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Conserved domains on  [gi|31979201|gb|AAP68701|]
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polyketide synthase, partial [fungal endophyte sp. CR475]

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 ...
 1-229 9.67e-102

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: 301.01  E-value: 9.67e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   1 APQVDPAQRLALMTVYEAVERSGIVADatpSTRRDRVGVFYGVTGNDWAETNSAQ--DIDMYLIPGGNRAFIPGRINYFY 78
Cdd:cd00833  81 AEAMDPQQRLLLEVAWEALEDAGYSPE---SLAGSRTGVFVGASSSDYLELLARDpdEIDAYAATGTSRAFLANRISYFF 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  79 KFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGNCKTFDDTADGYCRAEGV 158
Cdd:cd00833 158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGV 237

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31979201 159 GTVIIKRLEDAEADNDPILAVILDASTNHSSESESITRPHAGAQRAIFSKLMNQGVVDPKSVGYIEMHGTG 229
Cdd:cd00833 238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTG 308
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 1-229 9.67e-102

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: 301.01  E-value: 9.67e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   1 APQVDPAQRLALMTVYEAVERSGIVADatpSTRRDRVGVFYGVTGNDWAETNSAQ--DIDMYLIPGGNRAFIPGRINYFY 78
Cdd:cd00833  81 AEAMDPQQRLLLEVAWEALEDAGYSPE---SLAGSRTGVFVGASSSDYLELLARDpdEIDAYAATGTSRAFLANRISYFF 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  79 KFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGNCKTFDDTADGYCRAEGV 158
Cdd:cd00833 158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGV 237

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31979201 159 GTVIIKRLEDAEADNDPILAVILDASTNHSSESESITRPHAGAQRAIFSKLMNQGVVDPKSVGYIEMHGTG 229
Cdd:cd00833 238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTG 308
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 1-205 7.23e-80

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: 241.08  E-value: 7.23e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201      1 APQVDPAQRLALMTVYEAVERSGIVADATPSTRrdrVGVFYGVTGNDWaetnsaqdidmylipggnrafipgrinyfykf 80
Cdd:smart00825  45 AEAMDPQQRLLLEVAWEALEDAGIDPESLRGSR---TGVFVGVSSSDY-------------------------------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201     81 sgpSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGNCKTFDDTADGYCRAEGVGT 160
Cdd:smart00825  90 ---SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGV 166

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 31979201    161 VIIKRLEDAEADNDPILAVILDASTNHSSESESITRPHAGAQRAI 205
Cdd:smart00825 167 VVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQLLI 211
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-229 9.41e-80

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 259.80  E-value: 9.41e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201    1 APQVDPAQRLALMTVYEAVERSGIVADatpSTRRDRVGVFYGVTGNDWAE--TNSAQDIDMYLIPGGNRAFIPGRINYFY 78
Cdd:COG3321   85 AEAMDPQQRLLLEVAWEALEDAGYDPE---SLAGSRTGVFVGASSNDYALllLADPEAIDAYALTGNAKSVLAGRISYKL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   79 KFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGNCKTFDDTADGYCRAEGV 158
Cdd:COG3321  162 DLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGV 241

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31979201  159 GTVIIKRLEDAEADNDPILAVILDASTNHSSESESITRPHAGAQ-RAIFSKLMNQGvVDPKSVGYIEMHGTG 229
Cdd:COG3321  242 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQaAVIRRALADAG-VDPATVDYVEAHGTG 312
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 1-169 3.56e-59

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: 186.69  E-value: 3.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201     1 APQVDPAQRLALMTVYEAVERSGIVADatpSTRRDRVGVFYGVTGNDWAE----TNSAQDIDMY-LIPGGNRAFIPGRIN 75
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPD---SLDGSRTGVFIGSGIGDYAAllllDEDGGPRRGSpFAVGTMPSVIAGRIS 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201    76 YFYKFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGNCKTFDDTADGYCRA 155
Cdd:pfam00109 158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRG 237

                         170
                  ....*....|....
gi 31979201   156 EGVGTVIIKRLEDA 169
Cdd:pfam00109 238 EGVGAVVLKRLSDA 251
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 5-229 5.67e-19

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 84.36  E-value: 5.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201    5 DPAQRLALMTVYEAVERSGIvaDATPSTRRDRVGVFYGVTGNDWAETNSA---------QDIDMYLIPG--GNRAfiPGR 73
Cdd:PTZ00050  75 SRATHFAMAAAREALADAKL--DILSEKDQERIGVNIGSGIGSLADLTDEmktlyekghSRVSPYFIPKilGNMA--AGL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   74 INYFYKFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGN------CKTFDD 147
Cdd:PTZ00050 151 VAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYNddpqraSRPFDK 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  148 TADGYCRAEGVGTVIIKRLEDAEADNDPILAVILDASTnhSSESESITRPHA---GAQRAIFSKLMNQGVVDPKSVGYIE 224
Cdd:PTZ00050 231 DRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGS--SSDAHHITAPHPdgrGARRCMENALKDGANININDVDYVN 308


                 ....*
gi 31979201  225 MHGTG 229
Cdd:PTZ00050 309 AHATS 313
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 1-229 9.67e-102

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: 301.01  E-value: 9.67e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   1 APQVDPAQRLALMTVYEAVERSGIVADatpSTRRDRVGVFYGVTGNDWAETNSAQ--DIDMYLIPGGNRAFIPGRINYFY 78
Cdd:cd00833  81 AEAMDPQQRLLLEVAWEALEDAGYSPE---SLAGSRTGVFVGASSSDYLELLARDpdEIDAYAATGTSRAFLANRISYFF 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  79 KFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGNCKTFDDTADGYCRAEGV 158
Cdd:cd00833 158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGV 237

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31979201 159 GTVIIKRLEDAEADNDPILAVILDASTNHSSESESITRPHAGAQRAIFSKLMNQGVVDPKSVGYIEMHGTG 229
Cdd:cd00833 238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTG 308
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 1-205 7.23e-80

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: 241.08  E-value: 7.23e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201      1 APQVDPAQRLALMTVYEAVERSGIVADATPSTRrdrVGVFYGVTGNDWaetnsaqdidmylipggnrafipgrinyfykf 80
Cdd:smart00825  45 AEAMDPQQRLLLEVAWEALEDAGIDPESLRGSR---TGVFVGVSSSDY-------------------------------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201     81 sgpSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGNCKTFDDTADGYCRAEGVGT 160
Cdd:smart00825  90 ---SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGV 166

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 31979201    161 VIIKRLEDAEADNDPILAVILDASTNHSSESESITRPHAGAQRAI 205
Cdd:smart00825 167 VVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQLLI 211
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-229 9.41e-80

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 259.80  E-value: 9.41e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201    1 APQVDPAQRLALMTVYEAVERSGIVADatpSTRRDRVGVFYGVTGNDWAE--TNSAQDIDMYLIPGGNRAFIPGRINYFY 78
Cdd:COG3321   85 AEAMDPQQRLLLEVAWEALEDAGYDPE---SLAGSRTGVFVGASSNDYALllLADPEAIDAYALTGNAKSVLAGRISYKL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   79 KFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGNCKTFDDTADGYCRAEGV 158
Cdd:COG3321  162 DLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGV 241

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31979201  159 GTVIIKRLEDAEADNDPILAVILDASTNHSSESESITRPHAGAQ-RAIFSKLMNQGvVDPKSVGYIEMHGTG 229
Cdd:COG3321  242 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQaAVIRRALADAG-VDPATVDYVEAHGTG 312
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 1-169 3.56e-59

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: 186.69  E-value: 3.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201     1 APQVDPAQRLALMTVYEAVERSGIVADatpSTRRDRVGVFYGVTGNDWAE----TNSAQDIDMY-LIPGGNRAFIPGRIN 75
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPD---SLDGSRTGVFIGSGIGDYAAllllDEDGGPRRGSpFAVGTMPSVIAGRIS 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201    76 YFYKFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGNCKTFDDTADGYCRA 155
Cdd:pfam00109 158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRG 237

                         170
                  ....*....|....
gi 31979201   156 EGVGTVIIKRLEDA 169
Cdd:pfam00109 238 EGVGAVVLKRLSDA 251
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 1-229 1.04e-25

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: 103.00  E-value: 1.04e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   1 APQVDPAQRLALMTVYEAVERSGIVADATPstrRDRVGVFYGVTgndWAETNSAQDIDMYLIPGGNRAFIPGRINYF--- 77
Cdd:cd00834  65 LRRMDRFAQFALAAAEEALADAGLDPEELD---PERIGVVIGSG---IGGLATIEEAYRALLEKGPRRVSPFFVPMAlpn 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  78 ---------YKFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGN-----CK 143
Cdd:cd00834 139 maagqvairLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDdpekaSR 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201 144 TFDDTADGYCRAEGVGTVIIKRLEDAEADNDPILAVILDASTnhSSESESITRPH---AGAQRAIfSKLMNQGVVDPKSV 220
Cdd:cd00834 219 PFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGA--SSDAYHITAPDpdgEGAARAM-RAALADAGLSPEDI 295


                ....*....
gi 31979201 221 GYIEMHGTG 229
Cdd:cd00834 296 DYINAHGTS 304
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 5-229 1.47e-25

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: 102.87  E-value: 1.47e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   5 DPAQRLALMTVYEAVERSGIVADATPstrRDRVGVFYGVTGNDWAETNSAQDIdmyLIPGGNRA----FIP--------G 72
Cdd:COG0304  69 DRFTQYALAAAREALADAGLDLDEVD---PDRTGVIIGSGIGGLDTLEEAYRA---LLEKGPRRvspfFVPmmmpnmaaG 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  73 RINYFYKFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSkTGN------CKTFD 146
Cdd:COG0304 143 HVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALS-TRNddpekaSRPFD 221

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201 147 DTADGYCRAEGVGTVIIKRLEDAEADNDPILAVILDASTnhSSESESITRPH---AGAQRAIfSKLMNQGVVDPKSVGYI 223
Cdd:COG0304 222 KDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGA--SSDAYHITAPApdgEGAARAM-RAALKDAGLSPEDIDYI 298


                ....*.
gi 31979201 224 EMHGTG 229
Cdd:COG0304 299 NAHGTS 304
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 7-229 1.95e-25

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: 101.56  E-value: 1.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   7 AQRLALMTVYEAVERSGIVADATPSTRrdrVGVFYGVTGNDWAETNSAQD----IDMYLIPGGNRAFIPGRINYFYKFSG 82
Cdd:cd00825  11 VSILGFEAAERAIADAGLSREYQKNPI---VGVVVGTGGGSPRFQVFGADamraVGPYVVTKAMFPGASGQIATPLGIHG 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  83 PSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGNCKTFDDTADGYCRAEGVGTVI 162
Cdd:cd00825  88 PAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALV 167

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31979201 163 IKRLEDAEADNDPILAVILDASTNHSSESESITRPHAGAQRAIFSKLMNQGVVDPKSVGYIEMHGTG 229
Cdd:cd00825 168 VEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTG 234
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 3-229 6.04e-21

"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: 90.19  E-value: 6.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   3 QVDPAQRLALMTVYEAVERSGIvADATPSTRrDRVGVFYGVTGNDWAET-----NSAQDIDMYLIPGGNRA--FIPGRIN 75
Cdd:cd00828  68 IVDRTTLLALVATEEALADAGI-TDPYEVHP-SEVGVVVGSGMGGLRFLrrggkLDARAVNPYVSPKWMLSpnTVAGWVN 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  76 YFYKFS-GPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTnPDFHAGLDRGGFLSKTGN-----CKTFDDTA 149
Cdd:cd00828 146 ILLLSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL-EEGLSGFANMGALSTAEEepeemSRPFDETR 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201 150 DGYCRAEGVGTVIIKRLEDAEADNDPILAVILDASTNHSSESESITRPHAGAQRAIfSKLMNQGVVDPKSVGYIEMHGTG 229
Cdd:cd00828 225 DGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGIARAI-RTALAKAGLSLDDLDVISAHGTS 303
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 5-229 5.67e-19

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 84.36  E-value: 5.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201    5 DPAQRLALMTVYEAVERSGIvaDATPSTRRDRVGVFYGVTGNDWAETNSA---------QDIDMYLIPG--GNRAfiPGR 73
Cdd:PTZ00050  75 SRATHFAMAAAREALADAKL--DILSEKDQERIGVNIGSGIGSLADLTDEmktlyekghSRVSPYFIPKilGNMA--AGL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   74 INYFYKFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGN------CKTFDD 147
Cdd:PTZ00050 151 VAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYNddpqraSRPFDK 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  148 TADGYCRAEGVGTVIIKRLEDAEADNDPILAVILDASTnhSSESESITRPHA---GAQRAIFSKLMNQGVVDPKSVGYIE 224
Cdd:PTZ00050 231 DRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGS--SSDAHHITAPHPdgrGARRCMENALKDGANININDVDYVN 308


                 ....*
gi 31979201  225 MHGTG 229
Cdd:PTZ00050 309 AHATS 313
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
4-228 1.29e-13

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 69.05  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201    4 VDPAQRLALMTVYEAVERSGIVADATpstRRDRVGVFYGvTGNDWAETNSAQDIDMYliPGGNRA----FIPGRI-NYF- 77
Cdd:PRK07314  69 MDRFIQYGIAAAKQAVEDAGLEITEE---NADRIGVIIG-SGIGGLETIEEQHITLL--EKGPRRvspfFVPMAIiNMAa 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   78 ------YKFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPdfhagLDRGGF-----LSkTGN----- 141
Cdd:PRK07314 143 ghvsirYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITP-----LGIAGFaaaraLS-TRNddper 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  142 -CKTFDDTADGYCRAEGVGTVIIKRLEDAEADNDPILAVILDAStnHSSESESITRPH---AGAQRAIFSKLMNQGvVDP 217
Cdd:PRK07314 217 aSRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYG--MTGDAYHMTAPApdgEGAARAMKLALKDAG-INP 293

                        250
                 ....*....|.
gi 31979201  218 KSVGYIEMHGT 228
Cdd:PRK07314 294 EDIDYINAHGT 304
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 69-228 2.36e-13

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 68.28  E-value: 2.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   69 FIP--------GRINYFYKFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTG 140
Cdd:PLN02836 154 FVPrilinmaaGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKF 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  141 N------CKTFDDTADGYCRAEGVGTVIIKRLEDAEADNDPILAVIldASTNHSSESESITRPHAGAQRAIF--SKLMNQ 212
Cdd:PLN02836 234 NscpteaSRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEV--RGYGMSGDAHHITQPHEDGRGAVLamTRALQQ 311

                        170
                 ....*....|....*.
gi 31979201  213 GVVDPKSVGYIEMHGT 228
Cdd:PLN02836 312 SGLHPNQVDYVNAHAT 327
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
71-228 1.68e-12

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 65.79  E-value: 1.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   71 PGRINYFYKFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATnimtnpdfHAGLDR---GGF-----LSKTGN- 141
Cdd:PRK06333 153 AGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGT--------EAAIDRvslAGFaaaraLSTRFNd 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  142 -----CKTFDDTADGYCRAEGVGTVIIKRLEDAEADNDPILAVILDASTnhSSESESITRPH---AGAQRAIFSKLmNQG 213
Cdd:PRK06333 225 apeqaSRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGT--SADAYHMTAGPedgEGARRAMLIAL-RQA 301

                        170
                 ....*....|....*
gi 31979201  214 VVDPKSVGYIEMHGT 228
Cdd:PRK06333 302 GIPPEEVQHLNAHAT 316
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 177-229 4.42e-10

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: 55.27  E-value: 4.42e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 31979201   177 LAVILDASTNHSSESESITRPHAGAQRAIFSKLMNQGVVDPKSVGYIEMHGTG 229
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTG 53
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
89-229 4.65e-10

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 58.49  E-value: 4.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   89 TACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDfhaGLDRGGFLS--KTGN------CKTFDDTADGYCRAEGVGT 160
Cdd:PRK06501 173 TACASGATAIQLGVEAIRRGETDRALCIATDGSVSAE---ALIRFSLLSalSTQNdppekaSKPFSKDRDGFVMAEGAGA 249

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31979201  161 VIIKRLEDAEADNDPILAVILD----ASTNHSSESESITRPHAGAQRAifsKLMNQGvVDPKSVGYIEMHGTG 229
Cdd:PRK06501 250 LVLESLESAVARGAKILGIVAGcgekADSFHRTRSSPDGSPAIGAIRA---ALADAG-LTPEQIDYINAHGTS 318
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 9-229 1.72e-09

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 56.96  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201    9 RLALMTVYEAVERSGivADATPstrRDRVGVFygVTGNDWAETNSAQDIDMYlipGGNRAFIP-------------GRIN 75
Cdd:PRK07103  82 QAALAAAREAWRDAA--LGPVD---PDRIGLV--VGGSNLQQREQALVHETY---RDRPAFLRpsyglsfmdtdlvGLCS 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   76 YFYKFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIA-GATNIMTNPDFHAGLDRGGFLSKTGN------CKTFDDT 148
Cdd:PRK07103 152 EQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAvGALMDLSYWECQALRSLGAMGSDRFAdepeaaCRPFDQD 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  149 ADGYCRAEGVGTVIIKRLEDAEADNDPILAVI------LDA--STNHSSESESitrphagaqRAIFSKLMNQGvVDPKSV 220
Cdd:PRK07103 232 RDGFIYGEACGAVVLESAESARRRGARPYAKLlgwsmrLDAnrGPDPSLEGEM---------RVIRAALRRAG-LGPEDI 301


                 ....*....
gi 31979201  221 GYIEMHGTG 229
Cdd:PRK07103 302 DYVNPHGTG 310
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 7-229 2.06e-09

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: 55.91  E-value: 2.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   7 AQRLALMTVYEAVERSGIVADAtpstrrdRVGVFYGVTGNDWAETNSAQDIDMYL-IPGGnrafipgrinyfykfsgPSY 85
Cdd:cd00327   7 ASELGFEAAEQAIADAGLSKGP-------IVGVIVGTTGGSGEFSGAAGQLAYHLgISGG-----------------PAY 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  86 AVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTnpdfhagldrggflsktgncktfddtadgycRAEGVGTVIIKR 165
Cdd:cd00327  63 SVNQACATGLTALALAVQQVQNGKADIVLAGGSEEFV-------------------------------FGDGAAAAVVES 111

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31979201 166 LEDAEADNDPILAVILDASTnHSSESESITRPHAGAQRAIFSKLMNQGVVDPKSVGYIEMHGTG 229
Cdd:cd00327 112 EEHALRRGAHPQAEIVSTAA-TFDGASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTG 174
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 82-228 1.76e-08

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 54.21  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   82 GPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPdfhAGLdrGGF-----LSKTGN-----CKTFDDTADG 151
Cdd:PLN02787 282 GPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIP---IGL--GGFvacraLSQRNDdptkaSRPWDMNRDG 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  152 YCRAEGVGTVIIKRLEDAEADNDPILAVILDAStnHSSESESITRPH---AGAQRAIFSKLMNQGvVDPKSVGYIEMHGT 228
Cdd:PLN02787 357 FVMGEGAGVLLLEELEHAKKRGANIYAEFLGGS--FTCDAYHMTEPHpegAGVILCIEKALAQSG-VSKEDVNYINAHAT 433
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
57-228 2.47e-08

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 53.47  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   57 IDMYLIPGGNRAFIPGRINYFYKFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFL 136
Cdd:PRK08722 130 VSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKAL 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  137 SKTGN-----CKTFDDTADGYCRAEGVGTVIIKRLEDAEADNDPILAVILdaSTNHSSESESITRPH---AGAQRAIFSK 208
Cdd:PRK08722 210 STRNDepqkaSRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELV--GFGMSGDAYHMTSPSedgSGGALAMEAA 287

                        170       180
                 ....*....|....*....|
gi 31979201  209 LMNQGVVDPKsVGYIEMHGT 228
Cdd:PRK08722 288 MRDAGVTGEQ-IGYVNAHGT 306
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 49-228 3.87e-08

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 52.81  E-value: 3.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   49 AETNSAQDIDMYLIPGGNRAFIPGRINYFYKFSGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHA 128
Cdd:PRK14691  49 SDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLA 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  129 GLDRGGFLSKTGN------CKTFDDTADGYCRAEGVGTVIIKRLEDAEADNDPILAVILDASTNHSS-ESESITRPHAGA 201
Cdd:PRK14691 129 GFAAARALSTHFNstpekaSRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAyHMTSGAEDGDGA 208

                        170       180
                 ....*....|....*....|....*..
gi 31979201  202 QRAIFSKLMNQGVVdPKSVGYIEMHGT 228
Cdd:PRK14691 209 YRAMKIALRQAGIT-PEQVQHLNAHAT 234
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
145-229 2.39e-07

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 50.37  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  145 FDDTADGYCRAEGVGTVIIKRLEDAEADNDPILAVILDASTNhsSESESITRPHAGAQRAIFSKLMNQGVVDPKSVGYIE 224
Cdd:PRK09116 222 FDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTN--SDGAHVTQPQAETMQIAMELALKDAGLAPEDIGYVN 299


                 ....*
gi 31979201  225 MHGTG 229
Cdd:PRK09116 300 AHGTA 304
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 9-228 7.85e-07

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 48.96  E-value: 7.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201    9 RLALMTVYEAVERSGIVADATPStrrDRVGVFY--GVTGNDWAETNSA-------QDIDMYLIPGGNRAFIPGRINYFYK 79
Cdd:PRK08439  74 QLGLKAAREAMKDAGFLPEELDA---ERFGVSSasGIGGLPNIEKNSIicfekgpRKISPFFIPSALVNMLGGFISIEHG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   80 FSGPSYAVDTACSSAMSAIHIACNSLWRGDTD-CCIAGATNIMTnpdfhaGLDRGGFLS----KTGN------CKTFDDT 148
Cdd:PRK08439 151 LKGPNLSSVTACAAGTHAIIEAVKTIMLGGADkMLVVGAESAIC------PVGIGGFAAmkalSTRNddpkkaSRPFDKD 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201  149 ADGYCRAEGVGTVIIKRLEDAEADNDPILAVIldASTNHSSESESITRPHA-GAQRAIFSKLMNQGvvDPKsVGYIEMHG 227
Cdd:PRK08439 225 RDGFVMGEGAGALVLEEYESAKKRGAKIYAEI--IGFGESGDANHITSPAPeGPLRAMKAALEMAG--NPK-IDYINAHG 299


                 .
gi 31979201  228 T 228
Cdd:PRK08439 300 T 300
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
81-229 6.23e-06

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 46.20  E-value: 6.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   81 SGPSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTNPDFHAGLDRGGFLSKTGnCKTFDDTADGYCRAEGVGT 160
Cdd:PRK05952 136 QGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AYPFDRQREGLVLGEGGAI 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31979201  161 VIIKRLEDAEADNDPILAVIL------DAstNHSSESESITRphaGAQRAIFSKLMNQGVvDPKSVGYIEMHGTG 229
Cdd:PRK05952 215 LVLESAELAQKRGAKIYGQILgfgltcDA--YHMSAPEPDGK---SAIAAIQQCLARSGL-TPEDIDYIHAHGTA 283
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
89-229 1.73e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 45.11  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   89 TACSSAMSAIHIACNSLWRGDTDCCIAGA--TNIMTNPDfhAGLDRGGFLSKTGN------CKTFDDTADGYCRAEGVGT 160
Cdd:PRK07910 169 SACASGSEAIAQAWRQIVLGEADIAICGGveTRIEAVPI--AGFAQMRIVMSTNNddpagaCRPFDKDRDGFVFGEGGAL 246

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31979201  161 VIIKRLEDAEADNDPILAVILDASTnhSSESESITRPH---AGAQRAIFSKLMNQGvVDPKSVGYIEMHGTG 229
Cdd:PRK07910 247 MVIETEEHAKARGANILARIMGASI--TSDGFHMVAPDpngERAGHAMTRAIELAG-LTPGDIDHVNAHATG 315
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
81-229 2.12e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 44.45  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201   81 SGPSYAVDTACSSamSAIHIAcnSLWR----GDTDCCIAGATN---IMTNPDFHAgLDrggFLSKtGNCKTFDDTADGYC 153
Cdd:PRK09185 150 SGPAYTISTACSS--SAKVFA--SARRlleaGLCDAAIVGGVDslcRLTLNGFNS-LE---SLSP-QPCRPFSANRDGIN 220

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31979201  154 RAEGVGTVIIKRLEDAEadndpilavILDASTNHSSESESITRPH---AGAQRAIFSKLMNQGVvDPKSVGYIEMHGTG 229
Cdd:PRK09185 221 IGEAAAFFLLEREDDAA---------VALLGVGESSDAHHMSAPHpegLGAILAMQQALADAGL-APADIGYINLHGTA 289
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 83-136 6.89e-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: 43.24  E-value: 6.89e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 31979201  83 PSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTN-PDFHAGLDRGGFL 136
Cdd:cd00751  76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRaPYLLPKARRGGRL 130
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 83-158 1.65e-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: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979201    83 PSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTN------PDFHAGLDRG-----GFLSKTGNCKTFDD---- 147
Cdd:pfam00108  77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHapyalpTDARSGLKHGdekkhDLLIPDGLTDAFNGyhmg 156

                          90
                  ....*....|..
gi 31979201   148 -TADGYCRAEGV 158
Cdd:pfam00108 157 lTAENVAKKYGI 168
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 83-123 1.91e-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: 41.59  E-value: 1.91e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 31979201  83 PSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTN 123
Cdd:COG0183  80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSR 120
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
83-146 2.13e-03

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 38.47  E-value: 2.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31979201   83 PSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATNIMTnPDFHAGLDRGGflSKTGNCKTFD 146
Cdd:PRK06633  81 PGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMS-LGMHGSYIRAG--AKFGDIKMVD 141
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
 83-132 6.19e-03

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 37.25  E-value: 6.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 31979201   83 PSYAVDTACSSAMSAIHIACNSLWRGDTDCCIAGATN------IMTNPDFHAGLDR 132
Cdd:PRK08947  83 PAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEhmghvpMNHGVDFHPGLSK 138
 
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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