|
Name |
Accession |
Description |
Interval |
E-value |
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
7-437 |
3.71e-105 |
|
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: 343.39 E-value: 3.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGKRSIRDADTEDWGVDPTRflgPGRGVADQSSSIELAKPRGHD-FDASGFLLPAALL 85
Cdd:cd00833 5 IVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYY---PDPGKPGKTYTRRGGFLDDVDaFDAAFFGISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 86 GAQDRCIQWPLQVGRNALRDAGLWGGDL--SRVGMVLGSYAWAasaasdaiTRPLYDEALASAFAEAAPGHPLRLTAGRL 163
Cdd:cd00833 82 EAMDPQQRLLLEVAWEALEDAGYSPESLagSRTGVFVGASSSD--------YLELLARDPDEIDAYAATGTSRAFLANRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 164 qsgthpesarvsggittltARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAATQA 243
Cdd:cd00833 154 -------------------SYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGM 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 244 L-PDGTSnRPFDADSDGVAPADGAMALVLRRPD---SHRSTVYGTLRGMGLSSDGRGQTLTAPNPKGQKLACDRAYEQTG 319
Cdd:cd00833 215 LsPDGRC-RPFDADADGYVRGEGVGVVVLKRLSdalRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 320 ISPDTIAYVECHATGTKLGDRVELETVARVFGDNQP------VGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGI 393
Cdd:cd00833 294 VDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSadqpllIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHF 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2666213114 394 EKPLSR-DIAGTP-DIITQATPWPA--GHKRAAINAFGFGGVNAHLIV 437
Cdd:cd00833 374 ETPNPKiDFEESPlRVPTEARPWPApaGPRRAGVSSFGFGGTNAHVIL 421
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
7-487 |
2.01e-77 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 284.07 E-value: 2.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGKRSIRDADTEDWgvDPTRFLGPGRGVADQSSSielakPRG------HDFDASGFLL 80
Cdd:COG3321 8 IIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRW--DADAYYDPDPDAPGKTYV-----RWGgflddvDEFDALFFGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 81 P---AALLGAQDRCIqwpLQVGRNALRDAGLWGGDL--SRVGMVLGSYAWAASAASDaitrplydealasafaeaapGHP 155
Cdd:COG3321 81 SpreAEAMDPQQRLL---LEVAWEALEDAGYDPESLagSRTGVFVGASSNDYALLLL--------------------ADP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 156 LRLTAgrlQSGTHPESARVSGGIttltARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFAN 235
Cdd:COG3321 138 EAIDA---YALTGNAKSVLAGRI----SYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 236 FGFAATQAL-PDGTSnRPFDADSDGVAPADGAMALVLRR-----PDSHRstVYGTLRGMGLSSDGRGQTLTAPNPKGQKL 309
Cdd:COG3321 211 ILFSKGGMLsPDGRC-RAFDADADGYVRGEGVGVVVLKRlsdalRDGDR--IYAVIRGSAVNQDGRSNGLTAPNGPAQAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 310 ACDRAYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFGDNQP------VGSVKSNVGHLLTAAGIAGLVKTLLAMR 383
Cdd:COG3321 288 VIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPadqpcaIGSVKSNIGHLEAAAGVAGLIKAVLALR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 384 HGVIPATVGIEKPLSR-DIAGTP-DIITQATPWPAGHK--RAAINAFGFGGVNAHLIVDGPGQAAPETAPSRR------- 452
Cdd:COG3321 368 HGVLPPTLHFETPNPHiDFENSPfYVNTELRPWPAGGGprRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARppqllvl 447
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2666213114 453 --RGDAAL---LTGLGAAIGDCPDLN--AVARALAAGQPRLR 487
Cdd:COG3321 448 saKTEEALralAARLAAFLEAHPDLDlaDVAYTLATGRAHFE 489
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
7-437 |
3.51e-53 |
|
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: 189.08 E-value: 3.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGkrsIRDADtedwgvdptrflgpgrgvadqsssielakprghDFDASGFLLP---AA 83
Cdd:smart00825 3 IVGMSCRFPGADDPEEFWDLLLAG---LDDVD---------------------------------LFDAAFFGISpreAE 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 84 LLGAQDRCIqwpLQVGRNALRDAGLWGGDL--SRVGMVLGsyawaasaasdaitrplydealasafaeaapghplrltag 161
Cdd:smart00825 47 AMDPQQRLL---LEVAWEALEDAGIDPESLrgSRTGVFVG---------------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 162 rlqsGTHPESArvsggittltaralglggprYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAAT 241
Cdd:smart00825 84 ----VSSSDYS--------------------VTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRA 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 242 QAL-PDGTSnRPFDADSDGVAPADGAMALVLRR-----PDSHRstVYGTLRGMGLSSDGRGQTLTAPNPKGQklacdray 315
Cdd:smart00825 140 GMLsPDGRC-KTFDASADGYVRGEGVGVVVLKRlsdalRDGDP--ILAVIRGSAVNQDGRSNGITAPSGPAQ-------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 316 eqtgispdtiayveCHatgtklgdrveletvarvfgdnqpVGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEK 395
Cdd:smart00825 209 --------------LL------------------------IGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFET 250
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2666213114 396 PLSR-DIAGTP-DIITQATPWPAGHK--RAAINAFGFGGVNAHLIV 437
Cdd:smart00825 251 PNPHiDLEESPlRVPTELTPWPPPGRprRAGVSSFGFGGTNAHVIL 296
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
4-456 |
3.95e-50 |
|
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: 197.15 E-value: 3.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 4 PLDITGIACLVPDADTLDGFWQNLLAGKRSIRDADTEDWGVDPtrFLGPGRGVADQSSSielakPRGH-----DFDASGF 78
Cdd:TIGR02813 8 PIAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDD--YYDSDKSEADKSYC-----KRGGflpevDFNPMEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 79 LLPAALLGAQDRCIQWPLQVGRNALRDAGLWGG-DLSRVGMVLGSYAWAASAASDAiTRPLYDEALASAFAEAAPGHPLR 157
Cdd:TIGR02813 81 GLPPNILELTDISQLLSLVVAKEVLNDAGLPDGyDRDKIGITLGVGGGQKQSSSLN-ARLQYPVLKKVFKASGVEDEDSE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 158 LTAGRLQSG-THPESARVSGG----ITTLTARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTL 232
Cdd:TIGR02813 160 MLIKKFQDQyIHWEENSFPGSlgnvISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 233 FANFGFAATQALPDGTSNRPFDADSDGVAPADGAMALVLRR-PDSHRS--TVYGTLRGMGLSSDGRGQTLTAPNPKGQKL 309
Cdd:TIGR02813 240 FMYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRlEDAERDgdRIYAVIKGVGASSDGKFKSIYAPRPEGQAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 310 ACDRAYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFG-DNQ-----PVGSVKSNVGHLLTAAGIAGLVKTLLAMR 383
Cdd:TIGR02813 320 ALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSqDNDqkqhiALGSVKSQIGHTKSTAGTAGMIKAVLALH 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2666213114 384 HGVIPATVGIEKP-LSRDIAGTPDII-TQATPWPAGH----KRAAINAFGFGGVNAHLIVDgpgqaapETAPSRRRGDA 456
Cdd:TIGR02813 400 HKVLPPTINVDQPnPKLDIENSPFYLnTETRPWMQREdgtpRRAGISSFGFGGTNFHMVLE-------EYSPKHQRDDQ 471
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
282-394 |
7.01e-44 |
|
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: 155.42 E-value: 7.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 282 YGTLRGMGLSSDGRGQTLTAPNPKGQKLACDRAYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFGDNQ-----PV 356
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArkqplAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2666213114 357 GSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIE 394
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| FabA |
cd01287 |
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ... |
1656-1803 |
3.76e-43 |
|
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the type II, fatty acid synthase system that binds ACP and catalyzes both dehydration and isomerization reactions, apparently in the same active site. The FabA structure is a homodimer with two independent active sites located at the dimer interface. Each active site is tunnel-shaped and completely inaccessible to solvent. No metal ions or cofactors are required for ligand binding or catalysis.
Pssm-ID: 238614 Cd Length: 150 Bit Score: 154.72 E-value: 3.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1656 LRLPPAAIQFIDRVTSIEPAGGAHGLGGCEAEFQVNPQHWAIRAHFKDDPIFPGPCMMEGAFQLLQAYALSLGLQTAVTG 1735
Cdd:cd01287 1 PRLPGGQLLMLDRVTEIDPGGGTFGLGYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIWLGLGTGVDN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2666213114 1736 ARFQPLPHRPSLVRFRAQVLPQNQTFTYRADIVEIG-LTPEPYLIADIDLIDNGRVMGRVEGLGIRLTG 1803
Cdd:cd01287 81 PRFQGAPGGPGEWKYRGQITPHNKKVTYEVHIKEVGrDGPRPYIIADASLWVDGLRIYEAKDIAVRLVE 149
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
7-436 |
3.32e-42 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 161.32 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGK---RSIRDADTEDWgvdPTRFLGPGRGVADqsssielakprghdfDASGFLLPAA 83
Cdd:PRK06333 8 VTGMGAVSPLGCGVETFWQRLLAGQsgiRTLTDFPVGDL---ATKIGGQVPDLAE---------------DAEAGFDPDR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 84 LLGAQ-----DRCIQWPLQVGRNALRDAGLWGGDLS---RVGMVLGSYAWAASAASDAITRplydealasafaeaapghp 155
Cdd:PRK06333 70 YLDPKdqrkmDRFILFAMAAAKEALAQAGWDPDTLEdreRTATIIGSGVGGFPAIAEAVRT------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 156 lRLTAG--RLQSGTHPES-ARVSGGittLTARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTL 232
Cdd:PRK06333 131 -LDSRGprRLSPFTIPSFlTNMAAG---HVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 233 FANFGFAATQALPDGTSN------RPFDADSDGVAPADGAMALVLRRPDS---HRSTVYGTLRGMGLSSDGRGQTLTAPN 303
Cdd:PRK06333 207 VSLAGFAAARALSTRFNDapeqasRPFDRDRDGFVMGEGAGILVIETLEHalaRGAPPLAELVGYGTSADAYHMTAGPED 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 304 PKGQKLACDRAYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFGDNQ--PVGSVKSNVGHLLTAAGIAGLVKTLLA 381
Cdd:PRK06333 287 GEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVSglAVSSTKSATGHLLGAAGGVEAIFTILA 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2666213114 382 MRHGVIPATVGIEKPLSrDIAGTPDIITQATPWPAghKRAAINAFGFGGVNAHLI 436
Cdd:PRK06333 367 LRDQIAPPTLNLENPDP-AAEGLDVVANKARPMDM--DYALSNGFGFGGVNASIL 418
|
|
| pfaB_fam |
TIGR02816 |
PfaB family protein; The protein PfaB is part of four gene locus, similar to polyketide ... |
943-1314 |
6.64e-39 |
|
PfaB family protein; The protein PfaB is part of four gene locus, similar to polyketide biosynthesis systems, responsible for omega-3 polyunsaturated fatty acid biosynthesis in several high pressure and/or cold-adapted bacteria. The fairly permissive trusted cutoff set for this model allows detection of homologs encoded near homologs to other proteins of the locus: PfaA, PfaC, and/or PfaD. The likely role in every case is either polyunsaturated fatty acid or polyketide biosynthesis.
Pssm-ID: 131863 [Multi-domain] Cd Length: 538 Bit Score: 154.09 E-value: 6.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 943 KAQADWQSPRGSRFSPAPLGRD-----GKVAFVYSALNTAFTGLASRVAQLEPLAGERLSAaHRDAGATIRSEQLYprrl 1017
Cdd:TIGR02816 154 KGLIHYKTPAGSCFSLAPLGSNndnakAGLAFVYPGVGTVYADMFNDFHQYFPALFAKLER-EGDLKAMLQAEDIY---- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1018 tpldAEGRMQAEEALLQDnpaLINAGILSGWQYATLLTERVGLEPALQFGHSLGQATMMFASGAWTPGDAWLARLQELDG 1097
Cdd:TIGR02816 229 ----GEDPKHAAEMSLGD---LAIAGVGSSYLLTQLLCDEFAIKPDFALGYSKGEASMWASLGVWKNPHALIEKTQTDPI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1098 SLTRLSGDKQAVREAWQLAD-GQPVDWVNYLVLAPAAGVVEAAKQETRAYVSLINSpDEVTLVGERAACDRILQRLGAEA 1176
Cdd:TIGR02816 302 FTSAISGKLTAVREAWQLDDtAAEIQWNSFVVRCEAAPIEALLKDFPHAYLAIIQG-DTCVIAGCEAQCKALLAALGKRG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1177 VPAPDSLAMHCAPAERERAAIAERFTAQLSAQ-PQGLLFAGGA---------PAAWTPEAVAERVAGDLVSPLDFPALVD 1246
Cdd:TIGR02816 381 IAANRVTAMHTQPALQEHQNVMDFYLQPLCAElPMDIKFISAAdllaknqnsEQAIDSQSIANSIADTFCQTLDFTALIH 460
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2666213114 1247 QAYAQGARLFLELGPGGNCSRWIGK--------TLRGRPHATFALARRDQDDAAMLAKLLALLVAQRVPLDLAAAL 1314
Cdd:TIGR02816 461 HAQEQGAKLFVEIGADRQNCTLIDKinkqdgasSEQHQPCCTVAANAKGGEDITSLIKAIAQLISHQIPLSLQPFI 536
|
|
| FabA |
pfam07977 |
FabA-like domain; This enzyme domain has a HotDog fold. |
1658-1790 |
5.71e-29 |
|
FabA-like domain; This enzyme domain has a HotDog fold.
Pssm-ID: 429766 Cd Length: 132 Bit Score: 113.53 E-value: 5.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1658 LPPAAIQFIDRVTSIEPAGGAHGLGGCEAEFQVNPQHWAIRAHFKDDPIFPGPCMMEGAFQLLQAYALSLGLQTAVTGAR 1737
Cdd:pfam07977 1 LPHRYFLMLDRVTEIDPDGGKFGKGYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGRAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2666213114 1738 FqplphrPSLVRFRAQVLPQNQTFTYRADIVEIGLTPEPYLIADIDLIDNGRV 1790
Cdd:pfam07977 81 G------VDEVKFRGQVTPGDKQLRYEVEIKKIIEGRRGIGIADGRALVDGKV 127
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
490-1756 |
1.43e-22 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 106.11 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 490 PEGRHAGmPFPAPQGAYLDRVA-IDALKLRVPPNDISRMYPQQLLMLSVGDAALGGAGVAP----GSRTAVIIASAMDHS 564
Cdd:COG3321 51 PDPDAPG-KTYVRWGGFLDDVDeFDALFFGISPREAEAMDPQQRLLLEVAWEALEDAGYDPeslaGSRTGVFVGASSNDY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 565 GHRLMARwesswrledsldaagfelsdeerrnltqavreslHNPVDAVVMLSYVGSLLASRIAATWDFSGPALMLTGDET 644
Cdd:COG3321 130 ALLLLAD----------------------------------PEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 645 GALRALELGQRLLAEGEADAVLVGAIDLAGAIENLMVRQACGA----------DISAP---VGEGACALVLEP-ADAVR- 709
Cdd:COG3321 176 SSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMlspdgrcrafDADADgyvRGEGVGVVVLKRlSDALRd 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 710 ----------------------------AQG---RAAYAewrgagfgesaqaaaasiRAGIgqDAASAGLVESAG----- 753
Cdd:COG3321 256 gdriyavirgsavnqdgrsngltapngpAQAaviRRALA------------------DAGV--DPATVDYVEAHGtgtpl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 754 --PLPAADLL----GGRP-----ALSSAAAVFGHTRMTAPLLSVLHAALSLSGRSLPAWAGWNGA--QIPagLEEAHAYV 820
Cdd:COG3321 316 gdPIEAAALTaafgQGRPadqpcAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPnpHID--FENSPFYV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 821 PTDARPWfRPADGRRVAAVlardddgSS-------AQALLAETPAGIANKAVAPALPLLLPLAAADRDALLAQLAAHIAE 893
Cdd:COG3321 394 NTELRPW-PAGGGPRRAGV-------SSfgfggtnAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 894 LEKPAAD-------------AAALCRAAVLAHNPqaplalalvaddaagllEEARAALAQLPKAQADWQSPRGsrfspaP 960
Cdd:COG3321 466 LEAHPDLdladvaytlatgrAHFEHRLAVVASSR-----------------EELAAKLRALAAGEAAPGVVTG------A 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 961 LGRDGKVAFVYSALNTAFTGLASRVAQLEPL---AGERLSAAHRDAGATIRSEQLYPrrltplDAEGRMQAEEALLQdnP 1037
Cdd:COG3321 523 AAAAPKVAFLFPGQGSQYVGMGRELYETEPVfraALDECDALLRPHLGWSLREVLFP------DEEESRLDRTEVAQ--P 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1038 ALINAgilsgwQYA-TLLTERVGLEPALQFGHSLGQATMMFASGAWTPGDAwlARLqeldgsltrlsgdkqaVREAWQLA 1116
Cdd:COG3321 595 ALFAV------EYAlARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSLEDA--LRL----------------VAARGRLM 650
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1117 DGQPVDWVNYLVLAPAAGVVEAAKQETRAYVSLINSPDEVTLVGERAACDRILQRLGAEAVPA---PDSLAMHCA---PA 1190
Cdd:COG3321 651 QALPGGGAMLAVGLSEEEVEALLAGYDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRArrlPVSHAFHSPlmePA 730
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1191 ERERAAIAERFTAQlsaQPQGLLFAG--GAPAAwTPEAVAERVAGDLVSPLDFPALVDQAYAQGARLFLELGPGGNCSRW 1268
Cdd:COG3321 731 LEEFRAALAGVTPR---APRIPLISNvtGTWLT-GEALDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPVLTGL 806
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1269 IGKTLRGRPHAT-FALARRDQDDAAMLAKLLALLVAQRVPLDLAAALRVQPEEKKPalLKDLCFCRPPIAATLVEALRKQ 1347
Cdd:COG3321 807 VRQCLAAAGDAVvLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRGRRRVP--LPTYPFQREDAAAALLAAALAA 884
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1348 GLDQALARPSKILTLKPATQDAMTATTQTTQHTLAEQAERHRAELAASHASLASLLAGKPAADPAAAPKQPPLFNEADIM 1427
Cdd:COG3321 885 ALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGAL 964
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1428 EFAEGRVANVLGPKFAEIDRLPRRVRVPGAPFMAVSRVTALSGTYGKLEDSRIRTEYDIPKPAWNAVDGQVSYLSLDAQG 1507
Cdd:COG3321 965 LLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAA 1044
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1508 VLFLVGWLGIDFENRGNRAYRWLDAQLTYLDVMPQAGQCVEYDIHITQSFRNGDATLFKTDFLASVDGRPALKIDHCTAG 1587
Cdd:COG3321 1045 AAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAAL 1124
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1588 FFTYEELSKGAGITDQHRTPRKVAQTAFIPPLAPPRRSLDGADLLAISRGEIAQVLSPAHASGGRNPSLRLPPAAIQFID 1667
Cdd:COG3321 1125 LALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAAL 1204
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1668 RVTSIEPAGGAHGLGGCEAEFQVNPQHWAIRAHFKDDPIFPGPCMMEGAFQLLQAYALSLGLQTAVTGARFQPLPHRPSL 1747
Cdd:COG3321 1205 LAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAA 1284
|
....*....
gi 2666213114 1748 VRFRAQVLP 1756
Cdd:COG3321 1285 LALAAAAAA 1293
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
477-837 |
2.97e-19 |
|
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: 92.62 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 477 RALAAGQPRLRPLPEGRHAGMPFPAPQ----------GAYLDRVAI-DALKLRVPPNDISRMYPQQLLMLSVGDAALGGA 545
Cdd:cd00833 23 ENLLEGRDAISEIPEDRWDADGYYPDPgkpgktytrrGGFLDDVDAfDAAFFGISPREAEAMDPQQRLLLEVAWEALEDA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 546 GVAP----GSRTAVIIASAMDHSGHRLMARWESswrledsldaagfelsdeerrnltqavreslhnpVDAVVMLSYVGSL 621
Cdd:cd00833 103 GYSPeslaGSRTGVFVGASSSDYLELLARDPDE----------------------------------IDAYAATGTSRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 622 LASRIAATWDFSGPALMLTGDETGALRALELGQRLLAEGEADAVLVGAIDLAGAIENLMVRQACGA----DISAPV---- 693
Cdd:cd00833 149 LANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMlspdGRCRPFdada 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 694 -----GEGACALVLEP-ADAVRAqGRAAYAEWRGAG---FGESAQAAAAS-------IR-----AGIgqDAASAGLVESA 752
Cdd:cd00833 229 dgyvrGEGVGVVVLKRlSDALRD-GDRIYAVIRGSAvnqDGRTKGITAPSgeaqaalIRrayarAGV--DPSDIDYVEAH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 753 G----------------PLPAADLLGGRPALSSAAAVFGHTRMTAPLLSVLHAALSLSGRSLPAWAGWNGAQIPAGLEEA 816
Cdd:cd00833 306 GtgtplgdpievealakVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEES 385
|
410 420
....*....|....*....|.
gi 2666213114 817 HAYVPTDARPWFRPADGRRVA 837
Cdd:cd00833 386 PLRVPTEARPWPAPAGPRRAG 406
|
|
| PRK05174 |
PRK05174 |
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase; |
1630-1767 |
5.66e-16 |
|
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
Pssm-ID: 179953 Cd Length: 172 Bit Score: 77.56 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1630 DLLAISRGEIAqvlspahasGGRNPSLRLPPaaIQFIDRVTSIEPAGGAHGLGGCEAEFQVNPQHWAIRAHFKDDPIFPG 1709
Cdd:PRK05174 12 DLLACGRGELF---------GPGNAQLPAPP--MLMMDRITEISETGGEFGKGYIVAELDINPDLWFFGCHFIGDPVMPG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1710 pCM-MEGAFQLL-----------QAYALSLGlqtavtgarfqplphrpsLVRFRAQVLPQNQTFTYRADI 1767
Cdd:PRK05174 81 -CLgLDAMWQLVgfylgwlggpgKGRALGVG------------------EVKFTGQVLPTAKKVTYEIDI 131
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
460-706 |
3.04e-15 |
|
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: 77.68 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 460 TGLGAAIGDCPDLNAVARALAAGQPRLRPLPEGRH-----------AGMPFPAPQGAYLDRVAIDALKLRVPPNDISRMY 528
Cdd:pfam00109 6 VGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWdpdklydppsrIAGKIYTKWGGLDDIFDFDPLFFGISPREAERMD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 529 PQQLLMLSVGDAALGGAGVAP----GSRTAVIIASAMDHSGHrlmarwesswrlEDSLDAAGfelsdeerrnltQAVRES 604
Cdd:pfam00109 86 PQQRLLLEAAWEALEDAGITPdsldGSRTGVFIGSGIGDYAA------------LLLLDEDG------------GPRRGS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 605 LHnpvdavvMLSYVGSLLASRIAATWDFSGPALMLTGDETGALRALELGQRLLAEGEADAVLVGAIDLAGAIENLMVRQA 684
Cdd:pfam00109 142 PF-------AVGTMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSA 214
|
250 260 270
....*....|....*....|....*....|....*
gi 2666213114 685 CGAD-------ISAP------VGEGACALVLEPAD 706
Cdd:pfam00109 215 AGMLspdgpckAFDPfadgfvRGEGVGAVVLKRLS 249
|
|
| FabA |
COG0764 |
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ... |
1657-1770 |
1.85e-13 |
|
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and metabolism]; 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440527 Cd Length: 141 Bit Score: 69.45 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1657 RLP-PAAIQFIDRVTSIEPAGGAHglggceAEFQVNPQHWAIRAHFKDDPIFPGPCMMEGAFQLLQAYAL-SLGLQTAVT 1734
Cdd:COG0764 7 LLPhRYPFLLVDRVLEIDPGKSIV------AEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLkSEGLEGKGR 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 2666213114 1735 GARFqplpHRPSLVRFRAQVLPQNQtFTYRADIVEI 1770
Cdd:COG0764 81 LVYF----LGIDKVKFRGPVVPGDT-LTLEVEIKRV 111
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
1051-1275 |
3.31e-10 |
|
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 63.22 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1051 ATLLTERvGLEPALQFGHSLGQATMMFASGAWTPGDA-WLARL-----QEL----DGSLTRLSG-DKQAVREawqladgq 1119
Cdd:COG0331 73 YRALEEE-GIRPDAVAGHSLGEYSALVAAGALSFEDAlRLVRLrgrlmQEAvpagPGGMAAVLGlDDEEVEA-------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1120 pvdwvnylvlapaagVVEAAKQETRAYVSLINSPDEVTLVGERAACDRILQRL---GA-EAVPAPDSLAMHC---APAer 1192
Cdd:COG0331 144 ---------------LCAEAAQGEVVEIANYNSPGQIVISGEKEAVEAAAELAkeaGAkRAVPLPVSGPFHTplmAPA-- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1193 eraaiAERFTAQLS----AQPQGLLFAG--GAPaAWTPEAVAERVAGDLVSPLDFPALVDQAYAQGARLFLELGPGGNCS 1266
Cdd:COG0331 207 -----AEKLAEALAavtfADPKIPVVSNvdAAP-VTDPEEIRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLS 280
|
....*....
gi 2666213114 1267 RWIGKTLRG 1275
Cdd:COG0331 281 GLVKRIDPG 289
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
7-437 |
3.71e-105 |
|
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: 343.39 E-value: 3.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGKRSIRDADTEDWGVDPTRflgPGRGVADQSSSIELAKPRGHD-FDASGFLLPAALL 85
Cdd:cd00833 5 IVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYY---PDPGKPGKTYTRRGGFLDDVDaFDAAFFGISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 86 GAQDRCIQWPLQVGRNALRDAGLWGGDL--SRVGMVLGSYAWAasaasdaiTRPLYDEALASAFAEAAPGHPLRLTAGRL 163
Cdd:cd00833 82 EAMDPQQRLLLEVAWEALEDAGYSPESLagSRTGVFVGASSSD--------YLELLARDPDEIDAYAATGTSRAFLANRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 164 qsgthpesarvsggittltARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAATQA 243
Cdd:cd00833 154 -------------------SYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGM 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 244 L-PDGTSnRPFDADSDGVAPADGAMALVLRRPD---SHRSTVYGTLRGMGLSSDGRGQTLTAPNPKGQKLACDRAYEQTG 319
Cdd:cd00833 215 LsPDGRC-RPFDADADGYVRGEGVGVVVLKRLSdalRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 320 ISPDTIAYVECHATGTKLGDRVELETVARVFGDNQP------VGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGI 393
Cdd:cd00833 294 VDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSadqpllIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHF 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2666213114 394 EKPLSR-DIAGTP-DIITQATPWPA--GHKRAAINAFGFGGVNAHLIV 437
Cdd:cd00833 374 ETPNPKiDFEESPlRVPTEARPWPApaGPRRAGVSSFGFGGTNAHVIL 421
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
7-487 |
2.01e-77 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 284.07 E-value: 2.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGKRSIRDADTEDWgvDPTRFLGPGRGVADQSSSielakPRG------HDFDASGFLL 80
Cdd:COG3321 8 IIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRW--DADAYYDPDPDAPGKTYV-----RWGgflddvDEFDALFFGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 81 P---AALLGAQDRCIqwpLQVGRNALRDAGLWGGDL--SRVGMVLGSYAWAASAASDaitrplydealasafaeaapGHP 155
Cdd:COG3321 81 SpreAEAMDPQQRLL---LEVAWEALEDAGYDPESLagSRTGVFVGASSNDYALLLL--------------------ADP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 156 LRLTAgrlQSGTHPESARVSGGIttltARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFAN 235
Cdd:COG3321 138 EAIDA---YALTGNAKSVLAGRI----SYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 236 FGFAATQAL-PDGTSnRPFDADSDGVAPADGAMALVLRR-----PDSHRstVYGTLRGMGLSSDGRGQTLTAPNPKGQKL 309
Cdd:COG3321 211 ILFSKGGMLsPDGRC-RAFDADADGYVRGEGVGVVVLKRlsdalRDGDR--IYAVIRGSAVNQDGRSNGLTAPNGPAQAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 310 ACDRAYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFGDNQP------VGSVKSNVGHLLTAAGIAGLVKTLLAMR 383
Cdd:COG3321 288 VIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPadqpcaIGSVKSNIGHLEAAAGVAGLIKAVLALR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 384 HGVIPATVGIEKPLSR-DIAGTP-DIITQATPWPAGHK--RAAINAFGFGGVNAHLIVDGPGQAAPETAPSRR------- 452
Cdd:COG3321 368 HGVLPPTLHFETPNPHiDFENSPfYVNTELRPWPAGGGprRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARppqllvl 447
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2666213114 453 --RGDAAL---LTGLGAAIGDCPDLN--AVARALAAGQPRLR 487
Cdd:COG3321 448 saKTEEALralAARLAAFLEAHPDLDlaDVAYTLATGRAHFE 489
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
7-437 |
1.86e-65 |
|
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: 228.58 E-value: 1.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGKRSIRDADTEDWGVDPTRFLGPGRgvadqsssielakprghDFDASGFLLPAALLG 86
Cdd:cd00834 5 ITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVP-----------------DFDPEDYLDRKELRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 87 AqDRCIQWPLQVGRNALRDAGLWGG--DLSRVGMVLGSYAWAASAasdaitrpLYDEALASAFAEAAPGHPLrltagrlq 164
Cdd:cd00834 68 M-DRFAQFALAAAEEALADAGLDPEelDPERIGVVIGSGIGGLAT--------IEEAYRALLEKGPRRVSPF-------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 165 sgTHPesARVSGGITTLTARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAATQAL 244
Cdd:cd00834 131 --FVP--MALPNMAAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRAL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 245 ------PDGTSnRPFDADSDGVAPADGAMALVLRRPDSHRS---TVYGTLRGMGLSSDGRGQTLTAPNPKGQKLACDRAY 315
Cdd:cd00834 207 strnddPEKAS-RPFDKDRDGFVLGEGAGVLVLESLEHAKArgaKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAAL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 316 EQTGISPDTIAYVECHATGTKLGDRVELETVARVFGDNQ---PVGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVG 392
Cdd:cd00834 286 ADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVFGEHAkkvPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTIN 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2666213114 393 IEKPlsrDIAGTPDIIT-QATPWPAghKRAAINAFGFGGVNAHLIV 437
Cdd:cd00834 366 LEEP---DPECDLDYVPnEAREAPI--RYALSNSFGFGGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
7-437 |
6.38e-63 |
|
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: 221.12 E-value: 6.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGK---RSIRDADTEDWgvdPTRFLGPGRgvadqsssielakprghDFDASGFLlPAA 83
Cdd:COG0304 5 ITGLGAVSPLGNGVEEFWEALLAGRsgiRPITRFDASGL---PVRIAGEVK-----------------DFDPEEYL-DRK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 84 LLGAQDRCIQWPLQVGRNALRDAGLWGGDLS--RVGMVLGSYAWAASAASDAITRpLYDEAlasafaeaapghplrltAG 161
Cdd:COG0304 64 ELRRMDRFTQYALAAAREALADAGLDLDEVDpdRTGVIIGSGIGGLDTLEEAYRA-LLEKG-----------------PR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 162 RLQSGTHPESarVSGGITTLTARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAAT 241
Cdd:COG0304 126 RVSPFFVPMM--MPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 242 QAL------PDGTSnRPFDADSDGVAPADGAMALVLRRPDSHRS---TVYGTLRGMGLSSDGRGQTLTAPNPKGQKLACD 312
Cdd:COG0304 204 GALstrnddPEKAS-RPFDKDRDGFVLGEGAGVLVLEELEHAKArgaKIYAEVVGYGASSDAYHITAPAPDGEGAARAMR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 313 RAYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFGDNQ---PVGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPA 389
Cdd:COG0304 283 AALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVFGDHAykvPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPP 362
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2666213114 390 TVGIEkplsrdiagTPD-------IITQATPWPAghKRAAINAFGFGGVNAHLIV 437
Cdd:COG0304 363 TINLE---------NPDpecdldyVPNEAREAKI--DYALSNSFGFGGHNASLVF 406
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
7-437 |
3.51e-53 |
|
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: 189.08 E-value: 3.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGkrsIRDADtedwgvdptrflgpgrgvadqsssielakprghDFDASGFLLP---AA 83
Cdd:smart00825 3 IVGMSCRFPGADDPEEFWDLLLAG---LDDVD---------------------------------LFDAAFFGISpreAE 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 84 LLGAQDRCIqwpLQVGRNALRDAGLWGGDL--SRVGMVLGsyawaasaasdaitrplydealasafaeaapghplrltag 161
Cdd:smart00825 47 AMDPQQRLL---LEVAWEALEDAGIDPESLrgSRTGVFVG---------------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 162 rlqsGTHPESArvsggittltaralglggprYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAAT 241
Cdd:smart00825 84 ----VSSSDYS--------------------VTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRA 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 242 QAL-PDGTSnRPFDADSDGVAPADGAMALVLRR-----PDSHRstVYGTLRGMGLSSDGRGQTLTAPNPKGQklacdray 315
Cdd:smart00825 140 GMLsPDGRC-KTFDASADGYVRGEGVGVVVLKRlsdalRDGDP--ILAVIRGSAVNQDGRSNGITAPSGPAQ-------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 316 eqtgispdtiayveCHatgtklgdrveletvarvfgdnqpVGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEK 395
Cdd:smart00825 209 --------------LL------------------------IGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFET 250
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2666213114 396 PLSR-DIAGTP-DIITQATPWPAGHK--RAAINAFGFGGVNAHLIV 437
Cdd:smart00825 251 PNPHiDLEESPlRVPTELTPWPPPGRprRAGVSSFGFGGTNAHVIL 296
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
4-456 |
3.95e-50 |
|
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: 197.15 E-value: 3.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 4 PLDITGIACLVPDADTLDGFWQNLLAGKRSIRDADTEDWGVDPtrFLGPGRGVADQSSSielakPRGH-----DFDASGF 78
Cdd:TIGR02813 8 PIAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKDD--YYDSDKSEADKSYC-----KRGGflpevDFNPMEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 79 LLPAALLGAQDRCIQWPLQVGRNALRDAGLWGG-DLSRVGMVLGSYAWAASAASDAiTRPLYDEALASAFAEAAPGHPLR 157
Cdd:TIGR02813 81 GLPPNILELTDISQLLSLVVAKEVLNDAGLPDGyDRDKIGITLGVGGGQKQSSSLN-ARLQYPVLKKVFKASGVEDEDSE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 158 LTAGRLQSG-THPESARVSGG----ITTLTARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTL 232
Cdd:TIGR02813 160 MLIKKFQDQyIHWEENSFPGSlgnvISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 233 FANFGFAATQALPDGTSNRPFDADSDGVAPADGAMALVLRR-PDSHRS--TVYGTLRGMGLSSDGRGQTLTAPNPKGQKL 309
Cdd:TIGR02813 240 FMYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRlEDAERDgdRIYAVIKGVGASSDGKFKSIYAPRPEGQAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 310 ACDRAYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFG-DNQ-----PVGSVKSNVGHLLTAAGIAGLVKTLLAMR 383
Cdd:TIGR02813 320 ALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSqDNDqkqhiALGSVKSQIGHTKSTAGTAGMIKAVLALH 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2666213114 384 HGVIPATVGIEKP-LSRDIAGTPDII-TQATPWPAGH----KRAAINAFGFGGVNAHLIVDgpgqaapETAPSRRRGDA 456
Cdd:TIGR02813 400 HKVLPPTINVDQPnPKLDIENSPFYLnTETRPWMQREdgtpRRAGISSFGFGGTNFHMVLE-------EYSPKHQRDDQ 471
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
282-394 |
7.01e-44 |
|
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: 155.42 E-value: 7.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 282 YGTLRGMGLSSDGRGQTLTAPNPKGQKLACDRAYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFGDNQ-----PV 356
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArkqplAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2666213114 357 GSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIE 394
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| FabA |
cd01287 |
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ... |
1656-1803 |
3.76e-43 |
|
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the type II, fatty acid synthase system that binds ACP and catalyzes both dehydration and isomerization reactions, apparently in the same active site. The FabA structure is a homodimer with two independent active sites located at the dimer interface. Each active site is tunnel-shaped and completely inaccessible to solvent. No metal ions or cofactors are required for ligand binding or catalysis.
Pssm-ID: 238614 Cd Length: 150 Bit Score: 154.72 E-value: 3.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1656 LRLPPAAIQFIDRVTSIEPAGGAHGLGGCEAEFQVNPQHWAIRAHFKDDPIFPGPCMMEGAFQLLQAYALSLGLQTAVTG 1735
Cdd:cd01287 1 PRLPGGQLLMLDRVTEIDPGGGTFGLGYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIWLGLGTGVDN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2666213114 1736 ARFQPLPHRPSLVRFRAQVLPQNQTFTYRADIVEIG-LTPEPYLIADIDLIDNGRVMGRVEGLGIRLTG 1803
Cdd:cd01287 81 PRFQGAPGGPGEWKYRGQITPHNKKVTYEVHIKEVGrDGPRPYIIADASLWVDGLRIYEAKDIAVRLVE 149
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
7-436 |
3.32e-42 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 161.32 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGK---RSIRDADTEDWgvdPTRFLGPGRGVADqsssielakprghdfDASGFLLPAA 83
Cdd:PRK06333 8 VTGMGAVSPLGCGVETFWQRLLAGQsgiRTLTDFPVGDL---ATKIGGQVPDLAE---------------DAEAGFDPDR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 84 LLGAQ-----DRCIQWPLQVGRNALRDAGLWGGDLS---RVGMVLGSYAWAASAASDAITRplydealasafaeaapghp 155
Cdd:PRK06333 70 YLDPKdqrkmDRFILFAMAAAKEALAQAGWDPDTLEdreRTATIIGSGVGGFPAIAEAVRT------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 156 lRLTAG--RLQSGTHPES-ARVSGGittLTARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTL 232
Cdd:PRK06333 131 -LDSRGprRLSPFTIPSFlTNMAAG---HVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 233 FANFGFAATQALPDGTSN------RPFDADSDGVAPADGAMALVLRRPDS---HRSTVYGTLRGMGLSSDGRGQTLTAPN 303
Cdd:PRK06333 207 VSLAGFAAARALSTRFNDapeqasRPFDRDRDGFVMGEGAGILVIETLEHalaRGAPPLAELVGYGTSADAYHMTAGPED 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 304 PKGQKLACDRAYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFGDNQ--PVGSVKSNVGHLLTAAGIAGLVKTLLA 381
Cdd:PRK06333 287 GEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVSglAVSSTKSATGHLLGAAGGVEAIFTILA 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2666213114 382 MRHGVIPATVGIEKPLSrDIAGTPDIITQATPWPAghKRAAINAFGFGGVNAHLI 436
Cdd:PRK06333 367 LRDQIAPPTLNLENPDP-AAEGLDVVANKARPMDM--DYALSNGFGFGGVNASIL 418
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
19-436 |
7.42e-42 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 160.24 E-value: 7.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 19 TLDGFWQNLLAGK---RSIRDADTEDWGVDPtRFLGPGRGVADQSSSIElAKPRGHDFDASGFllpaALLGAQDRCIQWP 95
Cdd:PTZ00050 8 GAESTWEALIAGKsgiRKLTEFPKFLPDCIP-EQKALENLVAAMPCQIA-AEVDQSEFDPSDF----APTKRESRATHFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 96 LQVGRNALRDAGLWGG---DLSRVGMVLGSYAWAASAASDAITRpLYDEalasafaeaapGHplrltaGRLQSGTHPES- 171
Cdd:PTZ00050 82 MAAAREALADAKLDILsekDQERIGVNIGSGIGSLADLTDEMKT-LYEK-----------GH------SRVSPYFIPKIl 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 172 ARVSGGITTLTaraLGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAATQALPDGTSN- 250
Cdd:PTZ00050 144 GNMAAGLVAIK---HKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYNDd 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 251 -----RPFDADSDGVAPADGAMALVLRRPDSHRS---TVYGTLRGMGLSSDGrgQTLTAPNP--KGQKLACDRAYEQTG- 319
Cdd:PTZ00050 221 pqrasRPFDKDRAGFVMGEGAGILVLEELEHALRrgaKIYAEIRGYGSSSDA--HHITAPHPdgRGARRCMENALKDGAn 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 320 ISPDTIAYVECHATGTKLGDRVELETVARVFGDNQP----VGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEK 395
Cdd:PTZ00050 299 ININDVDYVNAHATSTPIGDKIELKAIKKVFGDSGApklyVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLEN 378
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2666213114 396 PlsrDIAGTPDIITQATPWPAGHKRAAI-NAFGFGGVNAHLI 436
Cdd:PTZ00050 379 P---DAECDLNLVQGKTAHPLQSIDAVLsTSFGFGGVNTALL 417
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
7-436 |
1.26e-40 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 156.10 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGK---RSIRDADTEDWgvdPTRFLGpgrgvadqsssiELakprgHDFDASGFLlPAA 83
Cdd:PRK07314 6 VTGLGAVSPLGNDVESTWKNLLAGKsgiGPITHFDTSDL---AVKIAG------------EV-----KDFNPDDYM-SRK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 84 LLGAQDRCIQWPLQVGRNALRDAGLWGGDLS--RVGMVLGSYAWAASAASDAITRpLYDealasafaeaapGHPLRLTAG 161
Cdd:PRK07314 65 EARRMDRFIQYGIAAAKQAVEDAGLEITEENadRIGVIIGSGIGGLETIEEQHIT-LLE------------KGPRRVSPF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 162 RLQSgthpesaRVSGGITTLTARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAAT 241
Cdd:PRK07314 132 FVPM-------AIINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 242 QAL------PDGTSnRPFDADSDGVAPADGAMALVLRRPDSHRS---TVYGTLRGMGLSSDGrgQTLTAPNPKGQ--KLA 310
Cdd:PRK07314 205 RALstrnddPERAS-RPFDKDRDGFVMGEGAGILVLEELEHAKArgaKIYAEVVGYGMTGDA--YHMTAPAPDGEgaARA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 311 CDRAYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFGD---NQPVGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVI 387
Cdd:PRK07314 282 MKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFGEhayKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVI 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2666213114 388 PATVGIEKPlsrDIAGTPDIITQaTPWPAGHKRAAINAFGFGGVNAHLI 436
Cdd:PRK07314 362 PPTINLDNP---DEECDLDYVPN-EARERKIDYALSNSFGFGGTNASLV 406
|
|
| pfaB_fam |
TIGR02816 |
PfaB family protein; The protein PfaB is part of four gene locus, similar to polyketide ... |
943-1314 |
6.64e-39 |
|
PfaB family protein; The protein PfaB is part of four gene locus, similar to polyketide biosynthesis systems, responsible for omega-3 polyunsaturated fatty acid biosynthesis in several high pressure and/or cold-adapted bacteria. The fairly permissive trusted cutoff set for this model allows detection of homologs encoded near homologs to other proteins of the locus: PfaA, PfaC, and/or PfaD. The likely role in every case is either polyunsaturated fatty acid or polyketide biosynthesis.
Pssm-ID: 131863 [Multi-domain] Cd Length: 538 Bit Score: 154.09 E-value: 6.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 943 KAQADWQSPRGSRFSPAPLGRD-----GKVAFVYSALNTAFTGLASRVAQLEPLAGERLSAaHRDAGATIRSEQLYprrl 1017
Cdd:TIGR02816 154 KGLIHYKTPAGSCFSLAPLGSNndnakAGLAFVYPGVGTVYADMFNDFHQYFPALFAKLER-EGDLKAMLQAEDIY---- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1018 tpldAEGRMQAEEALLQDnpaLINAGILSGWQYATLLTERVGLEPALQFGHSLGQATMMFASGAWTPGDAWLARLQELDG 1097
Cdd:TIGR02816 229 ----GEDPKHAAEMSLGD---LAIAGVGSSYLLTQLLCDEFAIKPDFALGYSKGEASMWASLGVWKNPHALIEKTQTDPI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1098 SLTRLSGDKQAVREAWQLAD-GQPVDWVNYLVLAPAAGVVEAAKQETRAYVSLINSpDEVTLVGERAACDRILQRLGAEA 1176
Cdd:TIGR02816 302 FTSAISGKLTAVREAWQLDDtAAEIQWNSFVVRCEAAPIEALLKDFPHAYLAIIQG-DTCVIAGCEAQCKALLAALGKRG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1177 VPAPDSLAMHCAPAERERAAIAERFTAQLSAQ-PQGLLFAGGA---------PAAWTPEAVAERVAGDLVSPLDFPALVD 1246
Cdd:TIGR02816 381 IAANRVTAMHTQPALQEHQNVMDFYLQPLCAElPMDIKFISAAdllaknqnsEQAIDSQSIANSIADTFCQTLDFTALIH 460
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2666213114 1247 QAYAQGARLFLELGPGGNCSRWIGK--------TLRGRPHATFALARRDQDDAAMLAKLLALLVAQRVPLDLAAAL 1314
Cdd:TIGR02816 461 HAQEQGAKLFVEIGADRQNCTLIDKinkqdgasSEQHQPCCTVAANAKGGEDITSLIKAIAQLISHQIPLSLQPFI 536
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
187-436 |
1.81e-38 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 149.88 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 187 GLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAATQALPD-----GTSNRPFDADSDGVA 261
Cdd:PRK08439 150 GLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrnddpKKASRPFDKDRDGFV 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 262 PADGAMALVLRRPDSHRS---TVYGTLRGMGLSSDGrgQTLTAPNPKGQKLACDRAYEQTGISPdtIAYVECHATGTKLG 338
Cdd:PRK08439 230 MGEGAGALVLEEYESAKKrgaKIYAEIIGFGESGDA--NHITSPAPEGPLRAMKAALEMAGNPK--IDYINAHGTSTPYN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 339 DRVELETVARVFGDNQ---PVGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEKPLSR-DIAGTPDIITQATPw 414
Cdd:PRK08439 306 DKNETAALKELFGSKEkvpPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPEcDLDYIPNVARKAEL- 384
|
250 260
....*....|....*....|..
gi 2666213114 415 paghKRAAINAFGFGGVNAHLI 436
Cdd:PRK08439 385 ----NVVMSNSFGFGGTNGVVI 402
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
187-440 |
1.36e-37 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 148.02 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 187 GLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAATQALPDG------TSNRPFDADSDGV 260
Cdd:PLN02836 172 GFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfnscptEASRPFDCDRDGF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 261 APADGAMALVLRRPDSHR---STVYGTLRGMGLSSDGRGQTLTAPNPKGQKLACDRAYEQTGISPDTIAYVECHATGTKL 337
Cdd:PLN02836 252 VIGEGAGVLVLEELEHAKrrgAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAHATSTPL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 338 GDRVELETVARVFGDNQPVG-----SVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEKPlsrDIAGTPDIITQAT 412
Cdd:PLN02836 332 GDAVEARAIKTVFSEHATSGglafsSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERP---DPIFDDGFVPLTA 408
|
250 260
....*....|....*....|....*....
gi 2666213114 413 PwPAGHKRAAI-NAFGFGGVNAHLIVDGP 440
Cdd:PLN02836 409 S-KAMLIRAALsNSFGFGGTNASLLFTSP 436
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
157-437 |
3.10e-37 |
|
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: 143.93 E-value: 3.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 157 RLTAGRLQSGTHPESARVSGGITTLTARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANF 236
Cdd:cd00825 54 FGADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 237 GFAATQALPDGTSNRPFDADSDGVAPADGAMALVLRRPDSHR---STVYGTLRGMGLSSDGRGQTLTAPNPKGQKLACDR 313
Cdd:cd00825 134 FDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEELEHALargAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 314 AYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFGDNQP-VGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVG 392
Cdd:cd00825 214 ALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGDKSPaVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIH 293
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2666213114 393 IEKPlsrDIAGTPdIITQATpwPAGHKRAAINAFGFGGVNAHLIV 437
Cdd:cd00825 294 IEEL---DEAGLN-IVTETT--PRELRTALLNGFGLGGTNATLVL 332
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
4-437 |
1.97e-36 |
|
"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: 143.73 E-value: 1.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 4 PLDITGIACLVPDA---DTLDGFWQNLLAGKRSIRDADTEDWGVDptrflgpgRGVADQsssielakPRGHDFDASGfll 80
Cdd:cd00828 2 RVVITGIGVVSPHGegcDEVEEFWEALREGRSGIAPVARLKSRFD--------RGVAGQ--------IPTGDIPGWD--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 81 pAALLGAQDRCIQWPLQVGRNALRDAGL---WGGDLSRVGMVLGSYAWAasaasdaiTRPLYDEalasafaeaapGHPLR 157
Cdd:cd00828 63 -AKRTGIVDRTTLLALVATEEALADAGItdpYEVHPSEVGVVVGSGMGG--------LRFLRRG-----------GKLDA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 158 LTAGRLQSGTHPESARVSGGITTLtaRALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFdTLFANFG 237
Cdd:cd00828 123 RAVNPYVSPKWMLSPNTVAGWVNI--LLLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDP-LEEGLSG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 238 FAATQAL------PDGTSnRPFDADSDGVAPADGAMALVLRRPDSHRS---TVYGTLRGMGLSSDGRGQTLTAPNPkGQK 308
Cdd:cd00828 200 FANMGALstaeeePEEMS-RPFDETRDGFVEAEGAGVLVLERAELALArgaPIYGRVAGTASTTDGAGRSVPAGGK-GIA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 309 LACDRAYEQTGISPDTIAYVECHATGTKLGDRVELETVARVF---GDNQPVGSVKSNVGHLLTAAGIAGLVKTLLAMRHG 385
Cdd:cd00828 278 RAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIAEVAgalGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHG 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2666213114 386 VIPATVGIEKPLsrDIAGTPDIITQATPWPAGHKRAAINAFGFGGVNAHLIV 437
Cdd:cd00828 358 LIPPTANLDDVD--PDVEHLSVVGLSRDLNLKVRAALVNAFGFGGSNAALVL 407
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
7-436 |
4.32e-36 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 142.83 E-value: 4.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGKRSIRDADTEDWGVDPTRFLGpgrgvadqsssieLAKprghDFDASGFLLPAALLg 86
Cdd:PRK08722 8 VTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAG-------------LVK----DFNCEEYMSKKDAR- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 87 AQDRCIQWPLQVGRNALRDAGLW--GGDLSRVGMVLGSYAWAASAASDAiTRPLYDEALASAFAEAAPGHPLRLTAGRLq 164
Cdd:PRK08722 70 KMDLFIQYGIAAGIQALDDSGLEvtEENAHRIGVAIGSGIGGLGLIEAG-HQALVEKGPRKVSPFFVPSTIVNMIAGNL- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 165 sgthpesarvsggittltARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAATQAL 244
Cdd:PRK08722 148 ------------------SIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 245 ------PDGTSnRPFDADSDGVAPADGAMALVLRRPDSHR---STVYGTLRGMGLSSDGRGQTLTAPNPKGQKLACDRAY 315
Cdd:PRK08722 210 strndePQKAS-RPWDKDRDGFVLGDGAGMMVLEEYEHAKargAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 316 EQTGISPDTIAYVECHATGTKLGDRVELETVARVFGDNQP----VGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATV 391
Cdd:PRK08722 289 RDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRALGEAGSkqvlVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTI 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2666213114 392 GIEKPlsrDIAGTPDIITQATPWPAGHKRAAINAFGFGGVNAHLI 436
Cdd:PRK08722 369 NLDDP---EEGLDIDLVPHTARKVESMEYAICNSFGFGGTNGSLI 410
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
7-436 |
3.40e-35 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 142.81 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGKRSIRDADTEDWGVDPTRFLGPGRgvadqsssielakprghDFDASGFLLPAaLLG 86
Cdd:PLN02787 133 VTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIK-----------------SFSTDGWVAPK-LSK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 87 AQDRCIQWPLQVGRNALRDAGLWGG-----DLSRVGMVLGSYAWAASAASDAItrplydealasafaeaapgHPLRLTAG 161
Cdd:PLN02787 195 RMDKFMLYLLTAGKKALADGGITEDvmkelDKTKCGVLIGSAMGGMKVFNDAI-------------------EALRISYR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 162 RLQSGTHPESARVSGgiTTLTARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAAT 241
Cdd:PLN02787 256 KMNPFCVPFATTNMG--SAMLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVAC 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 242 QALPDGTSN-----RPFDADSDGVAPADGAMALVLRRPDSHR---STVYGTLRGMGLSSDGRGQTLTAPNPKGQKLACDR 313
Cdd:PLN02787 334 RALSQRNDDptkasRPWDMNRDGFVMGEGAGVLLLEELEHAKkrgANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEK 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 314 AYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFGDNQP--VGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATV 391
Cdd:PLN02787 414 ALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFGQNPElrVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNI 493
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2666213114 392 GIEKPlsrDIAGTPDIITQATPWPAGHKRAAINAFGFGGVNAHLI 436
Cdd:PLN02787 494 NLENP---ESGVDTKVLVGPKKERLDIKVALSNSFGFGGHNSSIL 535
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
183-436 |
1.23e-33 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 134.97 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 183 ARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVvaaNGFDTL--FANFGFAATQALPDGTSnRPFDADSDGV 260
Cdd:PRK09185 144 RAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIV---GGVDSLcrLTLNGFNSLESLSPQPC-RPFSANRDGI 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 261 APADGAMALVLRRPDSHRSTvygtLRGMGLSSDGrgQTLTAPNP--KGQKLACDRAYEQTGISPDTIAYVECHATGTKLG 338
Cdd:PRK09185 220 NIGEAAAFFLLEREDDAAVA----LLGVGESSDA--HHMSAPHPegLGAILAMQQALADAGLAPADIGYINLHGTATPLN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 339 DRVELETVARVFGDNQPVGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEKPlsrDIAGTPDIITQATPwPAGH 418
Cdd:PRK09185 294 DAMESRAVAAVFGDGVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQP---DPALPPLYLVENAQ-ALAI 369
|
250
....*....|....*...
gi 2666213114 419 KRAAINAFGFGGVNAHLI 436
Cdd:PRK09185 370 RYVLSNSFAFGGNNCSLI 387
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
2-437 |
2.24e-33 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 134.77 E-value: 2.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 2 MFPLDITGIACLVPDADTLDGFWQNLLAGKRSIRDADTEDwgvdPTRFLGPGRGVADQSSSIELAkprghdfdasGFLLP 81
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPG----RQVPDDAGAGLASAFIGAELD----------SLALP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 82 AALLGAQDRCIQWPLQVG----RNALRDAGLWGGDLSRVGMVLGsyawaasaasdaitrplydealasafaeaapGHPL- 156
Cdd:PRK07103 67 ERLDAKLLRRASLSAQAAlaaaREAWRDAALGPVDPDRIGLVVG-------------------------------GSNLq 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 157 -RLTAGRLQS-GTHPESARVSGGITT-------LTARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAAn 227
Cdd:PRK07103 116 qREQALVHETyRDRPAFLRPSYGLSFmdtdlvgLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGA- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 228 gfdtlFANFGFAATQALPD----GTSN---------RPFDADSDGVAPADGAMALVLRRPDSHR---STVYGTLRGMGLS 291
Cdd:PRK07103 195 -----LMDLSYWECQALRSlgamGSDRfadepeaacRPFDQDRDGFIYGEACGAVVLESAESARrrgARPYAKLLGWSMR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 292 SDGRgqTLTAPNPKGQKLACDRAYEQTGISPDTIAYVECHATGTKLGDRVELETVARVFGDNQPVGSVKSNVGHLLTAAG 371
Cdd:PRK07103 270 LDAN--RGPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGDETELAALFASGLAHAWINATKSLTGHGLSAAG 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2666213114 372 IAGLVKTLLAMRHGVIPATVGIEKPLSRDIAgtpdiITQATPWPAGHKRAAINAFGFGGVNAHLIV 437
Cdd:PRK07103 348 IVELIATLLQMRAGFLHPSRNLDEPIDERFR-----WVGSTAESARIRYALSLSFGFGGINTALVL 408
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
7-273 |
1.18e-31 |
|
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: 125.44 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 7 ITGIACLVPDADTLDGFWQNLLAGKRSIRDADTEDWgvDPTRFLGPGRGVADQSSSIELAKPRGHDFDASGFLLPAALLG 86
Cdd:pfam00109 5 IVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRW--DPDKLYDPPSRIAGKIYTKWGGLDDIFDFDPLFFGISPREAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 87 AQDRCIQWPLQVGRNALRDAGLWGGDL--SRVGMVLGSYAWAASAasdaiTRPLYDEALASAFAEAAPGHPLRLTAGRLq 164
Cdd:pfam00109 83 RMDPQQRLLLEAAWEALEDAGITPDSLdgSRTGVFIGSGIGDYAA-----LLLLDEDGGPRRGSPFAVGTMPSVIAGRI- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 165 sgthpesarvsggittltARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAATQAL 244
Cdd:pfam00109 157 ------------------SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGML 218
|
250 260
....*....|....*....|....*....
gi 2666213114 245 PDGTSNRPFDADSDGVAPADGAMALVLRR 273
Cdd:pfam00109 219 SPDGPCKAFDPFADGFVRGEGVGAVVLKR 247
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
181-433 |
4.64e-31 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 127.09 E-value: 4.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 181 LTARALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAATQAL-PDGTSnrPFDADSDG 259
Cdd:PRK05952 128 AAARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALaKTGAY--PFDRQREG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 260 VAPADGAMALVLRRPDS--HRST-VYGTLRGMGLSSDGRGQTLTAPNPKGQKLACDRAYEQTGISPDTIAYVECHATGTK 336
Cdd:PRK05952 206 LVLGEGGAILVLESAELaqKRGAkIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 337 LGDRVELETVARVFGDNQPVGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEKPlSRDIagtpDIITQATPWPA 416
Cdd:PRK05952 286 LNDQREANLIQALFPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEP-EFDL----NFVRQAQQSPL 360
|
250
....*....|....*..
gi 2666213114 417 ghKRAAINAFGFGGVNA 433
Cdd:PRK05952 361 --QNVLCLSFGFGGQNA 375
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
198-436 |
4.60e-30 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 125.13 E-value: 4.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 198 ACATSLYAIHLAAMHIASGEADAMLVVAANG---------FDTLFAnfgfAATQALPDGTSNRPFDADSDGVAPADGAMA 268
Cdd:PRK06501 174 ACASGATAIQLGVEAIRRGETDRALCIATDGsvsaealirFSLLSA----LSTQNDPPEKASKPFSKDRDGFVMAEGAGA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 269 LVLRRPDSHR---STVYGTLRGMGLSSDGRGQTLTAPNPKGQKLACDRAYEQTGISPDTIAYVECHATGTKLGDRVELET 345
Cdd:PRK06501 250 LVLESLESAVargAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPENDKMEYLG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 346 VARVFGD---NQPVGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEKPlsrdiagTPDIITQATPwpaGHKRAA 422
Cdd:PRK06501 330 LSAVFGErlaSIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNP-------DPAIPLDVVP---NVARDA 399
|
250 260
....*....|....*....|
gi 2666213114 423 ------INAFGFGGVNAHLI 436
Cdd:PRK06501 400 rvtavlSNSFGFGGQNASLV 419
|
|
| FabA |
pfam07977 |
FabA-like domain; This enzyme domain has a HotDog fold. |
1658-1790 |
5.71e-29 |
|
FabA-like domain; This enzyme domain has a HotDog fold.
Pssm-ID: 429766 Cd Length: 132 Bit Score: 113.53 E-value: 5.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1658 LPPAAIQFIDRVTSIEPAGGAHGLGGCEAEFQVNPQHWAIRAHFKDDPIFPGPCMMEGAFQLLQAYALSLGLQTAVTGAR 1737
Cdd:pfam07977 1 LPHRYFLMLDRVTEIDPDGGKFGKGYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGRAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2666213114 1738 FqplphrPSLVRFRAQVLPQNQTFTYRADIVEIGLTPEPYLIADIDLIDNGRV 1790
Cdd:pfam07977 81 G------VDEVKFRGQVTPGDKQLRYEVEIKKIIEGRRGIGIADGRALVDGKV 127
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
190-437 |
1.26e-27 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 116.37 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 190 GPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAATQAL-------PDGTSnRPFDADSDGVAP 262
Cdd:PRK14691 82 GPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALsthfnstPEKAS-RPFDTARDGFVM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 263 ADGAMALVLRRPD---SHRSTVYGTLRGMGLSSDGRGQTLTAPNPKGQKLACDRAYEQTGISPDTIAYVECHATGTKLGD 339
Cdd:PRK14691 161 GEGAGLLIIEELEhalARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 340 RVELETVARVFGDNQ--PVGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEKPlsrDIAGTPDIITQATPWPAG 417
Cdd:PRK14691 241 LGEINAIKHLFGESNalAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENP---DPAAKGLNIIAGNAQPHD 317
|
250 260
....*....|....*....|
gi 2666213114 418 HKRAAINAFGFGGVNAHLIV 437
Cdd:PRK14691 318 MTYALSNGFGFAGVNASILL 337
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
187-436 |
3.93e-26 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 113.16 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 187 GLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLV--------VAANGFDTLFAnfgfAATQALPDGTSNRPFDADSD 258
Cdd:PRK09116 152 GLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAggaeelcpTEAAVFDTLFA----TSTRNDAPELTPRPFDANRD 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 259 GVAPADGAMALVLRRPDSHRS---TVYGTLRGMGLSSDGrgQTLTAPNPKGQKLACDRAYEQTGISPDTIAYVECHATGT 335
Cdd:PRK09116 228 GLVIGEGAGTLVLEELEHAKArgaTIYAEIVGFGTNSDG--AHVTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTAT 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 336 KLGDRVELETVARVFGDNQPVGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEKPLSRdiAGTPDIITQaTPWP 415
Cdd:PRK09116 306 DRGDIAESQATAAVFGARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPA--CGALDYIMG-EARE 382
|
250 260
....*....|....*....|.
gi 2666213114 416 AGHKRAAINAFGFGGVNAHLI 436
Cdd:PRK09116 383 IDTEYVMSNNFAFGGINTSLI 403
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
190-436 |
4.57e-25 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 110.15 E-value: 4.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 190 GPRYAIDAACATSLYAIHLAAMHIASGEADamlVVAANGFD-------TLFANFGFAATQ--ALPDgTSNRPFDADSDGV 260
Cdd:PRK07967 153 GVNYSISSACATSAHCIGNAVEQIQLGKQD---IVFAGGGEeldwemsCLFDAMGALSTKynDTPE-KASRAYDANRDGF 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 261 APADGAMALV---LRRPDSHRSTVYGTLRGMGLSSDGrgQTLTAPNPKGqKLACDRAYEQTGISPdtIAYVECHATGTKL 337
Cdd:PRK07967 229 VIAGGGGVVVveeLEHALARGAKIYAEIVGYGATSDG--YDMVAPSGEG-AVRCMQMALATVDTP--IDYINTHGTSTPV 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 338 GDRVELETVARVFGDNQP-VGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEKpLSRDIAGTPdIITQATpwpa 416
Cdd:PRK07967 304 GDVKELGAIREVFGDKSPaISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEE-LDPQAAGMP-IVTETT---- 377
|
250 260
....*....|....*....|....*
gi 2666213114 417 ghKRAAI-----NAFGFGGVNAHLI 436
Cdd:PRK07967 378 --DNAELttvmsNSFGFGGTNATLV 400
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
184-437 |
6.81e-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: 105.99 E-value: 6.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 184 RALGLGGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFdtlfanfgfaatqalpdgtsnrpfdadsdgvAPA 263
Cdd:cd00327 53 HLGISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF-------------------------------VFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 264 DGAMALVLRRPD---SHRSTVYGTLRGMGLSSDGRGQtLTAPNPKGQKLACDRAYEQTGISPDTIAYVECHATGTKLGDR 340
Cdd:cd00327 102 DGAAAAVVESEEhalRRGAHPQAEIVSTAATFDGASM-VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 341 VELETVARVFGDNQP-VGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATvgiekplsrdiagtpdiitqatpwPAGHK 419
Cdd:cd00327 181 VELALGLDPDGVRSPaVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT------------------------PREPR 236
|
250
....*....|....*...
gi 2666213114 420 RAAINAFGFGGVNAHLIV 437
Cdd:cd00327 237 TVLLLGFGLGGTNAAVVL 254
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
197-435 |
3.88e-24 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 107.51 E-value: 3.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 197 AACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFAATQAL-------PDGTSnRPFDADSDGVAPADGAMAL 269
Cdd:PRK07910 169 SACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVmstnnddPAGAC-RPFDKDRDGFVFGEGGALM 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 270 VLRRPDSHRS---TVYGTLRGMGLSSDGrgQTLTAPNPKGQKL--ACDRAYEQTGISPDTIAYVECHATGTKLGDRVELE 344
Cdd:PRK07910 248 VIETEEHAKArgaNILARIMGASITSDG--FHMVAPDPNGERAghAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 345 TVARVFGDNQP-VGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEKPlsrdiagTPDI---ITQATPWPAGHKR 420
Cdd:PRK07910 326 AINNALGGHRPaVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENL-------DPEIdldVVAGEPRPGNYRY 398
|
250
....*....|....*
gi 2666213114 421 AAINAFGFGGVNAHL 435
Cdd:PRK07910 399 AINNSFGFGGHNVAL 413
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
490-1756 |
1.43e-22 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 106.11 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 490 PEGRHAGmPFPAPQGAYLDRVA-IDALKLRVPPNDISRMYPQQLLMLSVGDAALGGAGVAP----GSRTAVIIASAMDHS 564
Cdd:COG3321 51 PDPDAPG-KTYVRWGGFLDDVDeFDALFFGISPREAEAMDPQQRLLLEVAWEALEDAGYDPeslaGSRTGVFVGASSNDY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 565 GHRLMARwesswrledsldaagfelsdeerrnltqavreslHNPVDAVVMLSYVGSLLASRIAATWDFSGPALMLTGDET 644
Cdd:COG3321 130 ALLLLAD----------------------------------PEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 645 GALRALELGQRLLAEGEADAVLVGAIDLAGAIENLMVRQACGA----------DISAP---VGEGACALVLEP-ADAVR- 709
Cdd:COG3321 176 SSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMlspdgrcrafDADADgyvRGEGVGVVVLKRlSDALRd 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 710 ----------------------------AQG---RAAYAewrgagfgesaqaaaasiRAGIgqDAASAGLVESAG----- 753
Cdd:COG3321 256 gdriyavirgsavnqdgrsngltapngpAQAaviRRALA------------------DAGV--DPATVDYVEAHGtgtpl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 754 --PLPAADLL----GGRP-----ALSSAAAVFGHTRMTAPLLSVLHAALSLSGRSLPAWAGWNGA--QIPagLEEAHAYV 820
Cdd:COG3321 316 gdPIEAAALTaafgQGRPadqpcAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPnpHID--FENSPFYV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 821 PTDARPWfRPADGRRVAAVlardddgSS-------AQALLAETPAGIANKAVAPALPLLLPLAAADRDALLAQLAAHIAE 893
Cdd:COG3321 394 NTELRPW-PAGGGPRRAGV-------SSfgfggtnAHVVLEEAPAAAPAAAAAARPPQLLVLSAKTEEALRALAARLAAF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 894 LEKPAAD-------------AAALCRAAVLAHNPqaplalalvaddaagllEEARAALAQLPKAQADWQSPRGsrfspaP 960
Cdd:COG3321 466 LEAHPDLdladvaytlatgrAHFEHRLAVVASSR-----------------EELAAKLRALAAGEAAPGVVTG------A 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 961 LGRDGKVAFVYSALNTAFTGLASRVAQLEPL---AGERLSAAHRDAGATIRSEQLYPrrltplDAEGRMQAEEALLQdnP 1037
Cdd:COG3321 523 AAAAPKVAFLFPGQGSQYVGMGRELYETEPVfraALDECDALLRPHLGWSLREVLFP------DEEESRLDRTEVAQ--P 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1038 ALINAgilsgwQYA-TLLTERVGLEPALQFGHSLGQATMMFASGAWTPGDAwlARLqeldgsltrlsgdkqaVREAWQLA 1116
Cdd:COG3321 595 ALFAV------EYAlARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSLEDA--LRL----------------VAARGRLM 650
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1117 DGQPVDWVNYLVLAPAAGVVEAAKQETRAYVSLINSPDEVTLVGERAACDRILQRLGAEAVPA---PDSLAMHCA---PA 1190
Cdd:COG3321 651 QALPGGGAMLAVGLSEEEVEALLAGYDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRArrlPVSHAFHSPlmePA 730
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1191 ERERAAIAERFTAQlsaQPQGLLFAG--GAPAAwTPEAVAERVAGDLVSPLDFPALVDQAYAQGARLFLELGPGGNCSRW 1268
Cdd:COG3321 731 LEEFRAALAGVTPR---APRIPLISNvtGTWLT-GEALDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPVLTGL 806
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1269 IGKTLRGRPHAT-FALARRDQDDAAMLAKLLALLVAQRVPLDLAAALRVQPEEKKPalLKDLCFCRPPIAATLVEALRKQ 1347
Cdd:COG3321 807 VRQCLAAAGDAVvLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRGRRRVP--LPTYPFQREDAAAALLAAALAA 884
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1348 GLDQALARPSKILTLKPATQDAMTATTQTTQHTLAEQAERHRAELAASHASLASLLAGKPAADPAAAPKQPPLFNEADIM 1427
Cdd:COG3321 885 ALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGAL 964
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1428 EFAEGRVANVLGPKFAEIDRLPRRVRVPGAPFMAVSRVTALSGTYGKLEDSRIRTEYDIPKPAWNAVDGQVSYLSLDAQG 1507
Cdd:COG3321 965 LLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAA 1044
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1508 VLFLVGWLGIDFENRGNRAYRWLDAQLTYLDVMPQAGQCVEYDIHITQSFRNGDATLFKTDFLASVDGRPALKIDHCTAG 1587
Cdd:COG3321 1045 AAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAAL 1124
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1588 FFTYEELSKGAGITDQHRTPRKVAQTAFIPPLAPPRRSLDGADLLAISRGEIAQVLSPAHASGGRNPSLRLPPAAIQFID 1667
Cdd:COG3321 1125 LALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAAL 1204
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1668 RVTSIEPAGGAHGLGGCEAEFQVNPQHWAIRAHFKDDPIFPGPCMMEGAFQLLQAYALSLGLQTAVTGARFQPLPHRPSL 1747
Cdd:COG3321 1205 LAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAA 1284
|
....*....
gi 2666213114 1748 VRFRAQVLP 1756
Cdd:COG3321 1285 LALAAAAAA 1293
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
477-837 |
2.97e-19 |
|
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: 92.62 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 477 RALAAGQPRLRPLPEGRHAGMPFPAPQ----------GAYLDRVAI-DALKLRVPPNDISRMYPQQLLMLSVGDAALGGA 545
Cdd:cd00833 23 ENLLEGRDAISEIPEDRWDADGYYPDPgkpgktytrrGGFLDDVDAfDAAFFGISPREAEAMDPQQRLLLEVAWEALEDA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 546 GVAP----GSRTAVIIASAMDHSGHRLMARWESswrledsldaagfelsdeerrnltqavreslhnpVDAVVMLSYVGSL 621
Cdd:cd00833 103 GYSPeslaGSRTGVFVGASSSDYLELLARDPDE----------------------------------IDAYAATGTSRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 622 LASRIAATWDFSGPALMLTGDETGALRALELGQRLLAEGEADAVLVGAIDLAGAIENLMVRQACGA----DISAPV---- 693
Cdd:cd00833 149 LANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMlspdGRCRPFdada 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 694 -----GEGACALVLEP-ADAVRAqGRAAYAEWRGAG---FGESAQAAAAS-------IR-----AGIgqDAASAGLVESA 752
Cdd:cd00833 229 dgyvrGEGVGVVVLKRlSDALRD-GDRIYAVIRGSAvnqDGRTKGITAPSgeaqaalIRrayarAGV--DPSDIDYVEAH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 753 G----------------PLPAADLLGGRPALSSAAAVFGHTRMTAPLLSVLHAALSLSGRSLPAWAGWNGAQIPAGLEEA 816
Cdd:cd00833 306 GtgtplgdpievealakVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEES 385
|
410 420
....*....|....*....|.
gi 2666213114 817 HAYVPTDARPWFRPADGRRVA 837
Cdd:cd00833 386 PLRVPTEARPWPAPAGPRRAG 406
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
187-437 |
1.05e-17 |
|
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: 87.42 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 187 GLGGPRYAIDAACATSLYAIHLAAMHIASGEAdamlVVAANGFDTLFANFGFAA---TQALPDGT----SNRPFDADSDG 259
Cdd:cd00832 149 GMRGPSGVVVAEQAGGLDALAQARRLVRRGTP----LVVSGGVDSALCPWGWVAqlsSGRLSTSDdparAYLPFDAAAAG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 260 VAPADGAMALVLRRPDSHRS---TVYGTLRGMGLSSDGRGQtltAPNPKGQKLACDRAYEQTGISPDTIAYVECHATGTK 336
Cdd:cd00832 225 YVPGEGGAILVLEDAAAARErgaRVYGEIAGYAATFDPPPG---SGRPPGLARAIRLALADAGLTPEDVDVVFADAAGVP 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 337 LGDRVELETVARVFG-DNQPVGSVKSNVGHLLTAAGIAGLVKTLLAMRHGVIPATVGIEKPlsrDIAGTPDIITqATPWP 415
Cdd:cd00832 302 ELDRAEAAALAAVFGpRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDV---PPAYGLDLVT-GRPRP 377
|
250 260
....*....|....*....|..
gi 2666213114 416 AGHKRAAINAFGFGGVNAHLIV 437
Cdd:cd00832 378 AALRTALVLARGRGGFNSALVV 399
|
|
| PRK05174 |
PRK05174 |
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase; |
1630-1767 |
5.66e-16 |
|
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
Pssm-ID: 179953 Cd Length: 172 Bit Score: 77.56 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1630 DLLAISRGEIAqvlspahasGGRNPSLRLPPaaIQFIDRVTSIEPAGGAHGLGGCEAEFQVNPQHWAIRAHFKDDPIFPG 1709
Cdd:PRK05174 12 DLLACGRGELF---------GPGNAQLPAPP--MLMMDRITEISETGGEFGKGYIVAELDINPDLWFFGCHFIGDPVMPG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1710 pCM-MEGAFQLL-----------QAYALSLGlqtavtgarfqplphrpsLVRFRAQVLPQNQTFTYRADI 1767
Cdd:PRK05174 81 -CLgLDAMWQLVgfylgwlggpgKGRALGVG------------------EVKFTGQVLPTAKKVTYEIDI 131
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
460-706 |
3.04e-15 |
|
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: 77.68 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 460 TGLGAAIGDCPDLNAVARALAAGQPRLRPLPEGRH-----------AGMPFPAPQGAYLDRVAIDALKLRVPPNDISRMY 528
Cdd:pfam00109 6 VGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWdpdklydppsrIAGKIYTKWGGLDDIFDFDPLFFGISPREAERMD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 529 PQQLLMLSVGDAALGGAGVAP----GSRTAVIIASAMDHSGHrlmarwesswrlEDSLDAAGfelsdeerrnltQAVRES 604
Cdd:pfam00109 86 PQQRLLLEAAWEALEDAGITPdsldGSRTGVFIGSGIGDYAA------------LLLLDEDG------------GPRRGS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 605 LHnpvdavvMLSYVGSLLASRIAATWDFSGPALMLTGDETGALRALELGQRLLAEGEADAVLVGAIDLAGAIENLMVRQA 684
Cdd:pfam00109 142 PF-------AVGTMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSA 214
|
250 260 270
....*....|....*....|....*....|....*
gi 2666213114 685 CGAD-------ISAP------VGEGACALVLEPAD 706
Cdd:pfam00109 215 AGMLspdgpckAFDPfadgfvRGEGVGAVVLKRLS 249
|
|
| FabA |
COG0764 |
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ... |
1657-1770 |
1.85e-13 |
|
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and metabolism]; 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440527 Cd Length: 141 Bit Score: 69.45 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1657 RLP-PAAIQFIDRVTSIEPAGGAHglggceAEFQVNPQHWAIRAHFKDDPIFPGPCMMEGAFQLLQAYAL-SLGLQTAVT 1734
Cdd:COG0764 7 LLPhRYPFLLVDRVLEIDPGKSIV------AEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLkSEGLEGKGR 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 2666213114 1735 GARFqplpHRPSLVRFRAQVLPQNQtFTYRADIVEI 1770
Cdd:COG0764 81 LVYF----LGIDKVKFRGPVVPGDT-LTLEVEIKRV 111
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
460-727 |
7.60e-11 |
|
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: 66.41 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 460 TGLGA--AIGDcpDLNAVARALAAGQPRLRPLPEGRHAGmpFPAPQGAYLDRVAIDAlklRVPPNDISRMYPQQLLMLSV 537
Cdd:cd00834 6 TGLGAvtPLGN--GVEEFWEALLAGRSGIRPITRFDASG--FPSRIAGEVPDFDPED---YLDRKELRRMDRFAQFALAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 538 GDAALGGAGVAPGS----RTAVIIASAMdhsghrlmarwesswrledsldaAGFELSDEERRNLTQAVRESlHNPVDAVV 613
Cdd:cd00834 79 AEEALADAGLDPEEldpeRIGVVIGSGI-----------------------GGLATIEEAYRALLEKGPRR-VSPFFVPM 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 614 MLSyvgSLLASRIAATWDFSGPALMLTGDETGALRALELGQRLLAEGEADAVLVGAID-------LAG--AIENLMVRQA 684
Cdd:cd00834 135 ALP---NMAAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEalitpltLAGfaALRALSTRND 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2666213114 685 CGADISAP---------VGEGACALVLEPADAVRAQGRAAYAEwrGAGFGES 727
Cdd:cd00834 212 DPEKASRPfdkdrdgfvLGEGAGVLVLESLEHAKARGAKIYAE--ILGYGAS 261
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
1051-1275 |
3.31e-10 |
|
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 63.22 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1051 ATLLTERvGLEPALQFGHSLGQATMMFASGAWTPGDA-WLARL-----QEL----DGSLTRLSG-DKQAVREawqladgq 1119
Cdd:COG0331 73 YRALEEE-GIRPDAVAGHSLGEYSALVAAGALSFEDAlRLVRLrgrlmQEAvpagPGGMAAVLGlDDEEVEA-------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1120 pvdwvnylvlapaagVVEAAKQETRAYVSLINSPDEVTLVGERAACDRILQRL---GA-EAVPAPDSLAMHC---APAer 1192
Cdd:COG0331 144 ---------------LCAEAAQGEVVEIANYNSPGQIVISGEKEAVEAAAELAkeaGAkRAVPLPVSGPFHTplmAPA-- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1193 eraaiAERFTAQLS----AQPQGLLFAG--GAPaAWTPEAVAERVAGDLVSPLDFPALVDQAYAQGARLFLELGPGGNCS 1266
Cdd:COG0331 207 -----AEKLAEALAavtfADPKIPVVSNvdAAP-VTDPEEIRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLS 280
|
....*....
gi 2666213114 1267 RWIGKTLRG 1275
Cdd:COG0331 281 GLVKRIDPG 289
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
489-853 |
7.59e-10 |
|
"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: 63.23 E-value: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 489 LPEGRHaGMPFPAPQGAYLDRVAIDALKLRVPPNDISRMY----PQQLLMLSVGDAALGGAGVAPG-----SRTAVIIAS 559
Cdd:cd00828 28 LREGRS-GIAPVARLKSRFDRGVAGQIPTGDIPGWDAKRTgivdRTTLLALVATEEALADAGITDPyevhpSEVGVVVGS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 560 AMdhsghrlmarweSSWRLEDsldaaGFELSDEERRNLTQAVR-ESLHNPVDAVVMLSYVGSllasriaatwdfSGPALM 638
Cdd:cd00828 107 GM------------GGLRFLR-----RGGKLDARAVNPYVSPKwMLSPNTVAGWVNILLLSS------------HGPIKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 639 LTGDETGALRALELGQRLLAEGEADAVLVGAIDL--------AGAIENLMVRQACGADISAP---------VGEGACALV 701
Cdd:cd00828 158 PVGACATALEALDLAVEAIRSGKADIVVVGGVEDpleeglsgFANMGALSTAEEEPEEMSRPfdetrdgfvEAEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 702 LEPADAVRAQGRAAYAEWRG-----AGFGESAQAAAASIRAGIGQDAASAGL--------------------VESAGPLP 756
Cdd:cd00828 238 LERAELALARGAPIYGRVAGtasttDGAGRSVPAGGKGIARAIRTALAKAGLslddldvisahgtstpandvAESRAIAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 757 AADLLGGRPALSSAAAVFGHTRMTAPLLSVLHAALSLSGRSLPAWAgwNGAQIPAGLEEAHayVPTDARPWFrpaDGRRV 836
Cdd:cd00828 318 VAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTA--NLDDVDPDVEHLS--VVGLSRDLN---LKVRA 390
|
410
....*....|....*..
gi 2666213114 837 AAVLARDDDGSSAQALL 853
Cdd:cd00828 391 ALVNAFGFGGSNAALVL 407
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
460-727 |
2.03e-09 |
|
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: 61.65 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 460 TGLGA--AIGDcpDLNAVARALAAGQPRLRPLPegRHAGMPFPAPQGAYLDRVAIDALklrVPPNDISRMYPQQLLMLSV 537
Cdd:COG0304 6 TGLGAvsPLGN--GVEEFWEALLAGRSGIRPIT--RFDASGLPVRIAGEVKDFDPEEY---LDRKELRRMDRFTQYALAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 538 GDAALGGAGVAPGS----RTAVIIASAMdhsghrlmarwesswrledsldaAGFELSDEERRNLtqavRESLHNPVDAVV 613
Cdd:COG0304 79 AREALADAGLDLDEvdpdRTGVIIGSGI-----------------------GGLDTLEEAYRAL----LEKGPRRVSPFF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 614 MLSYVGSLLASRIAATWDFSGPALMLTGDETGALRALELGQRLLAEGEADAVLVGAID-------LAG--AIENLMVRQA 684
Cdd:COG0304 132 VPMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEaaitplgLAGfdALGALSTRND 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2666213114 685 CGADISAP---------VGEGACALVLEPADAVRAQGRAAYAEWrgAGFGES 727
Cdd:COG0304 212 DPEKASRPfdkdrdgfvLGEGAGVLVLEELEHAKARGAKIYAEV--VGYGAS 261
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
408-452 |
1.98e-08 |
|
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.
Pssm-ID: 465059 [Multi-domain] Cd Length: 111 Bit Score: 54.09 E-value: 1.98e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2666213114 408 ITQATPWPAGhkRAAINAFGFGGVNAHLIVDG-PGQAAPETAPSRR 452
Cdd:pfam16197 16 VTEPTPWPGG--IVGVNSFGFGGANAHVILKSnPKPKIPPESPDNL 59
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
1034-1262 |
7.95e-06 |
|
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 49.77 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1034 QDNPALINAGILSgwqyATLLTERVGLEPALQFGHSLGQATMMFASGAWTPGDA-WLARLQ---------ELDGSLTRLS 1103
Cdd:TIGR00128 60 YTQPALYVVSAIL----YLKLKEQGGLKPDFAAGHSLGEYSALVAAGALDFETAlKLVKKRgelmqeavpEGGGAMAAVI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1104 G-DKQAVREAWQLADGQPVDWVNYlvlapaagvveaakqetrayvsliNSPDEVTLVGERAACDRI---LQRLGAE-AVP 1178
Cdd:TIGR00128 136 GlDEEQLAQACEEATENDVDLANF------------------------NSPGQVVISGTKDGVEAAaalFKEMGAKrAVP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1179 APDSLAMHCAPAERERAAIAERFTAQLSAQPQGLLFAGGAPAAWT-PEAVAERVAGDLVSPLDFPALVDQAYAQGARLFL 1257
Cdd:TIGR00128 192 LEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDAKPYTnGDRIKEKLSEQLTSPVRWTDSVEKLMARGVTEFA 271
|
....*
gi 2666213114 1258 ELGPG 1262
Cdd:TIGR00128 272 EVGPG 276
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
171-331 |
2.63e-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: 48.41 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 171 SARVSGGITTLTARALGL-GGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAAN--------------------GF 229
Cdd:cd00829 48 GGRFQSFPGALIAEYLGLlGKPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEkmsdvptgdeaggrasdlewEG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 230 DTLFANFGFAATQAL------------------------------PDGTSNRPFDAD--------------SDGVAPADG 265
Cdd:cd00829 128 PEPPGGLTPPALYALaarrymhrygttredlakvavknhrnaarnPYAQFRKPITVEdvlnsrmiadplrlLDCCPVSDG 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2666213114 266 AMALVL----RRPDSHRSTVYgtLRGMGLSSDGRgqTLTAPN----PKGQKLACDRAYEQTGISPDTIAYVECH 331
Cdd:cd00829 208 AAAVVLaseeRARELTDRPVW--ILGVGAASDTP--SLSERDdflsLDAARLAARRAYKMAGITPDDIDVAELY 277
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
620-793 |
2.93e-05 |
|
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: 48.40 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 620 SLLASRIAATWDFSGPALMLTGDETGALRALELGQRLLAEGEADAVLVGAIDLAgAIENLMVRQACGADISAP------- 692
Cdd:cd00825 73 PGASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEEL-AAPMDCEFDAMGALSTPEkasrtfd 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 693 -------VGEGACALVLEPADAVRAQGRAAYAEWRGAGFGESAQAAAASIRAGIGQDAASAGLVESAG------------ 753
Cdd:cd00825 152 aaadgfvFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGltvwdidylvah 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2666213114 754 --PLPAADLL----------GGRPALSSAAAVFGHTRMTAPLLSVLHAALSL 793
Cdd:cd00825 232 gtGTPIGDVKelkllrsefgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLML 283
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
183-379 |
1.01e-04 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 46.66 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 183 ARALGLGG-PRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAANGFDTLFANFGFA-ATQAlpDG------TSNRPFD 254
Cdd:cd00827 92 AELLGLTNaEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDEGSALePTLG--DGaaamlvSRNPGIL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 255 AD--------SDGVAPADGAMALVLRRPDSHRSTVYGTLRGMGLSSDGRGQTLTaPNPKGQKLACDRAYEQTGISpdtiA 326
Cdd:cd00827 170 AAgivsthstSDPGYDFSPYPVMDGGYPKPCKLAYAIRLTAEPAGRAVFEAAHK-LIAKVVRKALDRAGLSEDID----Y 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2666213114 327 YVECHATGTKLGDRVELETVARVFGDNQPVGSVKSNVGHLLTAAGIAGLVKTL 379
Cdd:cd00827 245 FVPHQPNGKKILEAVAKKLGGPPEKASQTRWILLRRVGNMYAASILLGLASLL 297
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
180-331 |
4.29e-04 |
|
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: 44.45 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 180 TLTARALGLGGPrYAID--AACATSLYAIHLAAMHIASGEADAMLVVAAngfDTL-----FAN------FGFAATQAL-- 244
Cdd:cd00830 91 CLVQARLGAKNA-AAFDinAACSGFLYGLSTAAGLIRSGGAKNVLVVGA---ETLsrildWTDrstavlFGDGAGAVVle 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 245 --PDGTSNRPFDADSDGvapaDGAMALVLRRPDSHRSTVYGTLRGMGLSSDGRG------QTLTApnpkgqklACDRAYE 316
Cdd:cd00830 167 atEEDPGILDSVLGSDG----SGADLLTIPAGGSRSPFEDAEGGDPYLVMDGREvfkfavRLMPE--------SIEEALE 234
|
170
....*....|....*
gi 2666213114 317 QTGISPDTIAYVECH 331
Cdd:cd00830 235 KAGLTPDDIDWFVPH 249
|
|
| FabZ |
cd01288 |
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ... |
1663-1756 |
5.72e-04 |
|
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily catalyzes the dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP, the third step in the elongation phase of the bacterial/ plastid, type II, fatty-acid biosynthesis pathway.
Pssm-ID: 238615 Cd Length: 131 Bit Score: 41.76 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 1663 IQFIDRVTSIEPAGGAHglggceAEFQVNPQHWAIRAHFKDDPIFPGPCMMEGAFQLLQAYALSLglqtavtgarfqPLP 1742
Cdd:cd01288 7 FLLVDRVLELEPGKSIV------AIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKS------------LED 68
|
90 100
....*....|....*....|..
gi 2666213114 1743 HRPSL--------VRFRAQVLP 1756
Cdd:cd01288 69 FEGKLvyfagidkARFRKPVVP 90
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
475-842 |
1.68e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 43.47 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 475 VARALAAGQPRLRPLPEGRHAGMPFPAPQGAYLDRVAIDAlkLRVPPNDISRMYPQQLLMLSVGDAALGGAGVAPGSRTA 554
Cdd:COG3903 568 LERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAA--AAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAA 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 555 VIIASAMDHSGHRLMARWESSWRLEDSLDAAGFELSDEERRNLTQAVRESLHNPVDAVVMLSYVGSLLASRIAATWDFSG 634
Cdd:COG3903 646 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAA 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 635 PALMLTGDETGALRALELGQRLLAEGEADAVLVGAIDLAGAIENLMVRQACGADISAPVGEGACALVLEPADAVRAQGRA 714
Cdd:COG3903 726 ALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAA 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 715 AYAEWRGAGFGESAQAAAASIRAGIGQDAASAGLVESAGPLPAADLLGGRPALSSAAAVFGHTRMTAPLLSVLHAALSLS 794
Cdd:COG3903 806 AAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALL 885
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2666213114 795 GRSLPAWAGWNGAQIPAGLEEAHAYVPTDARPWFRPADGRRVAAVLAR 842
Cdd:COG3903 886 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
183-331 |
2.97e-03 |
|
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: 42.02 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 183 ARALGL-GGPRYAIDAACATSLYAIHLAAMHIASGEADAMLVVAAngfDTL--FAN---------FGFAAT----QALPD 246
Cdd:COG0332 95 QHKLGAkNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGA---ETLsrIVDwtdrstcvlFGDGAGavvlEASEE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 247 GTSNRPFDADSDGvapaDGAMALVLRRPDSHRSTVYGTLRGMGLSSDGRG------QTLTApnpkgqklACDRAYEQTGI 320
Cdd:COG0332 172 GPGILGSVLGSDG----SGADLLVVPAGGSRNPPSPVDEGDHYLRMDGREvfkfavRNLPE--------VIREALEKAGL 239
|
170
....*....|.
gi 2666213114 321 SPDTIAYVECH 331
Cdd:COG0332 240 TLDDIDWFIPH 250
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
195-294 |
6.96e-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: 37.11 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 195 IDAACATSLYAIHLAAMHIASGEADAMLVVAAngfDTL--FANFgfaatqalpdgtSNRpfdadSDGVAPADGAMALVLR 272
Cdd:pfam08545 3 INAACSGFVYALSTAAALIRSGRAKNVLVIGA---ETLskILDW------------TDR-----STAVLFGDGAGAVVLE 62
|
90 100
....*....|....*....|..
gi 2666213114 273 RPDSHRSTVYGTLrgmgLSSDG 294
Cdd:pfam08545 63 ATDEPGARILDSV----LGSDG 80
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
183-225 |
7.40e-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: 7.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2666213114 183 AR--ALGLGGPR----YAIDAACATSLYAIHLAAMHIASGEADamLVVA 225
Cdd:COG0183 66 ARqaALLAGLPEsvpaVTVNRVCGSGLQAVALAAQAIAAGDAD--VVIA 112
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
616-721 |
7.97e-03 |
|
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: 40.12 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2666213114 616 SYVGSLLASRIAATWDFS-GPALMLTGDETGALRALELGQRLLAEGEADAVLVGAIDlagaienlmvrqacgadiSAPVG 694
Cdd:cd00327 40 SGEFSGAAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSE------------------EFVFG 101
|
90 100
....*....|....*....|....*..
gi 2666213114 695 EGACALVLEPADAVRAQGRAAYAEWRG 721
Cdd:cd00327 102 DGAAAAVVESEEHALRRGAHPQAEIVS 128
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
163-223 |
8.69e-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: 40.54 E-value: 8.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2666213114 163 LQSGTHPESARVSggittltARALGLGG--PRYAIDAACATSLYAIHLAAMHIASGEADAMLV 223
Cdd:cd00751 53 LQAGEGQNPARQA-------ALLAGLPEsvPATTVNRVCGSGLQAVALAAQSIAAGEADVVVA 108
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