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Conserved domains on  [gi|325071317|gb|ADY75763|]
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nonreducing polyketide synthase, partial [Stagonospora sp. CBMAI 1030]

Protein Classification

polyketide synthase( domain architecture ID 10093619)

polyketide synthase assembles complex polyketides via the head-to-tail fusion of acyl and malonyl building blocks; similar to Anser anser anser fatty acid synthase

CATH:  3.10.129.110|3.30.70.3290|3.40.47.10
Gene Ontology:  GO:0006633
SCOP:  4000245

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 1-241 3.89e-112

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: 327.98  E-value: 3.89e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   1 DPRFFNMSPREAFQTDPMQRMALMTAYEALEMSGYVPNrtpSTRLDRIGTFYGQTSDDWRETNAAQ--EVDTYFITGGVR 78
Cdd:cd00833   70 DAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGYSPE---SLAGSRTGVFVGASSSDYLELLARDpdEIDAYAATGTSR 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  79 AFGPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNTFDN 158
Cdd:cd00833  147 AFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDA 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 159 DADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTNHSADAISITHPHGPTQSILSASILDEAGVDPHDVDYVEMHG 238
Cdd:cd00833  227 DADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHG 306


                 ...
gi 325071317 239 TGT 241
Cdd:cd00833  307 TGT 309
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 1-241 3.89e-112

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: 327.98  E-value: 3.89e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   1 DPRFFNMSPREAFQTDPMQRMALMTAYEALEMSGYVPNrtpSTRLDRIGTFYGQTSDDWRETNAAQ--EVDTYFITGGVR 78
Cdd:cd00833   70 DAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGYSPE---SLAGSRTGVFVGASSSDYLELLARDpdEIDAYAATGTSR 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  79 AFGPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNTFDN 158
Cdd:cd00833  147 AFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDA 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 159 DADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTNHSADAISITHPHGPTQSILSASILDEAGVDPHDVDYVEMHG 238
Cdd:cd00833  227 DADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHG 306


                 ...
gi 325071317 239 TGT 241
Cdd:cd00833  307 TGT 309
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-241 2.84e-86

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 279.06  E-value: 2.84e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317    1 DPRFFNMSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPSTRldrIGTFYGQTSDDW--RETNAAQEVDTYFITGGVR 78
Cdd:COG3321    74 DALFFGISPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSR---TGVFVGASSNDYalLLLADPEAIDAYALTGNAK 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   79 AFGPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNTFDN 158
Cdd:COG3321   151 SVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDA 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  159 DADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTNHSADAISITHPHGPTQSILSASILDEAGVDPHDVDYVEMHG 238
Cdd:COG3321   231 DADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHG 310


                  ...
gi 325071317  239 TGT 241
Cdd:COG3321   311 TGT 313
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 1-213 2.04e-85

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: 255.72  E-value: 2.04e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317     1 DPRFFNMSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPSTRldrIGTFYGQTSDDWretnaaqevdtyfitggvraf 80
Cdd:smart00825  34 DAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSR---TGVFVGVSSSDY--------------------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317    81 gpgrinyyfgfsgpSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNTFDNDA 160
Cdd:smart00825  90 --------------SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASA 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 325071317   161 DGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTNHSADAISITHPHGPTQ 213
Cdd:smart00825 156 DGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ 208
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 1-180 1.77e-60

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: 190.54  E-value: 1.77e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317    1 DPRFFNMSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPSTRLDR-IGTFYGQTSDDWRETNAAQEVDTY-FITGGVR 78
Cdd:pfam00109  70 DPLFFGISPREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVfIGSGIGDYAALLLLDEDGGPRRGSpFAVGTMP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   79 AFGPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNTFDN 158
Cdd:pfam00109 150 SVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDP 229

                         170       180
                  ....*....|....*....|..
gi 325071317  159 DADGYCRADGCASVIVKRLDDA 180
Cdd:pfam00109 230 FADGFVRGEGVGAVVLKRLSDA 251
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 83-241 2.87e-22

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: 95.46  E-value: 2.87e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317    83 GRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNTFDNDADG 162
Cdd:TIGR02813  187 GRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNEDIQPFDIDSKG 266

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 325071317   163 YCRADGCASVIVKRLDDALADKDNILAVVLGTQTNHSADAISITHPHGPTQSILSASILDEAGVDPHDVDYVEMHGTGT 241
Cdd:TIGR02813  267 MMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGT 345
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
7-241 1.04e-18

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 84.28  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   7 MSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPStrLDRIGTFYG------QTSDDWRETNAAQEVDT-------YFI 73
Cdd:PRK06333  71 LDPKDQRKMDRFILFAMAAAKEALAQAGWDPDTLED--RERTATIIGsgvggfPAIAEAVRTLDSRGPRRlspftipSFL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  74 TGgvraFGPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNN- 152
Cdd:PRK06333 149 TN----MAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRFNd 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 153 -----CNTFDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTnhSADAISITHP----HGPTQSILSAsiLDE 223
Cdd:PRK06333 225 apeqaSRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGT--SADAYHMTAGpedgEGARRAMLIA--LRQ 300

                        250
                 ....*....|....*...
gi 325071317 224 AGVDPHDVDYVEMHGTGT 241
Cdd:PRK06333 301 AGIPPEEVQHLNAHATST 318
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 1-241 3.89e-112

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: 327.98  E-value: 3.89e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   1 DPRFFNMSPREAFQTDPMQRMALMTAYEALEMSGYVPNrtpSTRLDRIGTFYGQTSDDWRETNAAQ--EVDTYFITGGVR 78
Cdd:cd00833   70 DAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGYSPE---SLAGSRTGVFVGASSSDYLELLARDpdEIDAYAATGTSR 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  79 AFGPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNTFDN 158
Cdd:cd00833  147 AFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDA 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 159 DADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTNHSADAISITHPHGPTQSILSASILDEAGVDPHDVDYVEMHG 238
Cdd:cd00833  227 DADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHG 306


                 ...
gi 325071317 239 TGT 241
Cdd:cd00833  307 TGT 309
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-241 2.84e-86

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 279.06  E-value: 2.84e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317    1 DPRFFNMSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPSTRldrIGTFYGQTSDDW--RETNAAQEVDTYFITGGVR 78
Cdd:COG3321    74 DALFFGISPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSR---TGVFVGASSNDYalLLLADPEAIDAYALTGNAK 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   79 AFGPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNTFDN 158
Cdd:COG3321   151 SVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDA 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  159 DADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTNHSADAISITHPHGPTQSILSASILDEAGVDPHDVDYVEMHG 238
Cdd:COG3321   231 DADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHG 310


                  ...
gi 325071317  239 TGT 241
Cdd:COG3321   311 TGT 313
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 1-213 2.04e-85

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: 255.72  E-value: 2.04e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317     1 DPRFFNMSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPSTRldrIGTFYGQTSDDWretnaaqevdtyfitggvraf 80
Cdd:smart00825  34 DAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSR---TGVFVGVSSSDY--------------------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317    81 gpgrinyyfgfsgpSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNTFDNDA 160
Cdd:smart00825  90 --------------SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASA 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 325071317   161 DGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTNHSADAISITHPHGPTQ 213
Cdd:smart00825 156 DGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ 208
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 1-180 1.77e-60

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: 190.54  E-value: 1.77e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317    1 DPRFFNMSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPSTRLDR-IGTFYGQTSDDWRETNAAQEVDTY-FITGGVR 78
Cdd:pfam00109  70 DPLFFGISPREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVfIGSGIGDYAALLLLDEDGGPRRGSpFAVGTMP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   79 AFGPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNTFDN 158
Cdd:pfam00109 150 SVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDP 229

                         170       180
                  ....*....|....*....|..
gi 325071317  159 DADGYCRADGCASVIVKRLDDA 180
Cdd:pfam00109 230 FADGFVRGEGVGAVVLKRLSDA 251
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 7-241 2.63e-34

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: 126.88  E-value: 2.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   7 MSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPSTRLD-RIGTFYGQTSDdwretnaAQEVDTYFITGGVRAFGPGRI 85
Cdd:cd00834   60 LDRKELRRMDRFAQFALAAAEEALADAGLDPEELDPERIGvVIGSGIGGLAT-------IEEAYRALLEKGPRRVSPFFV 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  86 NY------------YFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNN- 152
Cdd:cd00834  133 PMalpnmaagqvaiRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDd 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 153 ----CNTFDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGtqTNHSADAISITHPH----GPTQSILSAsiLDEA 224
Cdd:cd00834  213 pekaSRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILG--YGASSDAYHITAPDpdgeGAARAMRAA--LADA 288

                        250
                 ....*....|....*..
gi 325071317 225 GVDPHDVDYVEMHGTGT 241
Cdd:cd00834  289 GLSPEDIDYINAHGTST 305
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 7-241 2.10e-31

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: 119.04  E-value: 2.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   7 MSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPStrlDRIGTFYGQTSDDWRETnaAQEVDTYFiTGGVRAFGP---- 82
Cdd:COG0304   60 LDRKELRRMDRFTQYALAAAREALADAGLDLDEVDP---DRTGVIIGSGIGGLDTL--EEAYRALL-EKGPRRVSPffvp 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  83 --------GRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNN-- 152
Cdd:COG0304  134 mmmpnmaaGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDdp 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 153 ---CNTFDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTnhSADAISITHPH----GPTQSILSAsiLDEAG 225
Cdd:COG0304  214 ekaSRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGA--SSDAYHITAPApdgeGAARAMRAA--LKDAG 289

                        250
                 ....*....|....*.
gi 325071317 226 VDPHDVDYVEMHGTGT 241
Cdd:COG0304  290 LSPEDIDYINAHGTST 305
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 19-241 3.44e-28

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: 109.26  E-value: 3.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  19 QRMALMTAYEALEMSGYVPNRTPSTRLDRI-GTFYGQTSDDWRETNAAQEVDTYFITGGVRAFGPGRINYYFGFSGPSLN 97
Cdd:cd00825   12 SILGFEAAERAIADAGLSREYQKNPIVGVVvGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAYD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  98 IDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNTFDNDADGYCRADGCASVIVKRL 177
Cdd:cd00825   92 VSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEEL 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 325071317 178 DDALADKDNILAVVLGTQTNHSADAISITHPHGPTQSILSASILDEAGVDPHDVDYVEMHGTGT 241
Cdd:cd00825  172 EHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGT 235
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 83-241 2.87e-22

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: 95.46  E-value: 2.87e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317    83 GRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNTFDNDADG 162
Cdd:TIGR02813  187 GRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNEDIQPFDIDSKG 266

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 325071317   163 YCRADGCASVIVKRLDDALADKDNILAVVLGTQTNHSADAISITHPHGPTQSILSASILDEAGVDPHDVDYVEMHGTGT 241
Cdd:TIGR02813  267 MMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGT 345
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 9-241 6.54e-20

"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: 87.49  E-value: 6.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   9 PREAFQTDPMQRMALMTAYEALEMSGYvpnrTPSTRL--DRIGTFYGQTSDDWRET-----NAAQEVDTYFITGG--VRA 79
Cdd:cd00828   63 AKRTGIVDRTTLLALVATEEALADAGI----TDPYEVhpSEVGVVVGSGMGGLRFLrrggkLDARAVNPYVSPKWmlSPN 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  80 FGPGRINYYFGFS-GPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGG--------LSCMTNSdifSGLSRGQFLSkN 150
Cdd:cd00828  139 TVAGWVNILLLSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGvedpleegLSGFANM---GALSTAEEEP-E 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 151 NNCNTFDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTNHSADAISITHPH-GPTQSILSAsiLDEAGVDPH 229
Cdd:cd00828  215 EMSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGkGIARAIRTA--LAKAGLSLD 292

                        250
                 ....*....|..
gi 325071317 230 DVDYVEMHGTGT 241
Cdd:cd00828  293 DLDVISAHGTST 304
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
7-241 1.04e-18

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 84.28  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   7 MSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPStrLDRIGTFYG------QTSDDWRETNAAQEVDT-------YFI 73
Cdd:PRK06333  71 LDPKDQRKMDRFILFAMAAAKEALAQAGWDPDTLED--RERTATIIGsgvggfPAIAEAVRTLDSRGPRRlspftipSFL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  74 TGgvraFGPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNN- 152
Cdd:PRK06333 149 TN----MAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRFNd 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 153 -----CNTFDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTnhSADAISITHP----HGPTQSILSAsiLDE 223
Cdd:PRK06333 225 apeqaSRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGT--SADAYHMTAGpedgEGARRAMLIA--LRQ 300

                        250
                 ....*....|....*...
gi 325071317 224 AGVDPHDVDYVEMHGTGT 241
Cdd:PRK06333 301 AGIPPEEVQHLNAHATST 318
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
7-241 7.59e-18

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 81.37  E-value: 7.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   7 MSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPStrlDRIGTFYG----------QTSDDWRETNAaQEVDTYFITGG 76
Cdd:PRK07314  61 MSRKEARRMDRFIQYGIAAAKQAVEDAGLEITEENA---DRIGVIIGsgiggletieEQHITLLEKGP-RRVSPFFVPMA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  77 VRAFGPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGlscmTNSDIfSGLSRGQF-----LSKNN 151
Cdd:PRK07314 137 IINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGG----AEAAI-TPLGIAGFaaaraLSTRN 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 152 N-----CNTFDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGTqtNHSADAISITHPH----GPTQSILSAsiLD 222
Cdd:PRK07314 212 DdperaSRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGY--GMTGDAYHMTAPApdgeGAARAMKLA--LK 287

                        250
                 ....*....|....*....
gi 325071317 223 EAGVDPHDVDYVEMHGTGT 241
Cdd:PRK07314 288 DAGINPEDIDYINAHGTST 306
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 1-241 3.16e-17

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 79.74  E-value: 3.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   1 DPRFFNMSPREafqtDPMQRMALMTAYEALEMSGYVPNrtPSTRLDRIGTFYGQTSDDWRETNAAQEVdtyfitggVRAF 80
Cdd:PTZ00050  64 DPSDFAPTKRE----SRATHFAMAAAREALADAKLDIL--SEKDQERIGVNIGSGIGSLADLTDEMKT--------LYEK 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  81 GPGRINYYF-----------------GFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSR 143
Cdd:PTZ00050 130 GHSRVSPYFipkilgnmaaglvaikhKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSR 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 144 GQFLS--KNNN----CNTFDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTnhSADAISITHPH----GPTQ 213
Cdd:PTZ00050 210 MRALCtkYNDDpqraSRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGS--SSDAHHITAPHpdgrGARR 287

                        250       260
                 ....*....|....*....|....*...
gi 325071317 214 SILSAsILDEAGVDPHDVDYVEMHGTGT 241
Cdd:PTZ00050 288 CMENA-LKDGANININDVDYVNAHATST 314
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
88-241 3.64e-17

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 79.50  E-value: 3.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  88 YFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGG---LSCMT-NSdiFSGLsrgQFLSkNNNCNTFDNDADGY 163
Cdd:PRK09185 146 YLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGvdsLCRLTlNG--FNSL---ESLS-PQPCRPFSANRDGI 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 164 CRADGCASVIVKRLDDaladkDNILavVLGTqtNHSADA--ISITHPHG--PTQSILSAsiLDEAGVDPHDVDYVEMHGT 239
Cdd:PRK09185 220 NIGEAAAFFLLEREDD-----AAVA--LLGV--GESSDAhhMSAPHPEGlgAILAMQQA--LADAGLAPADIGYINLHGT 288


                 ..
gi 325071317 240 GT 241
Cdd:PRK09185 289 AT 290
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 22-241 1.73e-16

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 77.91  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  22 ALMTAYEALEMSGYVPnrTPSTRLDR----IGTFYGQTSDdwrETNAAQ--------EVDTYFITGGVRAFGPGRINYYF 89
Cdd:PLN02836  97 ALCAADEALSDARWLP--SEDEAKERtgvsIGGGIGSITD---ILEAAQlicekrlrRLSPFFVPRILINMAAGHVSIRY 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  90 GFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLS-KNNNCNT-----FDNDADGY 163
Cdd:PLN02836 172 GFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALStKFNSCPTeasrpFDCDRDGF 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 164 CRADGCASVIVKRLDDALADKDNILAVVLGtqTNHSADAISITHPH-GPTQSILSAS-ILDEAGVDPHDVDYVEMHGTGT 241
Cdd:PLN02836 252 VIGEGAGVLVLEELEHAKRRGAKIYAEVRG--YGMSGDAHHITQPHeDGRGAVLAMTrALQQSGLHPNQVDYVNAHATST 329
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 188-241 1.36e-14

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: 67.98  E-value: 1.36e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 325071317  188 LAVVLGTQTNHSADAISITHPHGPTQSILSASILDEAGVDPHDVDYVEMHGTGT 241
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGT 54
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
4-241 2.59e-13

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 68.50  E-value: 2.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   4 FFNMSPREAfqTDPMQRMALMTAYEALEMSGYVPNRTPST----------------RLDRIGTFYGQTS-DDWRETNAAQ 66
Cdd:PRK06501  63 FLPESPFGA--SALSEALARLAAEEALAQAGIGKGDFPGPlflaappvelewparfALAAAVGDNDAPSyDRLLRAARGG 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  67 EVDTY---FITGGVRAfgpgRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAivggLSCMTNSDI------ 137
Cdd:PRK06501 141 RFDALherFQFGSIAD----RLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRA----LCIATDGSVsaeali 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 138 -FSGLSRgqfLSKNNN-----CNTFDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGT--------QTNHSADAI 203
Cdd:PRK06501 213 rFSLLSA---LSTQNDppekaSKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCgekadsfhRTRSSPDGS 289

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 325071317 204 SIThphgptQSILSAsiLDEAGVDPHDVDYVEMHGTGT 241
Cdd:PRK06501 290 PAI------GAIRAA--LADAGLTPEQIDYINAHGTST 319
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 7-241 3.23e-13

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 68.22  E-value: 3.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   7 MSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPStrlDRIGTFYG---------QTSDDWRETNAAQEVDTYFITGGV 77
Cdd:PRK08439  61 MDPKEVKKADRFIQLGLKAAREAMKDAGFLPEELDA---ERFGVSSAsgigglpniEKNSIICFEKGPRKISPFFIPSAL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  78 RAFGPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNN----- 152
Cdd:PRK08439 138 VNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDdpkka 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 153 CNTFDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGtqTNHSADAISITHP--HGPTQSILSAsiLDEAGVDPhd 230
Cdd:PRK08439 218 SRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIG--FGESGDANHITSPapEGPLRAMKAA--LEMAGNPK-- 291

                        250
                 ....*....|.
gi 325071317 231 VDYVEMHGTGT 241
Cdd:PRK08439 292 IDYINAHGTST 302
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 83-241 9.22e-13

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: 65.93  E-value: 9.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  83 GRINYYFGFS-GPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGlscmtnSDIFSglsrgqflsknnncntfdndad 161
Cdd:cd00327   48 GQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGG------SEEFV---------------------- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 162 gycRADGCASVIVKRLDDALADKDNILAVVLGTQTnHSADAISITHPHGPTQSILSASILDEAGVDPHDVDYVEMHGTGT 241
Cdd:cd00327  100 ---FGDGAAAAVVESEEHALRRGAHPQAEIVSTAA-TFDGASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGT 175
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
7-241 1.19e-11

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 63.60  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   7 MSPREAFQTDPMQRMALMTAYEALEMSGyvpnrTPSTRLDR----IGTFYGQTS------DDWREtnaaqevdtyfitGG 76
Cdd:PRK07910  72 LTRVELRRMSYLQRMSTVLGRRVWENAG-----SPEVDTNRlmvsIGTGLGSAEelvfayDDMRA-------------RG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  77 VRAFGPGRINYYFGfSGPSLNID-------------TACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSR 143
Cdd:PRK07910 134 LRAVSPLAVQMYMP-NGPAAAVGlerhakagvitpvSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQ 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 144 -GQFLSKNNN-----CNTFDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTNHSADAISITHPHGPTQSILS 217
Cdd:PRK07910 213 mRIVMSTNNDdpagaCRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAM 292

                        250       260
                 ....*....|....*....|....
gi 325071317 218 ASILDEAGVDPHDVDYVEMHGTGT 241
Cdd:PRK07910 293 TRAIELAGLTPGDIDHVNAHATGT 316
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
7-241 5.79e-10

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 58.48  E-value: 5.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317   7 MSPREAFQTDPMQRMALMTAYEALEMSGYVPNRTPSTRLD-RIGTFYG-----QTSDDWRETNAAQEVDTYFITGGVRAF 80
Cdd:PRK08722  63 MSKKDARKMDLFIQYGIAAGIQALDDSGLEVTEENAHRIGvAIGSGIGglgliEAGHQALVEKGPRKVSPFFVPSTIVNM 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  81 GPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNN-----CNT 155
Cdd:PRK08722 143 IAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDepqkaSRP 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 156 FDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGTqtNHSADAISITHPH--GPTQSILSASILDEAGVDPHDVDY 233
Cdd:PRK08722 223 WDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGF--GMSGDAYHMTSPSedGSGGALAMEAAMRDAGVTGEQIGY 300


                 ....*...
gi 325071317 234 VEMHGTGT 241
Cdd:PRK08722 301 VNAHGTST 308
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 83-241 6.91e-10

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 58.20  E-value: 6.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  83 GRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCN------TF 156
Cdd:PRK14691  72 GHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHFNSTpekasrPF 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 157 DNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTnhSADAISITH----PHGPTQSILSAsiLDEAGVDPHDVD 232
Cdd:PRK14691 152 DTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGT--SADAYHMTSgaedGDGAYRAMKIA--LRQAGITPEQVQ 227


                 ....*....
gi 325071317 233 YVEMHGTGT 241
Cdd:PRK14691 228 HLNAHATST 236
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
14-241 4.80e-09

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 55.76  E-value: 4.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  14 QTDPMQRMALMT--AYE-ALEMSGYVPNrtPSTRLDRIGTFYGQTSDDwreTNAAQEVDTYFITGGVRAF---------- 80
Cdd:PRK09116  66 KIRSMGRVSLMAtrASElALEDAGLLGD--PILTDGRMGIAYGSSTGS---TDPIGAFGTMLLEGSMSGItattyvrmmp 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  81 --GPGRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLS--CMTNSDIFSGL---SRgqflsKNNNC 153
Cdd:PRK09116 141 htTAVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEelCPTEAAVFDTLfatST-----RNDAP 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 154 NT----FDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTNhsADAISITHPHGPTQSILSASILDEAGVDPH 229
Cdd:PRK09116 216 ELtprpFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTN--SDGAHVTQPQAETMQIAMELALKDAGLAPE 293

                        250
                 ....*....|..
gi 325071317 230 DVDYVEMHGTGT 241
Cdd:PRK09116 294 DIGYVNAHGTAT 305
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 89-241 5.29e-09

3-oxoacyl-[acyl-carrier-protein] synthase II


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 55.76  E-value: 5.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  89 FGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNNCNT-----FDNDADGY 163
Cdd:PLN02787 278 LGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTkasrpWDMNRDGF 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 164 CRADGCASVIVKRLDDALADKDNILAVVLGTqtNHSADAISITHPHGPTQSILSA--SILDEAGVDPHDVDYVEMHGTGT 241
Cdd:PLN02787 358 VMGEGAGVLLLEELEHAKKRGANIYAEFLGG--SFTCDAYHMTEPHPEGAGVILCieKALAQSGVSKEDVNYINAHATST 435
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 20-241 1.12e-08

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 54.65  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  20 RMALMTAYEALEMSGYVPnrTPStrlDRIGTFYG----------QTSDDWRE-------TNAAQEVDTYFItggvrafgp 82
Cdd:PRK07103  82 QAALAAAREAWRDAALGP--VDP---DRIGLVVGgsnlqqreqaLVHETYRDrpaflrpSYGLSFMDTDLV--------- 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  83 GRINYYFGFSGPSLNIDTACSSSAAALQVACTSLWAKECDTAI-VGGLSCMTNSDIFSGLSRGQFLSK------NNNCNT 155
Cdd:PRK07103 148 GLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIaVGALMDLSYWECQALRSLGAMGSDrfadepEAACRP 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 156 FDNDADGYCRADGCASVIVKRLDDALADKDNILAVVLGTQTnhSADAISITHPHGPTQSILSASILDEAGVDPHDVDYVE 235
Cdd:PRK07103 228 FDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSM--RLDANRGPDPSLEGEMRVIRAALRRAGLGPEDIDYVN 305


                 ....*.
gi 325071317 236 MHGTGT 241
Cdd:PRK07103 306 PHGTGS 311
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 14-241 7.62e-07

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: 49.28  E-value: 7.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  14 QTDPMQRMALMTAYEALEMSGYVPNRTP------STRLDRIGTFYGQtsddwRE-----TNAAQEVDTYFITGGVRAFGP 82
Cdd:cd00832   67 QTDRMTRLALAAADWALADAGVDPAALPpydmgvVTASAAGGFEFGQ-----RElqklwSKGPRHVSAYQSFAWFYAVNT 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  83 GRINYYFGFSGPSLNIDTACSSSAAALQVACTSLwAKECDTAIVGGL-SCMTNSDIFSGLSRGqFLSKNNNCNT----FD 157
Cdd:cd00832  142 GQISIRHGMRGPSGVVVAEQAGGLDALAQARRLV-RRGTPLVVSGGVdSALCPWGWVAQLSSG-RLSTSDDPARaylpFD 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 158 NDADGYCRADGCASVIVKRLDDALADKDNILAVVLGtqtnHSADAISITHPHGPTQsiLSASI---LDEAGVDPHDVDYV 234
Cdd:cd00832  220 AAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAG----YAATFDPPPGSGRPPG--LARAIrlaLADAGLTPEDVDVV 293


                 ....*..
gi 325071317 235 EMHGTGT 241
Cdd:cd00832  294 FADAAGV 300
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
112-241 4.55e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 43.89  E-value: 4.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 112 AC-TSLWA----------KECDTAIVGGLSCMTNSDIFSGLSRGQFLSKNNnCNTFDNDADGYCRADGCASVIVKRLDDA 180
Cdd:PRK05952 145 ACaTGLWAiaqgveliqtGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AYPFDRQREGLVLGEGGAILVLESAELA 223

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 325071317 181 LADKDNILAVVLGTqtNHSADAISITHPHGPTQSILSA--SILDEAGVDPHDVDYVEMHGTGT 241
Cdd:PRK05952 224 QKRGAKIYGQILGF--GLTCDAYHMSAPEPDGKSAIAAiqQCLARSGLTPEDIDYIHAHGTAT 284
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 68-237 2.40e-03

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: 38.40  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317  68 VDTYFITGGVRAFGPGRINYYFGFSG-PSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGL----SCMTNSDIFS--- 139
Cdd:cd00829   42 VVGNAAGGRFQSFPGALIAEYLGLLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAekmsDVPTGDEAGGras 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325071317 140 ------------------------------GLSRGQF--LSKNNNCNTFDN---------DADGYCRA------------ 166
Cdd:cd00829  122 dlewegpeppggltppalyalaarrymhryGTTREDLakVAVKNHRNAARNpyaqfrkpiTVEDVLNSrmiadplrlldc 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 325071317 167 ----DGCASVIVKRLDDALADKDN---ILAVVLGTQTNHSADAISITHPHGPTQSILSAsiLDEAGVDPHDVDYVEMH 237
Cdd:cd00829  202 cpvsDGAAAVVLASEERARELTDRpvwILGVGAASDTPSLSERDDFLSLDAARLAARRA--YKMAGITPDDIDVAELY 277
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 94-144 3.63e-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: 37.67  E-value: 3.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 325071317   94 PSLNIDTACSSSAAALQVACTSLWAKECDTAIVGGLSCMTN------SDIFSGLSRG 144
Cdd:pfam00108  77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHapyalpTDARSGLKHG 133
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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