|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
16-398 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 659.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 16 AMGVVVTGLALDTALGDQLQTWTKLLQGKTAIKPKQPFINLPSFPLALQGNYPRSLGQLVPPLVQAAIDDAQLDPAEQPW 95
Cdd:PRK05952 1 MMKVVVTGIGLVSALGDLEQSWQRLLQGKSGIKLHQPFPELPPLPLGLIGNQPSSLEDLTKTVVTAALKDAGLTPPLTDC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 96 GVAIGSSRANQCHWEDWVGRNIKPPVAPNF--KLVDWWQTLPDQAARLAAQLLPEVTVMQCPMAACATGLWAIAQGVELI 173
Cdd:PRK05952 81 GVVIGSSRGCQGQWEKLARQMYQGDDSPDEelDLENWLDTLPHQAAIAAARQIGTQGPVLAPMAACATGLWAIAQGVELI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 174 RTGHCQRVLAGAVEAPITPLTLAGFSKMATLAPDGCYPFDRQRQGLVLGEGGALLVLETRELAQKRKARIYGEILGWGFS 253
Cdd:PRK05952 161 QTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTGAYPFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 254 CDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQTLFPQNPLITSSKGATGHTLGASG 333
Cdd:PRK05952 241 CDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALFPHRVAVSSTKGATGHTLGASG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499175128 334 AIAVALTLLSLHQQKLPPCVGLKEPEFPLNFVRiesvQPATSPLNYGLCLSFGFGGQNGAIAVGH 398
Cdd:PRK05952 321 ALGVAFSLLALRHQQLPPCVGLQEPEFDLNFVR----QAQQSPLQNVLCLSFGFGGQNAAIALGK 381
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
19-396 |
9.87e-129 |
|
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: 376.49 E-value: 9.87e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQ-TWTKLLQGKTAIKPKQPFiNLPSFPLALQGNYP-RSLGQLVPP-------------LVQA-- 81
Cdd:cd00834 3 VVITGLGAVTPLGNGVEeFWEALLAGRSGIRPITRF-DASGFPSRIAGEVPdFDPEDYLDRkelrrmdrfaqfaLAAAee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 82 AIDDAQLDPAEQP---WGVAIGSSRANQCHWEDWVGR---NIKPPVAPNFKlvdwWQTLPDQAARLAAQLLPEVTVMQCP 155
Cdd:cd00834 82 ALADAGLDPEELDperIGVVIGSGIGGLATIEEAYRAlleKGPRRVSPFFV----PMALPNMAAGQVAIRLGLRGPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 156 MAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLAPD------GCYPFDRQRQGLVLGEGGALLV 229
Cdd:cd00834 158 STACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRnddpekASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 230 LETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQ 309
Cdd:cd00834 238 LESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 310 TLFPQ---NPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEP--EFPLNFVRIESVQpatSPLNYGLCLS 384
Cdd:cd00834 318 RVFGEhakKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPdpECDLDYVPNEARE---APIRYALSNS 394
|
410
....*....|..
gi 499175128 385 FGFGGQNGAIAV 396
Cdd:cd00834 395 FGFGGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
19-397 |
1.91e-99 |
|
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: 301.63 E-value: 1.91e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQ-TWTKLLQGKTAIKPKQPF--INLPSFPLA------LQGNYPRSLGQLVPPLVQA-------A 82
Cdd:COG0304 3 VVITGLGAVSPLGNGVEeFWEALLAGRSGIRPITRFdaSGLPVRIAGevkdfdPEEYLDRKELRRMDRFTQYalaaareA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 83 IDDAQLDPAEQP---WGVAIGSSRANQCHWED----WVGRNIKPpVAPNFKLvdwwQTLPDQAARLAAQLL----PEVTV 151
Cdd:COG0304 83 LADAGLDLDEVDpdrTGVIIGSGIGGLDTLEEayraLLEKGPRR-VSPFFVP----MMMPNMAAGHVSIRFglkgPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 152 MqcpmAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLA------PDGCYPFDRQRQGLVLGEGG 225
Cdd:COG0304 158 S----TACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALStrnddpEKASRPFDKDRDGFVLGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 226 ALLVLETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREA 305
Cdd:COG0304 234 GVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 306 ALIQTLF---PQNPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKE--PEFPLNFVRIESVQPatsPLNYG 380
Cdd:COG0304 314 KAIKRVFgdhAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENpdPECDLDYVPNEAREA---KIDYA 390
|
410
....*....|....*..
gi 499175128 381 LCLSFGFGGQNGAIAVG 397
Cdd:COG0304 391 LSNSFGFGGHNASLVFK 407
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
244-356 |
7.21e-33 |
|
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: 119.60 E-value: 7.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 244 YGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQTLFPQNP-----LI 318
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArkqplAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 499175128 319 TSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLK 356
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
158-391 |
2.88e-22 |
|
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: 95.86 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 158 ACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLAPDG-CYPFDRQRQGLVLGEGGALLVLETRELA 236
Cdd:smart00825 96 ACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGrCKTFDASADGYVRGEGVGVVVLKRLSDA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 237 QKRKARIYGEILGWGFSCDAlhRStpafdnhsaqqavkhcltrSGLTpeqidliHPHGTGTLfndqreaaliqtlfpqnp 316
Cdd:smart00825 176 LRDGDPILAVIRGSAVNQDG--RS-------------------NGIT-------APSGPAQL------------------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 317 LITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEPEFPLNF----VRI--ESVQ-PATSPLNYGLCLSFGFGG 389
Cdd:smart00825 210 LIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLeespLRVptELTPwPPPGRPRRAGVSSFGFGG 289
|
..
gi 499175128 390 QN 391
Cdd:smart00825 290 TN 291
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
152-391 |
1.40e-19 |
|
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: 91.61 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 152 MQCPM-AACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKM-ATLAPDGCYPFDRQRQGLVLGEGGALLV 229
Cdd:TIGR02813 198 MNCVVdAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTpAFTTNEDIQPFDIDSKGMMIGEGIGMMA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 230 LETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQ 309
Cdd:TIGR02813 278 LKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLV 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 310 TLFPQNP------LITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEPEFPLN-----FVRIESVQP-----A 373
Cdd:TIGR02813 358 SVFSQDNdqkqhiALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDienspFYLNTETRPwmqreD 437
|
250
....*....|....*...
gi 499175128 374 TSPLNYGLClSFGFGGQN 391
Cdd:TIGR02813 438 GTPRRAGIS-SFGFGGTN 454
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
16-398 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 659.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 16 AMGVVVTGLALDTALGDQLQTWTKLLQGKTAIKPKQPFINLPSFPLALQGNYPRSLGQLVPPLVQAAIDDAQLDPAEQPW 95
Cdd:PRK05952 1 MMKVVVTGIGLVSALGDLEQSWQRLLQGKSGIKLHQPFPELPPLPLGLIGNQPSSLEDLTKTVVTAALKDAGLTPPLTDC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 96 GVAIGSSRANQCHWEDWVGRNIKPPVAPNF--KLVDWWQTLPDQAARLAAQLLPEVTVMQCPMAACATGLWAIAQGVELI 173
Cdd:PRK05952 81 GVVIGSSRGCQGQWEKLARQMYQGDDSPDEelDLENWLDTLPHQAAIAAARQIGTQGPVLAPMAACATGLWAIAQGVELI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 174 RTGHCQRVLAGAVEAPITPLTLAGFSKMATLAPDGCYPFDRQRQGLVLGEGGALLVLETRELAQKRKARIYGEILGWGFS 253
Cdd:PRK05952 161 QTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTGAYPFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 254 CDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQTLFPQNPLITSSKGATGHTLGASG 333
Cdd:PRK05952 241 CDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALFPHRVAVSSTKGATGHTLGASG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499175128 334 AIAVALTLLSLHQQKLPPCVGLKEPEFPLNFVRiesvQPATSPLNYGLCLSFGFGGQNGAIAVGH 398
Cdd:PRK05952 321 ALGVAFSLLALRHQQLPPCVGLQEPEFDLNFVR----QAQQSPLQNVLCLSFGFGGQNAAIALGK 381
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
19-396 |
9.87e-129 |
|
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: 376.49 E-value: 9.87e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQ-TWTKLLQGKTAIKPKQPFiNLPSFPLALQGNYP-RSLGQLVPP-------------LVQA-- 81
Cdd:cd00834 3 VVITGLGAVTPLGNGVEeFWEALLAGRSGIRPITRF-DASGFPSRIAGEVPdFDPEDYLDRkelrrmdrfaqfaLAAAee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 82 AIDDAQLDPAEQP---WGVAIGSSRANQCHWEDWVGR---NIKPPVAPNFKlvdwWQTLPDQAARLAAQLLPEVTVMQCP 155
Cdd:cd00834 82 ALADAGLDPEELDperIGVVIGSGIGGLATIEEAYRAlleKGPRRVSPFFV----PMALPNMAAGQVAIRLGLRGPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 156 MAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLAPD------GCYPFDRQRQGLVLGEGGALLV 229
Cdd:cd00834 158 STACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRnddpekASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 230 LETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQ 309
Cdd:cd00834 238 LESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 310 TLFPQ---NPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEP--EFPLNFVRIESVQpatSPLNYGLCLS 384
Cdd:cd00834 318 RVFGEhakKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPdpECDLDYVPNEARE---APIRYALSNS 394
|
410
....*....|..
gi 499175128 385 FGFGGQNGAIAV 396
Cdd:cd00834 395 FGFGGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
19-397 |
1.91e-99 |
|
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: 301.63 E-value: 1.91e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQ-TWTKLLQGKTAIKPKQPF--INLPSFPLA------LQGNYPRSLGQLVPPLVQA-------A 82
Cdd:COG0304 3 VVITGLGAVSPLGNGVEeFWEALLAGRSGIRPITRFdaSGLPVRIAGevkdfdPEEYLDRKELRRMDRFTQYalaaareA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 83 IDDAQLDPAEQP---WGVAIGSSRANQCHWED----WVGRNIKPpVAPNFKLvdwwQTLPDQAARLAAQLL----PEVTV 151
Cdd:COG0304 83 LADAGLDLDEVDpdrTGVIIGSGIGGLDTLEEayraLLEKGPRR-VSPFFVP----MMMPNMAAGHVSIRFglkgPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 152 MqcpmAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLA------PDGCYPFDRQRQGLVLGEGG 225
Cdd:COG0304 158 S----TACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALStrnddpEKASRPFDKDRDGFVLGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 226 ALLVLETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREA 305
Cdd:COG0304 234 GVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 306 ALIQTLF---PQNPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKE--PEFPLNFVRIESVQPatsPLNYG 380
Cdd:COG0304 314 KAIKRVFgdhAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENpdPECDLDYVPNEAREA---KIDYA 390
|
410
....*....|....*..
gi 499175128 381 LCLSFGFGGQNGAIAVG 397
Cdd:COG0304 391 LSNSFGFGGHNASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
19-397 |
1.98e-73 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 235.07 E-value: 1.98e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQ-TWTKLLQGKTAIKPKQPFIN----------LPSFPLAlqgnyprslgQLVPPL--------- 78
Cdd:PRK07314 4 VVVTGLGAVSPLGNDVEsTWKNLLAGKSGIGPITHFDTsdlavkiageVKDFNPD----------DYMSRKearrmdrfi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 79 ---VQA---AIDDAQLDPAEQP---WGVAIGSSranqchwedwVG-----------------RNIKPPVAPnfklvdwwQ 132
Cdd:PRK07314 74 qygIAAakqAVEDAGLEITEENadrIGVIIGSG----------IGgletieeqhitllekgpRRVSPFFVP--------M 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 133 TLPDQAARLAAQLLPEVTVMQCPMAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLA-----PD 207
Cdd:PRK07314 136 AIINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALStrnddPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 208 G-CYPFDRQRQGLVLGEGGALLVLETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQ 286
Cdd:PRK07314 216 RaSRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPED 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 287 IDLIHPHGTGTLFNDQREAALIQTLF---PQNPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEP--EFP 361
Cdd:PRK07314 296 IDYINAHGTSTPAGDKAETQAIKRVFgehAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPdeECD 375
|
410 420 430
....*....|....*....|....*....|....*.
gi 499175128 362 LNFVRIESVQpatSPLNYGLCLSFGFGGQNGAIAVG 397
Cdd:PRK07314 376 LDYVPNEARE---RKIDYALSNSFGFGGTNASLVFK 408
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
20-398 |
1.90e-67 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 219.95 E-value: 1.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 20 VVTGLALDTAlgdqlQTWTKLLQGKTAIKP-------KQPFINLPSFPLALQGNYPRSLGQLVPPL-------------- 78
Cdd:PTZ00050 1 VVTPLGVGAE-----STWEALIAGKSGIRKltefpkfLPDCIPEQKALENLVAAMPCQIAAEVDQSefdpsdfaptkres 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 79 ---------VQAAIDDAQLDPAEQ----PWGVAIGSSRANQchwEDwVGRNIKPPVAPNFKLVDWWqTLPDQAARLAAQL 145
Cdd:PTZ00050 76 rathfamaaAREALADAKLDILSEkdqeRIGVNIGSGIGSL---AD-LTDEMKTLYEKGHSRVSPY-FIPKILGNMAAGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 146 LPEVTVMQCPM----AACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLA------PD-GCYPFDR 214
Cdd:PTZ00050 151 VAIKHKLKGPSgsavTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtkynddPQrASRPFDK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 215 QRQGLVLGEGGALLVLETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTP-EQIDLIHPH 293
Cdd:PTZ00050 231 DRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINiNDVDYVNAH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 294 GTGTLFNDQREAALIQTLF----PQNPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEPEFP--LNFVRI 367
Cdd:PTZ00050 311 ATSTPIGDKIELKAIKKVFgdsgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAEcdLNLVQG 390
|
410 420 430
....*....|....*....|....*....|.
gi 499175128 368 ESVQPATSpLNYGLCLSFGFGGQNGAIAVGH 398
Cdd:PTZ00050 391 KTAHPLQS-IDAVLSTSFGFGGVNTALLFTK 420
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
19-394 |
3.20e-60 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 200.99 E-value: 3.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQT-WTKLLQGKTAIKPkqpfinLPSFPLalqGNYPRSLGQLVPPLVQA---------------- 81
Cdd:PRK06333 6 IVVTGMGAVSPLGCGVETfWQRLLAGQSGIRT------LTDFPV---GDLATKIGGQVPDLAEDaeagfdpdryldpkdq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 82 ----------------AIDDAQLDPAEQP----WGVAIGS------SRANQCHWEDWVG-RNIKPPVAPNFklvdwwqtL 134
Cdd:PRK06333 77 rkmdrfilfamaaakeALAQAGWDPDTLEdrerTATIIGSgvggfpAIAEAVRTLDSRGpRRLSPFTIPSF--------L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 135 PDQAARLAAQLLPEVTVMQCPMAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATL------APD- 207
Cdd:PRK06333 149 TNMAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALstrfndAPEq 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 208 GCYPFDRQRQGLVLGEGGALLVLETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQI 287
Cdd:PRK06333 229 ASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 288 DLIHPHGTGTLFNDQREAALIQTLF--PQNPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEPEFPLNFV 365
Cdd:PRK06333 309 QHLNAHATSTPVGDLGEVAAIKKVFghVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGL 388
|
410 420
....*....|....*....|....*....
gi 499175128 366 RIESVQPATSPLNYGLCLSFGFGGQNGAI 394
Cdd:PRK06333 389 DVVANKARPMDMDYALSNGFGFGGVNASI 417
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
19-399 |
7.03e-57 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 192.25 E-value: 7.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTAL-GDQLQTWTKLLQGKTAIKPKQ-PFINLPSFPLALQGNYPRSLgqlvpplvqaaidDAQLDPAE---- 92
Cdd:PRK07910 14 VVVTGIAMTTALaTDAETTWKLLLDGQSGIRTLDdPFVEEFDLPVRIGGHLLEEF-------------DHQLTRVElrrm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 93 ------------QPW-----------------GVAIGSSRANQCHWEDWVGRNIK--PPVAPNfklvdwwQTLPD-QAAR 140
Cdd:PRK07910 81 sylqrmstvlgrRVWenagspevdtnrlmvsiGTGLGSAEELVFAYDDMRARGLRavSPLAVQ-------MYMPNgPAAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 141 LAAQLLPEVTVMQcPMAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLA------PDG-CYPFD 213
Cdd:PRK07910 154 VGLERHAKAGVIT-PVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMstnnddPAGaCRPFD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 214 RQRQGLVLGEGGALLVLETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPH 293
Cdd:PRK07910 233 KDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 294 GTGTLFNDQREAALIQ-TLFPQNPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLK--EPEFPLNFVrieSV 370
Cdd:PRK07910 313 ATGTSVGDVAEGKAINnALGGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLEnlDPEIDLDVV---AG 389
|
410 420
....*....|....*....|....*....
gi 499175128 371 QPATSPLNYGLCLSFGFGGQNGAIAVGHA 399
Cdd:PRK07910 390 EPRPGNYRYAINNSFGFGGHNVALAFGRY 418
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
19-400 |
8.91e-55 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 186.92 E-value: 8.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQ-TWTKLLQGKTAIKPKQP----------------FINLPS--------------FPLALQGNY 67
Cdd:PLN02836 8 VVVTGLGLVTPLGCGVEtTWRRLIAGECGVRALTQddlkmksedeetqlytLDQLPSrvaalvprgtgpgdFDEELWLNS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 68 PRSLGQLVPPLVQA--AIDDAQLDPAEQP----WGVAIGS--------SRANQ--CHWEdwvGRNIKPPVAPnfklvdww 131
Cdd:PLN02836 88 RSSSRFIGYALCAAdeALSDARWLPSEDEakerTGVSIGGgigsitdiLEAAQliCEKR---LRRLSPFFVP-------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 132 QTLPDQAA-----RLAAQLlPEvtvmQCPMAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATL-- 204
Cdd:PLN02836 157 RILINMAAghvsiRYGFQG-PN----HAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALst 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 205 ----AP-DGCYPFDRQRQGLVLGEGGALLVLETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTR 279
Cdd:PLN02836 232 kfnsCPtEASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 280 SGLTPEQIDLIHPHGTGTLFNDQREAALIQTLF-----PQNPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVG 354
Cdd:PLN02836 312 SGLHPNQVDYVNAHATSTPLGDAVEARAIKTVFsehatSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLN 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 499175128 355 LKEPE--FPLNFVRIesVQPATSPLNYGLCLSFGFGGQNGAIAVGHAP 400
Cdd:PLN02836 392 LERPDpiFDDGFVPL--TASKAMLIRAALSNSFGFGGTNASLLFTSPP 437
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
158-394 |
1.64e-51 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 177.62 E-value: 1.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 158 ACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLAP------DGCYPFDRQRQGLVLGEGGALLVLE 231
Cdd:PRK08439 161 ACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrnddpkKASRPFDKDRDGFVMGEGAGALVLE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 232 TRELAQKRKARIYGEILGWGFSCDALHRSTPAFDnhSAQQAVKHCLTRSGLTPeqIDLIHPHGTGTLFNDQREAALIQTL 311
Cdd:PRK08439 241 EYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNETAALKEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 312 FPQN---PLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGL--KEPEFPLNFVriesvqPAT---SPLNYGLCL 383
Cdd:PRK08439 317 FGSKekvPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQetPDPECDLDYI------PNVarkAELNVVMSN 390
|
250
....*....|.
gi 499175128 384 SFGFGGQNGAI 394
Cdd:PRK08439 391 SFGFGGTNGVV 401
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
19-396 |
7.34e-49 |
|
"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: 170.70 E-value: 7.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQT----WTKLLQGKTAIKPKQPFinLPSFPLALQGNYP---------RSLGQLVPPL------V 79
Cdd:cd00828 3 VVITGIGVVSPHGEGCDEveefWEALREGRSGIAPVARL--KSRFDRGVAGQIPtgdipgwdaKRTGIVDRTTllalvaT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 80 QAAIDDAQLDPAEQ----PWGVAIGSSRANqchWEDWVGRNIKPPVAPNFKLVDWWQTLPDQ-AARLAAQLLPEVTVMQC 154
Cdd:cd00828 81 EEALADAGITDPYEvhpsEVGVVVGSGMGG---LRFLRRGGKLDARAVNPYVSPKWMLSPNTvAGWVNILLLSSHGPIKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 155 PMAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPItPLTLAGFSKMATLA-----PDGCY-PFDRQRQGLVLGEGGALL 228
Cdd:cd00828 158 PVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL-EEGLSGFANMGALStaeeePEEMSrPFDETRDGFVEAEGAGVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 229 VLETRELAQKRKARIYGEILGWGFSCDALHRSTPAF--DNHSAQQAVkhcLTRSGLTPEQIDLIHPHGTGTLFNDQREAA 306
Cdd:cd00828 237 VLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGgkGIARAIRTA---LAKAGLSLDDLDVISAHGTSTPANDVAESR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 307 LIQTLFP---QNPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKE--PEFPLNFVRIESvQPATSPLNYGL 381
Cdd:cd00828 314 AIAEVAGalgAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDvdPDVEHLSVVGLS-RDLNLKVRAAL 392
|
410
....*....|....*
gi 499175128 382 CLSFGFGGQNGAIAV 396
Cdd:cd00828 393 VNAFGFGGSNAALVL 407
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
19-398 |
1.40e-46 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 164.82 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQTWTK-LLQGKTAIKP-KQPFINLPSFPLALQG--NYPRSLGQLVPPL-------------VQA 81
Cdd:PRK07103 4 VVVTGVGVVSAIGQGRPSFAAaLLAGRHAFGVmRRPGRQVPDDAGAGLAsaFIGAELDSLALPErldakllrraslsAQA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 82 AI-------DDAQLDPAeQPWGVAI---GSS---RANQCHWEDWVGRnikPP-VAPNFKLvDWWQTlpDQAARLAAQLlp 147
Cdd:PRK07103 84 ALaaareawRDAALGPV-DPDRIGLvvgGSNlqqREQALVHETYRDR---PAfLRPSYGL-SFMDT--DLVGLCSEQF-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 148 EVTVMQCPM-AACATGLWAIAQGVELIRTGHCQRVLA-GAVeAPITPLTLAGFSKMATLAPD--------GCYPFDRQRQ 217
Cdd:PRK07103 155 GIRGEGFTVgGASASGQLAVIQAARLVQSGSVDACIAvGAL-MDLSYWECQALRSLGAMGSDrfadepeaACRPFDQDRD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 218 GLVLGEGGALLVLETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSaqQAVKHCLTRSGLTPEQIDLIHPHGTGT 297
Cdd:PRK07103 234 GFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEM--RVIRAALRRAGLGPEDIDYVNPHGTGS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 298 LFNDQREAALIQTLFPQNPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEPEFP-LNFVRiESVQPATsp 376
Cdd:PRK07103 312 PLGDETELAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPIDErFRWVG-STAESAR-- 388
|
410 420
....*....|....*....|..
gi 499175128 377 LNYGLCLSFGFGGQNGAIAVGH 398
Cdd:PRK07103 389 IRYALSLSFGFGGINTALVLER 410
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
157-391 |
2.50e-46 |
|
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: 164.27 E-value: 2.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 157 AACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLAPDG-CYPFDRQRQGLVLGEGGALLVLETREL 235
Cdd:cd00833 168 TACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGrCRPFDADADGYVRGEGVGVVVLKRLSD 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 236 AQKRKARIYGEILGWGFSCD--ALHRSTPafdNHSAQQAV-KHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQTLF 312
Cdd:cd00833 248 ALRDGDRIYAVIRGSAVNQDgrTKGITAP---SGEAQAALiRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKVF 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 313 PQNP------LITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEP-------EFPLNFVRieSVQP---ATSP 376
Cdd:cd00833 325 GGSRsadqplLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPnpkidfeESPLRVPT--EARPwpaPAGP 402
|
250
....*....|....*
gi 499175128 377 LNYGLClSFGFGGQN 391
Cdd:cd00833 403 RRAGVS-SFGFGGTN 416
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
158-394 |
3.09e-46 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 164.02 E-value: 3.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 158 ACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLAPD------GCYPFDRQRQGLVLGEGGALLVLE 231
Cdd:PRK08722 163 ACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRndepqkASRPWDKDRDGFVLGDGAGMMVLE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 232 TRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQ-- 309
Cdd:PRK08722 243 EYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKra 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 310 --TLFPQNPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEPEFPLNFVRIESVQPATSPLNYGLCLSFGF 387
Cdd:PRK08722 323 lgEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVESMEYAICNSFGF 402
|
....*..
gi 499175128 388 GGQNGAI 394
Cdd:PRK08722 403 GGTNGSL 409
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
158-400 |
8.08e-46 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 162.32 E-value: 8.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 158 ACATGLWAIAQGVELIRTGHCQRVLAGAVEApITPLTLAGFSKMATLAPDGCYPFDRQRQGLVLGEGGALLVLEtRELAq 237
Cdd:PRK09185 159 ACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLSPQPCRPFSANRDGINIGEAAAFFLLE-REDD- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 238 krkariyGEI--LGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQTLFPQN 315
Cdd:PRK09185 236 -------AAValLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVFGDG 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 316 PLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKE--PEFPLNFVRiesVQPATSPLNYGLCLSFGFGGQNGA 393
Cdd:PRK09185 309 VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQpdPALPPLYLV---ENAQALAIRYVLSNSFAFGGNNCS 385
|
....*..
gi 499175128 394 IAVGHAP 400
Cdd:PRK09185 386 LIFGRAD 392
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
19-400 |
1.29e-44 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 159.80 E-value: 1.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQ-TWTKLLQGKTAIKP--KQP-------------FINLP-------SFPLAL------------ 63
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKAdNWAALTAGESGIHTitRFPteglrtriagtvdFLPESpfgasalSEALARlaaeealaqagi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 64 -QGNYPRSLGQLVPPL-----VQAAIDDAQLDPAEQPWGVAIGSSRANQchWEDWVGRNIKPPVAPNFklvdwwqtlpdq 137
Cdd:PRK06501 93 gKGDFPGPLFLAAPPVelewpARFALAAAVGDNDAPSYDRLLRAARGGR--FDALHERFQFGSIADRL------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 138 AARLAAQLLPeVTVMqcpmAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATL-----APDGCY-P 211
Cdd:PRK06501 159 ADRFGTRGLP-ISLS----TACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALstqndPPEKASkP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 212 FDRQRQGLVLGEGGALLVLETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIH 291
Cdd:PRK06501 234 FSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYIN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 292 PHGTGTLFNDQREAALIQTLF----PQNPlITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVG--LKEPEFPLNFV 365
Cdd:PRK06501 314 AHGTSTPENDKMEYLGLSAVFgerlASIP-VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINydNPDPAIPLDVV 392
|
410 420 430
....*....|....*....|....*....|....*...
gi 499175128 366 riesvqPATS---PLNYGLCLSFGFGGQNGAIAVGHAP 400
Cdd:PRK06501 393 ------PNVArdaRVTAVLSNSFGFGGQNASLVLTAEP 424
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
155-394 |
1.41e-44 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 157.58 E-value: 1.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 155 PMAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLA------PD-GCYPFDRQRQGLVLGEGGAL 227
Cdd:PRK14691 87 PVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSthfnstPEkASRPFDTARDGFVMGEGAGL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 228 LVLETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAAL 307
Cdd:PRK14691 167 LIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 308 IQTLFPQ-NPL-ITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEPEFPLNFVRIESVQPATSPLNYGLCLSF 385
Cdd:PRK14691 247 IKHLFGEsNALaITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGNAQPHDMTYALSNGF 326
|
....*....
gi 499175128 386 GFGGQNGAI 394
Cdd:PRK14691 327 GFAGVNASI 335
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
19-391 |
5.97e-42 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 152.06 E-value: 5.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQTW-TKLLQGKTAIK--PK-QPFINL------PSFPLALQGNYPR----SLGQLVPPLVQA--- 81
Cdd:PRK09116 4 VVVTGMGGVTALGEDWQTIaARLKAGRNAVRrmPEwDRYDGLntrlaaPIDDFELPAHYTRkkirSMGRVSLMATRAsel 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 82 AIDDAQL--DPA--EQPWGVAIGSS-------RAnqchwedwVGRNIKPPVAPNFKLVDWWQTLPDQAA-------RLAA 143
Cdd:PRK09116 84 ALEDAGLlgDPIltDGRMGIAYGSStgstdpiGA--------FGTMLLEGSMSGITATTYVRMMPHTTAvnvglffGLKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 144 QLLPEVTvmqcpmaACATGLWAIAQGVELIRTGHCQRVLAGAVEApITPLTLAGFSKM-AT--------LAPDgcyPFDR 214
Cdd:PRK09116 156 RVIPTSS-------ACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLfATstrndapeLTPR---PFDA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 215 QRQGLVLGEGGALLVLETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDnhSAQQAVKHCLTRSGLTPEQIDLIHPHG 294
Cdd:PRK09116 225 NRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAE--TMQIAMELALKDAGLAPEDIGYVNAHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 295 TGTLFNDQREAALIQTLFPQNPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEPE---FPLNFVRIESVQ 371
Cdd:PRK09116 303 TATDRGDIAESQATAAVFGARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDpacGALDYIMGEARE 382
|
410 420
....*....|....*....|
gi 499175128 372 PATsplNYGLCLSFGFGGQN 391
Cdd:PRK09116 383 IDT---EYVMSNNFAFGGIN 399
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
19-394 |
1.51e-37 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 142.81 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQT-WTKLLQGKTAIKPKQPFiNLPSFPLALQG-------------NYPRSLGQLVPPLVQA--- 81
Cdd:PLN02787 131 VVVTGMGVVSPLGHDPDVfYNNLLEGVSGISEIERF-DCSQFPTRIAGeiksfstdgwvapKLSKRMDKFMLYLLTAgkk 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 82 AIDDA--------QLDPAEqpWGVAIGSSRANQCHWEDWVG------RNIKPPVAPnfklvdwWQTLPDQAARLAAQLL- 146
Cdd:PLN02787 210 ALADGgitedvmkELDKTK--CGVLIGSAMGGMKVFNDAIEalrisyRKMNPFCVP-------FATTNMGSAMLAMDLGw 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 147 --PEVTVMqcpmAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLA------PDGCYPFDRQRQG 218
Cdd:PLN02787 281 mgPNYSIS----TACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSqrnddpTKASRPWDMNRDG 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 219 LVLGEGGALLVLETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTL 298
Cdd:PLN02787 357 FVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTK 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 299 FNDQREAALIQTLFPQNP--LITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEPEFPLNFVRIESVQPATSP 376
Cdd:PLN02787 437 AGDLKEYQALMRCFGQNPelRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLD 516
|
410
....*....|....*...
gi 499175128 377 LNYGLCLSFGFGGQNGAI 394
Cdd:PLN02787 517 IKVALSNSFGFGGHNSSI 534
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
157-396 |
4.73e-33 |
|
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: 126.60 E-value: 4.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 157 AACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLAPDG-CYPFDRQRQGLVLGEGGALLVLETREL 235
Cdd:cd00825 94 AACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKaSRTFDAAADGFVFGDGAGALVVEELEH 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 236 AQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQTLF-PQ 314
Cdd:cd00825 174 ALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFgDK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 315 NPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEPEFPLNFVRIESVQpatSPLNYGLCLSFGFGGQNGAI 394
Cdd:cd00825 254 SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETTP---RELRTALLNGFGLGGTNATL 330
|
..
gi 499175128 395 AV 396
Cdd:cd00825 331 VL 332
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
244-356 |
7.21e-33 |
|
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: 119.60 E-value: 7.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 244 YGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQTLFPQNP-----LI 318
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArkqplAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 499175128 319 TSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLK 356
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
160-396 |
5.65e-30 |
|
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: 119.39 E-value: 5.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 160 ATGLWAIAQGVELIRTGHCQrVLAGAVEAPITPLTLAGFSKMATLA----PDGCY-PFDRQRQGLVLGEGGALLVLETRE 234
Cdd:cd00832 162 AGGLDALAQARRLVRRGTPL-VVSGGVDSALCPWGWVAQLSSGRLStsddPARAYlPFDAAAAGYVPGEGGAILVLEDAA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 235 LAQKRKARIYGEILGWGFSCDALHRS-TPAFDNHSAQQAvkhcLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQTLF- 312
Cdd:cd00832 241 AARERGARVYGEIAGYAATFDPPPGSgRPPGLARAIRLA----LADAGLTPEDVDVVFADAAGVPELDRAEAAALAAVFg 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 313 PQNPLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKE--PEFPLNFVRiesVQPATSPLNYGLCLSFGFGGQ 390
Cdd:cd00832 317 PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDvpPAYGLDLVT---GRPRPAALRTALVLARGRGGF 393
|
....*.
gi 499175128 391 NGAIAV 396
Cdd:cd00832 394 NSALVV 399
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
157-358 |
2.58e-29 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 120.75 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 157 AACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLAPDG-CYPFDRQRQGLVLGEGGALLVLETREL 235
Cdd:COG3321 172 TACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGrCRAFDADADGYVRGEGVGVVVLKRLSD 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 236 AQKRKARIYGEILGWGFSCDalHRST----PafdNHSAQQAV-KHCLTRSGLTPEQIDLIHPHGTGTLFNDQREA-ALIQ 309
Cdd:COG3321 252 ALRDGDRIYAVIRGSAVNQD--GRSNgltaP---NGPAQAAViRRALADAGVDPATVDYVEAHGTGTPLGDPIEAaALTA 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499175128 310 TL----FPQNPL-ITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEP 358
Cdd:COG3321 327 AFgqgrPADQPCaIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETP 380
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
157-391 |
7.78e-27 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 110.53 E-value: 7.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 157 AACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAgFSKMATLA------PD-GCYPFDRQRQGLVLGEGGALLV 229
Cdd:PRK07967 160 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALStkyndtPEkASRAYDANRDGFVIAGGGGVVV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 230 LETRELAQKRKARIYGEILGWGFSCDALHRSTPafdnhSAQQAVKhCLTRSGLTPE-QIDLIHPHGTGTLFNDQREAALI 308
Cdd:PRK07967 239 VEELEHALARGAKIYAEIVGYGATSDGYDMVAP-----SGEGAVR-CMQMALATVDtPIDYINTHGTSTPVGDVKELGAI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 309 QTLFPQN-PLITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKE--PEFP-LNFVR--IESVQpatspLNYGLC 382
Cdd:PRK07967 313 REVFGDKsPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEEldPQAAgMPIVTetTDNAE-----LTTVMS 387
|
....*....
gi 499175128 383 LSFGFGGQN 391
Cdd:PRK07967 388 NSFGFGGTN 396
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
157-396 |
8.25e-24 |
|
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: 99.44 E-value: 8.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 157 AACATGLWAIAQGVELIRTGHCQRVLAGAVEApitpltlagfskmatlapdgcypfdrqrqgLVLGEGGALLVLETRELA 236
Cdd:cd00327 66 QACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------FVFGDGAAAAVVESEEHA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 237 QKRKARIYGEILGWGFSCDALHRST-PAFDNhsAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQTLFPQN 315
Cdd:cd00327 116 LRRGAHPQAEIVSTAATFDGASMVPaVSGEG--LARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 316 -PLITSSKGATGHTLGASGAIAVALTLLSLhqqklppcvglkepefplnfvRIESVQPATSPLNYGLCLSFGFGGQNGAI 394
Cdd:cd00327 194 sPAVSATLIMTGHPLGAAGLAILDELLLML---------------------EHEFIPPTPREPRTVLLLGFGLGGTNAAV 252
|
..
gi 499175128 395 AV 396
Cdd:cd00327 253 VL 254
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
19-236 |
6.87e-23 |
|
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: 96.55 E-value: 6.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 19 VVVTGLALDTALGDQLQT-WTKLLQGKTAIKP-------------------------KQPFINLPSFPLALQGNYPRSLG 72
Cdd:pfam00109 3 VAIVGMGCRFPGGNDPEEfWENLLEGRDGISEipadrwdpdklydppsriagkiytkWGGLDDIFDFDPLFFGISPREAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 73 QLVPP----LVQA--AIDDAQLDPAEQP-------WGVAIGSSRANQCHWEDwvgrniKPPVAPNFKLVdwwQTLPDQAA 139
Cdd:pfam00109 83 RMDPQqrllLEAAweALEDAGITPDSLDgsrtgvfIGSGIGDYAALLLLDED------GGPRRGSPFAV---GTMPSVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 140 RLAAQLL----PEVTVMqcpmAACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLAPDG-CYPFDR 214
Cdd:pfam00109 154 GRISYFLglrgPSVTVD----TACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGpCKAFDP 229
|
250 260
....*....|....*....|..
gi 499175128 215 QRQGLVLGEGGALLVLETRELA 236
Cdd:pfam00109 230 FADGFVRGEGVGAVVLKRLSDA 251
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
158-391 |
2.88e-22 |
|
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: 95.86 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 158 ACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLAPDG-CYPFDRQRQGLVLGEGGALLVLETRELA 236
Cdd:smart00825 96 ACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGrCKTFDASADGYVRGEGVGVVVLKRLSDA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 237 QKRKARIYGEILGWGFSCDAlhRStpafdnhsaqqavkhcltrSGLTpeqidliHPHGTGTLfndqreaaliqtlfpqnp 316
Cdd:smart00825 176 LRDGDPILAVIRGSAVNQDG--RS-------------------NGIT-------APSGPAQL------------------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 317 LITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEPEFPLNF----VRI--ESVQ-PATSPLNYGLCLSFGFGG 389
Cdd:smart00825 210 LIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLeespLRVptELTPwPPPGRPRRAGVSSFGFGG 289
|
..
gi 499175128 390 QN 391
Cdd:smart00825 290 TN 291
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
152-391 |
1.40e-19 |
|
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: 91.61 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 152 MQCPM-AACATGLWAIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKM-ATLAPDGCYPFDRQRQGLVLGEGGALLV 229
Cdd:TIGR02813 198 MNCVVdAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTpAFTTNEDIQPFDIDSKGMMIGEGIGMMA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 230 LETRELAQKRKARIYGEILGWGFSCDALHRSTPAFDNHSAQQAVKHCLTRSGLTPEQIDLIHPHGTGTLFNDQREAALIQ 309
Cdd:TIGR02813 278 LKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLV 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 310 TLFPQNP------LITSSKGATGHTLGASGAIAVALTLLSLHQQKLPPCVGLKEPEFPLN-----FVRIESVQP-----A 373
Cdd:TIGR02813 358 SVFSQDNdqkqhiALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDienspFYLNTETRPwmqreD 437
|
250
....*....|....*...
gi 499175128 374 TSPLNYGLClSFGFGGQN 391
Cdd:TIGR02813 438 GTPRRAGIS-SFGFGGTN 454
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
69-293 |
5.28e-06 |
|
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: 48.03 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 69 RSLGQLVPPLVQAAIDDAQLDPAEQPWgvaigssranqchweDWVGrnikppvapnfkLVDWWQTLPDQAARLAAQLLPE 148
Cdd:cd00829 14 RSPLELAAEAARAALDDAGLEPADIDA---------------VVVG------------NAAGGRFQSFPGALIAEYLGLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 149 VTVMQCPMAACATGLWAIAQGVELIRTGHCQRVLAGAVEAP--------------------------------------- 189
Cdd:cd00829 67 GKPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMsdvptgdeaggrasdlewegpeppggltppalyalaarr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 190 ------ITPLTLAGFS-KM---ATLAPDGCYPFD----------------RQRQGLVLGEGGALLVLETRELAQKRKARi 243
Cdd:cd00829 147 ymhrygTTREDLAKVAvKNhrnAARNPYAQFRKPitvedvlnsrmiadplRLLDCCPVSDGAAAVVLASEERARELTDR- 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499175128 244 YGEILGWGFSCDALHRSTP--AFDNHSAQQAVKHCLTRSGLTPEQIDLIHPH 293
Cdd:cd00829 226 PVWILGVGAASDTPSLSERddFLSLDAARLAARRAYKMAGITPDDIDVAELY 277
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
212-360 |
3.42e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 45.71 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 212 FDRQRQ---GLVLGEGGALLVLETRELAQKRKARIYGEILG-WGfscDALHRSTPAFDNHSAQqavkhcLTRSGLTPEQI 287
Cdd:PRK06519 229 WSRGGEdggGFILGSGGAFLVLESREHAEARGARPYARISGvES---DRARRAPGDLEASLER------LLKPAGGLAAP 299
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499175128 288 DLIHPHGTGTLFNDQREAALIQTLFPqnPLITSSKGATGHTLGASGAIAVALTLLSL-HQQKLPPCVGLKEPEF 360
Cdd:PRK06519 300 TAVISGATGAHPATAEEKAALEAALA--GPVRGIGTLFGHTMEAQFPLGLALAALSVsKGALFPPFDASGEKPM 371
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
200-347 |
1.17e-04 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 43.76 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 200 KMATLAPdgcyPFDRQrqGLV-------LGEGGALLVLETRELAQKR----KARIYG--------EILGWGfscdalhrs 260
Cdd:TIGR01930 222 KLAKLKP----AFDPD--GTVtagnsspLNDGAAALLLMSEEKAKELgltpLARIVSfavagvdpEIMGLG--------- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 261 tPAFdnhsaqqAVKHCLTRSGLTPEQIDLIHphgtgtlFNdqrEAALIQTLFPQNPL-ITSSK----G---ATGHTLGAS 332
Cdd:TIGR01930 287 -PVP-------AIPKALKKAGLSISDIDLFE-------IN---EAFAAQVLACIKELgLDLEKvnvnGgaiALGHPLGAS 348
|
170
....*....|....*
gi 499175128 333 GAIAVALTLLSLHQQ 347
Cdd:TIGR01930 349 GARIVTTLLHELKRR 363
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
165-290 |
1.81e-04 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 43.09 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 165 AIAQGVELIRTGHCQRVLAGAVEAPITPLTLAGFSKMATLAPDGCypfdrqRQGLVLGEGGALLVLETRELAQKRKARiy 244
Cdd:PRK06147 139 ALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQN------SNGFIPGEAAAAVLLGRPAGGEAPGLP-- 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 499175128 245 geILGWGFSCDA--LHRSTPA-FDNHSAQQAVKHCLTRSGLTPEQIDLI 290
Cdd:PRK06147 211 --LLGLGLGREPapVGESEDLpLRGDGLTQAIRAALAEAGCGLEDMDYR 257
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
224-342 |
2.13e-04 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 43.22 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 224 GGALLVLETRELAQKRKARIYGEILGWGFSC--DALHRSTPAfdnhsaqQAVKHCLTRSGLTPEQIDLIHphgtgtlFNd 301
Cdd:PRK05790 253 GAAAVVVMSEAKAKELGLTPLARIVSYAVAGvdPAIMGIGPV-------PAIRKALEKAGWSLADLDLIE-------IN- 317
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 499175128 302 qrEAALIQTLFPQ-----NPLITSSKG---ATGHTLGASGAiAVALTLL 342
Cdd:PRK05790 318 --EAFAAQALAVEkelglDPEKVNVNGgaiALGHPIGASGA-RILVTLL 363
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
139-190 |
3.35e-04 |
|
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: 42.36 E-value: 3.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499175128 139 ARLAAQL--LPE----VTVMQcpmaACATGLWAIAQGVELIRTGHCQRVLAGAVE----API 190
Cdd:COG0183 66 ARQAALLagLPEsvpaVTVNR----VCGSGLQAVALAAQAIAAGDADVVIAGGVEsmsrAPM 123
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
137-187 |
6.53e-04 |
|
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: 41.70 E-value: 6.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 499175128 137 QAArLAAQLLPEVTVMQCPMAaCATGLWAIAQGVELIRTGHCQRVLAGAVE 187
Cdd:cd00751 64 QAA-LLAGLPESVPATTVNRV-CGSGLQAVALAAQSIAAGEADVVVAGGVE 112
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
132-208 |
2.09e-03 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 39.59 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499175128 132 QTLPDQAArLAAQL---LPEVTVMQcpmaACATGLWAIAQGVELIRTGHCQRVLAGAVE-----------APITPLTLAG 197
Cdd:pfam00108 60 QNPARQAA-LKAGIpdsAPAVTINK----VCGSGLKAVYLAAQSIASGDADVVLAGGVEsmshapyalptDARSGLKHGD 134
|
90
....*....|.
gi 499175128 198 FSKMATLAPDG 208
Cdd:pfam00108 135 EKKHDLLIPDG 145
|
|
| |
