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Conserved domains on  [gi|62083193|gb|AAX62327|]
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polyketide synthase, partial [fungal sp. K132]

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 ...
 1-255 7.60e-117

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: 340.69  E-value: 7.60e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   1 REALQMDPQQRIFLECVYEALENAGITSHEITGQKVGVFAGGSYPDYEINNTRDATAIPMYASTGTAMSLQANRVSYYFD 80
Cdd:cd00833  79 REAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFD 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  81 LNGPSVTVDTACSSSLSALHLACQSIRNGEmfnghC-----GGCHLNITPRGFHrhdtfQVSETGspvtyrs*lvipqrL 155
Cdd:cd00833 159 LRGPSLTVDTACSSSLVALHLACQSLRSGE-----CdlalvGGVNLILSPDMFV-----GFSKAG--------------M 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193 156 LSDTGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQVYEEARI 235
Cdd:cd00833 215 LSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGV 294

                       250       260
                ....*....|....*....|
gi 62083193 236 DPSLTAFVEAHGTGTQLGDP 255
Cdd:cd00833 295 DPSDIDYVEAHGTGTPLGDP 314
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 1-255 7.60e-117

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: 340.69  E-value: 7.60e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   1 REALQMDPQQRIFLECVYEALENAGITSHEITGQKVGVFAGGSYPDYEINNTRDATAIPMYASTGTAMSLQANRVSYYFD 80
Cdd:cd00833  79 REAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFD 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  81 LNGPSVTVDTACSSSLSALHLACQSIRNGEmfnghC-----GGCHLNITPRGFHrhdtfQVSETGspvtyrs*lvipqrL 155
Cdd:cd00833 159 LRGPSLTVDTACSSSLVALHLACQSLRSGE-----CdlalvGGVNLILSPDMFV-----GFSKAG--------------M 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193 156 LSDTGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQVYEEARI 235
Cdd:cd00833 215 LSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGV 294

                       250       260
                ....*....|....*....|
gi 62083193 236 DPSLTAFVEAHGTGTQLGDP 255
Cdd:cd00833 295 DPSDIDYVEAHGTGTPLGDP 314
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-255 3.88e-105

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 331.84  E-value: 3.88e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193    1 REALQMDPQQRIFLECVYEALENAGITSHEITGQKVGVFAGGSYPDYEINNTRDATAIPMYASTGTAMSLQANRVSYYFD 80
Cdd:COG3321   83 REAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLD 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   81 LNGPSVTVDTACSSSLSALHLACQSIRNGEmfnghC-----GGCHLNITPRGFHRHDtfqvsetgspvtyrs*lviPQRL 155
Cdd:COG3321  163 LRGPSVTVDTACSSSLVAVHLACQSLRSGE-----CdlalaGGVNLMLTPESFILFS-------------------KGGM 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  156 LSDTGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQVYEEARI 235
Cdd:COG3321  219 LSPDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGV 298

                        250       260
                 ....*....|....*....|
gi 62083193  236 DPSLTAFVEAHGTGTQLGDP 255
Cdd:COG3321  299 DPATVDYVEAHGTGTPLGDP 318
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 1-225 2.93e-79

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: 240.69  E-value: 2.93e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193      1 REALQMDPQQRIFLECVYEALENAGITSHEITGQKVGVFAGGSYPDYeinntrdataipmyastgtamslqanrvsyyfd 80
Cdd:smart00825  43 REAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY--------------------------------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193     81 lngpSVTVDTACSSSLSALHLACQSIRNGEmfnghC-----GGCHLNITPRGFHRHDtfqvsetgspvtyrs*lviPQRL 155
Cdd:smart00825  90 ----SVTVDTACSSSLVALHLACQSLRSGE-----CdmalaGGVNLILSPDTFVGLS-------------------RAGM 141

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193    156 LSDTGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEAL 225
Cdd:smart00825 142 LSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQLLI 211
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 1-189 9.52e-58

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: 184.38  E-value: 9.52e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193     1 REALQMDPQQRIFLECVYEALENAGITSHEITGQKVGVFAGGSYPDYEINNTRDATAIPMYAS---TGTAMSLQANRVSY 77
Cdd:pfam00109  79 REAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPRRGSpfaVGTMPSVIAGRISY 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193    78 YFDLNGPSVTVDTACSSSLSALHLACQSIRNGE---MFnghCGGCHLNITPRGFHRHDtfqvsetgspvtyrs*lviPQR 154
Cdd:pfam00109 159 FLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEadvAL---AGGVNLLLTPLGFAGFS-------------------AAG 216

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 62083193   155 LLSDTGRSYAFDHRGTGFGRGEGAGCIILKSLEDA 189
Cdd:pfam00109 217 MLSPDGPCKAFDPFADGFVRGEGVGAVVLKRLSDA 251
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 72-254 1.62e-24

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: 102.39  E-value: 1.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193     72 ANRVSYYFDLNGPSVTVDTACSSSLSALHLACQSI---RNGEMFNGhcGGCHLNitprgfhrhdtfqvsetgSPVTYRS* 148
Cdd:TIGR02813  186 SGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELlegRSEMMITG--GVCTDN------------------SPFMYMSF 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193    149 LVIPQRLLSDTGRSYAFDHRGTGFGrgEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQ 228
Cdd:TIGR02813  246 SKTPAFTTNEDIQPFDIDSKGMMIG--EGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKR 323

                          170       180
                   ....*....|....*....|....*.
gi 62083193    229 VYEEARIDPSLTAFVEAHGTGTQLGD 254
Cdd:TIGR02813  324 AYDDAGFAPHTCGLIEAHGTGTAAGD 349
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 17-254 9.71e-15

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 72.80  E-value: 9.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   17 VYEALENAGITSHEITGQ-KVGVFAGgsypdyeinntrdaTAIPMYASTGTAMSLQA----NRVSYYF------------ 79
Cdd:PTZ00050  85 AREALADAKLDILSEKDQeRIGVNIG--------------SGIGSLADLTDEMKTLYekghSRVSPYFipkilgnmaagl 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   80 -----DLNGPSVTVDTACSSSLSALHLACQSIRNGEMFNGHCGGCHLNITP---RGFHRhdtFQVSETGSPVTyrs*lvi 151
Cdd:PTZ00050 151 vaikhKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPvsfAGFSR---MRALCTKYNDD------- 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  152 PQRllsdtgRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGE-AQEALIRQVY 230
Cdd:PTZ00050 221 PQR------ASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRgARRCMENALK 294

                        250       260
                 ....*....|....*....|....
gi 62083193  231 EEARIDPSLTAFVEAHGTGTQLGD 254
Cdd:PTZ00050 295 DGANININDVDYVNAHATSTPIGD 318
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 1-255 7.60e-117

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: 340.69  E-value: 7.60e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   1 REALQMDPQQRIFLECVYEALENAGITSHEITGQKVGVFAGGSYPDYEINNTRDATAIPMYASTGTAMSLQANRVSYYFD 80
Cdd:cd00833  79 REAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFD 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  81 LNGPSVTVDTACSSSLSALHLACQSIRNGEmfnghC-----GGCHLNITPRGFHrhdtfQVSETGspvtyrs*lvipqrL 155
Cdd:cd00833 159 LRGPSLTVDTACSSSLVALHLACQSLRSGE-----CdlalvGGVNLILSPDMFV-----GFSKAG--------------M 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193 156 LSDTGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQVYEEARI 235
Cdd:cd00833 215 LSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGV 294

                       250       260
                ....*....|....*....|
gi 62083193 236 DPSLTAFVEAHGTGTQLGDP 255
Cdd:cd00833 295 DPSDIDYVEAHGTGTPLGDP 314
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-255 3.88e-105

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 331.84  E-value: 3.88e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193    1 REALQMDPQQRIFLECVYEALENAGITSHEITGQKVGVFAGGSYPDYEINNTRDATAIPMYASTGTAMSLQANRVSYYFD 80
Cdd:COG3321   83 REAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLD 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   81 LNGPSVTVDTACSSSLSALHLACQSIRNGEmfnghC-----GGCHLNITPRGFHRHDtfqvsetgspvtyrs*lviPQRL 155
Cdd:COG3321  163 LRGPSVTVDTACSSSLVAVHLACQSLRSGE-----CdlalaGGVNLMLTPESFILFS-------------------KGGM 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  156 LSDTGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQVYEEARI 235
Cdd:COG3321  219 LSPDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGV 298

                        250       260
                 ....*....|....*....|
gi 62083193  236 DPSLTAFVEAHGTGTQLGDP 255
Cdd:COG3321  299 DPATVDYVEAHGTGTPLGDP 318
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 1-225 2.93e-79

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: 240.69  E-value: 2.93e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193      1 REALQMDPQQRIFLECVYEALENAGITSHEITGQKVGVFAGGSYPDYeinntrdataipmyastgtamslqanrvsyyfd 80
Cdd:smart00825  43 REAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY--------------------------------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193     81 lngpSVTVDTACSSSLSALHLACQSIRNGEmfnghC-----GGCHLNITPRGFHRHDtfqvsetgspvtyrs*lviPQRL 155
Cdd:smart00825  90 ----SVTVDTACSSSLVALHLACQSLRSGE-----CdmalaGGVNLILSPDTFVGLS-------------------RAGM 141

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193    156 LSDTGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEAL 225
Cdd:smart00825 142 LSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQLLI 211
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 1-189 9.52e-58

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: 184.38  E-value: 9.52e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193     1 REALQMDPQQRIFLECVYEALENAGITSHEITGQKVGVFAGGSYPDYEINNTRDATAIPMYAS---TGTAMSLQANRVSY 77
Cdd:pfam00109  79 REAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPRRGSpfaVGTMPSVIAGRISY 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193    78 YFDLNGPSVTVDTACSSSLSALHLACQSIRNGE---MFnghCGGCHLNITPRGFHRHDtfqvsetgspvtyrs*lviPQR 154
Cdd:pfam00109 159 FLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEadvAL---AGGVNLLLTPLGFAGFS-------------------AAG 216

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 62083193   155 LLSDTGRSYAFDHRGTGFGRGEGAGCIILKSLEDA 189
Cdd:pfam00109 217 MLSPDGPCKAFDPFADGFVRGEGVGAVVLKRLSDA 251
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 9-255 3.74e-35

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: 128.14  E-value: 3.74e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   9 QQRIFLECVYEALENAGITSHEITGQKVGVFAGGSYPDYEINNTRDAT--AIPMYASTGTAMSLQANRVSYYFDLNGPSV 86
Cdd:cd00825  11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAmrAVGPYVVTKAMFPGASGQIATPLGIHGPAY 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  87 TVDTACSSSLSALHLACQSIRNGEMFNGHCGGCHLNITPrgfhrhdtfqvsetgspvtYRS*LVIPQRLLSDTGRSYAFD 166
Cdd:cd00825  91 DVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAP-------------------MDCEFDAMGALSTPEKASRTFD 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193 167 HRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQVYEEARIDPSLTAFVEAH 246
Cdd:cd00825 152 AAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAH 231


                ....*....
gi 62083193 247 GTGTQLGDP 255
Cdd:cd00825 232 GTGTPIGDV 240
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 1-254 6.94e-26

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: 104.41  E-value: 6.94e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   1 REALQMDPQQRIFLECVYEALENAGITSHEITGQKVGVFAG---GSYPD----YEINNTRDATAIPMYASTGTAMSLQAN 73
Cdd:COG0304  63 KELRRMDRFTQYALAAAREALADAGLDLDEVDPDRTGVIIGsgiGGLDTleeaYRALLEKGPRRVSPFFVPMMMPNMAAG 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  74 RVSYYFDLNGPSVTVDTACSSSLSALHLACQSIRNGE---MFnghCGGCHLNITPRGFHRHDTFQvsetgspvtyrs*lV 150
Cdd:COG0304 143 HVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRadvMI---AGGAEAAITPLGLAGFDALG--------------A 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193 151 IPQRLLSDTGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGrTRGIAM-PNGEAQEALIRQV 229
Cdd:COG0304 206 LSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDA-YHITAPaPDGEGAARAMRAA 284

                       250       260
                ....*....|....*....|....*
gi 62083193 230 YEEARIDPSLTAFVEAHGTGTQLGD 254
Cdd:COG0304 285 LKDAGLSPEDIDYINAHGTSTPLGD 309
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 1-255 9.63e-26

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: 104.16  E-value: 9.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   1 REALQMDPQQRIFLECVYEALENAGITSHEITGQKVGVFAGGSYPD-------YEINNTRDATAIPMYASTGTAMSLQAN 73
Cdd:cd00834  63 KELRRMDRFAQFALAAAEEALADAGLDPEELDPERIGVVIGSGIGGlatieeaYRALLEKGPRRVSPFFVPMALPNMAAG 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  74 RVSYYFDLNGPSVTVDTACSSSLSALHLACQSIRNGE---MFnghCGGCHLNITPRGFHRHDTFQVsetgspvtyrs*lv 150
Cdd:cd00834 143 QVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRadvVI---AGGAEALITPLTLAGFAALRA-------------- 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193 151 IPQRLLSDTGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQVY 230
Cdd:cd00834 206 LSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAAL 285

                       250       260
                ....*....|....*....|....*
gi 62083193 231 EEARIDPSLTAFVEAHGTGTQLGDP 255
Cdd:cd00834 286 ADAGLSPEDIDYINAHGTSTPLNDA 310
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 72-254 1.62e-24

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: 102.39  E-value: 1.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193     72 ANRVSYYFDLNGPSVTVDTACSSSLSALHLACQSI---RNGEMFNGhcGGCHLNitprgfhrhdtfqvsetgSPVTYRS* 148
Cdd:TIGR02813  186 SGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELlegRSEMMITG--GVCTDN------------------SPFMYMSF 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193    149 LVIPQRLLSDTGRSYAFDHRGTGFGrgEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQ 228
Cdd:TIGR02813  246 SKTPAFTTNEDIQPFDIDSKGMMIG--EGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKR 323

                          170       180
                   ....*....|....*....|....*.
gi 62083193    229 VYEEARIDPSLTAFVEAHGTGTQLGD 254
Cdd:TIGR02813  324 AYDDAGFAPHTCGLIEAHGTGTAAGD 349
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 5-255 1.05e-23

"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: 98.67  E-value: 1.05e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   5 QMDPQQRIFLECVYEALENAGIT-SHEITGQKVGVFAG---GSYPDYEINNTRDATAIPMYASTgtAMSLQAN----RVS 76
Cdd:cd00828  68 IVDRTTLLALVATEEALADAGITdPYEVHPSEVGVVVGsgmGGLRFLRRGGKLDARAVNPYVSP--KWMLSPNtvagWVN 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  77 YYFDLN-GPSVTVDTACSSSLSALHLACQSIRNGE---MFnghCGGCHLnITPRGFHrhdTFQVSETGSPVTYrs*lvip 152
Cdd:cd00828 146 ILLLSShGPIKTPVGACATALEALDLAVEAIRSGKadiVV---VGGVED-PLEEGLS---GFANMGALSTAEE------- 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193 153 qrllSDTGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIaMPNGEAQEALIRQVYEE 232
Cdd:cd00828 212 ----EPEEMSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSV-PAGGKGIARAIRTALAK 286

                       250       260
                ....*....|....*....|...
gi 62083193 233 ARIDPSLTAFVEAHGTGTQLGDP 255
Cdd:cd00828 287 AGLSLDDLDVISAHGTSTPANDV 309
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 9-255 1.42e-19

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: 84.80  E-value: 1.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   9 QQRIFLECVYEALENAGITSheitGQKVGVFAGGSYPDYEinntrdataipmyastgtaMSLQANRVSYYFDLN-GPSVT 87
Cdd:cd00327   7 ASELGFEAAEQAIADAGLSK----GPIVGVIVGTTGGSGE-------------------FSGAAGQLAYHLGISgGPAYS 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  88 VDTACSSSLSALHLACQSIRNGEMFNGHCGGCHLnitprgfhrhdtfqvsetgspvtyrs*lvipqrllsdtgrsyafdh 167
Cdd:cd00327  64 VNQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------------------------- 97

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193 168 rgtgFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRgIAMPNGEAQEALIRQVYEEARIDPSLTAFVEAHG 247
Cdd:cd00327  98 ----FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASM-VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHG 172


                ....*...
gi 62083193 248 TGTQLGDP 255
Cdd:cd00327 173 TGTPIGDA 180
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 198-255 1.80e-17

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: 75.68  E-value: 1.80e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 62083193   198 SVIINSGLNQDGRTRGIAMPNGEAQEALIRQVYEEARIDPSLTAFVEAHGTGTQLGDP 255
Cdd:pfam02801   2 AVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDP 59
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 17-254 9.71e-15

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 72.80  E-value: 9.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   17 VYEALENAGITSHEITGQ-KVGVFAGgsypdyeinntrdaTAIPMYASTGTAMSLQA----NRVSYYF------------ 79
Cdd:PTZ00050  85 AREALADAKLDILSEKDQeRIGVNIG--------------SGIGSLADLTDEMKTLYekghSRVSPYFipkilgnmaagl 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   80 -----DLNGPSVTVDTACSSSLSALHLACQSIRNGEMFNGHCGGCHLNITP---RGFHRhdtFQVSETGSPVTyrs*lvi 151
Cdd:PTZ00050 151 vaikhKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPvsfAGFSR---MRALCTKYNDD------- 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  152 PQRllsdtgRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGE-AQEALIRQVY 230
Cdd:PTZ00050 221 PQR------ASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRgARRCMENALK 294

                        250       260
                 ....*....|....*....|....
gi 62083193  231 EEARIDPSLTAFVEAHGTGTQLGD 254
Cdd:PTZ00050 295 DGANININDVDYVNAHATSTPIGD 318
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
20-254 6.81e-13

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 67.32  E-value: 6.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   20 ALENAGITSHE-ITGQKVGVFAG---GSYPD-------YEINNTRDATA---IPMYASTgTAmslqANrVSYYFDLNGPS 85
Cdd:PRK09116  84 ALEDAGLLGDPiLTDGRMGIAYGsstGSTDPigafgtmLLEGSMSGITAttyVRMMPHT-TA----VN-VGLFFGLKGRV 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   86 VTVDTACSSSLSALHLACQSIRNGE---MFNGhcGGCHLniTPRGFHRHDTFQVSET--GSPVTyrs*lvipqrllsdTG 160
Cdd:PRK09116 158 IPTSSACTSGSQGIGYAYEAIKYGYqtvMLAG--GAEEL--CPTEAAVFDTLFATSTrnDAPEL--------------TP 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  161 RSyaFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTrgIAMPNGEAQEALIRQVYEEARIDPSLT 240
Cdd:PRK09116 220 RP--FDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAH--VTQPQAETMQIAMELALKDAGLAPEDI 295

                        250
                 ....*....|....
gi 62083193  241 AFVEAHGTGTQLGD 254
Cdd:PRK09116 296 GYVNAHGTATDRGD 309
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
72-250 2.64e-12

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 65.81  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   72 ANRVSYYFDLNGPSVTVDTACSSSLSALHLACQSIRNGEMFNGHCGGCHLNITPRGFHRHDTFQ-VSETGSPvtyrs*lv 150
Cdd:PRK06501 155 ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSaLSTQNDP-------- 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  151 iPQrllsdtGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDG--RTRgiAMPNGEAQEALIRQ 228
Cdd:PRK06501 227 -PE------KASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSfhRTR--SSPDGSPAIGAIRA 297

                        170       180
                 ....*....|....*....|..
gi 62083193  229 VYEEARIDPSLTAFVEAHGTGT 250
Cdd:PRK06501 298 ALADAGLTPEQIDYINAHGTST 319
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 19-254 1.63e-11

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 63.60  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   19 EALENAGITSHEITGQKVGVFAG---GSYPDYE----INNTRDATAIPMYASTGTAMSLQANRVSYYFDLNGPSVTVDTA 91
Cdd:PRK08439  82 EAMKDAGFLPEELDAERFGVSSAsgiGGLPNIEknsiICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   92 CSSSLSALHLACQSIRNGEMFNGHCGGCHLNITPRGF----------HRHDTfqvsetgspvtyrs*lviPQRllsdtgR 161
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIggfaamkalsTRNDD------------------PKK------A 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  162 SYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIInsGLNQDGRTRGIAMPNGEAQEALIRQVYEEA---RIDps 238
Cdd:PRK08439 218 SRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEII--GFGESGDANHITSPAPEGPLRAMKAALEMAgnpKID-- 293

                        250
                 ....*....|....*.
gi 62083193  239 ltaFVEAHGTGTQLGD 254
Cdd:PRK08439 294 ---YINAHGTSTPYND 306
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 165-254 2.85e-11

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 62.74  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  165 FDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGrTRGIAmPNGEAQEALIRQVYEEARIDPSLTAFVE 244
Cdd:PRK07103 228 FDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDA-NRGPD-PSLEGEMRVIRAALRRAGLGPEDIDYVN 305

                         90
                 ....*....|
gi 62083193  245 AHGTGTQLGD 254
Cdd:PRK07103 306 PHGTGSPLGD 315
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
70-254 4.59e-11

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 62.32  E-value: 4.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   70 LQANRVSYYFDLNGPSVTVDTACSSSLSALHLACQSIRNGEMFNGHCGGCHLNITPrgfhrhdtfqVSETGspvtyrs*l 149
Cdd:PRK06333 151 MAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDR----------VSLAG--------- 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  150 VIPQRLLSdTGR-------SYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQ 222
Cdd:PRK06333 212 FAAARALS-TRFndapeqaSRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGA 290

                        170       180       190
                 ....*....|....*....|....*....|..
gi 62083193  223 EALIRQVYEEARIDPSLTAFVEAHGTGTQLGD 254
Cdd:PRK06333 291 RRAMLIALRQAGIPPEEVQHLNAHATSTPVGD 322
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
1-254 1.03e-10

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 60.96  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193    1 REALQMDPQQRIFLECVYEALENAGITSHEITGQKVGVFAG---GSYPDYEINNTRDAT---------AIPMyastgTAM 68
Cdd:PRK07314  64 KEARRMDRFIQYGIAAAKQAVEDAGLEITEENADRIGVIIGsgiGGLETIEEQHITLLEkgprrvspfFVPM-----AII 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   69 SLQANRVSYYFDLNGPSVTVDTACSSSLSALHLACQSIRNGE---MFnghCGGCHLNITPRGF----------HRHDTfq 135
Cdd:PRK07314 139 NMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDadvMV---AGGAEAAITPLGIagfaaaralsTRNDD-- 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  136 vsetgspvtyrs*lviPQRllsdtgRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIA 215
Cdd:PRK07314 214 ----------------PER------ASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAP 271

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 62083193  216 MPNGEAQEALIRQVYEEARIDPSLTAFVEAHGTGTQLGD 254
Cdd:PRK07314 272 APDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGD 310
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 31-254 3.76e-10

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 59.36  E-value: 3.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   31 ITGQKVGVFAGGSYPdYEINNTRDATAIPMYASTGTAMSLQANRVSYYFDLNGPSVTVDTACSSSLSALHLACQSIRNGE 110
Cdd:PRK14691  31 IIGAGIGGFPAIAHA-VRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  111 MFNGHCGGCHlnitprgfhrhdtfQVSETGSPVTYRS*LVIPQRLLSDTGR-SYAFDHRGTGFGRGEGAGCIILKSLEDA 189
Cdd:PRK14691 110 ADVALCGGAE--------------AVIDTVSLAGFAAARALSTHFNSTPEKaSRPFDTARDGFVMGEGAGLLIIEELEHA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62083193  190 EAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQVYEEARIDPSLTAFVEAHGTGTQLGD 254
Cdd:PRK14691 176 LARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGD 240
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
19-254 6.61e-10

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 58.86  E-value: 6.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   19 EALENAGITSHEITGQKVGVFAGGSYPDYEINNT-------RDATAIPMYASTGTAMSLQANRVSYYFDLNGPSVTVDTA 91
Cdd:PRK08722  84 QALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAghqalveKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTA 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   92 CSSSLSALHLACQSIRNGEMFNGHCGGCHLNITPRGfhrhdtfqVSETGSPVTYRS*LVIPQRllsdtgRSYAFDHRGTG 171
Cdd:PRK08722 164 CTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLG--------MAGFGAAKALSTRNDEPQK------ASRPWDKDRDG 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  172 FGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQVYEEARIDPSLTAFVEAHGTGTQ 251
Cdd:PRK08722 230 FVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTP 309


                 ...
gi 62083193  252 LGD 254
Cdd:PRK08722 310 AGD 312
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
156-254 1.08e-08

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 55.06  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  156 LSDTGrSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQVYEEARI 235
Cdd:PRK05952 191 LAKTG-AYPFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGL 269

                         90
                 ....*....|....*....
gi 62083193  236 DPSLTAFVEAHGTGTQLGD 254
Cdd:PRK05952 270 TPEDIDYIHAHGTATRLND 288
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 19-254 1.10e-08

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 55.37  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   19 EALENAGITS---HEITGQKVGVFAGGSYPDYEI-NNTRDATAIPM---------YASTGTAMSLQANRVSYYfdlnGPS 85
Cdd:PLN02787 209 KALADGGITEdvmKELDKTKCGVLIGSAMGGMKVfNDAIEALRISYrkmnpfcvpFATTNMGSAMLAMDLGWM----GPN 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   86 VTVDTACSSSLSALHLACQSIRNGEMFNGHCGGCHLNITPRGFhrhdtfqvsetGSPVTYRS*lvIPQRLLSDTGRSYAF 165
Cdd:PLN02787 285 YSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGL-----------GGFVACRA---LSQRNDDPTKASRPW 350

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  166 DHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALIRQVYEEARIDPSLTAFVEA 245
Cdd:PLN02787 351 DMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINA 430


                 ....*....
gi 62083193  246 HGTGTQLGD 254
Cdd:PLN02787 431 HATSTKAGD 439
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 72-254 1.96e-08

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 54.41  E-value: 1.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   72 ANRVSYYFDLNGPSVTVDTACSSSLSALHLACQSIRNGE---MFNGHCGGCHLNITPRGFHRHDTFQVSETGSPvtyrs* 148
Cdd:PLN02836 164 AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDadvMVAGGTESSIDALSIAGFSRSRALSTKFNSCP------ 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  149 lvipqrllsdTGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTrgIAMPNGEAQEAL--I 226
Cdd:PLN02836 238 ----------TEASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHH--ITQPHEDGRGAVlaM 305

                        170       180
                 ....*....|....*....|....*...
gi 62083193  227 RQVYEEARIDPSLTAFVEAHGTGTQLGD 254
Cdd:PLN02836 306 TRALQQSGLHPNQVDYVNAHATSTPLGD 333
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
82-254 3.67e-07

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 50.50  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   82 NGPSVTVD-------------TACSSSLSALHLACQSIRNGEMFNGHCGGCHLNITprgfhrhdtfqvsetGSPVTYRS* 148
Cdd:PRK07910 148 NGPAAAVGlerhakagvitpvSACASGSEAIAQAWRQIVLGEADIAICGGVETRIE---------------AVPIAGFAQ 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  149 LVIPQRLLSD--TGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTRGIAMPNGEAQEALI 226
Cdd:PRK07910 213 MRIVMSTNNDdpAGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAM 292

                        170       180
                 ....*....|....*....|....*...
gi 62083193  227 RQVYEEARIDPSLTAFVEAHGTGTQLGD 254
Cdd:PRK07910 293 TRAIELAGLTPGDIDHVNAHATGTSVGD 320
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 12-110 7.64e-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: 46.49  E-value: 7.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  12 IFLECVYEALENAGITSHEItgqkVGVFAGgsypdyeinntrdataipmYASTGTAMSLQANRVSYYFDLNG-PSVTVDT 90
Cdd:cd00829  19 LAAEAARAALDDAGLEPADI----DAVVVG-------------------NAAGGRFQSFPGALIAEYLGLLGkPATRVEA 75

                        90       100
                ....*....|....*....|
gi 62083193  91 ACSSSLSALHLACQSIRNGE 110
Cdd:cd00829  76 AGASGSAAVRAAAAAIASGL 95
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 84-111 9.97e-05

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: 42.85  E-value: 9.97e-05
                        10        20
                ....*....|....*....|....*...
gi 62083193  84 PSVTVDTACSSSLSALHLACQSIRNGEM 111
Cdd:cd00751  76 PATTVNRVCGSGLQAVALAAQSIAAGEA 103
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
19-255 1.33e-04

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 42.74  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   19 EALENAGITSHEITGQKVGVFAGGSYPD-YEINNTRDAT-------AIPMYASTGTAMSLQANRVSYYFDLNGPSVTVDT 90
Cdd:PRK07967  81 QAIADAGLSEEQVSNPRTGLIAGSGGGStRNQVEAADAMrgprgpkRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   91 ACSSSLSALHLACQSIRNGE---MFNGHCGGCHLNITprgfhrhdtFQVSETGSPVTYRS*lvIPQRllsdtgRSYAFDH 167
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKqdiVFAGGGEELDWEMS---------CLFDAMGALSTKYND--TPEK------ASRAYDA 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  168 RGTGFGRGEGAGCIILKSLEDAEAAGDVIRSVIINSGLNQDGRTrgIAMPNGEAQEALIRQVYE--EARIDpsltaFVEA 245
Cdd:PRK07967 224 NRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYD--MVAPSGEGAVRCMQMALAtvDTPID-----YINT 296

                        250
                 ....*....|
gi 62083193  246 HGTGTQLGDP 255
Cdd:PRK07967 297 HGTSTPVGDV 306
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 84-110 2.31e-04

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: 41.52  E-value: 2.31e-04
                          10        20
                  ....*....|....*....|....*..
gi 62083193    84 PSVTVDTACSSSLSALHLACQSIRNGE 110
Cdd:pfam00108  77 PAVTINKVCGSGLKAVYLAAQSIASGD 103
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 84-111 5.91e-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: 40.43  E-value: 5.91e-04
                        10        20
                ....*....|....*....|....*...
gi 62083193  84 PSVTVDTACSSSLSALHLACQSIRNGEM 111
Cdd:COG0183  80 PAVTVNRVCGSGLQAVALAAQAIAAGDA 107
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
72-254 7.46e-04

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 40.21  E-value: 7.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   72 ANRVSYYFDLNGPSVTVDTACSSSLSALHLACQSIRNGEMFNGHCGG----CHLniTPRGFHrhdtfqvsetgspvtyrs 147
Cdd:PRK09185 140 ADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGvdslCRL--TLNGFN------------------ 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193  148 *LvipqRLLSDtGRSYAFDHRGTGFGRGEGAGCIILKSLEDAEAAgdvirsvIINSGLNQDGRTRGIAMPNGEAQEALIR 227
Cdd:PRK09185 200 SL----ESLSP-QPCRPFSANRDGINIGEAAAFFLLEREDDAAVA-------LLGVGESSDAHHMSAPHPEGLGAILAMQ 267

                        170       180
                 ....*....|....*....|....*..
gi 62083193  228 QVYEEARIDPSLTAFVEAHGTGTQLGD 254
Cdd:PRK09185 268 QALADAGLAPADIGYINLHGTATPLND 294
PRK07516 PRK07516
thiolase domain-containing protein;
19-110 2.72e-03

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 38.39  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62083193   19 EALENAGITSHEITGQKVGVFAGGSYPDyeinntrDATAipmyastgtAMSLQANRvsyyfDL-NGPSVTVDTACSSSLS 97
Cdd:PRK07516  32 EALAHAGIAAGDVDGIFLGHFNAGFSPQ-------DFPA---------SLVLQADP-----ALrFKPATRVENACATGSA 90

                         90
                 ....*....|...
gi 62083193   98 ALHLACQSIRNGE 110
Cdd:PRK07516  91 AVYAALDAIEAGR 103
 
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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