|
Name |
Accession |
Description |
Interval |
E-value |
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
6-398 |
5.50e-147 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 438.90 E-value: 5.50e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 6 KRVVITGLGILSSLAENIQDFREALLNKKNGVKDSERF-AKWFENARAAEVLHDIEYSDLNEDVIDSLDNAALWAYKVGK 84
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFdASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 85 DALSQAGLMDSRDTLKETGMIVGVSSAGTEAFLPLFEQRMEDFSLRkalFSGAF------SSCCSSVSTLLGLQGGVELV 158
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRR---VSPFFvpmalpNMAAGQVAIRLGLRGPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 159 ATACTASPNAVGMAFDYIQNGKSKTMLAVGTE-PIYLPTFAGFYALNVMHPDT------CTPFS-GQSGMSIGEGAGAIV 230
Cdd:cd00834 158 STACASGAHAIGDAARLIRLGRADVVIAGGAEaLITPLTLAGFAALRALSTRNddpekaSRPFDkDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 231 LEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEANDRIETLAMK 310
Cdd:cd00834 238 LESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 311 KVFANH-DKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCDLDYVPNEFRDRKVNIFMKNNYAF 389
Cdd:cd00834 318 RVFGEHaKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGF 397
|
....*....
gi 15830543 390 GGNNCCMIL 398
Cdd:cd00834 398 GGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
6-399 |
1.77e-141 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 424.89 E-value: 1.77e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 6 KRVVITGLGILSSLAENIQDFREALLNKKNGVKDSERFAKW-FENARAAEVlHDIEYSD-LNEDVIDSLDNAALWAYKVG 83
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASgLPVRIAGEV-KDFDPEEyLDRKELRRMDRFTQYALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 84 KDALSQAGLMDSRDTLKETGMIVGVSSAGTEAFLPLFE-------QRMEDFSLRKALFSGAfsscCSSVSTLLGLQGGVE 156
Cdd:COG0304 80 REALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRallekgpRRVSPFFVPMMMPNMA----AGHVSIRFGLKGPNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 157 LVATACTASPNAVGMAFDYIQNGKSKTMLAVGTE-PIYLPTFAGFYALNVM-----HPDT-CTPFS-GQSGMSIGEGAGA 228
Cdd:COG0304 156 TVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALstrndDPEKaSRPFDkDRDGFVLGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 229 IVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEANDRIETLA 308
Cdd:COG0304 236 LVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 309 MKKVFANH-DKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCDLDYVPNEFRDRKVNIFMKNNY 387
Cdd:COG0304 316 IKRVFGDHaYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSF 395
|
410
....*....|..
gi 15830543 388 AFGGNNCCMILS 399
Cdd:COG0304 396 GFGGHNASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
5-398 |
2.80e-97 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 309.80 E-value: 2.80e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 5 RKRVVITGLGILSSLAENIQDFREALLNKKNGVKDSERFAKWFENAR-AAEVlhdieySDLN-EDVIDS-----LDNAAL 77
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKiAGEV------KDFNpDDYMSRkearrMDRFIQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 78 WAYKVGKDALSQAGLMDSRDTLKETGMIVGvSSAG-----TEAFLPLFEQ---RMEDFSLRKALFSGAfsscCSSVSTLL 149
Cdd:PRK07314 75 YGIAAAKQAVEDAGLEITEENADRIGVIIG-SGIGgletiEEQHITLLEKgprRVSPFFVPMAIINMA----AGHVSIRY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 150 GLQGGVELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTE-PIYLPTFAGFYALNVM-----HPDT-CTPF-SGQSGMS 221
Cdd:PRK07314 150 GAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEaAITPLGIAGFAAARALstrndDPERaSRPFdKDRDGFV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 222 IGEGAGAIVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEAN 301
Cdd:PRK07314 230 MGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 302 DRIETLAMKKVFANH-DKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCDLDYVPNEFRDRKVN 380
Cdd:PRK07314 310 DKAETQAIKRVFGEHaYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID 389
|
410
....*....|....*...
gi 15830543 381 IFMKNNYAFGGNNCCMIL 398
Cdd:PRK07314 390 YALSNSFGFGGTNASLVF 407
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
6-398 |
4.57e-76 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 253.37 E-value: 4.57e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 6 KRVVITGLGILSSLAENIQDFREALLNKKNGVKdseRFAKW--FE--NARAAEVLHDIEY-SDLNEDVIDSLDNAALWAY 80
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVR---RMPEWdrYDglNTRLAAPIDDFELpAHYTRKKIRSMGRVSLMAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 81 KVGKDALSQAGLMDSrDTLK--ETGMIVGVSSAGTEAFLP----LFEQRMEDFS----LRKALFSGAfssccSSVSTLLG 150
Cdd:PRK09116 79 RASELALEDAGLLGD-PILTdgRMGIAYGSSTGSTDPIGAfgtmLLEGSMSGITattyVRMMPHTTA-----VNVGLFFG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 151 LQGGVELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTEPIYLPTFAGF---YALNVM--HPD-TCTPF-SGQSGMSIG 223
Cdd:PRK09116 153 LKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFdtlFATSTRndAPElTPRPFdANRDGLVIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 224 EGAGAIVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGavQVMNKAMANAGVTPEQIDYVNAHGTGTEANDR 303
Cdd:PRK09116 233 EGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 304 IETLAMKKVFANhdKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNC-DLDYVPNEFRDRKVNIF 382
Cdd:PRK09116 311 AESQATAAVFGA--RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYV 388
|
410
....*....|....*.
gi 15830543 383 MKNNYAFGGNNCCMIL 398
Cdd:PRK09116 389 MSNNFAFGGINTSLIF 404
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
6-397 |
1.48e-75 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 251.96 E-value: 1.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 6 KRVVITGLGILSSLAENIQDFREALLNKKNGVKDSERF-AKWFENARAAEVlhdieySDLN-EDVIDSLDnaalwaykVG 83
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFdASDFPVQIAGEI------TDFDpTEVMDPKE--------VK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 84 K-DALSQAGLMDSRDTLKETGMIV--------GVSSAGTEAFLPLFEQ-----------RMEDFSLRKALFS--GAFssc 141
Cdd:PRK08439 68 KaDRFIQLGLKAAREAMKDAGFLPeeldaerfGVSSASGIGGLPNIEKnsiicfekgprKISPFFIPSALVNmlGGF--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 142 cssVSTLLGLQGGVELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTE----PIYLPTFAGFYALNVMHPDTCT---PF 214
Cdd:PRK08439 145 ---ISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAEsaicPVGIGGFAAMKALSTRNDDPKKasrPF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 215 SG-QSGMSIGEGAGAIVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPraSGAVQVMNKAMANAGVTPeqIDYVNA 293
Cdd:PRK08439 222 DKdRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGNPK--IDYINA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 294 HGTGTEANDRIETLAMKKVFANHDKL-LVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCDLDYVPN 372
Cdd:PRK08439 298 HGTSTPYNDKNETAALKELFGSKEKVpPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPN 377
|
410 420
....*....|....*....|....*
gi 15830543 373 EFRDRKVNIFMKNNYAFGGNNCCMI 397
Cdd:PRK08439 378 VARKAELNVVMSNSFGFGGTNGVVI 402
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
9-399 |
5.75e-75 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 250.77 E-value: 5.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 9 VITGLGIlsslaeNIQDFREALLNKKNGVKDSERFAKWFENARAAEVLHDIEYSDL---------NEDVIDSL------- 72
Cdd:PTZ00050 1 VVTPLGV------GAESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVAAMpcqiaaevdQSEFDPSDfaptkre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 73 DNAALWAYKVGKDALSQAGLMDSRDTLKE-TGMIVGVSSAG----TEAFLPLFE---QRMEDFSLRKALFSGAfsscCSS 144
Cdd:PTZ00050 75 SRATHFAMAAAREALADAKLDILSEKDQErIGVNIGSGIGSladlTDEMKTLYEkghSRVSPYFIPKILGNMA----AGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 145 VSTLLGLQGGVELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTEPIYLPT-FAGFYALNVM------HPDT-CTPFS- 215
Cdd:PTZ00050 151 VAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVsFAGFSRMRALctkyndDPQRaSRPFDk 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 216 GQSGMSIGEGAGAIVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTP-EQIDYVNAH 294
Cdd:PTZ00050 231 DRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINiNDVDYVNAH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 295 GTGTEANDRIETLAMKKVFANHD--KLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCDLDYVPN 372
Cdd:PTZ00050 311 ATSTPIGDKIELKAIKKVFGDSGapKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQG 390
|
410 420
....*....|....*....|....*....
gi 15830543 373 EFRDRKVNI--FMKNNYAFGGNNCCMILS 399
Cdd:PTZ00050 391 KTAHPLQSIdaVLSTSFGFGGVNTALLFT 419
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
3-399 |
9.65e-74 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 247.60 E-value: 9.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 3 TNRKRVVITGLGILSSLAENIQDFREALLNKKNGVKD---------SERFAKWFEN-ARAAEVLHDIEysdlneDVIDS- 71
Cdd:PRK06333 1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTltdfpvgdlATKIGGQVPDlAEDAEAGFDPD------RYLDPk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 72 ----LDNAALWAYKVGKDALSQAGLM-DSRDTLKETGMIVGVSSAGteafLPLFEQRMEDFSLRKALFSGAFSS------ 140
Cdd:PRK06333 75 dqrkMDRFILFAMAAAKEALAQAGWDpDTLEDRERTATIIGSGVGG----FPAIAEAVRTLDSRGPRRLSPFTIpsfltn 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 141 -CCSSVSTLLGLQGGVELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTE----PIYLPTFAGFYALNVMHPDT----C 211
Cdd:PRK06333 151 mAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEaaidRVSLAGFAAARALSTRFNDApeqaS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 212 TPF-SGQSGMSIGEGAGAIVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDY 290
Cdd:PRK06333 231 RPFdRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 291 VNAHGTGTEANDRIETLAMKKVFANHDKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCD-LDY 369
Cdd:PRK06333 311 LNAHATSTPVGDLGEVAAIKKVFGHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDV 390
|
410 420 430
....*....|....*....|....*....|
gi 15830543 370 VPNEFRDRKVNIFMKNNYAFGGNNCCMILS 399
Cdd:PRK06333 391 VANKARPMDMDYALSNGFGFGGVNASILFR 420
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
413-851 |
1.04e-64 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 222.66 E-value: 1.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 413 KRVAISGVGAVSAIGHTLNQVLENIWAQDHHVelgsvtfpddtleeakellavldesnQFAELFDEeysfseatlpeteS 492
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGI--------------------------RPITRFDA-------------S 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 493 NFKTF---QVSGLEPRKHLRRFDQRKATRGGTFALIALTEALEQAKRKIKR-DGDELGMIMGMSRGPQETTYKYLQSL-K 567
Cdd:COG0304 42 GLPVRiagEVKDFDPEEYLDRKELRRMDRFTQYALAAAREALADAGLDLDEvDPDRTGVIIGSGIGGLDTLEEAYRALlE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 568 PDPRKVRTSEFPGSLMNAIPTFCGISEGIKGYTTTLATGENSALGALTYGYEIVRQNLQPQVLVGGADEYFPSMSLY--- 644
Cdd:COG0304 122 KGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAgfd 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 645 -MDAVTQKIHMTAEASdyQIYGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCsntyfDA---SLLEEKS 720
Cdd:COG0304 202 aLGALSTRNDDPEKAS--RPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASS-----DAyhiTAPAPDG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 721 ASMALAIERALTHAGISAGDIDLVC--GTSNGSDDhsRIEIDAIYNTFAAQNPAVPVVNYNACFGFVASAAGLLNLAVIT 798
Cdd:COG0304 275 EGAARAMRAALKDAGLSPEDIDYINahGTSTPLGD--AAETKAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASV 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830543 799 DCIKKQAVPAIPNTVEfFDER--VNFV-RQSMKLALNHVLLVGATEGGNYYAFVIK 851
Cdd:COG0304 353 LALRDGVIPPTINLEN-PDPEcdLDYVpNEAREAKIDYALSNSFGFGGHNASLVFK 407
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
5-403 |
5.47e-62 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 215.65 E-value: 5.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 5 RKRVVITGLGILSSLAENIQDFREALLNKKNGVKDSERFAKWFENARAAEVLhDIeysdLNEDVIDSLDNAALWAYKVGK 84
Cdd:PRK06501 10 RPIVAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV-DF----LPESPFGASALSEALARLAAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 85 DALSQAGLMDS-------------------RDTL-KETGMIVGVS------SAGTEAFLPLFEQRMedfslrkalfsgaF 138
Cdd:PRK06501 85 EALAQAGIGKGdfpgplflaappvelewpaRFALaAAVGDNDAPSydrllrAARGGRFDALHERFQ-------------F 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 139 SSCCSSVSTLLGLQGGVELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTE----PIYLPTFAGFYALNVMH--PDTCT 212
Cdd:PRK06501 152 GSIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDgsvsAEALIRFSLLSALSTQNdpPEKAS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 213 -PFS-GQSGMSIGEGAGAIVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDY 290
Cdd:PRK06501 232 kPFSkDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 291 VNAHGTGTEANDRIETLAMKKVFANH-DKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCDLDY 369
Cdd:PRK06501 312 INAHGTSTPENDKMEYLGLSAVFGERlASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDV 391
|
410 420 430
....*....|....*....|....*....|....
gi 15830543 370 VPNEFRDRKVNIFMKNNYAFGGNNCCMILSMEPA 403
Cdd:PRK06501 392 VPNVARDARVTAVLSNSFGFGGQNASLVLTAEPA 425
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
4-398 |
1.77e-60 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 211.02 E-value: 1.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 4 NRKRVVITGLGILSSLAENIQDFREALLNKKNGVKDSERFAKWFENARAAEVLHDIEYSD-LNEDVIDSLDNAALWAYKV 82
Cdd:PRK08722 2 SKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEyMSKKDARKMDLFIQYGIAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 83 GKDALSQAGLMDSRDTLKETGMIVG-------VSSAGTEAFLPLFEQRMEDFSLRkalfSGAFSSCCSSVSTLLGLQGGV 155
Cdd:PRK08722 82 GIQALDDSGLEVTEENAHRIGVAIGsgigglgLIEAGHQALVEKGPRKVSPFFVP----STIVNMIAGNLSIMRGLRGPN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 156 ELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTEPIYLPT-FAGFYALNVMHPDTCTPFS-------GQSGMSIGEGAG 227
Cdd:PRK08722 158 IAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLgMAGFGAAKALSTRNDEPQKasrpwdkDRDGFVLGDGAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 228 AIVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEANDRIETL 307
Cdd:PRK08722 238 MMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 308 AMKKVF--ANHDKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCDLDYVPNEFRD-RKVNIFMK 384
Cdd:PRK08722 318 GIKRALgeAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKvESMEYAIC 397
|
410
....*....|....
gi 15830543 385 NNYAFGGNNCCMIL 398
Cdd:PRK08722 398 NSFGFGGTNGSLIF 411
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
6-402 |
9.65e-60 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 209.65 E-value: 9.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 6 KRVVITGLGILSSLAENIQDFREALLNKKNGVK----DSERFAKWFENAR-----------AAEVLHDIEYSDLNEDV-I 69
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRaltqDDLKMKSEDEETQlytldqlpsrvAALVPRGTGPGDFDEELwL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 70 DSLDNAALWAYKV--GKDALSQAGLMDSRDTLKE-TGMIVGvssAGTEAFLPLFE----------QRMEDFSLRKALFSG 136
Cdd:PLN02836 86 NSRSSSRFIGYALcaADEALSDARWLPSEDEAKErTGVSIG---GGIGSITDILEaaqlicekrlRRLSPFFVPRILINM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 137 AfsscCSSVSTLLGLQGGVELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTEP-IYLPTFAGF---YALNVMHPDTCT 212
Cdd:PLN02836 163 A----AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESsIDALSIAGFsrsRALSTKFNSCPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 213 ----PF-SGQSGMSIGEGAGAIVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQ 287
Cdd:PLN02836 239 easrPFdCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 288 IDYVNAHGTGTEANDRIETLAMKKVFANH---DKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPN 364
Cdd:PLN02836 319 VDYVNAHATSTPLGDAVEARAIKTVFSEHatsGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPI 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 15830543 365 CDLDYVP-NEFRDRKVNIFMKNNYAFGGNNCCMILSMEP 402
Cdd:PLN02836 399 FDDGFVPlTASKAMLIRAALSNSFGFGGTNASLLFTSPP 437
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
7-398 |
2.69e-55 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 197.01 E-value: 2.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 7 RVVITGLGILSSLAENIQDFREALLNKKNGVKD--SERF--AKWFENARAAE--------VLHDIEYSD-----LNEDVI 69
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEipEDRWdaDGYYPDPGKPGktytrrggFLDDVDAFDaaffgISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 70 DSLDNAALWAYKVGKDALSQAGLMDSRDTLKETGMIVGVSSAGTEAFLPLFEQRMEDFSLRKalfsGAFSSCCSSVSTLL 149
Cdd:cd00833 82 EAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATG----TSRAFLANRISYFF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 150 GLQGGVELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTEPIYLP-TFAGFYALNVMHPD-TCTPFSGQ-SGMSIGEGA 226
Cdd:cd00833 158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPdMFVGFSKAGMLSPDgRCRPFDADaDGYVRGEGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 227 GAIVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEANDRIET 306
Cdd:cd00833 238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 307 LAMKKVFANH----DKLLVSSTKSYFGHNIGAAGIVELI-ACLA----TLPdnrvlPTLNFSHARPNCDLD----YVPNE 373
Cdd:cd00833 318 EALAKVFGGSrsadQPLLIGSVKSNIGHLEAAAGLAGLIkVVLAlehgVIP-----PNLHFETPNPKIDFEesplRVPTE 392
|
410 420 430
....*....|....*....|....*....|..
gi 15830543 374 FRD-------RKVNIfmkNNYAFGGNNCCMIL 398
Cdd:cd00833 393 ARPwpapagpRRAGV---SSFGFGGTNAHVIL 421
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
3-399 |
3.76e-54 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 196.74 E-value: 3.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 3 TNRKRVVITGLGILSSLAENIQDFREALLNKKNGVKDSERF-AKWFENARAAEVLHDIEYSDLNEDVIDSLDNAALWAYK 81
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFdCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLT 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 82 VGKDALSQAGLM-DSRDTLKET--GMIVGVSSAGTEAFLPLFEQRMedFSLRKA-LFSGAFSSCCSSVSTL---LGLQGG 154
Cdd:PLN02787 206 AGKKALADGGITeDVMKELDKTkcGVLIGSAMGGMKVFNDAIEALR--ISYRKMnPFCVPFATTNMGSAMLamdLGWMGP 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 155 VELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTE----PIYLPTFAGFYALNVMHPD---TCTPFS-GQSGMSIGEGA 226
Cdd:PLN02787 284 NYSISTACATSNFCILNAANHIIRGEADVMLCGGSDaaiiPIGLGGFVACRALSQRNDDptkASRPWDmNRDGFVMGEGA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 227 GAIVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEANDRIET 306
Cdd:PLN02787 364 GVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEY 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 307 LAMKKVFANHDKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCDLDYVPNEFRDR-KVNIFMKN 385
Cdd:PLN02787 444 QALMRCFGQNPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERlDIKVALSN 523
|
410
....*....|....
gi 15830543 386 NYAFGGNNCCMILS 399
Cdd:PLN02787 524 SFGFGGHNSSILFA 537
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
103-399 |
3.56e-52 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 187.36 E-value: 3.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 103 GMIVGVSSAG---TEAFLPLFEQRM----EDFSLRK-ALFSGA-FssccssVSTLLGLQGGVELVATACTASPNAVGMAF 173
Cdd:PRK09185 98 GVVLGTSTSGileGELAYRRRDPAHgalpADYHYAQqELGSLAdF------LRAYLGLSGPAYTISTACSSSAKVFASAR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 174 DYIQNGKSKTMLAVGTEPIYLPTFAGFYALNVMHPDTCTPFS-GQSGMSIGEGAGAIVLE-EYEHAVArgatiygeILSY 251
Cdd:PRK09185 172 RLLEAGLCDAAIVGGVDSLCRLTLNGFNSLESLSPQPCRPFSaNRDGINIGEAAAFFLLErEDDAAVA--------LLGV 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 252 ATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEANDRIETLAMKKVFANHdkLLVSSTKSYFGHN 331
Cdd:PRK09185 244 GESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVFGDG--VPCSSTKGLTGHT 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830543 332 IGAAGIVELIACLATLPDNRVLPTLNFSHARPNCDLDYVPNEFRDRKVNIFMKNNYAFGGNNCCMILS 399
Cdd:PRK09185 322 LGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAIRYVLSNSFAFGGNNCSLIFG 389
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
6-399 |
1.58e-51 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 186.03 E-value: 1.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 6 KRVVITGLGILSSLAENIQDFREALLNKKNGVKDSERFAkwfENARAAEVLHDIeysDLN-EDVIDS-----LDNAALWA 79
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFA---EMGMRSQVWGNV---KLDpTGLIDRkvmrfMGDASAYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 80 YKVGKDALSQAGLMDSRDTLKETGMIVGVSSAGTEAFL--------PLFEQRMEDFSLRKALFSGAfSSCcssVSTLLGL 151
Cdd:PRK07967 76 YLAMEQAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVeaadamrgPRGPKRVGPYAVTKAMASTV-SAC---LATPFKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 152 QGGVELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTEPIYLPTFAGFYALNVM---HPDTCTPFS-----GQSGMSIG 223
Cdd:PRK07967 152 KGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALstkYNDTPEKASraydaNRDGFVIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 224 EGAGAIVLEEYEHAVARGATIYGEILSYATSCDafhetGPD---PRASGAVQVMNKAMANAGvTPeqIDYVNAHGTGTEA 300
Cdd:PRK07967 232 GGGGVVVVEELEHALARGAKIYAEIVGYGATSD-----GYDmvaPSGEGAVRCMQMALATVD-TP--IDYINTHGTSTPV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 301 NDRIETLAMKKVFANhDKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPN-CDLDYVPNEFRDRKV 379
Cdd:PRK07967 304 GDVKELGAIREVFGD-KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAEL 382
|
410 420
....*....|....*....|
gi 15830543 380 NIFMKNNYAFGGNNCCMILS 399
Cdd:PRK07967 383 TTVMSNSFGFGGTNATLVFR 402
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
7-398 |
3.98e-50 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 181.87 E-value: 3.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 7 RVVITGLGILSSLAENI---QDFREALLNKKNGVKDSERFAKWFENARAAEV-LHDIEYSDLNEDVIdsLDNAALWAYKV 82
Cdd:cd00828 2 RVVITGIGVVSPHGEGCdevEEFWEALREGRSGIAPVARLKSRFDRGVAGQIpTGDIPGWDAKRTGI--VDRTTLLALVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 83 GKDALSQAGLMDS-RDTLKETGMIVGVSSAGTEAFLPLFEQRME---DFSLRKALFSGAFSSCCssVSTLLGLQGGVEL- 157
Cdd:cd00828 80 TEEALADAGITDPyEVHPSEVGVVVGSGMGGLRFLRRGGKLDARavnPYVSPKWMLSPNTVAGW--VNILLLSSHGPIKt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 158 VATACTASPNAVGMAFDYIQNGKSKTMLAVGTEPIYLPTFAGFYALNVMHPDT-------CTPFSGQSGMSIGEGAGAIV 230
Cdd:cd00828 158 PVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTAEeepeemsRPFDETRDGFVEAEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 231 LEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRAsGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEANDRIETLAMK 310
Cdd:cd00828 238 LERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGK-GIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 311 KVFANHDKLL-VSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCDLDYVPNEFRD--RKVNIFMKNNY 387
Cdd:cd00828 317 EVAGALGAPLpVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDlnLKVRAALVNAF 396
|
410
....*....|.
gi 15830543 388 AFGGNNCCMIL 398
Cdd:cd00828 397 GFGGSNAALVL 407
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
7-399 |
2.09e-48 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 176.40 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 7 RVVITGLGILSSLAENIQDFrEALLNKKNGVKDSERFAKWFENARAAEVLHDIEYSDLNEDVIDSldnaalwaykvgkdA 86
Cdd:PRK05952 3 KVVVTGIGLVSALGDLEQSW-QRLLQGKSGIKLHQPFPELPPLPLGLIGNQPSSLEDLTKTVVTA--------------A 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 87 LSQAGLMDSrdtLKETGMIVGvSSAGTEAFLPLFEQRM--EDFSLRKALFSGAF-----SSCCSSVSTLLGLQGGVELVA 159
Cdd:PRK05952 68 LKDAGLTPP---LTDCGVVIG-SSRGCQGQWEKLARQMyqGDDSPDEELDLENWldtlpHQAAIAAARQIGTQGPVLAPM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 160 TACTASPNAVGMAFDYIQNGKSKTMLAVGTE-PIYLPTFAGFYALNVMHPDTCTPFSGQ-SGMSIGEGAGAIVLEEYEHA 237
Cdd:PRK05952 144 AACATGLWAIAQGVELIQTGQCQRVIAGAVEaPITPLTLAGFQQMGALAKTGAYPFDRQrEGLVLGEGGAILVLESAELA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 238 VARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEANDRIETLAMKKVFANhd 317
Cdd:PRK05952 224 QKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALFPH-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 318 KLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFShaRPNCDLDYVPNEfRDRKVNIFMKNNYAFGGNNCCMI 397
Cdd:PRK05952 302 RVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQ--EPEFDLNFVRQA-QQSPLQNVLCLSFGFGGQNAAIA 378
|
..
gi 15830543 398 LS 399
Cdd:PRK05952 379 LG 380
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
413-775 |
3.29e-46 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 170.80 E-value: 3.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 413 KRVAISGVGAVSAIGHTLNQVLENIWAQDHHVelGSVTFPDDTleeakellavlDESNQFAElfdeeysfseatlpetes 492
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGI--RPITRFDAS-----------GFPSRIAG------------------ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 493 nfktfQVSGLEPRKHLRRFDQRKATRGGTFALIALTEALEQAK-RKIKRDGDELGMIMGMSRGPQETTYKYLQSLKPD-P 570
Cdd:cd00834 50 -----EVPDFDPEDYLDRKELRRMDRFAQFALAAAEEALADAGlDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKgP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 571 RKVRTSEFPGSLMNAIPTFCGISEGIKGYTTTLATGENSALGALTYGYEIVRQNLQPQVLVGGADEYFPSMSLY----MD 646
Cdd:cd00834 125 RRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAgfaaLR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 647 AVTQKIHMTAEASdyQIYGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCsntyfDA---SLLEEKSASM 723
Cdd:cd00834 205 ALSTRNDDPEKAS--RPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASS-----DAyhiTAPDPDGEGA 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15830543 724 ALAIERALTHAGISAGDIDLVC--GTSNGSDDhsRIEIDAIYNTFAAQNPAVPV 775
Cdd:cd00834 278 ARAMRAALADAGLSPEDIDYINahGTSTPLND--AAESKAIKRVFGEHAKKVPV 329
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
5-398 |
9.25e-46 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 169.44 E-value: 9.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 5 RKRVVITGLGILSSLAENIQDFREALLNKKNG---VKDSERFAKWFENARAAEVLHDIEYSDLnedvidsLDNAALWAYK 81
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAfgvMRRPGRQVPDDAGAGLASAFIGAELDSL-------ALPERLDAKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 82 VGKDALS-QAGLMDSRDTLKE----------TGMIVGVSS-AGTEAFL--PLFEQRMEDFSLRKALfSGAFSSCCSSVST 147
Cdd:PRK07103 74 LRRASLSaQAALAAAREAWRDaalgpvdpdrIGLVVGGSNlQQREQALvhETYRDRPAFLRPSYGL-SFMDTDLVGLCSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 148 LLGLQGgVELVATACTASPN-AVGMAFDYIQNGKSKTMLAVG--TEPIYLpTFAGFYALNVM-------HPD-TCTPFS- 215
Cdd:PRK07103 153 QFGIRG-EGFTVGGASASGQlAVIQAARLVQSGSVDACIAVGalMDLSYW-ECQALRSLGAMgsdrfadEPEaACRPFDq 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 216 GQSGMSIGEGAGAIVLEEYEHAVARGATIYGEILSYATSCDAfhETGPDPRASGAVQVMNKAMANAGVTPEQIDYVNAHG 295
Cdd:PRK07103 231 DRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDA--NRGPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 296 TGTEANDRIETLAMKKVFANHdkLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFshARP-NCDLDYVPNEF 374
Cdd:PRK07103 309 TGSPLGDETELAALFASGLAH--AWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNL--DEPiDERFRWVGSTA 384
|
410 420
....*....|....*....|....
gi 15830543 375 RDRKVNIFMKNNYAFGGNNCCMIL 398
Cdd:PRK07103 385 ESARIRYALSLSFGFGGINTALVL 408
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
86-398 |
1.41e-42 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 158.18 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 86 ALSQAGLMDSRDTLKETGMIVGvSSAGTEAFLPLFEQRMED---FSLRKALFSGAfsSCCssVSTLLGLQGGVELVATAC 162
Cdd:cd00825 22 AIADAGLSREYQKNPIVGVVVG-TGGGSPRFQVFGADAMRAvgpYVVTKAMFPGA--SGQ--IATPLGIHGPAYDVSAAC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 163 TASPNAVGMAFDYIQNGKSKTMLAVGTE----PIYLPTFAGFYALNvmHPDTCTPFSGQS-GMSIGEGAGAIVLEEYEHA 237
Cdd:cd00825 97 AGSLHALSLAADAVQNGKQDIVLAGGSEelaaPMDCEFDAMGALST--PEKASRTFDAAAdGFVFGDGAGALVVEELEHA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 238 VARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEANDRIETLAMKKVFANHd 317
Cdd:cd00825 175 LARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGDK- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 318 KLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFshARPNCDLDYVPNEFRDRKVNIFMKNNYAFGGNNCCMI 397
Cdd:cd00825 254 SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHI--EELDEAGLNIVTETTPRELRTALLNGFGLGGTNATLV 331
|
.
gi 15830543 398 L 398
Cdd:cd00825 332 L 332
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
8-393 |
1.48e-39 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 151.81 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 8 VVITGLGILSSLAENIQDFREALLNKKNGVKdseRFAKWFenaraaevlhdIEYSD--------LNEDVIDSLDNAALW- 78
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIR---TLDDPF-----------VEEFDlpvrigghLLEEFDHQLTRVELRr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 79 -------AYKVGKDALSQAGL--MDSRDTLKETGMIVGVSSAGTEAFLPLFEQRMED---FSLRKALFSGAfsscCSSVS 146
Cdd:PRK07910 80 msylqrmSTVLGRRVWENAGSpeVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAvspLAVQMYMPNGP----AAAVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 147 TLLGLQGGVELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTE------PIylptfAGFYALN-VMH------PDTCTP 213
Cdd:PRK07910 156 LERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVEtrieavPI-----AGFAQMRiVMStnnddpAGACRP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 214 FS-GQSGMSIGEGAGAIVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDYVN 292
Cdd:PRK07910 231 FDkDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 293 AHGTGTEANDRIETLAMKKVFANHdKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCDLDYVPN 372
Cdd:PRK07910 311 AHATGTSVGDVAEGKAINNALGGH-RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAG 389
|
410 420
....*....|....*....|.
gi 15830543 373 EFRDRKVNIFMKNNYAFGGNN 393
Cdd:PRK07910 390 EPRPGNYRYAINNSFGFGGHN 410
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
245-358 |
2.97e-39 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 141.17 E-value: 2.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 245 YGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEANDRIETLAMKKVFANH---DKLLV 321
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGarkQPLAI 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 15830543 322 SSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNF 358
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
78-398 |
4.43e-39 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 148.34 E-value: 4.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 78 WAYK--VGKDALSQAglmDSRDTLKETGMIVGVSSAGTEAFLPLFE-------QRMEDFSLRKALFSGAfsscCSSVSTL 148
Cdd:PRK14691 5 WRYKwiTFHPSLTHA---DNTEKQERTATIIGAGIGGFPAIAHAVRtsdsrgpKRLSPFTVPSFLVNLA----AGHVSIK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 149 LGLQGGVELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTEPIY-LPTFAGFYALNVMH------PDTCT-PF-SGQSG 219
Cdd:PRK14691 78 HHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIdTVSLAGFAAARALSthfnstPEKASrPFdTARDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 220 MSIGEGAGAIVLEEYEHAVARGATIYGEILSYATSCDAFHETGPDPRASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTE 299
Cdd:PRK14691 158 FVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 300 ANDRIETLAMKKVFANHDKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCD-LDYVPNEFRDRK 378
Cdd:PRK14691 238 VGDLGEINAIKHLFGESNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHD 317
|
330 340
....*....|....*....|
gi 15830543 379 VNIFMKNNYAFGGNNCCMIL 398
Cdd:PRK14691 318 MTYALSNGFGFAGVNASILL 337
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
86-398 |
6.51e-35 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 144.24 E-value: 6.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 86 ALSQAGLmdSRDTLK--ETGMIVGVSSAGTEAFLPLFEQRMEDFSLRkalfSGAFSSCCSSVSTLLGLQGGVELVATACT 163
Cdd:COG3321 102 ALEDAGY--DPESLAgsRTGVFVGASSNDYALLLLADPEAIDAYALT----GNAKSVLAGRISYKLDLRGPSVTVDTACS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 164 ASPNAVGMAFDYIQNGKSKTMLAVGTEpIYLP--TFAGFYALNVMHPD-TCTPFSGQS-GMSIGEGAGAIVLEEYEHAVA 239
Cdd:COG3321 176 SSLVAVHLACQSLRSGECDLALAGGVN-LMLTpeSFILFSKGGMLSPDgRCRAFDADAdGYVRGEGVGVVVLKRLSDALR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 240 RGATIYGEILSYATSCDafhetGPD-----PRASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEANDRIETLAMKKVFA 314
Cdd:COG3321 255 DGDRIYAVIRGSAVNQD-----GRSngltaPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 315 NHDK----LLVSSTKSYFGHNIGAAGIVELI-ACLA----TLPdnrvlPTLNFSHARPNCDLD----YVPNEFRDRK--- 378
Cdd:COG3321 330 QGRPadqpCAIGSVKSNIGHLEAAAGVAGLIkAVLAlrhgVLP-----PTLHFETPNPHIDFEnspfYVNTELRPWPagg 404
|
330 340
....*....|....*....|....*.
gi 15830543 379 ------VNIFmknnyAFGGNNCCMIL 398
Cdd:COG3321 405 gprragVSSF-----GFGGTNAHVVL 425
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
135-341 |
2.11e-29 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 117.93 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 135 SGAFSSCCSSVSTLLGLQGGVEL-VATACTASPNAVGMAFDYIQNGKSKTMLAVGTEPIylptfagfyalnvmhpdtctp 213
Cdd:cd00327 40 SGEFSGAAGQLAYHLGISGGPAYsVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF--------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 214 fsgqsgmSIGEGAGAIVLEEYEHAVARGATIYGEILSYATSCDAFHEtGPDPRASGAVQVMNKAMANAGVTPEQIDYVNA 293
Cdd:cd00327 99 -------VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASM-VPAVSGEGLARAARKALEGAGLTPSDIDYVEA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15830543 294 HGTGTEANDRIETLAMKKVFANHDkLLVSSTKSYFGHNIGAAGIVELI 341
Cdd:cd00327 171 HGTGTPIGDAVELALGLDPDGVRS-PAVSATLIMTGHPLGAAGLAILD 217
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
6-237 |
3.34e-25 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 105.41 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 6 KRVVITGLGILSSLAENIQDFREALLNKKNGVK--DSERF--AKWFENARAAE--------VLHDIEYSDLNEDVI---- 69
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISeiPADRWdpDKLYDPPSRIAgkiytkwgGLDDIFDFDPLFFGIspre 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 70 -DSLDNAALWAYKVGKDALSQAGLMDSRDTLKETGMIVGVSSAGTEAFLPLFEqrMEDFSLRKALFSGAFSSCCSS-VST 147
Cdd:pfam00109 81 aERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDE--DGGPRRGSPFAVGTMPSVIAGrISY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 148 LLGLQGGVELVATACTASPNAVGMAFDYIQNGKSKTMLAVGTEPIYLP-TFAGFYALNVMHPD-TCTPFS-GQSGMSIGE 224
Cdd:pfam00109 159 FLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPlGFAGFSAAGMLSPDgPCKAFDpFADGFVRGE 238
|
250
....*....|...
gi 15830543 225 GAGAIVLEEYEHA 237
Cdd:pfam00109 239 GVGAVVLKRLSDA 251
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
6-370 |
1.20e-22 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 101.28 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 6 KRVVITGLGILSSLAENIQDFREALLNKKNGVKDSERFAKWFENARAAEVLHDIEYSD-LNEDVIDSLDNAALWAYKVGK 84
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEhLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 85 DALSQAGLMDSRDTLKETGMIVGVSSAGTEaflplFEQR-MEDFSLRKALFSGAFSSCCS-------SVSTLLGLQGGVE 156
Cdd:cd00832 81 WALADAGVDPAALPPYDMGVVTASAAGGFE-----FGQReLQKLWSKGPRHVSAYQSFAWfyavntgQISIRHGMRGPSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 157 LVATACTASPNAVGMAFDYIQNGkSKTMLAVGTEPIYLPtfagfYALnVMH-----------PDTC-TPFSGQ-SGMSIG 223
Cdd:cd00832 156 VVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCP-----WGW-VAQlssgrlstsddPARAyLPFDAAaAGYVPG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 224 EGAGAIVLEEYEHAVARGATIYGEILSYATSCDafhetgPDP---RASGAVQVMNKAMANAGVTPEQIDYVNAHGTGTEA 300
Cdd:cd00832 229 EGGAILVLEDAAAARERGARVYGEIAGYAATFD------PPPgsgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPE 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 301 NDRIETLAMKKVFANHdKLLVSSTKSYFGHNIGAAGIVELIACLATLPDNRVLPTLNFSHARPNCDLDYV 370
Cdd:cd00832 303 LDRAEAAALAAVFGPR-GVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLV 371
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
412-771 |
3.52e-21 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 96.98 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 412 SKRVAISGVGAVSAIGHTLNQVLENIWAQDHHVElgsvtfpddtleeakellaVLDESNQFAELfdeeysfsEATLPETE 491
Cdd:PRK09116 1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVR-------------------RMPEWDRYDGL--------NTRLAAPI 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 492 SNFktfqvsglEPRKHLrrfdQRKATRG-GTFALIAL--TE-ALEQAK---RKIKRDGdELGMIMGMSRGPQETTYKYLQ 564
Cdd:PRK09116 54 DDF--------ELPAHY----TRKKIRSmGRVSLMATraSElALEDAGllgDPILTDG-RMGIAYGSSTGSTDPIGAFGT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 565 SLKP-DPRKVRTSEFPGSLMNAIPTFCGISEGIKGYTTTLATGENSALGALTYGYEIVRQNLQPQVLVGGADEYFPSMSL 643
Cdd:PRK09116 121 MLLEgSMSGITATTYVRMMPHTTAVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 644 YMD---AVTQK---IHMTAEASDyqiygKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCsntyfDAS-LL 716
Cdd:PRK09116 201 VFDtlfATSTRndaPELTPRPFD-----ANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNS-----DGAhVT 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15830543 717 EEKSASMALAIERALTHAGISAGDIDLVCGTSNGSDDHSRIEIDAIYNTFAAQNP 771
Cdd:PRK09116 271 QPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAAVFGARMP 325
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
504-844 |
7.41e-21 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 95.97 E-value: 7.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 504 PRKHLRRFDQrkATRGGTFALIALTEALEQAKrkIKR----DGDELGMIMGMSRGPQETTYKYLqslKPDPRKVRTSEFP 579
Cdd:cd00828 59 PGWDAKRTGI--VDRTTLLALVATEEALADAG--ITDpyevHPSEVGVVVGSGMGGLRFLRRGG---KLDARAVNPYVSP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 580 GsLMNAIPTFCG-IS---EGIKGYTTTLATGENSALGALTYGYEIVRQNLQPQVLVGGADEYFPSMSLYMDAvtqkihMT 655
Cdd:cd00828 132 K-WMLSPNTVAGwVNillLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFAN------MG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 656 AEASDYQIYGKDPQ-------GYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGkscsnTYFDAS--LLEEKSASMALA 726
Cdd:cd00828 205 ALSTAEEEPEEMSRpfdetrdGFVEAEGAGVLVLERAELALARGAPIYGRVAGTA-----STTDGAgrSVPAGGKGIARA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 727 IERALTHAGISAGDIDLVCGTSNGSDDHSRIEIDAIYNTFAAQNPAVPVVNYNACFGFVASAAGLLNLAVITDCIKKQAV 806
Cdd:cd00828 280 IRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLI 359
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15830543 807 PAIPNTVEFFDE----RVNFVRQSMKLALNHVLLVGATEGGN 844
Cdd:cd00828 360 PPTANLDDVDPDvehlSVVGLSRDLNLKVRAALVNAFGFGGS 401
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
498-812 |
9.07e-20 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 92.42 E-value: 9.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 498 QVSGLEPRKHL--RRFDQR-KATRggtFALIALTEALEQAK-RKIKRDGDELGMIMGMSRGPQETTYKYLQSL-KPDPRK 572
Cdd:cd00832 50 EVPDFDAAEHLpgRLLPQTdRMTR---LALAAADWALADAGvDPAALPPYDMGVVTASAAGGFEFGQRELQKLwSKGPRH 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 573 VRTSEFPGSLMNAIPTFCGISEGIKGYTTTLATGENSALGALTYGYEIVRQNLqPQVLVGGADeyfPSMSLYMDAVTQKI 652
Cdd:cd00832 127 VSAYQSFAWFYAVNTGQISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRRGT-PLVVSGGVD---SALCPWGWVAQLSS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 653 HMTAEASD----YQIYGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKScsntyFDASLLEEKSASMALAIE 728
Cdd:cd00832 203 GRLSTSDDparaYLPFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAAT-----FDPPPGSGRPPGLARAIR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 729 RALTHAGISAGDIDLVCGTSNGSDDHSRIEIDAIYNTFAAQnpAVPVVNYNACFGFVASAAGLLNLAVITDCIKKQAVPA 808
Cdd:cd00832 278 LALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAVFGPR--GVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPP 355
|
....
gi 15830543 809 IPNT 812
Cdd:cd00832 356 TVNV 359
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
413-775 |
7.16e-19 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 89.85 E-value: 7.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 413 KRVAISGVGAVSAIGHTLNQVLENIWAqdhhvelgsvtfpddtleeAKELLAVLDEsnqfaelFDEeysfseatlpeteS 492
Cdd:PRK07314 2 RRVVVTGLGAVSPLGNDVESTWKNLLA-------------------GKSGIGPITH-------FDT-------------S 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 493 NFKTF---QVSGLEPRKHLRRFDQRKATRGGTFALIALTEALEQAKRKIKR-DGDELGMIMGMSRGP----QETTYKYLQ 564
Cdd:PRK07314 43 DLAVKiagEVKDFNPDDYMSRKEARRMDRFIQYGIAAAKQAVEDAGLEITEeNADRIGVIIGSGIGGletiEEQHITLLE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 565 SlkpDPRKVrtSEF--PGSLMNAIPTFCGISEGIKGYTTTLATGENSALGALTYGYEIVRQNLQPQVLVGGADEYFPSMS 642
Cdd:PRK07314 123 K---GPRRV--SPFfvPMAIINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 643 L----YMDAVTQKIHMTAEASdyQIYGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCsntyfDA----S 714
Cdd:PRK07314 198 IagfaAARALSTRNDDPERAS--RPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTG-----DAyhmtA 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830543 715 LLEEKSASmALAIERALTHAGISAGDIDLVC--GTSNGSDDhsRIEIDAIYNTFAAQNPAVPV 775
Cdd:PRK07314 271 PAPDGEGA-ARAMKLALKDAGINPEDIDYINahGTSTPAGD--KAETQAIKRVFGEHAYKVAV 330
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
525-835 |
1.02e-17 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 85.87 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 525 IALTEALEQAKrkIKRDGDELGMIMGMSRGPQ---ET-TYKYLQSLKPDPRKVRTSEFPGSL--MNAIPTFCGIseGIKG 598
Cdd:PRK05952 62 TVVTAALKDAG--LTPPLTDCGVVIGSSRGCQgqwEKlARQMYQGDDSPDEELDLENWLDTLphQAAIAAARQI--GTQG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 599 Y----TTTLATGensaLGALTYGYEIVRQNLQPQVLVGGADEYFPSMSLymdAVTQKIHMTAEASDYQiYGKDPQGYVPG 674
Cdd:PRK05952 138 PvlapMAACATG----LWAIAQGVELIQTGQCQRVIAGAVEAPITPLTL---AGFQQMGALAKTGAYP-FDRQREGLVLG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 675 EGACMLLLEDPQLAVARGAEVLAEVVGYGKSCSNTYFDASLLEEKSAsmALAIERALTHAGISAGDIDLV--CGTSNGSD 752
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSA--IAAIQQCLARSGLTPEDIDYIhaHGTATRLN 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 753 DhsRIEIDAIYNTFAaqnPAVPVVNYNACFGFVASAAGLLNLAVITDCIKKQAVPaiP----NTVEFfdeRVNFVRQSMK 828
Cdd:PRK05952 288 D--QREANLIQALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLP--PcvglQEPEF---DLNFVRQAQQ 357
|
....*..
gi 15830543 829 LALNHVL 835
Cdd:PRK05952 358 SPLQNVL 364
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
413-836 |
1.82e-16 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 82.39 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 413 KRVAISGVGAVSAIGhtlnqvleniwaqdhhveLGSVTFPDdtleeakellAVLDESNQFAELFDEEYSFSEATLPETES 492
Cdd:PRK07103 2 DEVVVTGVGVVSAIG------------------QGRPSFAA----------ALLAGRHAFGVMRRPGRQVPDDAGAGLAS 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 493 NFKTFQVSGLEPRKHLRRFDQRKATRGGTFALIALTEALEQAKRKiKRDGDELGMIMGMSRGPQETTYKYLQSLKPDPRK 572
Cdd:PRK07103 54 AFIGAELDSLALPERLDAKLLRRASLSAQAALAAAREAWRDAALG-PVDPDRIGLVVGGSNLQQREQALVHETYRDRPAF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 573 VRTSeFPGSLMNAipTFCG-ISE--GIKGYTTTLATGENSALGALTYGYEIVRQNLQPQVLVGGADEYFPSMSLymdavt 649
Cdd:PRK07103 133 LRPS-YGLSFMDT--DLVGlCSEqfGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWEC------ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 650 QKIH-MTAEASDYQI---------YGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGkscsnTYFDASLLEEK 719
Cdd:PRK07103 204 QALRsLGAMGSDRFAdepeaacrpFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWS-----MRLDANRGPDP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 720 S-ASMALAIERALTHAGISAGDIDLVCGTSNGSDDHSRIEIDAIyntFAAQNPAVPVVNYNACFGFVASAAGLLNL-AVI 797
Cdd:PRK07103 279 SlEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGDETELAAL---FASGLAHAWINATKSLTGHGLSAAGIVELiATL 355
|
410 420 430
....*....|....*....|....*....|....*....
gi 15830543 798 TDcIKKQAVPAIPNTVEFFDERVNFVRQSMKLALNHVLL 836
Cdd:PRK07103 356 LQ-MRAGFLHPSRNLDEPIDERFRWVGSTAESARIRYAL 393
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
412-766 |
3.86e-16 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 81.58 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 412 SKRVAISGVGAVSAIGhtlNQVlENIWAQDHHVELGSVTFPDDTLEeakellavlDESNQFAelfdeeysfseATLPETE 491
Cdd:PRK06333 3 KKRIVVTGMGAVSPLG---CGV-ETFWQRLLAGQSGIRTLTDFPVG---------DLATKIG-----------GQVPDLA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 492 SNFKtfqvSGLEPRKHLRRFDQRKATRGGTFALIALTEALEQAKRKIKRDGDEL--GMIMGMSRGPQETTYKYLQSL-KP 568
Cdd:PRK06333 59 EDAE----AGFDPDRYLDPKDQRKMDRFILFAMAAAKEALAQAGWDPDTLEDRErtATIIGSGVGGFPAIAEAVRTLdSR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 569 DPRKVRTSEFPGSLMNAIPTFCGISEGIKG----YTTTLATGeNSALGAltyGYEIVRQNLQPQVLVGGADEYFPSMSLY 644
Cdd:PRK06333 135 GPRRLSPFTIPSFLTNMAAGHVSIRYGFKGplgaPVTACAAG-VQAIGD---AARLIRSGEADVAVCGGTEAAIDRVSLA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 645 MDAV-----TQKIHMTAEASdyQIYGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCsntyfDASLL--- 716
Cdd:PRK06333 211 GFAAaralsTRFNDAPEQAS--RPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSA-----DAYHMtag 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15830543 717 EEKSASMALAIERALTHAGISAGDIDLVC--GTSNGSDDHSriEIDAIYNTF 766
Cdd:PRK06333 284 PEDGEGARRAMLIALRQAGIPPEEVQHLNahATSTPVGDLG--EVAAIKKVF 333
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
158-398 |
5.12e-16 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 79.68 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 158 VATACTASPNAVGMAFDYIQNGKSKTMLAVGTEPIYLP-TFAGFYALNVMHPD-TCTPFSGQ-SGMSIGEGAGAIVLEEY 234
Cdd:smart00825 93 VDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPdTFVGLSRAGMLSPDgRCKTFDASaDGYVRGEGVGVVVLKRL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 235 EHAVARGATIYGEILSYATSCDAFHE--TGPDPRAsgavQvmnkamanagvtpeqidyvnahgtgteandrietlamkkv 312
Cdd:smart00825 173 SDALRDGDPILAVIRGSAVNQDGRSNgiTAPSGPA----Q---------------------------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 313 fanhdkLLVSSTKSYFGHNIGAAGIVELI-ACLA----TLPdnrvlPTLNFSHARPNCDLD----YVPNEFRD------- 376
Cdd:smart00825 209 ------LLIGSVKSNIGHLEAAAGVAGLIkVVLAlkhgVIP-----PTLHFETPNPHIDLEesplRVPTELTPwpppgrp 277
|
250 260
....*....|....*....|..
gi 15830543 377 RKVNIfmkNNYAFGGNNCCMIL 398
Cdd:smart00825 278 RRAGV---SSFGFGGTNAHVIL 296
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
570-811 |
3.99e-15 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 77.85 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 570 PRKVRTSEFPGSLMNAIPTFCGISEGIKGYTTTLATGENSALGALTYGYEIVRQNLQPQVLVGGADEYFPSMSLY----M 645
Cdd:PRK14691 54 PKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAgfaaA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 646 DAVTQKIHMTAEASDyQIYGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCSNTYFDASLLEEKSASMAL 725
Cdd:PRK14691 134 RALSTHFNSTPEKAS-RPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAM 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 726 AIerALTHAGISAGDIDLVCGTSNGSDDHSRIEIDAIYNTFAAQNpAVPVVNYNACFGFVASAAGLLNLAVITDCIKKQA 805
Cdd:PRK14691 213 KI--ALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESN-ALAITSTKSATGHLLGAAGGLETIFTVLALRDQI 289
|
....*.
gi 15830543 806 VPAIPN 811
Cdd:PRK14691 290 VPATLN 295
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
515-811 |
7.47e-15 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 77.81 E-value: 7.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 515 KATRGGTFALIALTEALEQAKRKI--KRDGDELGMIMGMSRGPQET---TYKYLQSLKPdpRKVRTSEFPGSLMNAIPTF 589
Cdd:PTZ00050 73 RESRATHFAMAAAREALADAKLDIlsEKDQERIGVNIGSGIGSLADltdEMKTLYEKGH--SRVSPYFIPKILGNMAAGL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 590 CGISEGIKG----YTTTLATGENSALGALTYgyeiVRQNLQPQVLVGGADEYFPSMSLY----MDAVTQKIH-MTAEASd 660
Cdd:PTZ00050 151 VAIKHKLKGpsgsAVTACATGAHCIGEAFRW----IKYGEADIMICGGTEASITPVSFAgfsrMRALCTKYNdDPQRAS- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 661 yQIYGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCSNTYFDASLLEEKSASmaLAIERALTHAG-ISAG 739
Cdd:PTZ00050 226 -RPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGAR--RCMENALKDGAnININ 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830543 740 DIDLV-C-GTSNGSDDhsRIEIDAIYNTFA-AQNPAVPVVNYNACFGFVASAAGLLNLAVITDCIKKQAVPAIPN 811
Cdd:PTZ00050 303 DVDYVnAhATSTPIGD--KIELKAIKKVFGdSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTIN 375
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
499-811 |
9.58e-15 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 77.35 E-value: 9.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 499 VSGLEPRKHLRRFDQRKATRGGTFALIALTEALEQAKRKI-KRDGDELGMIMGMSRGPQ---ETTYKYLqsLKPDPRKVR 574
Cdd:PRK08722 54 VKDFNCEEYMSKKDARKMDLFIQYGIAAGIQALDDSGLEVtEENAHRIGVAIGSGIGGLgliEAGHQAL--VEKGPRKVS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 575 TSEFPGSLMNAIPTFCGISEGIKGYTTTLATGENSALGALTYGYEIVRQNLQPQVLVGGADEyfPSMSLYMDAVTQKIHM 654
Cdd:PRK08722 132 PFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEK--ASTPLGMAGFGAAKAL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 655 TAEASDYQI----YGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKScSNTYFDASLLEEKSASmALAIERA 730
Cdd:PRK08722 210 STRNDEPQKasrpWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMS-GDAYHMTSPSEDGSGG-ALAMEAA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 731 LTHAGISAGDIDLVC--GTSNGSDDHSriEIDAIYNTFA-AQNPAVPVVNYNACFGFVASAAGLLNLAVITDCIKKQAVP 807
Cdd:PRK08722 288 MRDAGVTGEQIGYVNahGTSTPAGDVA--EIKGIKRALGeAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVP 365
|
....
gi 15830543 808 AIPN 811
Cdd:PRK08722 366 PTIN 369
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
521-850 |
1.59e-13 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 72.67 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 521 TFALIALTEALEQAKRKIKRDGDEL-GMIMGMSRGPQETTYKYLQSLKP-DPRKVRTSEFPGSlmnaipTFCGISE-GIK 597
Cdd:cd00825 13 ILGFEAAERAIADAGLSREYQKNPIvGVVVGTGGGSPRFQVFGADAMRAvGPYVVTKAMFPGA------SGQIATPlGIH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 598 GYTTTLATGENSALGALTYGYEIVRQNLQPQVLVGGADEYFPSMSLYMDAvtqKIHMTAEASDYQIYGKDPQGYVPGEGA 677
Cdd:cd00825 87 GPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDA---MGALSTPEKASRTFDAAADGFVFGDGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 678 CMLLLEDPQLAVARGAEVLAEVVGYGKSCSNTYfdASLLEEKSASMALAIERALTHAGISAGDIDLVCGTSNGSDDHSRI 757
Cdd:cd00825 164 GALVVEELEHALARGAHIYAEIVGTAATIDGAG--MGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 758 EIDAIYNTFAAQNPAVPVVNYNacFGFVASAAGLLNLAVITDCIKKQAVPAIPNTVEFFDERVNFVRQSMKLALNHVLLV 837
Cdd:cd00825 242 ELKLLRSEFGDKSPAVSATKAM--TGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETTPRELRTALLN 319
|
330
....*....|...
gi 15830543 838 GATEGGNYYAFVI 850
Cdd:cd00825 320 GFGLGGTNATLVL 332
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
529-811 |
5.25e-13 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 71.82 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 529 EALEQAKRKIKR-DGDELGMIMGMSrgpqetTYKYLQSLKPDPRKVRTSEFPGSLMNAIPTFcgISE--GIKGYTTTLAT 605
Cdd:cd00833 97 EALEDAGYSPESlAGSRTGVFVGAS------SSDYLELLARDPDEIDAYAATGTSRAFLANR--ISYffDLRGPSLTVDT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 606 GENSALGALTYGYEIVRQNLQPQVLVGGAD-EYFPSMSLYMDavtqKIHMTAEASDYQIYGKDPQGYVPGEGACMLLLED 684
Cdd:cd00833 169 ACSSSLVALHLACQSLRSGECDLALVGGVNlILSPDMFVGFS----KAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 685 PQLAVARGAEVLAEVVGYGKSC---SNTYFDASlleekSASMALAIERALTHAGISAGDIDLV-C---GTSNGsDdhsRI 757
Cdd:cd00833 245 LSDALRDGDRIYAVIRGSAVNQdgrTKGITAPS-----GEAQAALIRRAYARAGVDPSDIDYVeAhgtGTPLG-D---PI 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830543 758 EIDAIYNTFAAQNPAVpvvnyNACF-GFVAS-------AAGLLNLAVITDCIKKQAVPAIPN 811
Cdd:cd00833 316 EVEALAKVFGGSRSAD-----QPLLiGSVKSnighleaAAGLAGLIKVVLALEHGVIPPNLH 372
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
413-798 |
2.14e-12 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 69.76 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 413 KRVAISGVGAVSAIGHTLNQVLENIWAQDHHVelgsvtfpdDTLEeakellavldesnqfaeLFD-EEYSFSEATlpete 491
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGI---------KKIT-----------------LFDaSDFPVQIAG----- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 492 snfktfQVSGLEPRKHLRRFDQRKATRGGTFALIALTEALEQAKRKIKR-DGDELGMIMGMSRGPQETTYK-YLQSLKPD 569
Cdd:PRK08439 51 ------EITDFDPTEVMDPKEVKKADRFIQLGLKAAREAMKDAGFLPEElDAERFGVSSASGIGGLPNIEKnSIICFEKG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 570 PRKVRTSEFPGSLMNAIPTFCGISEGIKGYTTTLATGENSALGALTYGYEIVRQNLQPQVLVGGADEY--------FPSM 641
Cdd:PRK08439 125 PRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAicpvgiggFAAM 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 642 SlymdAVTQKIHMTAEASdyQIYGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCsntyfDASLLEEKSA 721
Cdd:PRK08439 205 K----ALSTRNDDPKKAS--RPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESG-----DANHITSPAP 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15830543 722 SMAL-AIERALTHAGISAGDIDLVCGTSNGSDDHSriEIDAIYNTFAAQNPAVPVVNYNACFGFVASAAGLLNlAVIT 798
Cdd:PRK08439 274 EGPLrAMKAALEMAGNPKIDYINAHGTSTPYNDKN--ETAALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIE-AVIS 348
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
413-790 |
6.29e-11 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 65.77 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 413 KRVAISGVGAVSAIGHTLNQVLENIwaqdhhvelgsvtfpddtleeakellavLDESNQFAELfdeeYSFSEATLP-ETE 491
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNL----------------------------LEGVSGISEI----ERFDCSQFPtRIA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 492 SNFKTFQVSGLEPRKHLRRFDQrkatrggtFALIALTealeqAKRKIKRDG-------DEL-----GMIMGMSRGPQETT 559
Cdd:PLN02787 177 GEIKSFSTDGWVAPKLSKRMDK--------FMLYLLT-----AGKKALADGgitedvmKELdktkcGVLIGSAMGGMKVF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 560 YKYLQSLKPDPRKVRTSEFPGSLMNAIPTFCGISEGIKG----YTTTLATGENSALGALTYgyeiVRQNLQPQVLVGGAD 635
Cdd:PLN02787 244 NDAIEALRISYRKMNPFCVPFATTNMGSAMLAMDLGWMGpnysISTACATSNFCILNAANH----IIRGEADVMLCGGSD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 636 EYFPSMSL----YMDAVTQKIHMTAEASdyQIYGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCsntyf 711
Cdd:PLN02787 320 AAIIPIGLggfvACRALSQRNDDPTKAS--RPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTC----- 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 712 DASLLEE---KSASMALAIERALTHAGISAGDIDLVCGTSNGSDDHSRIEIDAIYNTFaAQNPAVPVVNYNACFGFVASA 788
Cdd:PLN02787 393 DAYHMTEphpEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCF-GQNPELRVNSTKSMIGHLLGA 471
|
..
gi 15830543 789 AG 790
Cdd:PLN02787 472 AG 473
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
413-773 |
1.24e-10 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 64.31 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 413 KRVAISGVGAVSAIGHTLNQVLENiwaqdhhvelgsvtfpddtLEEAKELLAvldesnqfaelFDEEYSfseatlpetES 492
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLAS-------------------LREGRSGIT-----------FSPEFA---------EM 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 493 NFKTfQVSG---LEPRKHLRRFDQRKATRGGTFALIALTEALEQAKRKIKRDGDE-LGMIMGmSRGPqeTTYKYLQSL-- 566
Cdd:PRK07967 43 GMRS-QVWGnvkLDPTGLIDRKVMRFMGDASAYAYLAMEQAIADAGLSEEQVSNPrTGLIAG-SGGG--STRNQVEAAda 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 567 ---KPDPRKVRTSEFPGSLMNAIPTFCGISEGIKGYTTTLATGENSALGALTYGYEIVRQNLQPQVLVGGADEYFPSMSL 643
Cdd:PRK07967 119 mrgPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSC 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 644 YMDAvtqkihMTAEASDY--------QIYGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCSNTYFDASL 715
Cdd:PRK07967 199 LFDA------MGALSTKYndtpekasRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPS 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830543 716 LE--EKSASMALaieralthAGISaGDIDLVC--GTSNGSDDHSriEIDAIYNTFAAQNPAV 773
Cdd:PRK07967 273 GEgaVRCMQMAL--------ATVD-TPIDYINthGTSTPVGDVK--ELGAIREVFGDKSPAI 323
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
73-337 |
5.37e-09 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 58.71 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 73 DNAALWAYKVGKDALSQAGLmdsrdTLKETGMIVgVSSAGTEAFLPlfeqrmedfslrkalfSGAfssccSSVSTLLGLQ 152
Cdd:cd00830 48 ETTSDLAVEAAKKALEDAGI-----DADDIDLII-VATSTPDYLFP----------------ATA-----CLVQARLGAK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 153 GGVEL-VATACTASPNAVGMAFDYIQNGKSKTMLAVGTEpiylpTFAGFyaLNVMHPDTCTPFsgqsgmsiGEGAGAIVL 231
Cdd:cd00830 101 NAAAFdINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAE-----TLSRI--LDWTDRSTAVLF--------GDGAGAVVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 232 EEYEHAVARGATI------YGEILSYATSCDAFHETGPDPRASG-----------AVQVM----NKAMANAGVTPEQIDY 290
Cdd:cd00830 166 EATEEDPGILDSVlgsdgsGADLLTIPAGGSRSPFEDAEGGDPYlvmdgrevfkfAVRLMpesiEEALEKAGLTPDDIDW 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15830543 291 VNAHgtgtEANDRIETLAMKKVFANHDKllVSSTKSYFGhNIGAAGI 337
Cdd:cd00830 246 FVPH----QANLRIIEAVAKRLGLPEEK--VVVNLDRYG-NTSAASI 285
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
664-773 |
2.44e-08 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 57.05 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 664 YGKDPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCSNTYFDASLLEEKSAsmALAIERALTHAGISAGDIDL 743
Cdd:PRK07910 231 FDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERA--GHAMTRAIELAGLTPGDIDH 308
|
90 100 110
....*....|....*....|....*....|
gi 15830543 744 VCGTSNGSDDHSRIEIDAIYNTFAAQNPAV 773
Cdd:PRK07910 309 VNAHATGTSVGDVAEGKAINNALGGHRPAV 338
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
595-790 |
3.40e-08 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 56.56 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 595 GIKGYTTTLATGENSALGALTYGYEIVRQNLQPQVLVGGAD-----EYFPSMSLyMDAVTQKIHMTAEASdyQIYGKDPQ 669
Cdd:PRK06501 163 GTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDgsvsaEALIRFSL-LSALSTQNDPPEKAS--KPFSKDRD 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 670 GYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCSNtyFDASLLEEKSASMALAIERALTHAGISAGDIDLVC--GT 747
Cdd:PRK06501 240 GFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADS--FHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINahGT 317
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15830543 748 SNGSDDhsRIEIDAIYNTFAAQNPAVPVVNYNACFGFVASAAG 790
Cdd:PRK06501 318 STPEND--KMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAG 358
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
522-683 |
3.49e-08 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 55.33 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 522 FALIALTEALEQAKRKIKR-DGDELGMIMGMSRGpqetTYKYLQSLKPDPRKVRTSEFP-GSLMNAIPTFCGISEGIKGY 599
Cdd:pfam00109 90 LLLEAAWEALEDAGITPDSlDGSRTGVFIGSGIG----DYAALLLLDEDGGPRRGSPFAvGTMPSVIAGRISYFLGLRGP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 600 TTTLATGENSALGALTYGYEIVRQNLQPQVLVGGADEYFPSMSLY----MDAVTQKIHMTAeasdyqiYGKDPQGYVPGE 675
Cdd:pfam00109 166 SVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAgfsaAGMLSPDGPCKA-------FDPFADGFVRGE 238
|
....*...
gi 15830543 676 GACMLLLE 683
Cdd:pfam00109 239 GVGAVVLK 246
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
667-772 |
3.87e-08 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 56.72 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 667 DPQGYVPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKSCSNTYFDASLLEEKSAsmALAIERALTHAGISAGDIDLVCG 746
Cdd:PLN02836 247 DRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGA--VLAMTRALQQSGLHPNQVDYVNA 324
|
90 100
....*....|....*....|....*.
gi 15830543 747 TSNGSDDHSRIEIDAIYNTFAAQNPA 772
Cdd:PLN02836 325 HATSTPLGDAVEARAIKTVFSEHATS 350
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
79-337 |
2.57e-07 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 53.58 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 79 AYKVGKDALSQAGLmdsrdTLKETGMIVgVSSAGTEAFLPlfeqrmedfslrkalfsgafsSCCSSVSTLLGLQGGVEL- 157
Cdd:COG0332 55 AVEAARKALEAAGI-----DPEDIDLII-VATVTPDYLFP---------------------STACLVQHKLGAKNAAAFd 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 158 VATACTASPNAVGMAFDYIQNGKSKTMLAVGTEpiylpTFAGFyaLNVMHPDTCTPFsgqsgmsiGEGAGAIVLEEYE-- 235
Cdd:COG0332 108 INAACSGFVYALSVAAALIRSGQAKNVLVVGAE-----TLSRI--VDWTDRSTCVLF--------GDGAGAVVLEASEeg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 236 ----HAVARGATIYGEIL---SYATSCDAFHETGPDPR------------ASGAVQVMNKAMANAGVTPEQIDYVNAHgt 296
Cdd:COG0332 173 pgilGSVLGSDGSGADLLvvpAGGSRNPPSPVDEGDHYlrmdgrevfkfaVRNLPEVIREALEKAGLTLDDIDWFIPH-- 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15830543 297 gtEANDRI-ETLA------MKKVFANHDKllvsstksyFGhNIGAAGI 337
Cdd:COG0332 251 --QANLRIiEAVAkrlglpEEKVVVNIDR---------YG-NTSAASI 286
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
1-335 |
7.01e-07 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 52.65 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 1 MKTNRKRVVITGLGILSSLAENIqDFREALLNKKNG--VKDSERFAKWfenaraaeVLHDIEYSDLNEDVIDSLDNAAL- 77
Cdd:PRK06519 1 MRMQPNDVVITGIGLVSSLGEGL-DAHWNALSAGRPqpNVDTETFAPY--------PVHPLPEIDWSQQIPKRGDQRQMe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 78 -W----AYKVGKdALSQAGLMDSRDTLKETGMIVG---------VSSA-------GTEAFLPLFEQRMEDfsLRKALFsg 136
Cdd:PRK06519 72 tWqrlgTYAAGL-ALDDAGIKGNEELLSTMDMIVAagggerdiaVDTAilnearkRNDRGVLLNERLMTE--LRPTLF-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 137 afsscCSSVSTLLGlqGGVELVATACTASP----------NAVGMAFDYIQNGKSKTMLaVGT-------EPIYLPTFAG 199
Cdd:PRK06519 147 -----LAQLSNLLA--GNISIVHKVTGSSRtfmgeesagvSAIEIAFARIASGQSDHAL-VGGaynaerpDMLLLYELGG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 200 FYALNVMHPDTCTPFSGQSGMSIGEGAGAIVLEEYEHAVARGATIYGEILSYatscdafhETGPDPRASGAVQ-VMNKAM 278
Cdd:PRK06519 219 LLLKGGWAPVWSRGGEDGGGFILGSGGAFLVLESREHAEARGARPYARISGV--------ESDRARRAPGDLEaSLERLL 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15830543 279 ANAGVTPEQiDYVNAHGTGTEAndriETLAMKKVFANHDKLLVSSTKSYFGHNIGAA 335
Cdd:PRK06519 291 KPAGGLAAP-TAVISGATGAHP----ATAEEKAALEAALAGPVRGIGTLFGHTMEAQ 342
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
696-811 |
4.33e-06 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 46.41 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 696 LAEVVGYGKSCSNtyFDASLLEEKSASMALAIERALTHAGISAGDIDLV--CGTSNGSDDhsRIEIDAIYNTFAAQNPAV 773
Cdd:pfam02801 1 YAVIKGSAVNHDG--RHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVeaHGTGTPLGD--PIEAEALKRVFGSGARKQ 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15830543 774 PVvnynacfgFVAS----------AAGLLNLAVITDCIKKQAVPAIPN 811
Cdd:pfam02801 77 PL--------AIGSvksnighlegAAGAAGLIKVVLALRHGVIPPTLN 116
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
523-756 |
5.60e-06 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 49.25 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 523 ALIALTEALEQAKRkikRDGDELGMIMGmsrgpqettykylqsLKPDPRKVRTSEFPGSLMNAIPTFCGISegIKGYTTT 602
Cdd:PRK06147 69 AAPAIAEALEGLPA---LDASEAPLLLC---------------VAEEERPGRPPDLEERLLRELEARLGLR--LEPGSAV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 603 LATGENSALGALTYGYEIVRQNLQPQVLVGGADEYfpsmslymdaVTQKIHMTAEASDYQIYGKDPQGYVPGEGACMLLL 682
Cdd:PRK06147 129 IARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSL----------LTGPTLAHYEARDRLLTSQNSNGFIPGEAAAAVLL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830543 683 EDPQLAVARGAEVLAevVGYGKScSNTYFDASLLEEKSASMALAIERALTHAGISAGDIDLVCGTSNGsdDHSR 756
Cdd:PRK06147 199 GRPAGGEAPGLPLLG--LGLGRE-PAPVGESEDLPLRGDGLTQAIRAALAEAGCGLEDMDYRIADLNG--EQYR 267
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
79-354 |
1.04e-05 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 48.32 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 79 AYKVGKDALSQAGLmdsrdTLKETGMIVgVSSAGTEAFLPlfeqrmedfslrkalfsgafsSCCSSVSTLLGLQ--GGVE 156
Cdd:PRK12879 57 AIKAAERALARAGL-----DAEDIDLII-VATTTPDYLFP---------------------STASQVQARLGIPnaAAFD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 157 LVAtACTASPNAVGMAFDYIQNGKSKTMLAVGTEPIylptfaGFYaLNVMHPDTCTPFsgqsgmsiGEGAGAIVLEEYEH 236
Cdd:PRK12879 110 INA-ACAGFLYGLETANGLITSGLYKKVLVIGAERL------SKV-TDYTDRTTCILF--------GDGAGAVVLEATEN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 237 AVARGATIYG------EILSYATSCDAFHETG----PDPRASG------AVQVMNKAM----ANAGVTPEQIDYVNAHgt 296
Cdd:PRK12879 174 EPGFIDYVLGtdgdggDILYRTGLGTTMDRDAlsgdGYIVQNGrevfkwAVRTMPKGArqvlEKAGLTKDDIDWVIPH-- 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15830543 297 gtEANDR-IETLAMKKVFANHdKLLVSSTksYFGhNIGAAGIVeLIACLAtLPDNRVLP 354
Cdd:PRK12879 252 --QANLRiIESLCEKLGIPME-KTLVSVE--YYG-NTSAATIP-LALDLA-LEQGKIKP 302
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
79-318 |
1.08e-05 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 48.15 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 79 AYKVGKDALSQAGLmdsrdTLKETGM-IVGVSSAgteaflplfeqrmedfslrkalfSGAFSSCCSSVSTLLGLQGGVEL 157
Cdd:PRK09352 56 ATEAAKKALEAAGI-----DPEDIDLiIVATTTP-----------------------DYAFPSTACLVQARLGAKNAAAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 158 -VATACTASPNAVGMAFDYIQNGKSKTMLAVGTEpiylpTFAGFyalnvMHPD---TCTPFsgqsgmsiGEGAGAIVLEE 233
Cdd:PRK09352 108 dLSAACSGFVYALSTADQFIRSGAYKNVLVIGAE-----KLSRI-----VDWTdrsTCVLF--------GDGAGAVVLGA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 234 YE---------HAVARgatiYGEILsYATSCDAFHETGPDP-RASG------AVQVM----NKAMANAGVTPEQIDYVNA 293
Cdd:PRK09352 170 SEepgilsthlGSDGS----YGDLL-YLPGGGSRGPASPGYlRMEGrevfkfAVRELakvaREALEAAGLTPEDIDWLVP 244
|
250 260 270
....*....|....*....|....*....|..
gi 15830543 294 HgtgtEANDRI-ETLA------MKKVFANHDK 318
Cdd:PRK09352 245 H----QANLRIiDATAkklglpMEKVVVTVDK 272
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
672-810 |
4.83e-05 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 45.90 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 672 VPGEGACMLLLEDPQLAVARGAEVLAEVVGYGKscsnTYFDASLLEEKSASM-ALAIERALTHAGISAGDIDLV----CG 746
Cdd:cd00327 99 VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAA----TFDGASMVPAVSGEGlARAARKALEGAGLTPSDIDYVeahgTG 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830543 747 TSNGsddhSRIEIDAIYNTFAAQNPAVPVVnyNACFGFVASAAGLLNLAVITDCIKKQAVPAIP 810
Cdd:cd00327 175 TPIG----DAVELALGLDPDGVRSPAVSAT--LIMTGHPLGAAGLAILDELLLMLEHEFIPPTP 232
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
221-345 |
5.09e-05 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 46.62 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 221 SIGEGAGAIVLEEYEHAVARGATIYGEILSYAtscDAfhETGPDPRASGAVQVMNKAMANAGVTPEQIDY--VN-AHGTG 297
Cdd:PLN02644 249 SISDGAAALVLVSGEKALELGLQVIAKIRGYA---DA--AQAPELFTTAPALAIPKALKHAGLEASQVDYyeINeAFSVV 323
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15830543 298 TEANDRIETLamkkvfaNHDKLLVSSTKSYFGHNIGAAG---IVELIACLA 345
Cdd:PLN02644 324 ALANQKLLGL-------DPEKVNVHGGAVSLGHPIGCSGariLVTLLGVLR 367
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
217-291 |
1.82e-04 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 44.63 E-value: 1.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830543 217 QSGMSIGEGAGAIVLEEYEHAVARGATIYGeiLSYATSCDAFHETGPDP-RASGAVQVMNKAMANAGVTPEQIDYV 291
Cdd:PRK06147 184 SNGFIPGEAAAAVLLGRPAGGEAPGLPLLG--LGLGREPAPVGESEDLPlRGDGLTQAIRAALAEAGCGLEDMDYR 257
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
675-743 |
2.52e-04 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 44.31 E-value: 2.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 675 EGACMLLLEDPQLAVARGAEVLAEVVGYGkscsntyfDASLLEEK-SASMALAIERALTHAGISAGDIDL 743
Cdd:PLN02644 252 DGAAALVLVSGEKALELGLQVIAKIRGYA--------DAAQAPELfTTAPALAIPKALKHAGLEASQVDY 313
|
|
| ASKHA_NBD_benz_CoA_BzdQ |
cd24106 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and ... |
246-297 |
1.03e-03 |
|
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and similar proteins; bzd-type benzoyl-CoA reductase BzdQ is encoded by the gene bzdQ from a benzoate-inducible catabolic operon in Azoarcus sp. The bzd-type benzoyl-CoA reductase system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for several different aromatic compounds, such as phenol and toluene. BzdQ may function the same as the A subunit of benzoyl-CoA reductase BcrA from Thauera aromatica and benzoyl-CoA reductase BadF from Rhodopseudomonas palustris.
Pssm-ID: 466956 Cd Length: 253 Bit Score: 41.82 E-value: 1.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15830543 246 GEILSYATScdafhETGPDPRASgAVQVMNKAMANAGVTPEQIDYVNAHGTG 297
Cdd:cd24106 19 GELYAYSNM-----RTGSDSPES-AQKALNAALEKTGLKLEDIHYIVGTGYG 64
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
676-744 |
3.11e-03 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 40.93 E-value: 3.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830543 676 GACMLLLEDPQLAVARGAEVLAEVVGYG-KSCSNTYFdaslleekSASMALAIERALTHAGISAGDIDLV 744
Cdd:cd00751 247 GAAAVLLMSEEKAKELGLKPLARIVGYAvAGVDPAIM--------GIGPVPAIPKALKRAGLTLDDIDLI 308
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
217-291 |
3.53e-03 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 40.82 E-value: 3.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830543 217 QSGMSigEGAGAIVLEEYEHAVARGATIYGEILSYATscdafheTGPDPR--ASGAVQVMNKAMANAGVTPEQIDYV 291
Cdd:COG0183 245 ASGIN--DGAAALLLMSEEAAKELGLKPLARIVAYAV-------AGVDPEimGIGPVPATRKALARAGLTLDDIDLI 312
|
|
| |
