|
Name |
Accession |
Description |
Interval |
E-value |
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
9-422 |
1.85e-161 |
|
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: 460.72 E-value: 1.85e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 9 HKVVVTGLGETTPLGGTVATTWDAMLRGESGLGLLEDEsWAKDLPPLLGGRAK-VDPGTGLGHQQRRRLSRSAQFAVTAA 87
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRF-DASGLPVRIAGEVKdFDPEEYLDRKELRRMDRFTQYALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 88 AEAWADAGLDEGSVTPSRVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGNGSAAAVALLVNARLGVHATVN 167
Cdd:COG0304 80 REALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVST 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 168 ACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRVDDPASACRPYDADRDGMVLGEGAGILVLE 247
Cdd:COG0304 160 ACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 248 SERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMAV 327
Cdd:COG0304 240 ELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 328 FGDADGDatqgPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHGGPLKLGPEqiIAVKN 407
Cdd:COG0304 320 FGDHAYK----VPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID--YALSN 393
|
410
....*....|....*
gi 2768338898 408 SAGFGGHNVALTFRA 422
Cdd:COG0304 394 SFGFGGHNASLVFKR 408
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
9-420 |
5.20e-152 |
|
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: 436.58 E-value: 5.20e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 9 HKVVVTGLGETTPLGGTVATTWDAMLRGESGLGLLEDEsWAKDLPPLLGGRAK-VDPGTGLGHQQRRRLSRSAQFAVTAA 87
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRF-DASGFPSRIAGEVPdFDPEDYLDRKELRRMDRFAQFALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 88 AEAWADAGLDEGSVTPSRVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGNGSAAAVALLVNARLGVHATVN 167
Cdd:cd00834 80 EEALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVST 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 168 ACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRVDDPASACRPYDADRDGMVLGEGAGILVLE 247
Cdd:cd00834 160 ACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 248 SERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMAV 327
Cdd:cd00834 240 SLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 328 FgdadGDATQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHGGPLKLGPEqiIAVKN 407
Cdd:cd00834 320 F----GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR--YALSN 393
|
410
....*....|...
gi 2768338898 408 SAGFGGHNVALTF 420
Cdd:cd00834 394 SFGFGGHNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
11-421 |
2.95e-139 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 404.17 E-value: 2.95e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 11 VVVTGLGETTPLGGTVATTWDAMLRGESGLGLLEDESwAKDLPPLLGGRAK-VDPGTGLGHQQRRRLSRSAQFAVTAAAE 89
Cdd:PRK07314 4 VVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFD-TSDLAVKIAGEVKdFNPDDYMSRKEARRMDRFIQYGIAAAKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 90 AWADAGLDEGSVTPSRVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGNGSAAAVALLVNARLGVHATVNAC 169
Cdd:PRK07314 83 AVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVTAC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 170 SSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRVDDPASACRPYDADRDGMVLGEGAGILVLESE 249
Cdd:PRK07314 163 ATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLEEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 250 RHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMAVFG 329
Cdd:PRK07314 243 EHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 330 DADGDAtqgpALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHGGPLKLGPEqiIAVKNSA 409
Cdd:PRK07314 323 EHAYKV----AVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID--YALSNSF 396
|
410
....*....|..
gi 2768338898 410 GFGGHNVALTFR 421
Cdd:PRK07314 397 GFGGTNASLVFK 408
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
9-421 |
1.57e-138 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 402.25 E-value: 1.57e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 9 HKVVVTGLGETTPLGGTVATTWDAMLRGESGLGLLeDESWAKDLPPLLGGRAK-VDPGTGLGHQQRRRLSRSAQFAVTAA 87
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPI-TRFDASDLPVKIAGEVKdFDPEDYIDKKEARRMDRFIQYALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 88 AEAWADAGLDEGSVTPSRVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGNGSAAAVALLVNARLGVHATVN 167
Cdd:TIGR03150 80 KEAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 168 ACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRVDDPASACRPYDADRDGMVLGEGAGILVLE 247
Cdd:TIGR03150 160 ACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 248 SERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMAV 327
Cdd:TIGR03150 240 ELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 328 FGDAdgdaTQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHGGPLKLGPEqiIAVKN 407
Cdd:TIGR03150 320 FGDH----AYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID--YALSN 393
|
410
....*....|....
gi 2768338898 408 SAGFGGHNVALTFR 421
Cdd:TIGR03150 394 SFGFGGTNASLVFK 407
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
10-421 |
3.47e-111 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 333.12 E-value: 3.47e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 10 KVVVTGLGETTPLGGTVATTWDAMLRGESGLGLLEDEsWAKDLPPLLGG---------RAKVDPGTGLGHQQRRRLSRSA 80
Cdd:PRK06333 5 RIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDF-PVGDLATKIGGqvpdlaedaEAGFDPDRYLDPKDQRKMDRFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 81 QFAVTAAAEAWADAGLDEGSVT-PSRVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGNGSAAAVALLVNAR 159
Cdd:PRK06333 84 LFAMAAAKEALAQAGWDPDTLEdRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGFK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 160 LGVHATVNACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRV-DDPASACRPYDADRDGMVLG 238
Cdd:PRK06333 164 GPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRFnDAPEQASRPFDRDRDGFVMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 239 EGAGILVLESERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDA 318
Cdd:PRK06333 244 EGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGDL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 319 AEARAVMAVFGDADgdatqGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLD-EGLSVDVVHGGPLKL 397
Cdd:PRK06333 324 GEVAAIKKVFGHVS-----GLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDpAAEGLDVVANKARPM 398
|
410 420
....*....|....*....|....
gi 2768338898 398 GPEqiIAVKNSAGFGGHNVALTFR 421
Cdd:PRK06333 399 DMD--YALSNGFGFGGVNASILFR 420
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
11-420 |
1.41e-110 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 331.69 E-value: 1.41e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 11 VVVTGLGETTPLGGTVATTWDAMLRGESGLGLLEDESWAK-DLPPLLGGRAKVDPGTGLGHQQRRRLSRSAQFAVTAAAE 89
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEEfDLPVRIGGHLLEEFDHQLTRVELRRMSYLQRMSTVLGRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 90 AWADAGLDEgsVTPSRVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGNGSAAAVALLVNARLGVHATVNAC 169
Cdd:PRK07910 94 VWENAGSPE--VDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVSAC 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 170 SSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRA-LSQRVDDPASACRPYDADRDGMVLGEGAGILVLES 248
Cdd:PRK07910 172 ASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGALMVIET 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 249 ERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMAVF 328
Cdd:PRK07910 252 EEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNAL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 329 GdadgdaTQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHGGPLKlgPEQIIAVKNS 408
Cdd:PRK07910 332 G------GHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRP--GNYRYAINNS 403
|
410
....*....|..
gi 2768338898 409 AGFGGHNVALTF 420
Cdd:PRK07910 404 FGFGGHNVALAF 415
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
20-421 |
3.04e-105 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 317.79 E-value: 3.04e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 20 TPLGGTVATTWDAMLRGESGL----------------GLLEDESWAKdLPPLLGGRAKVDPGTGLGHQQRRRLSRSAQFA 83
Cdd:PTZ00050 3 TPLGVGAESTWEALIAGKSGIrkltefpkflpdcipeQKALENLVAA-MPCQIAAEVDQSEFDPSDFAPTKRESRATHFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 84 VTAAAEAWADAGLDEGS-VTPSRVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGNGSAAAVALLVNARLGV 162
Cdd:PTZ00050 82 MAAAREALADAKLDILSeKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKLKGPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 163 HATVNACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRV-DDPASACRPYDADRDGMVLGEGA 241
Cdd:PTZ00050 162 GSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYnDDPQRASRPFDKDRAGFVMGEGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 242 GILVLESERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLAD-ADVTPADVAHFNANGTATAPGDAAE 320
Cdd:PTZ00050 242 GILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDgANININDVDYVNAHATSTPIGDKIE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 321 ARAVMAVFGDadgDATQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHGGPLKLGPE 400
Cdd:PTZ00050 322 LKAIKKVFGD---SGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPLQS 398
|
410 420
....*....|....*....|.
gi 2768338898 401 QIIAVKNSAGFGGHNVALTFR 421
Cdd:PTZ00050 399 IDAVLSTSFGFGGVNTALLFT 419
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
10-420 |
9.22e-88 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 273.59 E-value: 9.22e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 10 KVVVTGLGETTPLGGTVATTWDAMLRGESGLGLLEDES-------WAKDLPPL--LGGR--AKVDPGTGLGHQQRRRL-- 76
Cdd:PLN02836 7 RVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDlkmksedEETQLYTLdqLPSRvaALVPRGTGPGDFDEELWln 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 77 -SRSAQFAVTAAAEAWADagLDEGSVTPS------RVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGNGSA 149
Cdd:PLN02836 87 sRSSSRFIGYALCAADEA--LSDARWLPSedeakeRTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINMAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 150 AAVALLVNARLGVHATVNACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRVDD-PASACRPY 228
Cdd:PLN02836 165 GHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKFNScPTEASRPF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 229 DADRDGMVLGEGAGILVLESERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNA 308
Cdd:PLN02836 245 DCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 309 NGTATAPGDAAEARAVMAVFGDAdgDATQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEglsvd 388
Cdd:PLN02836 325 HATSTPLGDAVEARAIKTVFSEH--ATSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDP----- 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 2768338898 389 VVHGG--PLKLGPEQII--AVKNSAGFGGHNVALTF 420
Cdd:PLN02836 398 IFDDGfvPLTASKAMLIraALSNSFGFGGTNASLLF 433
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
10-421 |
6.63e-85 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 265.71 E-value: 6.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 10 KVVVTGLGETTPLGGTVATTWDAMLRGESGLGLLEDESWAKDLPPLLGGRAKVDPGTGLGHQQRRRLSRSAQFAVTAAAE 89
Cdd:PRK08722 5 RVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAGIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 90 AWADAGLDEGSVTPSRVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGNGSAAAVALLVNARLGVHATVNAC 169
Cdd:PRK08722 85 ALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTAC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 170 SSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRVDDPASACRPYDADRDGMVLGEGAGILVLESE 249
Cdd:PRK08722 165 TTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMVLEEY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 250 RHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMAVFG 329
Cdd:PRK08722 245 EHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRALG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 330 DADGDATqgpALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHGGPLKLGPEQiIAVKNSA 409
Cdd:PRK08722 325 EAGSKQV---LVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVESME-YAICNSF 400
|
410
....*....|..
gi 2768338898 410 GFGGHNVALTFR 421
Cdd:PRK08722 401 GFGGTNGSLIFK 412
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
7-420 |
3.82e-80 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 257.21 E-value: 3.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 7 ENHKVVVTGLGETTPLGGTVATTWDAMLRGESGLGLLEDESwAKDLPPLLGGRAKVDPGTG-LGHQQRRRLSRSAQFAVT 85
Cdd:PLN02787 127 KQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFD-CSQFPTRIAGEIKSFSTDGwVAPKLSKRMDKFMLYLLT 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 86 AAAEAWADAGLDE---GSVTPSRVAVAVSAALGDMTAIIDGWETLKTrGWRRVPPMTVPMSMGNGSAAAVALLVNARLGV 162
Cdd:PLN02787 206 AGKKALADGGITEdvmKELDKTKCGVLIGSAMGGMKVFNDAIEALRI-SYRKMNPFCVPFATTNMGSAMLAMDLGWMGPN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 163 HATVNACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRVDDPASACRPYDADRDGMVLGEGAG 242
Cdd:PLN02787 285 YSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGAG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 243 ILVLESERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEAR 322
Cdd:PLN02787 365 VLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQ 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 323 AVMAVFGdadgdatQGPALSAN--KSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHgGPLKLGPE 400
Cdd:PLN02787 445 ALMRCFG-------QNPELRVNstKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLV-GPKKERLD 516
|
410 420
....*....|....*....|
gi 2768338898 401 QIIAVKNSAGFGGHNVALTF 420
Cdd:PLN02787 517 IKVALSNSFGFGGHNSSILF 536
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
9-421 |
1.74e-76 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 243.49 E-value: 1.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 9 HKVVVTGLGETTPLGGTVATTWDAMLRGESGLGLLE--DeswAKDLPPLLGGRAK-VDPGTGLGHQQRRRLSRSAQFAVT 85
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITlfD---ASDFPVQIAGEITdFDPTEVMDPKEVKKADRFIQLGLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 86 AAAEAWADAGLDEGSVTPSRVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGNGSAAAVALLVNARLGVHAT 165
Cdd:PRK08439 79 AAREAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 166 VNACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRVDDPASACRPYDADRDGMVLGEGAGILV 245
Cdd:PRK08439 159 VTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 246 LESERHARERGARIYAELAGVGITSDAYHMVQPEPNgtGTAAAVRASLADADVTPADvaHFNANGTATAPGDAAEARAVM 325
Cdd:PRK08439 239 LEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAGNPKID--YINAHGTSTPYNDKNETAALK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 326 AVFGDADgdatQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHGGPLKLGPEqiIAV 405
Cdd:PRK08439 315 ELFGSKE----KVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELN--VVM 388
|
410
....*....|....*.
gi 2768338898 406 KNSAGFGGHNVALTFR 421
Cdd:PRK08439 389 SNSFGFGGTNGVVIFK 404
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
10-421 |
1.39e-68 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 222.94 E-value: 1.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 10 KVVVTGLGETTPLGGTVATTWDAMLRGESGLGLLEDESWAKDLPPLLGgrAKVDPGTGLGHQQRRRL---SRSAQFAVTA 86
Cdd:PRK09116 3 RVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYDGLNTRLA--APIDDFELPAHYTRKKIrsmGRVSLMATRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 87 AAEAWADAGL-DEGSVTPSRVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGNGSAAAVALLVNARLGVHAT 165
Cdd:PRK09116 81 SELALEDAGLlGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRVIPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 166 VNACSSGTQALVTAAELIRRGEADVVVAGGAEApLHPMVLSSFAAMRALSQRVDDPASACRPYDADRDGMVLGEGAGILV 245
Cdd:PRK09116 161 SSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGAGTLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 246 LESERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTaaAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVM 325
Cdd:PRK09116 240 LEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQI--AMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 326 AVFGDadgdatQGPaLSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGL-SVDVVHGGPLKLGPEqiIA 404
Cdd:PRK09116 318 AVFGA------RMP-ISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTE--YV 388
|
410
....*....|....*..
gi 2768338898 405 VKNSAGFGGHNVALTFR 421
Cdd:PRK09116 389 MSNNFAFGGINTSLIFK 405
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
9-418 |
3.44e-66 |
|
"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: 216.92 E-value: 3.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 9 HKVVVTGLGETTPLG---GTVATTWDAMLRGESGLGLLEDESwaKDLPPLLGGRAKVDPGTGLGHQQRRRLSRSAQFAVT 85
Cdd:cd00828 1 SRVVITGIGVVSPHGegcDEVEEFWEALREGRSGIAPVARLK--SRFDRGVAGQIPTGDIPGWDAKRTGIVDRTTLLALV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 86 AAAEAWADAGL-DEGSVTPSRVAVAVSAALGDMTAIIDGWETLktrgWRRVPPMTVP--MSMGNGSAAAVALLVNARLGV 162
Cdd:cd00828 79 ATEEALADAGItDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLD----ARAVNPYVSPkwMLSPNTVAGWVNILLLSSHGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 163 HATVN-ACSSGTQALVTAAELIRRGEADVVVAGGAEAPLhPMVLSSFAAMRALSQRVDDPASACRPYDADRDGMVLGEGA 241
Cdd:cd00828 155 IKTPVgACATALEALDLAVEAIRSGKADIVVVGGVEDPL-EEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 242 GILVLESERHARERGARIYAELAGVGITSDAYHMVQPePNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEA 321
Cdd:cd00828 234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVP-AGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAES 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 322 RAVMAVFGDADGDatqgPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHGGPLKLGPEQ 401
Cdd:cd00828 313 RAIAEVAGALGAP----LPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLKV 388
|
410
....*....|....*..
gi 2768338898 402 IIAVKNSAGFGGHNVAL 418
Cdd:cd00828 389 RAALVNAFGFGGSNAAL 405
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
9-421 |
3.61e-66 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 216.85 E-value: 3.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 9 HKVVVTGLGETTPLGGTVATTWDAMLRGESGLGLleDESWAK-DLPPLLGGRAKVDPGTGLGHQQRRRLSRSAQFAVTAA 87
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITF--SPEFAEmGMRSQVWGNVKLDPTGLIDRKVMRFMGDASAYAYLAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 88 AEAWADAGLDEGSVTPSRVAVAVSAALGDMTAIIDGWETLKT-RGWRRVPPMTVPMSMGNGSAAAVALLVNARlGVHATV 166
Cdd:PRK07967 80 EQAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGpRGPKRVGPYAVTKAMASTVSACLATPFKIK-GVNYSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 167 -NACSSGTQALVTAAELIRRGEADVVVAGGAEApLHPMVLSSFAAMRALSQRVDD-PASACRPYDADRDGMVLGEGAGIL 244
Cdd:PRK07967 159 sSACATSAHCIGNAVEQIQLGKQDIVFAGGGEE-LDWEMSCLFDAMGALSTKYNDtPEKASRAYDANRDGFVIAGGGGVV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 245 VLESERHARERGARIYAELAGVGITSDAYHMVQpePNGTGTAAAVRASLADADvTPADvaHFNANGTATAPGDAAEARAV 324
Cdd:PRK07967 238 VVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMALATVD-TPID--YINTHGTSTPVGDVKELGAI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 325 MAVFGDadgdatQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEglsvdVVHGGPL--------K 396
Cdd:PRK07967 313 REVFGD------KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDP-----QAAGMPIvtettdnaE 381
|
410 420
....*....|....*....|....*
gi 2768338898 397 LGpeqiIAVKNSAGFGGHNVALTFR 421
Cdd:PRK07967 382 LT----TVMSNSFGFGGTNATLVFR 402
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
168-425 |
1.62e-64 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 212.95 E-value: 1.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 168 ACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRVDDPASACRPYDADRDGMVLGEGAGILVLE 247
Cdd:PRK06501 174 ACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDRDGFVMAEGAGALVLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 248 SERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMAV 327
Cdd:PRK06501 254 SLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPENDKMEYLGLSAV 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 328 FGDAdgdATQGPaLSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVhggPLKLGPEQIIAV-K 406
Cdd:PRK06501 334 FGER---LASIP-VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVV---PNVARDARVTAVlS 406
|
250
....*....|....*....
gi 2768338898 407 NSAGFGGHNVALTFRAEKG 425
Cdd:PRK06501 407 NSFGFGGQNASLVLTAEPA 425
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
105-421 |
4.55e-63 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 206.89 E-value: 4.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 105 RVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGNGSAAAVALLVNARLGVHATVNACSSGTQALVTAAELIR 184
Cdd:PRK14691 27 RTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 185 RGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRVDD-PASACRPYDADRDGMVLGEGAGILVLESERHARERGARIYAEL 263
Cdd:PRK14691 107 NNEADVALCGGAEAVIDTVSLAGFAAARALSTHFNStPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 264 AGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMAVFGDADgdatqGPALSA 343
Cdd:PRK14691 187 VGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESN-----ALAITS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 344 NKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLD---EGLSVDVVHGGPlklgPEQIIAVKNSAGFGGHNVALTF 420
Cdd:PRK14691 262 TKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDpaaKGLNIIAGNAQP----HDMTYALSNGFGFAGVNASILL 337
|
.
gi 2768338898 421 R 421
Cdd:PRK14691 338 K 338
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
10-418 |
3.73e-62 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 205.67 E-value: 3.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 10 KVVVTGLGETTPLGgTVATTWDAMLRGESGLGLLEDESwakDLPPLlggrakvdPgTGLGHQQRRRLSRSAQfavtaaae 89
Cdd:PRK05952 3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGIKLHQPFP---ELPPL--------P-LGLIGNQPSSLEDLTK-------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 90 AWADAGLDEGSVTPSRVAVAVsaALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGN-------GSAAAVALLVNARLGV 162
Cdd:PRK05952 62 TVVTAALKDAGLTPPLTDCGV--VIGSSRGCQGQWEKLARQMYQGDDSPDEELDLENwldtlphQAAIAAARQIGTQGPV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 163 HATVNACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQrvddpaSACRPYDADRDGMVLGEGAG 242
Cdd:PRK05952 140 LAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK------TGAYPFDRQREGLVLGEGGA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 243 ILVLESERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEAR 322
Cdd:PRK05952 214 ILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREAN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 323 AVMAVFGdadgdatQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLS-VDVVHGGPLKlgpeQ 401
Cdd:PRK05952 294 LIQALFP-------HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLNfVRQAQQSPLQ----N 362
|
410
....*....|....*..
gi 2768338898 402 IIAVknSAGFGGHNVAL 418
Cdd:PRK05952 363 VLCL--SFGFGGQNAAI 377
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
11-420 |
3.11e-56 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 190.44 E-value: 3.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 11 VVVTGLGETTPLGGTVATTWDAMLRGESGlGLLEDESWAKDLPPLLGGRAKVD---PGTGLGHQQRR--RLSRSA--QFA 83
Cdd:PRK09185 4 VYISAFGATSALGRGLDAILAALRAGRAS-GMRPCDFWLVDLPTWVGEVVGVElpaLPAALAAFDCRnnRLALLAlqQIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 84 VTAAAEAWadagldegSVTPSRVAVAvsaaLGDMTAIIDGWETLKTRgwRRVPPMTVP-------MSMGNGSAAAVAllv 156
Cdd:PRK09185 83 PAVEAAIA--------RYGADRIGVV----LGTSTSGILEGELAYRR--RDPAHGALPadyhyaqQELGSLADFLRA--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 157 naRLGVH---ATV-NACSSGTQALVTAAELIRRGEADVVVAGGAEApLHPMVLSSFAAMRALSqrvddpASACRPYDADR 232
Cdd:PRK09185 146 --YLGLSgpaYTIsTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLS------PQPCRPFSANR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 233 DGMVLGEGAGILVLEserhaRERGARIYaeLAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTA 312
Cdd:PRK09185 217 DGINIGEAAAFFLLE-----REDDAAVA--LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 313 TAPGDAAEARAVMAVFGDadgdatqGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHG 392
Cdd:PRK09185 290 TPLNDAMESRAVAAVFGD-------GVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVE 362
|
410 420
....*....|....*....|....*...
gi 2768338898 393 GPLKLGPEQIIAvkNSAGFGGHNVALTF 420
Cdd:PRK09185 363 NAQALAIRYVLS--NSFAFGGNNCSLIF 388
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
11-421 |
3.44e-55 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 187.93 E-value: 3.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 11 VVVTGLGETTPLGGTVATTWDAMLRGESGLGLLEDE-----SWAKDL--PPLLGGR-AKVDPGTGLGHQQRRRLSRSAQF 82
Cdd:PRK07103 4 VVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPgrqvpDDAGAGlaSAFIGAElDSLALPERLDAKLLRRASLSAQA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 83 AVTAAAEAWADAGLDEgsVTPSRVAVAVSaalGDMTAIIDGWETLKTrgWRRVPPMTVPMSMGNGSAAAVALLVNARLGV 162
Cdd:PRK07103 84 ALAAAREAWRDAALGP--VDPDRIGLVVG---GSNLQQREQALVHET--YRDRPAFLRPSYGLSFMDTDLVGLCSEQFGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 163 HA---TVNACS-SGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRAL-SQR-VDDPASACRPYDADRDGMV 236
Cdd:PRK07103 157 RGegfTVGGASaSGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMgSDRfADEPEAACRPFDQDRDGFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 237 LGEGAGILVLESERHARERGARIYAELAGVGITSDAYHmvQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPG 316
Cdd:PRK07103 237 YGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANR--GPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 317 DAAEARAVmavfgdaDGDATQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNftrLDE--GLSVDVVHGGP 394
Cdd:PRK07103 315 DETELAAL-------FASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRN---LDEpiDERFRWVGSTA 384
|
410 420
....*....|....*....|....*...
gi 2768338898 395 lklGPEQI-IAVKNSAGFGGHNVALTFR 421
Cdd:PRK07103 385 ---ESARIrYALSLSFGFGGINTALVLE 409
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
168-418 |
3.47e-52 |
|
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: 180.45 E-value: 3.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 168 ACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSqrvddPASACRPYDADRDGMVLGEGAGILVLE 247
Cdd:cd00833 169 ACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRCRPFDADADGYVRGEGVGVVVLK 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 248 SERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMAV 327
Cdd:cd00833 244 RLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKV 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 328 FGdADGDATQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRL-----DEGLSVDVVH-GGPLKLGPEQ 401
Cdd:cd00833 324 FG-GSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPnpkidFEESPLRVPTeARPWPAPAGP 402
|
250
....*....|....*..
gi 2768338898 402 IIAVKNSAGFGGHNVAL 418
Cdd:cd00833 403 RRAGVSSFGFGGTNAHV 419
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
9-418 |
5.42e-49 |
|
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: 171.39 E-value: 5.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 9 HKVVVTGLGETTPLGGTVATTWDAMLRGESGLGLLEDESWAKDLPPLLGGRAKVDPGTGLGHQQRRRLSRSAQFAVTAAA 88
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 89 EAWADAGLDEGSVTPSRVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPM----------TVPMSMGNGSAAAVallvna 158
Cdd:cd00832 81 WALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYqsfawfyavnTGQISIRHGMRGPS------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 159 rlGVHATVNAcsSGTQALVTAAELIRRGeADVVVAGGAEAPLHPMVLSSFAAMRALSqRVDDPASACRPYDADRDGMVLG 238
Cdd:cd00832 155 --GVVVAEQA--GGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLS-TSDDPARAYLPFDAAAAGYVPG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 239 EGAGILVLESERHARERGARIYAELAGVGITSDayhmvqPEP---NGTGTAAAVRASLADADVTPADVAHFNANGTATAP 315
Cdd:cd00832 229 EGGAILVLEDAAAARERGARVYGEIAGYAATFD------PPPgsgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 316 GDAAEARAVMAVFGdadgdaTQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHGGPL 395
Cdd:cd00832 303 LDRAEAAALAAVFG------PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPR 376
|
410 420
....*....|....*....|...
gi 2768338898 396 KLGPEqiIAVKNSAGFGGHNVAL 418
Cdd:cd00832 377 PAALR--TALVLARGRGGFNSAL 397
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
95-418 |
1.22e-43 |
|
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: 155.49 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 95 GLDEGSVTPSRVAVAVSAALGDMTAIIDGWETLKTRGWRRVPPMTVPMSMGngsaaavalLVNARLGVHA----TVNACS 170
Cdd:cd00825 27 GLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGASG---------QIATPLGIHGpaydVSAACA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 171 SGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSqrvddPASACRPYDADRDGMVLGEGAGILVLESER 250
Cdd:cd00825 98 GSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST-----PEKASRTFDAAADGFVFGDGAGALVVEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 251 HARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMAVFGD 330
Cdd:cd00825 173 HALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 331 adgdatQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVDVVHGGPLKLGPeqiiAVKNSAG 410
Cdd:cd00825 253 ------KSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETTPRELRT----ALLNGFG 322
|
....*...
gi 2768338898 411 FGGHNVAL 418
Cdd:cd00825 323 LGGTNATL 330
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
168-381 |
1.48e-39 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 151.56 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 168 ACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSqrvddPASACRPYDADRDGMVLGEGAGILVLE 247
Cdd:COG3321 173 ACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS-----PDGRCRAFDADADGYVRGEGVGVVVLK 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 248 SERHARERGARIYAELAGVGITSD-------AyhmvqpePNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAE 320
Cdd:COG3321 248 RLSDALRDGDRIYAVIRGSAVNQDgrsngltA-------PNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIE 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2768338898 321 ARAVMAVFGdADGDATQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRL 381
Cdd:COG3321 321 AAALTAAFG-QGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETP 380
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
260-379 |
2.91e-38 |
|
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: 134.23 E-value: 2.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 260 YAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMAVFGdaDGDATQGP 339
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFG--SGARKQPL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2768338898 340 ALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFT 379
Cdd:pfam02801 79 AIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
11-252 |
1.10e-29 |
|
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: 115.81 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 11 VVVTGLGETTPLGGTVATTWDAMLRGESGLGLLEDESWA----KDLPPLLGGRAKVDPGT------------GLGHQQRR 74
Cdd:pfam00109 3 VAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDpdklYDPPSRIAGKIYTKWGGlddifdfdplffGISPREAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 75 RLSRSAQFAVTAAAEAWADAGLDEGSVTPSRVAVAVSAALGDMTAIIDGWETLktrGWRRVPPMTVPMsMGNGSAAAVAL 154
Cdd:pfam00109 83 RMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDG---GPRRGSPFAVGT-MPSVIAGRISY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 155 LVNARLGVHATVNACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQrvDDPasaCRPYDADRDG 234
Cdd:pfam00109 159 FLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGP---CKAFDPFADG 233
|
250
....*....|....*...
gi 2768338898 235 MVLGEGAGILVLESERHA 252
Cdd:pfam00109 234 FVRGEGVGAVVLKRLSDA 251
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
168-388 |
3.17e-29 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 120.88 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 168 ACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQRVDdpasaCRPYDADRDGMVLGEGAGILVLE 247
Cdd:TIGR02813 205 ACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED-----IQPFDIDSKGMMIGEGIGMMALK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 248 SERHARERGARIYAELAGVGITSDAYHMVQPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMAV 327
Cdd:TIGR02813 280 RLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSV 359
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2768338898 328 FGDaDGDATQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLDEGLSVD 388
Cdd:TIGR02813 360 FSQ-DNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDIE 419
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
167-376 |
9.95e-25 |
|
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: 102.14 E-value: 9.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 167 NACSSGTQALVTAAELIRRGEADVVVAGGAEAplhpmvlssfaamralsqrvddpasacrpydadrdgMVLGEGAGILVL 246
Cdd:cd00327 66 QACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FVFGDGAAAAVV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 247 ESERHARERGARIYAELAGVGITSDAYHMVqPEPNGTGTAAAVRASLADADVTPADVAHFNANGTATAPGDAAEARAVMA 326
Cdd:cd00327 110 ESEEHALRRGAHPQAEIVSTAATFDGASMV-PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2768338898 327 VFGDadgdatQGPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTR 376
Cdd:cd00327 189 PDGV------RSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPTP 232
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
168-418 |
3.22e-24 |
|
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: 101.64 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 168 ACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSqrvddPASACRPYDADRDGMVLGEGAGILVLE 247
Cdd:smart00825 96 ACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVVLK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 248 SERHARERGARIYAELAGVGITSDAyhmvqpepngtgtaaavrasladadvtpadvahfNANGtATAPGDAAearavmav 327
Cdd:smart00825 171 RLSDALRDGDPILAVIRGSAVNQDG----------------------------------RSNG-ITAPSGPA-------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 328 fgdadgdatQgPALSANKSMTGHSLGAAGAIESITTVLALHHGLVPPTRNFTRLD-----EGLSVDVV--------HGGP 394
Cdd:smart00825 208 ---------Q-LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNphidlEESPLRVPteltpwppPGRP 277
|
250 260
....*....|....*....|....
gi 2768338898 395 LklgpeqIIAVkNSAGFGGHNVAL 418
Cdd:smart00825 278 R------RAGV-SSFGFGGTNAHV 294
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
170-355 |
9.96e-12 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 66.13 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 170 SSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFAAMRALSQrvDDPASACRPYDADRDGMVLGEGAGILVLESE 249
Cdd:PRK06519 176 SAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLK--GGWAPVWSRGGEDGGGFILGSGGAFLVLESR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 250 RHARERGARIYAELAGVGitSDayhmvQPEPNGTGTAAAVRASLADADVTPADVAHFnaNGTATAPGDAAEARAVMavfg 329
Cdd:PRK06519 254 EHAEARGARPYARISGVE--SD-----RARRAPGDLEASLERLLKPAGGLAAPTAVI--SGATGAHPATAEEKAAL---- 320
|
170 180
....*....|....*....|....*.
gi 2768338898 330 dadgDATQGPALSANKSMTGHSLGAA 355
Cdd:PRK06519 321 ----EAALAGPVRGIGTLFGHTMEAQ 342
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
165-256 |
9.75e-09 |
|
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: 57.00 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 165 TVN-ACSSGTQALVTAAELIRRGEADVVVAGGAEAP-LHPMVLSSFAAMRALSQRVDDPASACRPYDAdRDGMVLGEGAg 242
Cdd:COG0183 83 TVNrVCGSGLQAVALAAQAIAAGDADVVIAGGVESMsRAPMLLPKARWGYRMNAKLVDPMINPGLTDP-YTGLSMGETA- 160
|
90
....*....|....
gi 2768338898 243 ilvlesERHARERG 256
Cdd:COG0183 161 ------ENVAERYG 168
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
165-197 |
1.00e-06 |
|
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: 50.56 E-value: 1.00e-06
10 20 30
....*....|....*....|....*....|....
gi 2768338898 165 TVN-ACSSGTQALVTAAELIRRGEADVVVAGGAE 197
Cdd:cd00751 79 TVNrVCGSGLQAVALAAQSIAAGEADVVVAGGVE 112
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
165-206 |
3.73e-06 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 48.76 E-value: 3.73e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2768338898 165 TVN-ACSSGTQALVTAAELIRRGEADVVVAGGAEA-PLHPMVLS 206
Cdd:TIGR01930 78 TVNrQCASGLQAVILAAQLIRAGEADVVVAGGVESmSRVPYGVP 121
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
167-306 |
1.54e-05 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 46.87 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 167 NACSSGTQALVTAAELIRRGEADVVVAGGAEAPLHPMVLSSFA-------------------------AMRALSQR---- 217
Cdd:cd00829 75 AAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGgrasdlewegpeppggltppalyalAARRYMHRygtt 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 218 --------VDDPASACR-PY----------DADRDGMV-----------LGEGAGILVLESERHARERGARiYAELAGVG 267
Cdd:cd00829 155 redlakvaVKNHRNAARnPYaqfrkpitveDVLNSRMIadplrlldccpVSDGAAAVVLASEERARELTDR-PVWILGVG 233
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2768338898 268 ITSDAYHMVQPEPNGTGTAA--AVRASLADADVTPADVAHF 306
Cdd:cd00829 234 AASDTPSLSERDDFLSLDAArlAARRAYKMAGITPDDIDVA 274
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
165-197 |
2.66e-05 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 45.91 E-value: 2.66e-05
10 20 30
....*....|....*....|....*....|....
gi 2768338898 165 TVNA-CSSGTQALVTAAELIRRGEADVVVAGGAE 197
Cdd:PRK05790 83 TINKvCGSGLKAVALAAQAIRAGDADIVVAGGQE 116
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
165-197 |
9.79e-05 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 43.83 E-value: 9.79e-05
10 20 30
....*....|....*....|....*....|....
gi 2768338898 165 TVN-ACSSGTQALVTAAELIRRGEADVVVAGGAE 197
Cdd:pfam00108 80 TINkVCGSGLKAVYLAAQSIASGDADVVLAGGVE 113
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
169-197 |
2.61e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 43.05 E-value: 2.61e-04
10 20
....*....|....*....|....*....
gi 2768338898 169 CSSGTQALVTAAELIRRGEADVVVAGGAE 197
Cdd:PRK06205 88 CGSGLQAVITAAMQVQTGAADVVIAGGAE 116
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
165-197 |
1.32e-03 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 40.71 E-value: 1.32e-03
10 20 30
....*....|....*....|....*....|....
gi 2768338898 165 TVN-ACSSGTQALVTAAELIRRGEADVVVAGGAE 197
Cdd:PRK09051 85 NVNrLCGSGLQAIVSAAQAILLGDADVAIGGGAE 118
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
164-198 |
2.84e-03 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 39.75 E-value: 2.84e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2768338898 164 ATVNA-CSSGTQALVTAAELIRRGEADVVVAGGAEA 198
Cdd:PRK07108 84 MTVNRfCSSGLQTIALAAQRVIAGEGDVFVAGGVES 119
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
164-198 |
4.12e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 39.31 E-value: 4.12e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2768338898 164 ATVN-ACSSGTQALVTAAELIRRGEADVVVAGGAEA 198
Cdd:PRK08235 82 ETVNkVCASGLRAVTLADQIIRAGDASVIVAGGMES 117
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
164-197 |
5.43e-03 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 38.78 E-value: 5.43e-03
10 20 30
....*....|....*....|....*....|....*
gi 2768338898 164 ATVNA-CSSGTQALVTAAELIRRGEADVVVAGGAE 197
Cdd:PRK09050 84 TTINRlCGSGMDAVGTAARAIKAGEAELMIAGGVE 118
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
165-198 |
6.09e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 38.58 E-value: 6.09e-03
10 20 30
....*....|....*....|....*....|....*
gi 2768338898 165 TVNA-CSSGTQALVTAAELIRRGEADVVVAGGAEA 198
Cdd:PRK07661 85 TINRyCSSGLQSIAYGAERIMLGHSEAVIAGGAES 119
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
167-259 |
9.51e-03 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 34.80 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2768338898 167 NACSSGTQALVTAAELIRRGEADVVVAGGAEaplhpmvlssfaamrALSQRVDdpasacrpyDADRDGMVL-GEGAGILV 245
Cdd:pfam08545 5 AACSGFVYALSTAAALIRSGRAKNVLVIGAE---------------TLSKILD---------WTDRSTAVLfGDGAGAVV 60
|
90
....*....|....
gi 2768338898 246 LEserHARERGARI 259
Cdd:pfam08545 61 LE---ATDEPGARI 71
|
|
| |
