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 621 EDSTFLSTQKDLISAGQGM--------IDVQLLVVNRTD-------RLVPcaVGEMGEIYVRSGGLAEGYLD-PSATAek 684
Cdd:cd05910 245 GSRELLATTTAATSGGAGTcvgrpipgVRVRIIEIDDEPiaewddtLELP--RGEIGEITVTGPTVTPTYVNrPVATA-- 320
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589279984 685 fvmnwfgqdlkredtlIGPAREHWFGIRDRMyrsGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVR 763
Cdd:cd05910 321 ----------------LAKIDDNSEGFWHRM---GDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVR 380
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
13-182 |
1.94e-08 |
|
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: 58.59 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 13 PASELKAKLDRWSERLSALPS-LALPTDYPRPSPAKLVESFQTLPIPPSLTPALLRLTLEYSTlypssplpTPYHLLLTS 91
Cdd:cd19540 184 PDSLAARQLAYWRETLAGLPEeLELPTDRPRPAVASYRGGTVEFTIDAELHARLAALAREHGA--------TLFMVLHAA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 92 FSILLFRY---------TP-----DPSLVlyPTV--AVNstpsthPLLLKMELSPEMSFFEILHQVLTQEIIAT--QDsV 153
Cdd:cd19540 256 LAVLLSRLgagddipigTPvagrgDEALD--DLVgmFVN------TLVLRTDVSGDPTFAELLARVRETDLAAFahQD-V 326
|
170 180 190
....*....|....*....|....*....|....*...
gi 589279984 154 PLSTLVDHLKPEG-----PLFRVRF----FDSTTLEMD 182
Cdd:cd19540 327 PFERLVEALNPPRstarhPLFQVMLafqnTAAATLELP 364
|
|
| 3b-HSD-like_SDR_e |
cd05241 |
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ... |
1014-1266 |
2.37e-08 |
|
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: 57.44 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1014 TVFLTGATGFLGGFILNDLLTNRSSRikkVICLVRSSSLEKgqerlinsctlLGIWNPSwlsenKLEIIIGDLSKPQFDL 1093
Cdd:cd05241 1 SVLVTGGSGFFGERLVKQLLERGGTY---VRSFDIAPPGEA-----------LSAWQHP-----NIEFLKGDITDRNDVE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1094 SSKSwdylskETDAILHNGAIVHWVYPYEKLKPTNVLSTLECLKLCCQGGkMKSFTFVSSTSVLDTEGFIKKSDEELQNg 1173
Cdd:cd05241 62 QALS------GADCVFHTAAIVPLAGPRDLYWEVNVGGTQNVLDACQRCG-VQKFVYTSSSSVIFGGQNIHNGDETLPY- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1174 ndgLREDDDLeqgkkglvtgYGQSKWVAEKLIMMA-QNNGLRGWIVRPGYVMGdsksavtNTDDFIWRMVKGCLQLGL-- 1250
Cdd:cd05241 134 ---PPLDSDM----------YAETKAIAEIIVLEAnGRDDLLTCALRPAGIFG-------PGDQGLVPILFEWAEKGLvk 193
|
250
....*....|....*...
gi 589279984 1251 --IPDINNSINLVPVDHV 1266
Cdd:cd05241 194 fvFGRGNNLVDFTYVHNL 211
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
454-866 |
3.64e-08 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 57.73 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 454 PDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSKFTMLSGIAHD-PIQRDMFTPLFLGAELYV---PTS 529
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSfGLTGCLWLPLLSGIKVVFhpnPLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 530 ddigtPGRLAEWMDDCQVSVTHLTPA-MGQLLSAQATRQIPSLLNAFFVGDVLtkRDCTRLQHLAK-NVCIINMYGTTET 607
Cdd:cd05909 226 -----YKKIPELIYDKKATILLGTPTfLRGYARAAHPEDFSSLRLVVAGAEKL--KDTLRQEFQEKfGIRILEGYGTTEC 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 608 QRAVSYFAIPSVNEDSTFlstqkdlisagqGM----IDVQLLVVnrtDRLVPCAVGEMGEIYVRSGGLAEGYL-DPSATA 682
Cdd:cd05909 299 SPVISVNTPQSPNKEGTV------------GRplpgMEVKIVSV---ETHEEVPIGEGGLLLVRGPNVMLGYLnEPELTS 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 683 EKFVMNWfgqdlkredtligparehwfgirdrmYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRH--P 760
Cdd:cd05909 364 FAFGDGW--------------------------YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlpE 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 761 LVRENVTLVRRDKDEEKVLVSYFVPINDnleglisesdnpqddeeveeeeenekdlkmemlrgvrryrrlIKDIREYLRK 840
Cdd:cd05909 418 DNEVAVVSVPDGRKGEKIVLLTTTTDTD------------------------------------------PSSLNDILKN 455
|
410 420
....*....|....*....|....*..
gi 589279984 841 -KLPSYAVPSVYFPLSKLPLNPNGKVD 866
Cdd:cd05909 456 aGISNLAKPSYIHQVEEIPLLGTGKPD 482
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
313-744 |
4.20e-08 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 57.75 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 313 KGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKg 392
Cdd:cd05933 4 DKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEAN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 393 LLVIEKAGELAKIVKdfIKDKLD-LKILIP---SISLSSNGKEEYQDILEKYQNLSQTPTGIILGPDSP---ATLSFTSG 465
Cdd:cd05933 83 ILVVENQKQLQKILQ--IQDKLPhLKAIIQykePLKEKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPnqcCTLIYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 466 STGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSK-------FTMLSGIAHDPIqrDMFTPLFLGAELYVPTSDD------- 531
Cdd:cd05933 161 TTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesvvsYLPLSHIAAQIL--DIWLPIKVGGQVYFAQPDAlkgtlvk 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 532 ----------IGTPgRLAEWMDDCQVSVTH---------LTPAMGQLLSAQATRQ---IPSLLNA--------------- 574
Cdd:cd05933 239 tlrevrptafMGVP-RVWEKIQEKMKAVGAksgtlkrkiASWAKGVGLETNLKLMggeSPSPLFYrlakklvfkkvrkal 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 575 -------FFVGDVLTKRDcTRLQHLAKNVCIINMYGTTETQRAVsyfaipSVNEDSTFlstqkDLISAGQGMIDVQLLVV 647
Cdd:cd05933 318 gldrcqkFFTGAAPISRE-TLEFFLSLNIPIMELYGMSETSGPH------TISNPQAY-----RLLSCGKALPGCKTKIH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 648 NrtdrlvPCAVGeMGEIYVRSGGLAEGYLD-PSATAEKFvmnwfgqdlkreDTligparEHWFgirdrmyRSGDLGRYLP 726
Cdd:cd05933 386 N------PDADG-IGEICFWGRHVFMGYLNmEDKTEEAI------------DE------DGWL-------HSGDLGKLDE 433
|
490
....*....|....*...
gi 589279984 727 DGNVECTGRADDQIKIRG 744
Cdd:cd05933 434 DGFLYITGRIKELIITAG 451
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
412-762 |
5.15e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 57.34 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 412 DKLDLkiliPSISLSSNGKEEYQDILEKYQNLSQTPTgiiLGPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRF 491
Cdd:PRK13388 114 DGLDL----PGVRVLDVDTPAYAELVAAAGALTPHRE---VDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 492 GLnekskftmlsgIAHDPIQRDMftPLFLGAELYVPTSDDIGTPGRLAE--------WMDDCQ-VSVTHLT---PAMGQL 559
Cdd:PRK13388 187 GL-----------TRDDVCYVSM--PLFHSNAVMAGWAPAVASGAAVALpakfsasgFLDDVRrYGATYFNyvgKPLAYI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 560 LsaqATRQIP-----SLLNAFfvGDVLTKRDCTRLQHLAkNVCIINMYGTTETqravsyfAIPSVNEDSTFLStqkdliS 634
Cdd:PRK13388 254 L---ATPERPddadnPLRVAF--GNEASPRDIAEFSRRF-GCQVEDGYGSSEG-------AVIVVREPGTPPG------S 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 635 AGQGMIDVqlLVVNrTDRLVPCAVGE-------------MGEIYVRSG-GLAEGYL-DPSATAEKfvmnwfgqdlkredt 699
Cdd:PRK13388 315 IGRGAPGV--AIYN-PETLTECAVARfdahgallnadeaIGELVNTAGaGFFEGYYnNPEATAER--------------- 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 589279984 700 ligparehwfgIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLV 762
Cdd:PRK13388 377 -----------MRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAI 428
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
325-764 |
8.02e-08 |
|
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: 56.71 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 325 KASNVIAH-CliqnGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFsvvdpaYPPNRQ-----IVY-LEVSNPKGLLVIE 397
Cdd:cd05928 53 KAANVLSGaC----GLQRGDRVAVILPRVPEWWLVNVACIRTGLVF------IPGTIQltakdILYrLQASKAKCIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 398 kagELAKIVKDFIKDKLDLKIlipSISLSSNGKEEYQDILEKYQNLSQTPTGIILGPDSPATLSFTSGSTGIPKGVKGRH 477
Cdd:cd05928 123 ---ELAPEVDSVASECPSLKT---KLLVSEKSRDGWLNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 478 YSLTHFFPwMSKRFGLNEKSKFTML----SGIAHDPIQrDMFTPLFLGAELYV---PTSDDIGTPGRLAEWmddcqvSVT 550
Cdd:cd05928 197 SSLGLGLK-VNGRYWLDLTASDIMWntsdTGWIKSAWS-SLFEPWIQGACVFVhhlPRFDPLVILKTLSSY------PIT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 551 HL--TPAMGQLLSAQ--ATRQIPSLLNAFFVGDVLTKRDCTRLQHLAkNVCIINMYGTTETqravsyfaipsVNEDSTFL 626
Cdd:cd05928 269 TFcgAPTVYRMLVQQdlSSYKFPSLQHCVTGGEPLNPEVLEKWKAQT-GLDIYEGYGQTET-----------GLICANFK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 627 STQKDLISAGQGMI--DVQllVVNRTDRLVPcaVGEMGEIYVRSG-----GLAEGYLD-PSATAEKfvmnwfgqdlkred 698
Cdd:cd05928 337 GMKIKPGSMGKASPpyDVQ--IIDDNGNVLP--PGTEGDIGIRVKpirpfGLFSGYVDnPEKTAAT-------------- 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 589279984 699 tligparehwfgIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE 764
Cdd:cd05928 399 ------------IRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVE 452
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
833-958 |
9.57e-08 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 55.53 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 833 DIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDKPKLPFPDTSLVPTVPTTDSTMLTP-TQKTIHDIWLKLLPSPPNTI 911
Cdd:COG3433 160 AALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETAlTEEELRADVAELLGVDPEEI 239
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 589279984 912 GMEEIFFDMGGHSILATRLIFEIRKTFvVNAPLGLVFDKPTIGGQAR 958
Cdd:COG3433 240 DPDDNLFDLGLDSIRLMQLVERWRKAG-LDVSFADLAEHPTLAAWWA 285
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
6-173 |
9.80e-08 |
|
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: 56.12 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 6 LVNGTTTPASELKAKLDRWSERLSALPS-LALPTDYPRPSPAKLVESFQTLPIPPSLTPALLRLTLEY-STLypssplpt 83
Cdd:cd19538 177 LLGDESDPDSLIARQLAYWKKQLAGLPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLAKDNnVTL-------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 84 pYHLLLTSFSILLFRYTPDPSLVLYPTVA--------------VNStpsthpLLLKMELSPEMSFFEILHQVLTQEIIA- 148
Cdd:cd19538 249 -FMVLQAGFAALLTRLGAGTDIPIGSPVAgrnddsledlvgffVNT------LVLRTDTSGNPSFRELLERVKETNLEAy 321
|
170 180 190
....*....|....*....|....*....|.
gi 589279984 149 -TQDsVPLSTLVDHLKPEG-----PLFRVRF 173
Cdd:cd19538 322 eHQD-IPFERLVEALNPTRsrsrhPLFQIML 351
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
294-764 |
1.22e-07 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 56.23 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 294 DKLCVIQSEQTNGIMEGPSKGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVfsvvd 373
Cdd:PRK08008 14 DDLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 374 pAYPPNRQIVYLEVS-----NPKGLLVIEkagelAKIVKDFIKDKLDLKILIPSISLSSNGKEEYQDILEKYQNLSQTPT 448
Cdd:PRK08008 89 -MVPINARLLREESAwilqnSQASLLVTS-----AQFYPMYRQIQQEDATPLRHICLTRVALPADDGVSSFTQLKAQQPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 449 GII----LGPDSPATLSFTSGSTGIPKGVKGRHYSLT---HFFPWMSKrfgLNEKSKF-TMLSGIaHDPIQRDMFTPLF- 519
Cdd:PRK08008 163 TLCyappLSTDDTAEILFTSGTTSRPKGVVITHYNLRfagYYSAWQCA---LRDDDVYlTVMPAF-HIDCQCTAAMAAFs 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 520 LGAELYVptsddIGTPGRLAEWMDDC--QVSVTHLTPAMGQLLSAQ---ATRQIPSLLNAFFVGDVLT--KRD-CTRLqh 591
Cdd:PRK08008 239 AGATFVL-----LEKYSARAFWGQVCkyRATITECIPMMIRTLMVQppsANDRQHCLREVMFYLNLSDqeKDAfEERF-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 592 lakNVCIINMYGTTETqravsyfaIPSVNEDSTflSTQKDLISAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRsgGL 671
Cdd:PRK08008 312 ---GVRLLTSYGMTET--------IVGIIGDRP--GDKRRWPSIGRPGFCYEAEIRDDHNRPLP--AGEIGEICIK--GV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 672 A------EGYLDPSATAEKFvmnwfgqdlkredtligpAREHWFGIRDRMYRSGDLGRYLPDgnvectgRADDQIKIRGF 745
Cdd:PRK08008 375 PgktifkEYYLDPKATAKVL------------------EADGWLHTGDTGYVDEEGFFYFVD-------RRCNMIKRGGE 429
|
490
....*....|....*....
gi 589279984 746 RIELGEIDTHLSRHPLVRE 764
Cdd:PRK08008 430 NVSCVELENIIATHPKIQD 448
|
|
| Arna_like_SDR_e |
cd05257 |
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ... |
1014-1251 |
1.73e-07 |
|
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. 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: 187567 [Multi-domain] Cd Length: 316 Bit Score: 54.61 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1014 TVFLTGATGFLGGFILNDLLTNRSsrikKVICLVRSSSLEKgqerlinsctllgiWN-PSWLSENKLEIIIGDLSKPQFd 1092
Cdd:cd05257 1 NVLVTGADGFIGSHLTERLLREGH----EVRALDIYNSFNS--------------WGlLDNAVHDRFHFISGDVRDASE- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1093 lssksWDYLSKETDAILHNGAIVHWVYPY---EKLKPTNVLSTLECLKLCCQGGKmKSFTFVSSTSVLDTEGFIKksdee 1169
Cdd:cd05257 62 -----VEYLVKKCDVVFHLAALIAIPYSYtapLSYVETNVFGTLNVLEAACVLYR-KRVVHTSTSEVYGTAQDVP----- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1170 lqngndgLREDDDLEQGKKGLvTGYGQSKWVAEKLIM-MAQNNGLRGWIVRPGYVMGDSKSAVTNTDDFIWRMVKGCLQL 1248
Cdd:cd05257 131 -------IDEDHPLLYINKPR-SPYSASKQGADRLAYsYGRSFGLPVTIIRPFNTYGPRQSARAVIPTIISQRAIGQRLI 202
|
...
gi 589279984 1249 GLI 1251
Cdd:cd05257 203 NLG 205
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
21-173 |
3.09e-07 |
|
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: 54.69 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 21 LDRWSERLSALPSLALPTDYPRPSPAKLVESFQTLPIPPSLTPALLRLTLEYSTlypssplpTPYHLLLTSFSILLFRYT 100
Cdd:cd19539 192 LDFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAKRARS--------SLFMVLLAAYCVLLRRYT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 101 PDPSLVLyptvavnSTPS---THPLL------------LKMELSPEMSFFEILHQVLTQEIIA-TQDSVPLSTLVDHLKP 164
Cdd:cd19539 264 GQTDIVV-------GTPVagrNHPRFestvgffvnllpLRVDVSDCATFRDLIARVRKALVDAqRHQELPFQQLVAELPV 336
|
170
....*....|....
gi 589279984 165 E-----GPLFRVRF 173
Cdd:cd19539 337 DrdagrHPLVQIVF 350
|
|
| 3b-HSD_HSDB1_like_SDR_e |
cd09811 |
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ... |
1017-1226 |
9.65e-07 |
|
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: 52.89 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1017 LTGATGFLGGFILNDLLtNRSSRIKKViclvRSSSLEKGQERLINSCTLLGiwnpswlsENKLEIIIGDLSKPQFDLSSk 1096
Cdd:cd09811 4 VTGGGGFLGQHIIRLLL-ERKEELKEI----RVLDKAFGPELIEHFEKSQG--------KTYVTDIEGDIKDLSFLFRA- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1097 swdylSKETDAILHNGAIVHWVYP--YEKLKPTNVLSTLECLKLCCQGGkMKSFTFVSSTSVLdtegFIKKSDEELQNGN 1174
Cdd:cd09811 70 -----CQGVSVVIHTAAIVDVFGPpnYEELEEVNVNGTQAVLEACVQNN-VKRLVYTSSIEVA----GPNFKGRPIFNGV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 589279984 1175 dglrEDDDLEQGKKglvTGYGQSKWVAEKLIMMAQNNGLRGWIV------RPGYVMGD 1226
Cdd:cd09811 140 ----EDTPYEDTST---PPYASSKLLAENIVLNANGAPLKQGGYlvtcalRPMYIYGE 190
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
716-784 |
1.04e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 53.21 E-value: 1.04e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589279984 716 YRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTLVRRDKDEEKVLVSYFV 784
Cdd:PTZ00237 494 YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLV 562
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
281-482 |
1.51e-06 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 52.72 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 281 IPDIFSANAKKYPDKLCVIqseqtngimegpSKGrKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVM 360
Cdd:PRK07059 25 LADLLEESFRQYADRPAFI------------CMG-KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 361 GILKAGGVFSVVDPAYPPnRQIVY-LEVSNPKGLLVIEK-AGELAKIV-KDFIK--------DKLDLKILI--------- 420
Cdd:PRK07059 92 AVLRAGYVVVNVNPLYTP-RELEHqLKDSGAEAIVVLENfATTVQQVLaKTAVKhvvvasmgDLLGFKGHIvnfvvrrvk 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 589279984 421 ---PSISLSsnGKEEYQDILEKYQNLSQTPTGiiLGPDSPATLSFTSGSTGIPKGVkgrhySLTH 482
Cdd:PRK07059 171 kmvPAWSLP--GHVRFNDALAEGARQTFKPVK--LGPDDVAFLQYTGGTTGVSKGA-----TLLH 226
|
|
| 3Beta_HSD |
pfam01073 |
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ... |
1018-1251 |
1.52e-06 |
|
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: 51.60 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1018 TGATGFLGGFILNDLLTNRSSRIKKVICLVrssslekgqerlinsctllgiWNPSWLSE----NKLEIIIGDLSKPQFdl 1093
Cdd:pfam01073 3 TGGGGFLGRHIIKLLVREGELKEVRVFDLR---------------------ESPELLEDfsksNVIKYIQGDVTDKDD-- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1094 ssksWDYLSKETDAILHNGAI--VHWVYPYEKLKPTNVLSTLECLKLCCQGGkMKSFTFVSSTSVLdtegFIKKSDEELQ 1171
Cdd:pfam01073 60 ----LDNALEGVDVVIHTASAvdVFGKYTFDEIMKVNVKGTQNVLEACVKAG-VRVLVYTSSAEVV----GPNSYGQPIL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1172 NGNDGLREDDDLeqgkkglVTGYGQSKWVAEKLIMMAQNNGLRG------WIVRPGYVMGDSksavtntDDFIWRMVKGC 1245
Cdd:pfam01073 131 NGDEETPYESTH-------QDAYPRSKAIAEKLVLKANGRPLKNggrlytCALRPAGIYGEG-------DRLLVPFIVNL 196
|
....*.
gi 589279984 1246 LQLGLI 1251
Cdd:pfam01073 197 AKLGLA 202
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
453-769 |
5.83e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 50.58 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 453 GPDSPATLSFTSGSTGIPKGVKGRHYSLT-------HFFP------WMS-----KRFGLNEKSKFTMLSGI----AHDPI 510
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLanqraclKFFSpkeddvMMSflppfHAYGFNSCTLFPLLSGVpvvfAYNPL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 511 QrdmftplflgaelyvptsddigtPGRLAEWMDDCQVSVTHLTPAMGQLLSAQATRQ---IPSLLNAFFVGDVLTKRDCT 587
Cdd:PRK06334 261 Y-----------------------PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQescLPSLRFVVIGGDAFKDSLYQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 588 RLQHLAKNVCIINMYGTTETQRAVSYfaipsVNEDSTflstqKDLISAGQGMIDVQLLVVNRTDRlVPCAVGEMGEIYVR 667
Cdd:PRK06334 318 EALKTFPHIQLRQGYGTTECSPVITI-----NTVNSP-----KHESCVGMPIRGMDVLIVSEETK-VPVSSGETGLVLTR 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 668 SGGLAEGYLDpsataekfvmNWFGQdlkredTLIGPAREHWfgirdrmYRSGDLGRYLPDGNVECTGRADDQIKIRGFRI 747
Cdd:PRK06334 387 GTSLFSGYLG----------EDFGQ------GFVELGGETW-------YVTGDLGYVDRHGELFLKGRLSRFVKIGAEMV 443
|
330 340
....*....|....*....|....*
gi 589279984 748 ELGEIDTHLSRH---PLVRENVTLV 769
Cdd:PRK06334 444 SLEALESILMEGfgqNAADHAGPLV 468
|
|
| AR_like_SDR_e |
cd05193 |
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ... |
1015-1227 |
6.24e-06 |
|
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: 49.92 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1015 VFLTGATGFLGGFILNDLLtnrsSRIKKVICLVRSSSLEKgqerlinSCTLLGIWNPswlSENKLEIIIGDLSKPQfdls 1094
Cdd:cd05193 1 VLVTGASGFVASHVVEQLL----ERGYKVRATVRDPSKVK-------KVNHLLDLDA---KPGRLELAVADLTDEQ---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1095 skSWDYLSKETDAILHNGAIVHWV--YPYEKLKPtNVLSTLECLKLCCQGGKMKSFTFVSSTSVLDtegfIKKSDEELQN 1172
Cdd:cd05193 63 --SFDEVIKGCAGVFHVATPVSFSskDPNEVIKP-AIGGTLNALKAAAAAKSVKRFVLTSSAGSVL----IPKPNVEGIV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 589279984 1173 GNDGLREDDDLEQGKKGLVTGYGQSKWVAEKLIM-MAQNNGLRGWIVRPGYVMGDS 1227
Cdd:cd05193 136 LDEKSWNLEEFDSDPKKSAWVYAASKTLAEKAAWkFADENNIDLITVIPTLTIGTI 191
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
24-175 |
6.66e-06 |
|
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: 50.41 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 24 WSERLS-ALPSLALPTDYPRPSPAKLVESFQTLPIPPSLTPALLRLTLEYSTlypssplpTPYHLLLTSFSILLFRYTPD 102
Cdd:pfam00668 198 WLEQLEgELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLAKAHGT--------TLNDVLLAAYGLLLSRYTGQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 103 PSLVLYPTVAVNSTP----------STHPLLLKMElsPEMSFFEILHQVLTQ--EIIATQDsVPLSTLVDHLKPEGPLFR 170
Cdd:pfam00668 270 DDIVVGTPGSGRPSPdiermvgmfvNTLPLRIDPK--GGKTFSELIKRVQEDllSAEPHQG-YPFGDLVNDLRLPRDLSR 346
|
....*
gi 589279984 171 VRFFD 175
Cdd:pfam00668 347 HPLFD 351
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
318-760 |
7.91e-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: 50.22 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 318 FTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLVIE 397
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 398 KAgeLAKIVKDFIKDKLDLKILIPSislssnGKEEYQDILEKYQNLSQ-TPTGIILGPDSP---------ATLSFTSGST 467
Cdd:cd17642 125 KG--LQKVLNVQKKLKIIKTIIILD------SKEDYKGYQCLYTFITQnLPPGFNEYDFKPpsfdrdeqvALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 468 GIPKGVKGRHYSL-THFFPWMSKRFGLNEKSKFTMLSGIahdPIQR--DMFTPL---FLGAEL-YVPTSDDigtpgrlae 540
Cdd:cd17642 197 GLPKGVQLTHKNIvARFSHARDPIFGNQIIPDTAILTVI---PFHHgfGMFTTLgylICGFRVvLMYKFEE--------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 541 wmddcqvsvtHLTPAMGQLLSAQATRQIPSLLNAFFVGDVLTKRDCTRLQHLA-------KNV-----------CIINMY 602
Cdd:cd17642 265 ----------ELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIAsggaplsKEVgeavakrfklpGIRQGY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 603 GTTETQRAVsyfaIPSVNEDSTFLSTQKDLISAGQGMIDV---QLLVVNRTdrlvpcavgemGEIYVRSGGLAEGYL-DP 678
Cdd:cd17642 335 GLTETTSAI----LITPEGDDKPGAVGKVVPFFYAKVVDLdtgKTLGPNER-----------GELCVKGPMIMKGYVnNP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 679 SATaekfvmnwfgqdlkreDTLIgparehwfgIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSR 758
Cdd:cd17642 400 EAT----------------KALI---------DKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQ 454
|
..
gi 589279984 759 HP 760
Cdd:cd17642 455 HP 456
|
|
| UDP_G4E_4_SDR_e |
cd05232 |
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ... |
1014-1225 |
1.08e-05 |
|
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: 49.27 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1014 TVFLTGATGFLGGFiLNDLLTNRSSrikKVICLVRSSslekgqERLINSCTLLGIWNPSWLSEnkleiiigdlskpqfdl 1093
Cdd:cd05232 1 KVLVTGANGFIGRA-LVDKLLSRGE---EVRIAVRNA------ENAEPSVVLAELPDIDSFTD----------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1094 sskswdyLSKETDAILHNGAIVH-----WVYPYEKLKPTNVLSTLECLKLCCQGGkMKSFTFVSSTSVldtegfikksde 1168
Cdd:cd05232 54 -------LFLGVDAVVHLAARVHvmndqGADPLSDYRKVNTELTRRLARAAARQG-VKRFVFLSSVKV------------ 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 589279984 1169 elqNGNDG----LREDDD-LEQgkkglvTGYGQSKWVAEKLIMMAQNN-GLRGWIVRPGYVMG 1225
Cdd:cd05232 114 ---NGEGTvgapFDETDPpAPQ------DAYGRSKLEAERALLELGASdGMEVVILRPPMVYG 167
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
454-865 |
1.82e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 49.23 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 454 PDSPATLSFTSGSTGIPKG------------VKGRHyslthffpWMSkrfGLNEKSKfTMLSGIahdpiqrdmftPLF-- 519
Cdd:PRK05605 218 PDDVALILYTSGTTGKPKGaqlthrnlfanaAQGKA--------WVP---GLGDGPE-RVLAAL-----------PMFha 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 520 ------------LGAELYV-PTSDdigtpgrLAEWMDDCQVSVTHLTPAM----GQLLSAQATRQIP--SLLNAFFVGDV 580
Cdd:PRK05605 275 ygltlcltlavsIGGELVLlPAPD-------IDLILDAMKKHPPTWLPGVpplyEKIAEAAEERGVDlsGVRNAFSGAMA 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 581 LTKRDCTRLQHLAKNVcIINMYGTTET-----------QRAVSYFAIPsvnedstFLSTqkdlisagqgmiDVQllVVNR 649
Cdd:PRK05605 348 LPVSTVELWEKLTGGL-LVEGYGLTETspiivgnpmsdDRRPGYVGVP-------FPDT------------EVR--IVDP 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 650 TDRLVPCAVGEMGEIYVRSGGLAEGYL-DPSATAEKFVMNWFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDG 728
Cdd:PRK05605 406 EDPDETMPDGEEGELLVRGPQVFKGYWnRPEETAKSFLDGWF--------------------------RTGDVVVMEEDG 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 729 NVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVREN--VTLVRRDKDEEkvLVSYFVPIndnlEGLISESDnpqddeev 806
Cdd:PRK05605 460 FIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAavVGLPREDGSEE--VVAAVVLE----PGAALDPE-------- 525
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 589279984 807 eeeeenekdlkmemlrgvrryrrlikDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGKV 865
Cdd:PRK05605 526 --------------------------GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
317-510 |
2.09e-05 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 48.83 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 317 TFTYGQIDKASNVIAHCLI-QNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLLV 395
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 396 iekAGELAKIVKDFIKD--KLDLKILIPSISLSSNGKEeyqDILEKYQNLSQTPTGIIL----GPDSPATLSFTSGSTGI 469
Cdd:cd05938 85 ---APELQEAVEEVLPAlrADGVSVWYLSHTSNTEGVI---SLLDKVDAASDEPVPASLrahvTIKSPALYIYTSGTTGL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 589279984 470 PKGVKgrhysLTHFFPWMSkrfglnekSKFTMLSGIAHDPI 510
Cdd:cd05938 159 PKAAR-----ISHLRVLQC--------SGFLSLCGVTADDV 186
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
3-170 |
2.89e-05 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. 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 this X-domain, 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, and dual E/C (epimerization and condensation) domains. 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 X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 48.24 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 3 ESALVNGTTTPASELKAKLDRWSERLSALPS-LALPTDYPRPSpaklVESFQTLPIPPSLtPALLRLTLEYSTLYPSSPL 81
Cdd:cd19546 177 ERELLAGEDDRDSLIGDQIAYWRDALAGAPDeLELPTDRPRPV----LPSRRAGAVPLRL-DAEVHARLMEAAESAGATM 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 82 PTPYHLLLTsfsILLFRYTPDPSLVLyPTVAVNST----------PSTHPLLLKMELSPEMSFFEILHQV--LTQEIIAT 149
Cdd:cd19546 252 FTVVQAALA---MLLTRLGAGTDVTV-GTVLPRDDeegdlegmvgPFARPLALRTDLSGDPTFRELLGRVreAVREARRH 327
|
170 180
....*....|....*....|.
gi 589279984 150 QDsVPLSTLVDHLKPEGPLFR 170
Cdd:cd19546 328 QD-VPFERLAELLALPPSADR 347
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
317-482 |
3.12e-05 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 48.33 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 317 TFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKglLVI 396
Cdd:PRK07514 28 RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPA--LVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 397 ---EKAGELAKIVKdfikdkldlKILIPSI-SLSSNGKeeyQDILEKYQNLSQTPTGIILGPDSPATLSFTSGSTGIPKG 472
Cdd:PRK07514 106 cdpANFAWLSKIAA---------AAGAPHVeTLDADGT---GSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKG 173
|
170
....*....|
gi 589279984 473 VKgrhysLTH 482
Cdd:PRK07514 174 AM-----LSH 178
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
650-762 |
3.32e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 48.40 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 650 TDRLVPcAVGE-MGEIYVRSGGLAEGYL-DPSATAEKFVMNWFgqdlkredtligpareHwfgirdrmyrSGDLGRYLPD 727
Cdd:PRK08162 377 TMQPVP-ADGEtIGEIMFRGNIVMKGYLkNPKATEEAFAGGWF----------------H----------TGDLAVLHPD 429
|
90 100 110
....*....|....*....|....*....|....*
gi 589279984 728 GNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLV 762
Cdd:PRK08162 430 GYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAV 464
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
599-867 |
5.13e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 47.57 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 599 INMYGTTETqravsyfaipsVNEDsTFLSTQKDLI---SAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGY 675
Cdd:PRK06145 294 IDAYGLTET-----------CSGD-TLMEAGREIEkigSTGRALAHVEIRIADGAGRWLP--PNMKGEICMRGPKVTKGY 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 676 L-DPSATAEKFVMNWFgqdlkredtligparehwfgirdrmyRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDT 754
Cdd:PRK06145 360 WkDPEKTAEAFYGDWF--------------------------RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVER 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 755 HLSRHPLVRENVTL-VRRDKDEEKVLVSYFVPINDNLEglisesdnpqddeeveeeeenekdlkmemlrgvrryrrlIKD 833
Cdd:PRK06145 414 VIYELPEVAEAAVIgVHDDRWGERITAVVVLNPGATLT---------------------------------------LEA 454
|
250 260 270
....*....|....*....|....*....|....
gi 589279984 834 IREYLRKKLPSYAVPSVYFPLSKLPLNPNGKVDK 867
Cdd:PRK06145 455 LDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLK 488
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
312-473 |
5.28e-05 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 47.70 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 312 SKGRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPK 391
Cdd:PRK05857 36 CDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 392 GLLVIEKAGELAKIVKDFIKDkldlkilIPSISLSSNGKEEYQDILEKYQNLSQTPTgiiLGPDSPATLSFTSGSTGIPK 471
Cdd:PRK05857 116 AALVAPGSKMASSAVPEALHS-------IPVIAVDIAAVTRESEHSLDAASLAGNAD---QGSEDPLAMIFTSGTTGEPK 185
|
..
gi 589279984 472 GV 473
Cdd:PRK05857 186 AV 187
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
16-74 |
8.68e-05 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 45.80 E-value: 8.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 16 ELKAKLDRWSERLS-ALPSLALPTDYPRPSPAKLVESFQTLPIPPSLTPALLRLTLEYST 74
Cdd:COG4908 181 ALEKQLEYWRQQLAgAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKAHGA 240
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
830-864 |
1.50e-04 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 41.38 E-value: 1.50e-04
10 20 30
....*....|....*....|....*....|....*
gi 589279984 830 LIKDIREYLRKKLPSYAVPSVYFPLSKLPLNPNGK 864
Cdd:pfam13193 42 LEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
15-171 |
1.52e-04 |
|
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: 46.10 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 15 SELKAKLDRWSERLSALP---SLaLP---TDypRPSPAKLVESFQTLPIPPSLTPALLRLTLEYSTlypssplpTPYHLL 88
Cdd:cd20483 185 PLVQPLLDFWKEKLEGIPdasKL-LPfakAE--RPPVKDYERSTVEATLDKELLARMKRICAQHAV--------TPFMFL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 89 LTSFSILLFRYTPDPSLVL--------YPTV------AVNSTPsthpllLKMELSPEMSFFEILHQVLTQEIIATQDS-V 153
Cdd:cd20483 254 LAAFRAFLYRYTEDEDLTIgmvdgdrpHPDFddlvgfFVNMLP------IRCRMDCDMSFDDLLESTKTTCLEAYEHSaV 327
|
170 180
....*....|....*....|...
gi 589279984 154 PLSTLVDHLKPE-----GPLFRV 171
Cdd:cd20483 328 PFDYIVDALDVPrstshFPIGQI 350
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
657-760 |
1.88e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 45.83 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 657 AVGEMgeIYVRSGGLAEGYL-DPSATAEKfvmnwfgqdlkredtligparehwfgIRDRMYRSGDLGRYLPDGNVECTGR 735
Cdd:PRK07867 351 AIGEL--VNTAGPGGFEGYYnDPEADAER--------------------------MRGGVYWSGDLAYRDADGYAYFAGR 402
|
90 100
....*....|....*....|....*
gi 589279984 736 ADDQIKIRGFRIELGEIDTHLSRHP 760
Cdd:PRK07867 403 LGDWMRVDGENLGTAPIERILLRYP 427
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
314-477 |
3.51e-04 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 44.87 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 314 GRKTFTYGQIDKASNVIAHCLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAY--PPN-----RQIVylE 386
Cdd:PRK08180 66 GWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYslVSQdfgklRHVL--E 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 387 VSNPkGLLVIEKAGELAKIVKdfIKDKLDLKILIPSISLSSNGKEEYQDILEkyqnlsQTPTGII------LGPDSPATL 460
Cdd:PRK08180 144 LLTP-GLVFADDGAAFARALA--AVVPADVEVVAVRGAVPGRAATPFAALLA------TPPTAAVdaahaaVGPDTIAKF 214
|
170
....*....|....*..
gi 589279984 461 SFTSGSTGIPKGVKGRH 477
Cdd:PRK08180 215 LFTSGSTGLPKAVINTH 231
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
455-764 |
3.66e-04 |
|
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: 44.87 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 455 DSPATLSFTSGSTGIPKGVKGRH--YSLTHF--FPWMSKRFG---LNEKSkftmlSGIAHDPIQrDMFTPLFLGAELYV- 526
Cdd:cd05974 85 DDPMLLYFTSGTTSKPKLVEHTHrsYPVGHLstMYWIGLKPGdvhWNISS-----PGWAKHAWS-CFFAPWNAGATVFLf 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 527 --PTSDdigtPGRLAEWMDDCQVSVTHLTPAMGQLLSAQA-TRQIPSLLNAFFVGDVLTKRDCTRLQHlAKNVCIINMYG 603
Cdd:cd05974 159 nyARFD----AKRVLAALVRYGVTTLCAPPTVWRMLIQQDlASFDVKLREVVGAGEPLNPEVIEQVRR-AWGLTIRDGYG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 604 TTETQRAVSyfaipsvNEDSTFLSTQkdliSAGQGMIDVQLLVVNRTDRlvPCAVGEMGEIY--VRSGGLAEGYL-DPSA 680
Cdd:cd05974 234 QTETTALVG-------NSPGQPVKAG----SMGRPLPGYRVALLDPDGA--PATEGEVALDLgdTRPVGLMKGYAgDPDK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 681 TAEkfvmnwfgqdlkredtligparehwfGIRDRMYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHP 760
Cdd:cd05974 301 TAH--------------------------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHP 354
|
....
gi 589279984 761 LVRE 764
Cdd:cd05974 355 AVAE 358
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
711-780 |
4.67e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 44.37 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 711 IRdrmYRSGDLGRYLPDgnvEC------------TGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVTL-VRRDKDEEK 777
Cdd:COG1541 295 IR---YRTGDLTRLLPE---PCpcgrthprigriLGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIvVDREGGLDE 368
|
...
gi 589279984 778 VLV 780
Cdd:COG1541 369 LTV 371
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
601-766 |
4.96e-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: 44.18 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 601 MYGTTETQRAVSYfaIPSVNEDStflstqkdliSAGQGMIDVQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYL-DPS 679
Cdd:cd17637 142 LYGQTETSGLVTL--SPYRERPG----------SAGRPGPLVRVRIVDDNDRPVP--AGETGEIVVRGPLVFQGYWnLPE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 680 ATAEKFvmnwfgqdlkredtligpaREHWfgirdrmYRSGDLGRYLPDGNVECTGR--ADDQIKIRGFRIELGEIDTHLS 757
Cdd:cd17637 208 LTAYTF-------------------RNGW-------HHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVIL 261
|
....*....
gi 589279984 758 RHPLVRENV 766
Cdd:cd17637 262 EHPAIAEVC 270
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
289-800 |
6.09e-04 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 44.53 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 289 AKKYPDKLCVIQSeqtngimegpskGRKTFTYGQIDKASNVIAHcLIQNGLKKEEVVMVYAARSVEMVVCVMGILKAGGV 368
Cdd:PRK08633 625 AKRNWSRLAVADS------------TGGELSYGKALTGALALAR-LLKRELKDEENVGILLPPSVAGALANLALLLAGKV 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 369 fsVVDPAYppnrqivyleVSNPKGLL-VIEKAGeLAKIV--KDFIkDKLDLKILIpsISLSSNGKEEY-QDILEKYQNLS 444
Cdd:PRK08633 692 --PVNLNY----------TASEAALKsAIEQAQ-IKTVItsRKFL-EKLKNKGFD--LELPENVKVIYlEDLKAKISKVD 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 445 QT---------PTGIIL-------GPDSPATLSFTSGSTGIPKGVKGRHYSLTHFFPWMSKRFGLNEKSkfTMLSGIahd 508
Cdd:PRK08633 756 KLtallaarllPARLLKrlygptfKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDD--VILSSL--- 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 509 piqrdmftPLF----LGAELYVPTSDDIGtpgrlaewmddcqvSVTHLTPAMGqLLSAQATRQ--------IPSLLNAFF 576
Cdd:PRK08633 831 --------PFFhsfgLTVTLWLPLLEGIK--------------VVYHPDPTDA-LGIAKLVAKhratillgTPTFLRLYL 887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 577 VGDVLTKRDCTRL-------QHLAKNVC----------IINMYGTTETQRAVSyFAIPSVNEDSTFLSTQKDLISAGQGM 639
Cdd:PRK08633 888 RNKKLHPLMFASLrlvvagaEKLKPEVAdafeekfgirILEGYGATETSPVAS-VNLPDVLAADFKRQTGSKEGSVGMPL 966
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 640 IDVQLLVVNrTDRLVPCAVGEMGEIYVRSGGLAEGYL-DPSATAEkfVMnwfgqdlkREDTLIGparehWfgirdrmYRS 718
Cdd:PRK08633 967 PGVAVRIVD-PETFEELPPGEDGLILIGGPQVMKGYLgDPEKTAE--VI--------KDIDGIG-----W-------YVT 1023
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 719 GDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLS---RHPLVRENVTLVRRDKDEEKVLVSYFVPIND--NLEGL 793
Cdd:PRK08633 1024 GDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAkalGGEEVVFAVTAVPDEKKGEKLVVLHTCGAEDveELKRA 1103
|
....*..
gi 589279984 794 ISESDNP 800
Cdd:PRK08633 1104 IKESGLP 1110
|
|
| SDR_a1 |
cd05265 |
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ... |
1142-1244 |
6.61e-04 |
|
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: 43.05 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1142 GGKMKSFTFVSSTSVLDTEGFIKKSDEELQNGndglrEDDDLEQGKKglvtgYGQSKWVAEKLIMmaQNNGLRGWIVRPG 1221
Cdd:cd05265 87 KGRVKQYIFISSASVYLKPGRVITESTPLREP-----DAVGLSDPWD-----YGRGKRAAEDVLI--EAAAFPYTIVRPP 154
|
90 100
....*....|....*....|....*.
gi 589279984 1222 YVMGdsksAVTNTDD---FIWRMVKG 1244
Cdd:cd05265 155 YIYG----PGDYTGRlayFFDRLARG 176
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
903-960 |
7.92e-04 |
|
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: 39.93 E-value: 7.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 589279984 903 LLPSPPNTIGMEEIFFDMGGHSILATRLIFEIRKTFVVNAPLGLVFDKPTIGGQAREV 960
Cdd:smart00823 25 LGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
616-746 |
1.35e-03 |
|
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: 43.11 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 616 IPSVNEDStfLSTQKDLISAGQGMIDVQLLVVNrTDRLVPCAVGEMGEIYVRSGGLAEGYL----DPSATAEKFVMNWFG 691
Cdd:cd05905 346 VVRLDERD--KPNSLPLQDSGKVLPGAQVAIVN-PETKGLCKDGEIGEIWVNSPANASGYFlldgETNDTFKVFPSTRLS 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589279984 692 qdlkredtligparehwFGIRDRMY-RSGDLGrYLpdGNVECT-------------GRADDQIKIRGFR 746
Cdd:cd05905 423 -----------------TGITNNSYaRTGLLG-FL--RPTKCTdlnveehdllfvvGSIDETLEVRGLR 471
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
642-764 |
1.61e-03 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 42.29 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 642 VQLLVVNRTDRLVPcaVGEMGEIYVRSGGLAEGYLD-PSATAEKFvmnwfgqdlkredtligparehwfgiRDRMYRSGD 720
Cdd:cd17636 172 VQVRILDEDGREVP--DGEVGEIVARGPTVMAGYWNrPEVNARRT--------------------------RGGWHHTND 223
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 589279984 721 LGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE 764
Cdd:cd17636 224 LGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVAD 267
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
316-480 |
1.78e-03 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 42.56 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 316 KTFTYGQIDKASNVIAHCLIQN-GLKKEEVVMVYAARSVEMVVCVMGILKAGGVFSVVDPAYPPNRQIVYLEVSNPKGLL 394
Cdd:PRK08751 49 KTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 395 VIEKAGE----------LAKIVKDFIKDKLD-------------LKILIPSISLssNGKEEYQDILEKYQNLSQTPTGIi 451
Cdd:PRK08751 129 VIDNFGTtvqqviadtpVKQVITTGLGDMLGfpkaalvnfvvkyVKKLVPEYRI--NGAIRFREALALGRKHSMPTLQI- 205
|
170 180
....*....|....*....|....*....
gi 589279984 452 lGPDSPATLSFTSGSTGIPKGVKGRHYSL 480
Cdd:PRK08751 206 -EPDDIAFLQYTGGTTGVAKGAMLTHRNL 233
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
715-764 |
2.94e-03 |
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acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 42.05 E-value: 2.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 589279984 715 MYRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRE 764
Cdd:PRK00174 484 MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAE 533
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| UDP_invert_4-6DH_SDR_e |
cd05237 |
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ... |
1014-1243 |
3.59e-03 |
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UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. 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: 187548 [Multi-domain] Cd Length: 287 Bit Score: 41.06 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1014 TVFLTGATGFLGGFILNDLLtnrSSRIKKVICLVRSsslEKGQERLINSCtllgiwnPSWLSENKLEIIIGDLSKPQFDL 1093
Cdd:cd05237 4 TILVTGGAGSIGSELVRQIL---KFGPKKLIVFDRD---ENKLHELVREL-------RSRFPHDKLRFIIGDVRDKERLR 70
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1094 SSkswdYLSKETDAILHNGAIVHwV-----YPYEKLKpTNVLSTLECLKLCCQGGkMKSFTFVSS------TSVldtegf 1162
Cdd:cd05237 71 RA----FKERGPDIVFHAAALKH-VpsmedNPEEAIK-TNVLGTKNVIDAAIENG-VEKFVCISTdkavnpVNV------ 137
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 1163 ikksdeelqngndglredddleqgkkglvtgYGQSKWVAEKLIMMAQNNGLRGWI--VRPGYVMGDSKSAVTntddFIWR 1240
Cdd:cd05237 138 -------------------------------MGATKRVAEKLLLAKNEYSSSTKFstVRFGNVLGSRGSVLP----LFKK 182
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...
gi 589279984 1241 MVK 1243
Cdd:cd05237 183 QIK 185
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| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
716-870 |
4.36e-03 |
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(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 41.51 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 716 YRSGDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVReNVTLVRRDkDE---EKvlvSY-FVPINDNLE 791
Cdd:PRK10946 411 YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVI-HAALVSME-DElmgEK---SCaFLVVKEPLK 485
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 792 GLIsesdnpqddeeveeeeenekdlkmemlrgVRRYRRLiKDIREYlrkKLPSY--AVPSvyfplskLPLNPNGKVDKPK 869
Cdd:PRK10946 486 AVQ-----------------------------LRRFLRE-QGIAEF---KLPDRveCVDS-------LPLTAVGKVDKKQ 525
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gi 589279984 870 L 870
Cdd:PRK10946 526 L 526
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| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
641-767 |
4.43e-03 |
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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: 41.19 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589279984 641 DVQLLVVNRTDRLVPCAVGEMGEIYVRSGGLA--EGYLDPSATAEKFVMNWFGQDlkredtligparehwfgirDRMYRS 718
Cdd:cd05940 267 ESGEPIRDAEGRCIKVPRGEPGLLISRINPLEpfDGYTDPAATEKKILRDVFKKG-------------------DAWFNT 327
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90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 589279984 719 GDLGRYLPDGNVECTGRADDQIKIRGFRIELGEIDTHLSRHPLVRENVT 767
Cdd:cd05940 328 GDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANV 376
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