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Conserved domains on  [gi|31979197|gb|AAP68699|]
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polyketide synthase, partial [fungal endophyte sp. CR38]

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 1.73e-103

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: 305.64  E-value: 1.73e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   1 AFQTDPMQRMALTTAYEALEMSGYVPNrtpSTRLDRIGTFYGQTSDDWREINAAQ--QVDTYFITGGVRAFGPGRINYHF 78
Cdd:cd00833  81 AEAMDPQQRLLLEVAWEALEDAGYSPE---SLAGSRTGVFVGASSSDYLELLARDpdEIDAYAATGTSRAFLANRISYFF 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  79 GFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGPCATFDNDADGYCRGDGC 158
Cdd:cd00833 158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGV 237

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31979197 159 ASVIVKRLEDAIADEDRVLAVILGTATNHSADAISITHPHGPTQSILSRSILDEAGVDPVDVDYVEMHGTG 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 1.73e-103

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: 305.64  E-value: 1.73e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   1 AFQTDPMQRMALTTAYEALEMSGYVPNrtpSTRLDRIGTFYGQTSDDWREINAAQ--QVDTYFITGGVRAFGPGRINYHF 78
Cdd:cd00833  81 AEAMDPQQRLLLEVAWEALEDAGYSPE---SLAGSRTGVFVGASSSDYLELLARDpdEIDAYAATGTSRAFLANRISYFF 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  79 GFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGPCATFDNDADGYCRGDGC 158
Cdd:cd00833 158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGV 237

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31979197 159 ASVIVKRLEDAIADEDRVLAVILGTATNHSADAISITHPHGPTQSILSRSILDEAGVDPVDVDYVEMHGTG 229
Cdd:cd00833 238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTG 308
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-229 1.18e-78

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 256.72  E-value: 1.18e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197    1 AFQTDPMQRMALTTAYEALEMSGYVPNRTPSTRldrIGTFYGQTSDDW--REINAAQQVDTYFITGGVRAFGPGRINYHF 78
Cdd:COG3321   85 AEAMDPQQRLLLEVAWEALEDAGYDPESLAGSR---TGVFVGASSNDYalLLLADPEAIDAYALTGNAKSVLAGRISYKL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   79 GFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGPCATFDNDADGYCRGDGC 158
Cdd:COG3321  162 DLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGV 241

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31979197  159 ASVIVKRLEDAIADEDRVLAVILGTATNHSADAISITHPHGPTQSILSRSILDEAGVDPVDVDYVEMHGTG 229
Cdd:COG3321  242 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTG 312
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 1-202 7.03e-77

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: 233.38  E-value: 7.03e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197      1 AFQTDPMQRMALTTAYEALEMSGYVPNRTPSTRldrIGTFYGQTSDDWreinaaqqvdtyfitggvrafgpgrinyhfgf 80
Cdd:smart00825  45 AEAMDPQQRLLLEVAWEALEDAGIDPESLRGSR---TGVFVGVSSSDY-------------------------------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197     81 sgpSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGPCATFDNDADGYCRGDGCAS 160
Cdd:smart00825  90 ---SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGV 166

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 31979197    161 VIVKRLEDAIADEDRVLAVILGTATNHSADAISITHPHGPTQ 202
Cdd:smart00825 167 VVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ 208
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 1-169 9.35e-54

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: 173.20  E-value: 9.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197     1 AFQTDPMQRMALTTAYEALEMSGYVPNRTPSTRLDR-IGTFYGQTSDDWREINAAQQVDTY-FITGGVRAFGPGRINYHF 78
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVfIGSGIGDYAALLLLDEDGGPRRGSpFAVGTMPSVIAGRISYFL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197    79 GFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGPCATFDNDADGYCRGDGC 158
Cdd:pfam00109 161 GLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGV 240

                         170
                  ....*....|.
gi 31979197   159 ASVIVKRLEDA 169
Cdd:pfam00109 241 GAVVLKRLSDA 251
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 5-229 4.67e-16

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 76.27  E-value: 4.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197    5 DPMQRMALTTAYEALEMSGYVPNrtPSTRLDRIGTFYGQTSDDWREINAA---------QQVDTYFITGGVRAFGPGRIN 75
Cdd:PTZ00050  75 SRATHFAMAAAREALADAKLDIL--SEKDQERIGVNIGSGIGSLADLTDEmktlyekghSRVSPYFIPKILGNMAAGLVA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   76 YHFGFSGPSLNIDTACSSSAAAMQVActALWAR--DCDTAIVGGLSCMTNPDIFSGLSRGQFLSKK---GP---CATFDN 147
Cdd:PTZ00050 153 IKHKLKGPSGSAVTACATGAHCIGEA--FRWIKygEADIMICGGTEASITPVSFAGFSRMRALCTKyndDPqraSRPFDK 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  148 DADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTATnhSADAISITHPH----GPTQSILSrSILDEAGVDPVDVDYV 223
Cdd:PTZ00050 231 DRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGS--SSDAHHITAPHpdgrGARRCMEN-ALKDGANININDVDYV 307


                 ....*.
gi 31979197  224 EMHGTG 229
Cdd:PTZ00050 308 NAHATS 313
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 1-229 1.73e-103

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: 305.64  E-value: 1.73e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   1 AFQTDPMQRMALTTAYEALEMSGYVPNrtpSTRLDRIGTFYGQTSDDWREINAAQ--QVDTYFITGGVRAFGPGRINYHF 78
Cdd:cd00833  81 AEAMDPQQRLLLEVAWEALEDAGYSPE---SLAGSRTGVFVGASSSDYLELLARDpdEIDAYAATGTSRAFLANRISYFF 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  79 GFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGPCATFDNDADGYCRGDGC 158
Cdd:cd00833 158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGV 237

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31979197 159 ASVIVKRLEDAIADEDRVLAVILGTATNHSADAISITHPHGPTQSILSRSILDEAGVDPVDVDYVEMHGTG 229
Cdd:cd00833 238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTG 308
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-229 1.18e-78

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 256.72  E-value: 1.18e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197    1 AFQTDPMQRMALTTAYEALEMSGYVPNRTPSTRldrIGTFYGQTSDDW--REINAAQQVDTYFITGGVRAFGPGRINYHF 78
Cdd:COG3321   85 AEAMDPQQRLLLEVAWEALEDAGYDPESLAGSR---TGVFVGASSNDYalLLLADPEAIDAYALTGNAKSVLAGRISYKL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   79 GFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGPCATFDNDADGYCRGDGC 158
Cdd:COG3321  162 DLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGV 241

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31979197  159 ASVIVKRLEDAIADEDRVLAVILGTATNHSADAISITHPHGPTQSILSRSILDEAGVDPVDVDYVEMHGTG 229
Cdd:COG3321  242 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTG 312
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 1-202 7.03e-77

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: 233.38  E-value: 7.03e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197      1 AFQTDPMQRMALTTAYEALEMSGYVPNRTPSTRldrIGTFYGQTSDDWreinaaqqvdtyfitggvrafgpgrinyhfgf 80
Cdd:smart00825  45 AEAMDPQQRLLLEVAWEALEDAGIDPESLRGSR---TGVFVGVSSSDY-------------------------------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197     81 sgpSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGPCATFDNDADGYCRGDGCAS 160
Cdd:smart00825  90 ---SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGV 166

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 31979197    161 VIVKRLEDAIADEDRVLAVILGTATNHSADAISITHPHGPTQ 202
Cdd:smart00825 167 VVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ 208
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 1-169 9.35e-54

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: 173.20  E-value: 9.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197     1 AFQTDPMQRMALTTAYEALEMSGYVPNRTPSTRLDR-IGTFYGQTSDDWREINAAQQVDTY-FITGGVRAFGPGRINYHF 78
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVfIGSGIGDYAALLLLDEDGGPRRGSpFAVGTMPSVIAGRISYFL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197    79 GFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGPCATFDNDADGYCRGDGC 158
Cdd:pfam00109 161 GLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGV 240

                         170
                  ....*....|.
gi 31979197   159 ASVIVKRLEDA 169
Cdd:pfam00109 241 GAVVLKRLSDA 251
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 4-229 7.41e-32

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: 119.95  E-value: 7.41e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   4 TDPMQRMALTTAYEALEMSGYVPNRTPStrlDRIGTFYGQTSDDWREINAAQQVdtyFITGGVRAFGPGRINYH------ 77
Cdd:cd00834  68 MDRFAQFALAAAEEALADAGLDPEELDP---ERIGVVIGSGIGGLATIEEAYRA---LLEKGPRRVSPFFVPMAlpnmaa 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  78 ------FGFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSK-----KGPCATFD 146
Cdd:cd00834 142 gqvairLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrnddpEKASRPFD 221

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197 147 NDADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTATnhSADAISITHPH----GPTQSIlsRSILDEAGVDPVDVDY 222
Cdd:cd00834 222 KDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGA--SSDAYHITAPDpdgeGAARAM--RAALADAGLSPEDIDY 297


                ....*..
gi 31979197 223 VEMHGTG 229
Cdd:cd00834 298 INAHGTS 304
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 8-229 3.36e-30

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: 114.27  E-value: 3.36e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   8 QRMALTTAYEALEMSGYVPNRTPSTRLDRI-GTFYGQTSDDWREINAAQQVDTYFITGGVRAFGPGRINYHFGFSGPSLN 86
Cdd:cd00825  12 SILGFEAAERAIADAGLSREYQKNPIVGVVvGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAYD 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  87 IDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGPCATFDNDADGYCRGDGCASVIVKRL 166
Cdd:cd00825  92 VSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEEL 171

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31979197 167 EDAIADEDRVLAVILGTATNHSADAISITHPHGPTQSILSRSILDEAGVDPVDVDYVEMHGTG 229
Cdd:cd00825 172 EHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTG 234
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 3-229 6.29e-29

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: 112.11  E-value: 6.29e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   3 QTDPMQRMALTTAYEALEMSGYVPNRTPStrlDRIGTFYGQTSDDWREInaAQQVDTYFiTGGVRAFGP----------- 71
Cdd:COG0304  67 RMDRFTQYALAAAREALADAGLDLDEVDP---DRTGVIIGSGIGGLDTL--EEAYRALL-EKGPRRVSPffvpmmmpnma 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  72 -GRINYHFGFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKK-----GPCATF 145
Cdd:COG0304 141 aGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRnddpeKASRPF 220

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197 146 DNDADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTATnhSADAISITHPH----GPTQSIlsRSILDEAGVDPVDVD 221
Cdd:COG0304 221 DKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGA--SSDAYHITAPApdgeGAARAM--RAALKDAGLSPEDID 296


                ....*...
gi 31979197 222 YVEMHGTG 229
Cdd:COG0304 297 YINAHGTS 304
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 2-229 2.11e-19

"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: 85.57  E-value: 2.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   2 FQTDPMQRMALTTAYEALEMSGYvpnrTPSTRL--DRIGTFYGQTSDDWREI-----NAAQQVDTYFITGG--VRAFGPG 72
Cdd:cd00828  67 GIVDRTTLLALVATEEALADAGI----TDPYEVhpSEVGVVVGSGMGGLRFLrrggkLDARAVNPYVSPKWmlSPNTVAG 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  73 RINYHFGFS-GPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTnPDIFSGLSRGQFLS--KKGP---CATFD 146
Cdd:cd00828 143 WVNILLLSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL-EEGLSGFANMGALStaEEEPeemSRPFD 221

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197 147 NDADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTATNHSADAISITHPH-GPTQSIlsRSILDEAGVDPVDVDYVEM 225
Cdd:cd00828 222 ETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGkGIARAI--RTALAKAGLSLDDLDVISA 299


                ....
gi 31979197 226 HGTG 229
Cdd:cd00828 300 HGTS 303
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 5-229 4.67e-16

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 76.27  E-value: 4.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197    5 DPMQRMALTTAYEALEMSGYVPNrtPSTRLDRIGTFYGQTSDDWREINAA---------QQVDTYFITGGVRAFGPGRIN 75
Cdd:PTZ00050  75 SRATHFAMAAAREALADAKLDIL--SEKDQERIGVNIGSGIGSLADLTDEmktlyekghSRVSPYFIPKILGNMAAGLVA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   76 YHFGFSGPSLNIDTACSSSAAAMQVActALWAR--DCDTAIVGGLSCMTNPDIFSGLSRGQFLSKK---GP---CATFDN 147
Cdd:PTZ00050 153 IKHKLKGPSGSAVTACATGAHCIGEA--FRWIKygEADIMICGGTEASITPVSFAGFSRMRALCTKyndDPqraSRPFDK 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  148 DADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTATnhSADAISITHPH----GPTQSILSrSILDEAGVDPVDVDYV 223
Cdd:PTZ00050 231 DRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGS--SSDAHHITAPHpdgrGARRCMEN-ALKDGANININDVDYV 307


                 ....*.
gi 31979197  224 EMHGTG 229
Cdd:PTZ00050 308 NAHATS 313
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
77-229 1.05e-15

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 74.88  E-value: 1.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   77 HFGFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGG---LSCMT-NPdiFSGLsrgQFLSkKGPCATFDNDADGY 152
Cdd:PRK09185 146 YLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGvdsLCRLTlNG--FNSL---ESLS-PQPCRPFSANRDGI 219

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31979197  153 CRGDGCASVIVKRledaiADEDRVLavILGTAtnHSADA--ISITHPHGPTQSILSRSILDEAGVDPVDVDYVEMHGTG 229
Cdd:PRK09185 220 NIGEAAAFFLLER-----EDDAAVA--LLGVG--ESSDAhhMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTA 289
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 11-228 1.42e-15

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 74.83  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   11 ALTTAYEALEMSGYVPnrTPSTRLDR----IGTFYGQTSDdwrEINAAQ--------QVDTYFITGGVRAFGPGRINYHF 78
Cdd:PLN02836  97 ALCAADEALSDARWLP--SEDEAKERtgvsIGGGIGSITD---ILEAAQlicekrlrRLSPFFVPRILINMAAGHVSIRY 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   79 GFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKK-GPCAT-----FDNDADGY 152
Cdd:PLN02836 172 GFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTeasrpFDCDRDGF 251

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31979197  153 CRGDGCASVIVKRLEDAIADEDRVLAVILGTATnhSADAISITHPH--GPTQSILSRSILDEAGVDPVDVDYVEMHGT 228
Cdd:PLN02836 252 VIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGM--SGDAHHITQPHedGRGAVLAMTRALQQSGLHPNQVDYVNAHAT 327
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
5-228 1.65e-15

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 74.44  E-value: 1.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197    5 DPMQRMALTTAYEALEMSGYVPNRTPStrlDRIGTFYGQTSDDWREInaAQQVDTYfITGGVRAFGP------------G 72
Cdd:PRK07314  70 DRFIQYGIAAAKQAVEDAGLEITEENA---DRIGVIIGSGIGGLETI--EEQHITL-LEKGPRRVSPffvpmaiinmaaG 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   73 RINYHFGFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGP-----CATFDN 147
Cdd:PRK07314 144 HVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDdperaSRPFDK 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  148 DADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTAtnHSADAISITHPH----GPTQSIlsRSILDEAGVDPVDVDYV 223
Cdd:PRK07314 224 DRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYG--MTGDAYHMTAPApdgeGAARAM--KLALKDAGINPEDIDYI 299


                 ....*
gi 31979197  224 EMHGT 228
Cdd:PRK07314 300 NAHGT 304
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 72-229 4.71e-15

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: 71.71  E-value: 4.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  72 GRINYHFGFS-GPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGlscmtnpdifsglsrgqflskkgpcatfdndAD 150
Cdd:cd00327  48 GQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGG-------------------------------SE 96

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31979197 151 GYCRGDGCASVIVKRLEDAIADEDRVLAVILGTATnHSADAISITHPHGPTQSILSRSILDEAGVDPVDVDYVEMHGTG 229
Cdd:cd00327  97 EFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAA-TFDGASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTG 174
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 177-229 1.69e-14

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 67.21  E-value: 1.69e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 31979197   177 LAVILGTATNHSADAISITHPHGPTQSILSRSILDEAGVDPVDVDYVEMHGTG 229
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTG 53
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
5-228 1.66e-13

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 68.87  E-value: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197    5 DPMQRMALTTAYEALEMSGYVPNRTPStrLDRIGTFYGQTSDDWREI-NAAQQVDT------------YFITGgvraFGP 71
Cdd:PRK06333  80 DRFILFAMAAAKEALAQAGWDPDTLED--RERTATIIGSGVGGFPAIaEAVRTLDSrgprrlspftipSFLTN----MAA 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   72 GRINYHFGFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKG------PCATF 145
Cdd:PRK06333 154 GHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRFndapeqASRPF 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  146 DNDADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTATnhSADAISITHP----HGPTQSILsrSILDEAGVDPVDVD 221
Cdd:PRK06333 234 DRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGT--SADAYHMTAGpedgEGARRAML--IALRQAGIPPEEVQ 309


                 ....*..
gi 31979197  222 YVEMHGT 228
Cdd:PRK06333 310 HLNAHAT 316
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 9-229 5.26e-11

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 61.20  E-value: 5.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197    9 RMALTTAYEALEMSGYVPnrTPStrlDRIGTFYG----------QTSDDWRE----INAA---QQVDTYFItggvrafgp 71
Cdd:PRK07103  82 QAALAAAREAWRDAALGP--VDP---DRIGLVVGgsnlqqreqaLVHETYRDrpafLRPSyglSFMDTDLV--------- 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   72 GRINYHFGFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAI-VGGLSCMTNPDIFSGLSRGQFLSKKG------PCAT 144
Cdd:PRK07103 148 GLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIaVGALMDLSYWECQALRSLGAMGSDRFadepeaACRP 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  145 FDNDADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTATnhSADAISITHPHGPTQSILSRSILDEAGVDPVDVDYVE 224
Cdd:PRK07103 228 FDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSM--RLDANRGPDPSLEGEMRVIRAALRRAGLGPEDIDYVN 305


                 ....*
gi 31979197  225 MHGTG 229
Cdd:PRK07103 306 PHGTG 310
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 55-228 9.24e-11

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 60.52  E-value: 9.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   55 QQVDTYFITGGVRAFGPGRINYHFGFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQ 134
Cdd:PRK08439 126 RKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMK 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  135 FLSK-----KGPCATFDNDADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTAtnHSADAISITHP--HGPTQSIlsR 207
Cdd:PRK08439 206 ALSTrnddpKKASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFG--ESGDANHITSPapEGPLRAM--K 281

                        170       180
                 ....*....|....*....|.
gi 31979197  208 SILDEAGVDPvdVDYVEMHGT 228
Cdd:PRK08439 282 AALEMAGNPK--IDYINAHGT 300
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
78-229 1.89e-10

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 59.64  E-value: 1.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   78 FGFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDI---FSGLSRgqfLSKKG--PCAT---FDNDA 149
Cdd:PRK06501 162 FGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEAlirFSLLSA---LSTQNdpPEKAskpFSKDR 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  150 DGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTAtnHSADAISITH--PHGPTQSILSRSILDEAGVDPVDVDYVEMHG 227
Cdd:PRK06501 239 DGFVMAEGAGALVLESLESAVARGAKILGIVAGCG--EKADSFHRTRssPDGSPAIGAIRAALADAGLTPEQIDYINAHG 316


                 ..
gi 31979197  228 TG 229
Cdd:PRK06501 317 TS 318
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
55-228 1.35e-09

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 57.32  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   55 QQVDTYFITGGVRAFGPGRINYHFGFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQ 134
Cdd:PRK08722 128 RKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAK 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  135 FLSKKG--PCAT---FDNDADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTATnhSADAISITHPH--GPTQSILSR 207
Cdd:PRK08722 208 ALSTRNdePQKAsrpWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGM--SGDAYHMTSPSedGSGGALAME 285

                        170       180
                 ....*....|....*....|.
gi 31979197  208 SILDEAGVDPVDVDYVEMHGT 228
Cdd:PRK08722 286 AAMRDAGVTGEQIGYVNAHGT 306
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 72-228 2.03e-09

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 56.66  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   72 GRINYHFGFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSK------KGPCATF 145
Cdd:PRK14691  72 GHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfnstpEKASRPF 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  146 DNDADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTATnhSADAISITH--PHGPTQSILSRSILDEAGVDPVDVDYV 223
Cdd:PRK14691 152 DTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGT--SADAYHMTSgaEDGDGAYRAMKIALRQAGITPEQVQHL 229


                 ....*
gi 31979197  224 EMHGT 228
Cdd:PRK14691 230 NAHAT 234
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
7-229 4.28e-09

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 55.89  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197    7 MQRMALTTAYEALEMSGyvpnrTPSTRLDR----IGTFYGQTS------DDWREinaaqqvdtyfitGGVRAFGPGRINY 76
Cdd:PRK07910  83 LQRMSTVLGRRVWENAG-----SPEVDTNRlmvsIGTGLGSAEelvfayDDMRA-------------RGLRAVSPLAVQM 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   77 HFGfSGPSLNID-------------TACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSR-GQFLSKK--- 139
Cdd:PRK07910 145 YMP-NGPAAAVGlerhakagvitpvSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQmRIVMSTNndd 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  140 --GPCATFDNDADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTATNHSADAISITHPHG-PTQSILSRSIlDEAGVD 216
Cdd:PRK07910 224 paGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGeRAGHAMTRAI-ELAGLT 302

                        250
                 ....*....|...
gi 31979197  217 PVDVDYVEMHGTG 229
Cdd:PRK07910 303 PGDIDHVNAHATG 315
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 3-223 4.53e-09

Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.


Pssm-ID: 238428 [Multi-domain]  Cd Length: 399  Bit Score: 55.83  E-value: 4.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   3 QTDPMQRMALTTAYEALEMSGYVPNRTP------STRLDRIGTFYGQtsddwREINA-----AQQVDTYFITGGVRAFGP 71
Cdd:cd00832  67 QTDRMTRLALAAADWALADAGVDPAALPpydmgvVTASAAGGFEFGQ-----RELQKlwskgPRHVSAYQSFAWFYAVNT 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  72 GRINYHFGFSGPSLNIdtaCSSSAAAMQVACTA--LWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGPCAT----F 145
Cdd:cd00832 142 GQISIRHGMRGPSGVV---VAEQAGGLDALAQArrLVRRGTPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARaylpF 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197 146 DNDADGYCRGDGCASVIVKRLEDAIADEDRVLAVILGTATNHSADAisitHPHGPTQsiLSRSI---LDEAGVDPVDVDY 222
Cdd:cd00832 219 DAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPP----GSGRPPG--LARAIrlaLADAGLTPEDVDV 292


                .
gi 31979197 223 V 223
Cdd:cd00832 293 V 293
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 78-228 1.21e-07

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 51.52  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197   78 FGFSGPSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGPCAT-----FDNDADGY 152
Cdd:PLN02787 278 LGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTkasrpWDMNRDGF 357

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31979197  153 CRGDGCASVIVKRLEDAIADEDRVLAVILGTAtnHSADAISITHPHGPTQSIL--SRSILDEAGVDPVDVDYVEMHGT 228
Cdd:PLN02787 358 VMGEGAGVLLLEELEHAKKRGANIYAEFLGGS--FTCDAYHMTEPHPEGAGVIlcIEKALAQSGVSKEDVNYINAHAT 433
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
101-229 1.79e-07

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 50.82  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  101 AC-TALWA----------RDCDTAIVGGLSCMTNPDIFSGLSRGQFLSKKGpCATFDNDADGYCRGDGCASVIVKRLEDA 169
Cdd:PRK05952 145 ACaTGLWAiaqgveliqtGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AYPFDRQREGLVLGEGGAILVLESAELA 223

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31979197  170 IADEDRVLAVILGTATnhSADAISITHP----HGPTQSIlsRSILDEAGVDPVDVDYVEMHGTG 229
Cdd:PRK05952 224 QKRGAKIYGQILGFGL--TCDAYHMSAPepdgKSAIAAI--QQCLARSGLTPEDIDYIHAHGTA 283
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
 47-226 6.94e-04

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: 39.94  E-value: 6.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197  47 DWREINAAqqVDTYFITGGVRAFGPGRINYHFGFSG-PSLNIDTACSSSAAAMQVACTALWARDCDTAIVGG-------- 117
Cdd:cd00829  34 EPADIDAV--VVGNAAGGRFQSFPGALIAEYLGLLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGaekmsdvp 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197 118 -------------------LSCMTNPDIF----------SGLSRGQF--LSKKG-------PCATFDND----------- 148
Cdd:cd00829 112 tgdeaggrasdlewegpepPGGLTPPALYalaarrymhrYGTTREDLakVAVKNhrnaarnPYAQFRKPitvedvlnsrm 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31979197 149 -ADGYCR------GDGCASVIVKRLEDAIADEDR---VLAVILGTATNHSADAISITHPHGPTQSIlsRSILDEAGVDPV 218
Cdd:cd00829 192 iADPLRLldccpvSDGAAAVVLASEERARELTDRpvwILGVGAASDTPSLSERDDFLSLDAARLAA--RRAYKMAGITPD 269


                ....*...
gi 31979197 219 DVDYVEMH 226
Cdd:cd00829 270 DIDVAELY 277
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
 83-133 5.79e-03

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.


Pssm-ID: 459676 [Multi-domain]  Cd Length: 260  Bit Score: 36.90  E-value: 5.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 31979197    83 PSLNIDTACSSSAAAMQVACTALWARDCDTAIVGGLSCMTN------PDIFSGLSRG 133
Cdd:pfam00108  77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHapyalpTDARSGLKHG 133
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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