NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15596195|ref|NP_249689|]
View 

hypothetical protein PA0998 [Pseudomonas aeruginosa PAO1]

Protein Classification

3-oxoacyl-ACP synthase III family protein( domain architecture ID 11417379)

3-oxoacyl-ACP synthase III family protein such as Pseudomonas aeruginosa 2-heptyl-4(1H)-quinolone synthase subunits PqsB and PqsC, which form a complex that catalyzes the condensation of 2-aminobenzoylacetate (2-ABA) and octanoyl-CoA to form 2-heptyl-4(1H)-quinolone

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
2-342 2.88e-59

3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 440101 [Multi-domain]  Cd Length: 323  Bit Score: 193.79  E-value: 2.88e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   2 HKVKLAAITCELPARSYENDDpvFAAVPDLSESW-WQFWGVNRRGYFDPrnGENEFSLVVRAAERLLRSSDTAPDSVDML 80
Cdd:COG0332   1 RNVRILGTGSYLPERVVTNDD--LEKRLDTSDEWiEERTGIRERRIAAP--DETTSDLAVEAARKALEAAGIDPEDIDLI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  81 ICSASSPIMtdagdvlpdlrgrLYPRMANVLSKQLGLSRALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSEYIS 160
Cdd:COG0332  77 IVATVTPDY-------------LFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLS 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 161 NLLDFTSR-TSTLFADGCAVALLTRGDDDSCdLLASAEHSDATFYEVATGRWRLPENPTGEAKPRLYFsLFSDGQnKMAS 239
Cdd:COG0332 144 RIVDWTDRsTCVLFGDGAGAVVLEASEEGPG-ILGSVLGSDGSGADLLVVPAGGSRNPPSPVDEGDHY-LRMDGR-EVFK 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 240 FVPTNVPIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLREGKIR 319
Cdd:COG0332 221 FAVRNLPEVIREALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIK 300
                       330       340
                ....*....|....*....|...
gi 15596195 320 PGDRIVMAGAATGWGFAAQVWQL 342
Cdd:COG0332 301 PGDLVLLAGFGAGLTWGAAVLRW 323
 
Name Accession Description Interval E-value
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
2-342 2.88e-59

3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440101 [Multi-domain]  Cd Length: 323  Bit Score: 193.79  E-value: 2.88e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   2 HKVKLAAITCELPARSYENDDpvFAAVPDLSESW-WQFWGVNRRGYFDPrnGENEFSLVVRAAERLLRSSDTAPDSVDML 80
Cdd:COG0332   1 RNVRILGTGSYLPERVVTNDD--LEKRLDTSDEWiEERTGIRERRIAAP--DETTSDLAVEAARKALEAAGIDPEDIDLI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  81 ICSASSPIMtdagdvlpdlrgrLYPRMANVLSKQLGLSRALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSEYIS 160
Cdd:COG0332  77 IVATVTPDY-------------LFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLS 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 161 NLLDFTSR-TSTLFADGCAVALLTRGDDDSCdLLASAEHSDATFYEVATGRWRLPENPTGEAKPRLYFsLFSDGQnKMAS 239
Cdd:COG0332 144 RIVDWTDRsTCVLFGDGAGAVVLEASEEGPG-ILGSVLGSDGSGADLLVVPAGGSRNPPSPVDEGDHY-LRMDGR-EVFK 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 240 FVPTNVPIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLREGKIR 319
Cdd:COG0332 221 FAVRNLPEVIREALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIK 300
                       330       340
                ....*....|....*....|...
gi 15596195 320 PGDRIVMAGAATGWGFAAQVWQL 342
Cdd:COG0332 301 PGDLVLLAGFGAGLTWGAAVLRW 323
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
3-340 8.95e-54

Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.


Pssm-ID: 238426 [Multi-domain]  Cd Length: 320  Bit Score: 179.27  E-value: 8.95e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   3 KVKLAAITCELPARSYENDDpvFAAVPDLSESWwq-fwGVNRRGYFDPrnGENEFSLVVRAAERLLRSSDTAPDSVDMLI 81
Cdd:cd00830   1 NARILGIGSYLPERVVTNDE--LEKRLDTSDEWirtrtGIRERRIADP--GETTSDLAVEAAKKALEDAGIDADDIDLII 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  82 CSASSPimtdagdvlpdlrGRLYPRMANVLSKQLGLSRALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSEYISN 161
Cdd:cd00830  77 VATSTP-------------DYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSR 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 162 LLDFTSR-TSTLFADGCAVALLTRGDDDScDLLASAEHSDATFYE---VATGRWRLPENPTGEAKPRLYFslfsDGQNKM 237
Cdd:cd00830 144 ILDWTDRsTAVLFGDGAGAVVLEATEEDP-GILDSVLGSDGSGADlltIPAGGSRSPFEDAEGGDPYLVM----DGREVF 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 238 aSFVPTNVPIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLREGK 317
Cdd:cd00830 219 -KFAVRLMPESIEEALEKAGLTPDDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGK 297
                       330       340
                ....*....|....*....|...
gi 15596195 318 IRPGDRIVMAGAATGWGFAAQVW 340
Cdd:cd00830 298 LKKGDLVLLLGFGAGLTWGAALL 320
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
1-343 7.15e-41

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


Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 145.78  E-value: 7.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195    1 MHKVKLAAITCELPARSYENDDpvFAAVPDLSESW-WQFWGVNRRGYFDPrngeNEFS--LVVRAAERLLRSSDTAPDSV 77
Cdd:PRK12879   2 MSYARITGIGTYVPPRVLTNDD--LETFIDTSDEWiVQRTGIKERRIAHV----EEYTsdLAIKAAERALARAGLDAEDI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   78 DMLICSASSPimtDAgdvlpdlrgrLYPRMANVLSKQLGLSRALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSE 157
Cdd:PRK12879  76 DLIIVATTTP---DY----------LFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAE 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  158 YISNLLDFTSR-TSTLFADGCAVALLTRgDDDSCDLLASAEHSDATFYEV--ATGRWRlPENPTGEAKprlYFSLFSDGQ 234
Cdd:PRK12879 143 RLSKVTDYTDRtTCILFGDGAGAVVLEA-TENEPGFIDYVLGTDGDGGDIlyRTGLGT-TMDRDALSG---DGYIVQNGR 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  235 nKMASFVPTNVPIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLR 314
Cdd:PRK12879 218 -EVFKWAVRTMPKGARQVLEKAGLTKDDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALE 296
                        330       340
                 ....*....|....*....|....*....
gi 15596195  315 EGKIRPGDRIVMAGAATGWGFAAQVWQLG 343
Cdd:PRK12879 297 QGKIKPGDTLLLYGFGAGLTWAALLVKWG 325
ACP_syn_III_C pfam08541
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ...
253-342 1.12e-27

3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.


Pssm-ID: 430060  Cd Length: 90  Bit Score: 103.73  E-value: 1.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   253 LEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLREGKIRPGDRIVMAGAATG 332
Cdd:pfam08541   1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80
                          90
                  ....*....|
gi 15596195   333 WGFAAQVWQL 342
Cdd:pfam08541  81 LTWGAALLRW 90
 
Name Accession Description Interval E-value
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
2-342 2.88e-59

3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440101 [Multi-domain]  Cd Length: 323  Bit Score: 193.79  E-value: 2.88e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   2 HKVKLAAITCELPARSYENDDpvFAAVPDLSESW-WQFWGVNRRGYFDPrnGENEFSLVVRAAERLLRSSDTAPDSVDML 80
Cdd:COG0332   1 RNVRILGTGSYLPERVVTNDD--LEKRLDTSDEWiEERTGIRERRIAAP--DETTSDLAVEAARKALEAAGIDPEDIDLI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  81 ICSASSPIMtdagdvlpdlrgrLYPRMANVLSKQLGLSRALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSEYIS 160
Cdd:COG0332  77 IVATVTPDY-------------LFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLS 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 161 NLLDFTSR-TSTLFADGCAVALLTRGDDDSCdLLASAEHSDATFYEVATGRWRLPENPTGEAKPRLYFsLFSDGQnKMAS 239
Cdd:COG0332 144 RIVDWTDRsTCVLFGDGAGAVVLEASEEGPG-ILGSVLGSDGSGADLLVVPAGGSRNPPSPVDEGDHY-LRMDGR-EVFK 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 240 FVPTNVPIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLREGKIR 319
Cdd:COG0332 221 FAVRNLPEVIREALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIK 300
                       330       340
                ....*....|....*....|...
gi 15596195 320 PGDRIVMAGAATGWGFAAQVWQL 342
Cdd:COG0332 301 PGDLVLLAGFGAGLTWGAAVLRW 323
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
3-340 8.95e-54

Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.


Pssm-ID: 238426 [Multi-domain]  Cd Length: 320  Bit Score: 179.27  E-value: 8.95e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   3 KVKLAAITCELPARSYENDDpvFAAVPDLSESWwq-fwGVNRRGYFDPrnGENEFSLVVRAAERLLRSSDTAPDSVDMLI 81
Cdd:cd00830   1 NARILGIGSYLPERVVTNDE--LEKRLDTSDEWirtrtGIRERRIADP--GETTSDLAVEAAKKALEDAGIDADDIDLII 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  82 CSASSPimtdagdvlpdlrGRLYPRMANVLSKQLGLSRALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSEYISN 161
Cdd:cd00830  77 VATSTP-------------DYLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSR 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 162 LLDFTSR-TSTLFADGCAVALLTRGDDDScDLLASAEHSDATFYE---VATGRWRLPENPTGEAKPRLYFslfsDGQNKM 237
Cdd:cd00830 144 ILDWTDRsTAVLFGDGAGAVVLEATEEDP-GILDSVLGSDGSGADlltIPAGGSRSPFEDAEGGDPYLVM----DGREVF 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 238 aSFVPTNVPIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLREGK 317
Cdd:cd00830 219 -KFAVRLMPESIEEALEKAGLTPDDIDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGK 297
                       330       340
                ....*....|....*....|...
gi 15596195 318 IRPGDRIVMAGAATGWGFAAQVW 340
Cdd:cd00830 298 LKKGDLVLLLGFGAGLTWGAALL 320
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
3-340 4.54e-47

"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.


Pssm-ID: 238423 [Multi-domain]  Cd Length: 324  Bit Score: 162.22  E-value: 4.54e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   3 KVKLAAITCELPARSYENDDPVFAAVPDLSESWWqfwGVNRRGYFDPRngENEFSLVVRAAERLLRSSDTAPDSVDMLIC 82
Cdd:cd00827   1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTT---GIGQRHMAGDD--EDVPTMAVEAARRALERAGIDPDDIGLLIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  83 SASSPImtDAGdvlpdlrgrlyPRMANVLSKQLGLSRALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSEYISNL 162
Cdd:cd00827  76 ATESPI--DKG-----------KSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 163 LDFTSRTSTLFADGCAVALLTRGDD-DSCDLLASAEHSDATF----YEVATGRWRLPENptgeakpRLYFSLFSDGQNK- 236
Cdd:cd00827 143 LDEGSALEPTLGDGAAAMLVSRNPGiLAAGIVSTHSTSDPGYdfspYPVMDGGYPKPCK-------LAYAIRLTAEPAGr 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 237 -MASFVPTNVPIAMRRALEKAGLgSDDIDYFVFHQP-APFLVKAWAEGIGARPEQYQLTMGD----TGVMISVSIPYTLM 310
Cdd:cd00827 216 aVFEAAHKLIAKVVRKALDRAGL-SEDIDYFVPHQPnGKKILEAVAKKLGGPPEKASQTRWIllrrVGNMYAASILLGLA 294
                       330       340       350
                ....*....|....*....|....*....|
gi 15596195 311 TGLREGKIRPGDRIVMAGAATGWGFAAQVW 340
Cdd:cd00827 295 SLLESGKLKAGDRVLLFSYGSGFTAEAFVL 324
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
1-343 7.15e-41

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


Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 145.78  E-value: 7.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195    1 MHKVKLAAITCELPARSYENDDpvFAAVPDLSESW-WQFWGVNRRGYFDPrngeNEFS--LVVRAAERLLRSSDTAPDSV 77
Cdd:PRK12879   2 MSYARITGIGTYVPPRVLTNDD--LETFIDTSDEWiVQRTGIKERRIAHV----EEYTsdLAIKAAERALARAGLDAEDI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   78 DMLICSASSPimtDAgdvlpdlrgrLYPRMANVLSKQLGLSRALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSE 157
Cdd:PRK12879  76 DLIIVATTTP---DY----------LFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAE 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  158 YISNLLDFTSR-TSTLFADGCAVALLTRgDDDSCDLLASAEHSDATFYEV--ATGRWRlPENPTGEAKprlYFSLFSDGQ 234
Cdd:PRK12879 143 RLSKVTDYTDRtTCILFGDGAGAVVLEA-TENEPGFIDYVLGTDGDGGDIlyRTGLGT-TMDRDALSG---DGYIVQNGR 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  235 nKMASFVPTNVPIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLR 314
Cdd:PRK12879 218 -EVFKWAVRTMPKGARQVLEKAGLTKDDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALE 296
                        330       340
                 ....*....|....*....|....*....
gi 15596195  315 EGKIRPGDRIVMAGAATGWGFAAQVWQLG 343
Cdd:PRK12879 297 QGKIKPGDTLLLYGFGAGLTWAALLVKWG 325
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
52-339 5.25e-38

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 137.90  E-value: 5.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   52 GENEFSLVVRAAERLLRSSDTAPDSVDMLICSASSPIMtdagdvlpdlrgrLYPRMANVLSKQLGLSRALPLDSQMECAS 131
Cdd:PRK09352  49 DETTSDLATEAAKKALEAAGIDPEDIDLIIVATTTPDY-------------AFPSTACLVQARLGAKNAAAFDLSAACSG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  132 FLLNLRLAASMIRQGKAEKVLVVCSEYISNLLDFTSRTST-LFADGCAVALLTRGDDDscDLLASAEHSDATFYEVATgr 210
Cdd:PRK09352 116 FVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTCvLFGDGAGAVVLGASEEP--GILSTHLGSDGSYGDLLY-- 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  211 wrLPENPTGEAKPRLYFSLfsDGQN--KMASfvpTNVPIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPE 288
Cdd:PRK09352 192 --LPGGGSRGPASPGYLRM--EGREvfKFAV---RELAKVAREALEAAGLTPEDIDWLVPHQANLRIIDATAKKLGLPME 264
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15596195  289 QYQLTMGDTGVMISVSIPYTLMTGLREGKIRPGDRIVMAGAATGWGFAAQV 339
Cdd:PRK09352 265 KVVVTVDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTWGAAL 315
PLN02326 PLN02326
3-oxoacyl-[acyl-carrier-protein] synthase III
5-340 1.84e-35

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


Pssm-ID: 215185  Cd Length: 379  Bit Score: 132.55  E-value: 1.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195    5 KLAAITCELPARSYENDDpvFAAVPDLSESWWqfwgVNRRGYFDPR---NGENEFSLVVRAAERLLRSSDTAPDSVDMLI 81
Cdd:PLN02326  49 KLVGCGSAVPKLLITNDD--LSKLVDTSDEWI----ATRTGIRNRRvlsGDETLTSLAVEAAKKALEMAGVDPEDVDLVL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   82 CSASSPimtdagdvlPDLRGRlyprmANVLSKQLGLSRALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSEYISN 161
Cdd:PLN02326 123 LCTSSP---------DDLFGS-----APQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSR 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  162 LLDFTSR-TSTLFADGCAVALLTRGDDDSCDLLASAEHSD--------ATFYEVATGRWRLPENPTGEAKPR--LYFSLF 230
Cdd:PLN02326 189 YVDWTDRgTCILFGDGAGAVVLQACDDDEDGLLGFDMHSDgnghkhlhATFKGEDDDSSGGNTNGVGDFPPKkaSYSCIQ 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  231 SDGQnKMASFVPTNVPIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLM 310
Cdd:PLN02326 269 MNGK-EVFKFAVRCVPQVIESALQKAGLTAESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALD 347
                        330       340       350
                 ....*....|....*....|....*....|..
gi 15596195  311 TGLREGKIRPGDRIVMAGAATG--WGFAAQVW 340
Cdd:PLN02326 348 EAVRSGKVKKGDVIATAGFGAGltWGSAIVRW 379
ACP_syn_III_C pfam08541
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ...
253-342 1.12e-27

3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.


Pssm-ID: 430060  Cd Length: 90  Bit Score: 103.73  E-value: 1.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   253 LEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLREGKIRPGDRIVMAGAATG 332
Cdd:pfam08541   1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKLKPGDLVLLVGFGAG 80
                          90
                  ....*....|
gi 15596195   333 WGFAAQVWQL 342
Cdd:pfam08541  81 LTWGAALLRW 90
PRK05963 PRK05963
beta-ketoacyl-ACP synthase III;
58-342 6.35e-24

beta-ketoacyl-ACP synthase III;


Pssm-ID: 180328 [Multi-domain]  Cd Length: 326  Bit Score: 100.18  E-value: 6.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   58 LVVRAAERLLRSSDTAPDSVDMLICSASSPimtdagdvlpdlrGRLYPRMANVLSKQLGLSRALPLDSQMECASFLLNLR 137
Cdd:PRK05963  55 LAASAGDMALSDAGIERSDIALTLLATSTP-------------DHLLPPSAPLLAHRLGLQNSGAIDLAGACAGFLYALV 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  138 LAASMIR-QGKAekVLVVCSEYISNLLDFTSR-TSTLFADGCAVALLTRGDDDSCDLLASAEHSDATFYE---VATGRWR 212
Cdd:PRK05963 122 LADGFVRaQGKP--VLVVAANILSRRINMAERaSAVLFADAAGAVVLAPSAKANSGVLGSQLISDGSHYDlikIPAGGSA 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  213 LPENPTGEAKPRLYfsLFSDGQNKMASFVP--TNvpiAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQY 290
Cdd:PRK05963 200 RPFAPERDASEFLM--TMQDGRAVFTEAVRmmSG---ASQNVLASAAMTPQDIDRFFPHQANARIVDKVCETIGIPRAKA 274
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15596195  291 QLTMGDTGVMISVSIPYTLMTGLREGKIRPGDRIVMAGAATGWGFAAQVWQL 342
Cdd:PRK05963 275 ASTLETYGNSSAATIPLSLSLANLEQPLREGERLLFAAAGAGMTGGAVVMRV 326
PRK07204 PRK07204
beta-ketoacyl-ACP synthase III;
1-337 1.01e-23

beta-ketoacyl-ACP synthase III;


Pssm-ID: 235964  Cd Length: 329  Bit Score: 99.52  E-value: 1.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195    1 MHKVKLAAITCELPARSyenddpVFAAVPD----LSESWWQF-WGVNRRGYFDprnGENEFSLVVRAAERLLRSSDTAPD 75
Cdd:PRK07204   2 KRYISIKGIGTYLPKRK------VDSLELDkkldLPEGWVLKkSGVKTRHFVD---GETSSYMGAEAAKKAVEDAKLTLD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   76 SVDMLICS---ASSPImtdagdvlpdlrgrlyPRMANVLSKQLGLSRA-LP-LDSQMECASFLLNLRLAASMIRQGKAEK 150
Cdd:PRK07204  73 DIDCIICAsgtIQQAI----------------PCTASLIQEQLGLQHSgIPcFDINSTCLSFITALDTISYAIECGRYKR 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  151 VLVVCSEYISNLLDFTSR-TSTLFADGCAVALLTRGDDDSCDLLASAE-HSD-ATFYEVATGRWRLPenPTGEAKPRLYF 227
Cdd:PRK07204 137 VLIISSEISSVGLNWGQNeSCILFGDGAAAVVITKGDHSSRILASHMEtYSSgAHLSEIRGGGTMIH--PREYSEERKED 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  228 SLFS-DGQN--KMASFVPTNVpiaMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVS 304
Cdd:PRK07204 215 FLFDmNGRAifKLSSKYLMKF---IDKLLMDAGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAAS 291
                        330       340       350
                 ....*....|....*....|....*....|...
gi 15596195  305 IPYTLMTGLREGKIRPGDRIVMAGaaTGWGFAA 337
Cdd:PRK07204 292 IPVALFEAIKQKKVQRGNKILLLG--TSAGLSI 322
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
123-200 1.48e-22

3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.


Pssm-ID: 430064 [Multi-domain]  Cd Length: 80  Bit Score: 89.88  E-value: 1.48e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596195   123 LDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSEYISNLLDFTSR-TSTLFADGCAVALLTRGDDDSCDLLASAEHSD 200
Cdd:pfam08545   1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRsTAVLFGDGAGAVVLEATDEPGARILDSVLGSD 79
fabH CHL00203
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
26-341 2.55e-21

3-oxoacyl-acyl-carrier-protein synthase 3; Provisional


Pssm-ID: 164577 [Multi-domain]  Cd Length: 326  Bit Score: 93.09  E-value: 2.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   26 AAVPDLSESWWQF---------WGVNRRGYFDPRNGENEFSLVVRAAERLLRSSDTA---PDSVDMLICSASSPimtdag 93
Cdd:CHL00203  10 SSVPNFSVENQQFediietsdhWISTRTGIKKRHLAPSSTSLTKLAAEAANKALDKAhmdPLEIDLIILATSTP------ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   94 dvlPDLRGRlyprmANVLSKQLGLSRALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSEYISNLLDFTSRTST-L 172
Cdd:CHL00203  84 ---DDLFGS-----ASQLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCiL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  173 FADGCAVALLTRGDDDS------CDLLASAEHSDATFYEVATGRWRLPENPTGEakprlYFSLFSDGQnKMASFVPTNVP 246
Cdd:CHL00203 156 FGDGAGAAIIGASYENSilgfklCTDGKLNSHLQLMNKPVNNQSFGTTKLPQGQ-----YQSISMNGK-EVYKFAVFQVP 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  247 IAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLREGKIRPGDRIVM 326
Cdd:CHL00203 230 AVIIKCLNALNISIDEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQPGQIIVL 309
                        330
                 ....*....|....*..
gi 15596195  327 AGAATG--WGFAAQVWQ 341
Cdd:CHL00203 310 SGFGAGltWGAIVLKWK 326
PRK06840 PRK06840
3-oxoacyl-ACP synthase;
49-345 3.16e-19

3-oxoacyl-ACP synthase;


Pssm-ID: 235872  Cd Length: 339  Bit Score: 86.98  E-value: 3.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   49 PRNGENEFSLVVRAAERLLRSSDTAPDSVDMLICSASS----PIMTDAGDVlpdlrgrlyprmanvlSKQLGLSRALPLD 124
Cdd:PRK06840  47 PGPEDHTSDMAIAAAKPALKQAGVDPAAIDVVIYIGSEhkdyPVWSSAPKI----------------QHEIGAKNAWAFD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  125 SQMECASFLLNLRLAASMIR-QGKAEKVLVVCSEYISNLLDFTS-RTSTLF--ADGCAVALLTRGDDDScDLLASAEHSD 200
Cdd:PRK06840 111 IMAVCASFPIALKVAKDLLYsDPSIENVLLVGGYRNSDLVDYDNpRTRFMFnfAAGGSAALLKKDAGKN-RILGSAIITD 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  201 ATFYE---VATGRWRLPENPTGEAKPRLYFSLFSD-------GQNKMASFVPTnvpiaMRRALEKAGLGSDDIDYFVFHQ 270
Cdd:PRK06840 190 GSFSEdvrVPAGGTKQPASPETVENRQHYLDVIDPesmkerlDEVSIPNFLKV-----IREALRKSGYTPKDIDYLAILH 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596195  271 PAPFLVKAWAEGIGARPEQyQLTMGDTGVMISVSIPYTLMTGLREGKIRPGDRIVMAGAATGWGFAAQVWQLGEV 345
Cdd:PRK06840 265 MKRSAHIALLEGLGLTEEQ-AIYLDEYGHLGQLDQILSLHLALEQGKLKDGDLVVLVSAGTGYTWAATVIRWGPV 338
BH0617 COG3424
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ...
58-338 2.07e-17

Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442650 [Multi-domain]  Cd Length: 351  Bit Score: 82.11  E-value: 2.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  58 LVVRAAERLLRSSDTAPDSVDMLICSASSPIMTdagdvlP--DLRgrlyprmanvLSKQLGLSRA---LPLdSQMECASF 132
Cdd:COG3424  80 LAEEAARRALDKAGLDPEDIDHLVTVSCTGFAA------PglDAR----------LINRLGLRPDvrrLPV-GGMGCAAG 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 133 LLNLRLAASMIRQGKAEKVLVVCSEY-----------ISNLLdftsrTSTLFADGCAVALLTrGDDDSCDLLaSAEHSDA 201
Cdd:COG3424 143 AAGLRRAADFLRADPDAVVLVVCVELcsltfqrdddsKDNLV-----ANALFGDGAAAVVVS-GDPRPGPGP-RILAFRS 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 202 TFYEVATG--RWRLpenptGEAKPRLYFSlfsdgqNKMASFVPTNVPIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAW 279
Cdd:COG3424 216 YLIPDTEDvmGWDV-----GDTGFRMVLS------PEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAV 284
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596195 280 AEGIGARPEQYQLT---MGDTGVMISVSIPYTLMTGLREGKIRPGDRIVMagAATGWGFAAQ 338
Cdd:COG3424 285 EEALGLPPEALAHSrevLREYGNMSSATVLFVLERLLEEGAPAPGERGLA--MAFGPGFTAE 344
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
60-332 1.86e-14

Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.


Pssm-ID: 238427 [Multi-domain]  Cd Length: 361  Bit Score: 73.41  E-value: 1.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  60 VRAAERLLRSSDTAPDSVDMLICSASSPIMTDAGDVlpdlrgrlypRMANvlskQLGLS---RALPLdSQMECASFLLNL 136
Cdd:cd00831  90 EEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDA----------MLIN----RLGLRpdvKRYNL-GGMGCSAGAIAL 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 137 RLAASMIRQGKAEKVLVVCSEYIS----------NLLdftsrTSTLFADGCAVALLTRGDDDSCDLLASAEHSDA--TFY 204
Cdd:cd00831 155 DLAKDLLEANPGARVLVVSTELCSlwyrgpdhrsMLV-----GNALFGDGAAAVLLSNDPRDRRRERPLFELVRAasTLL 229
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 205 EVATG--RWRLPENptgeakpRLYFSLFSDGQNKMASFVPTNVPIAMRRAleKAGLGSDDIDYFVFHQPAPFLVKAWAEG 282
Cdd:cd00831 230 PDSEDamGWHLGEE-------GLTFVLSRDVPRLVEKNLERVLRKLLARL--GIGLFKLAFDHWCVHPGGRAVLDAVEKA 300
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15596195 283 IGARPEQYQL---TMGDTGVMISVSIPYTLMTGLREGKIRPGDRIVMAGAATG 332
Cdd:cd00831 301 LGLSPEDLEAsrmVLRRYGNMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPG 353
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
60-328 2.73e-12

3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 442651 [Multi-domain]  Cd Length: 382  Bit Score: 67.13  E-value: 2.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  60 VRAAERLLRSSDTAPDSVDMLI-CSASSPimtDAGDvlpdlrgrlyPrMANVLSKQLGLSR-ALPLDSQMECASFLLNLR 137
Cdd:COG3425  56 ANAARRALDRAGIDPSDIGAVYvGTESGP---DASK----------P-IATYVHGALGLPPnCRAFELKFACYAGTAALQ 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 138 LAASMIRQGKAEKVLVVCSEyisnlldfTSRT---STL---FADGcAVALLTRGDDDSCDLLASA-------------EH 198
Cdd:COG3425 122 AALGWVASGPNKKALVIASD--------IARYgpgSAGeytQGAG-AVAMLVGADPRIAEIEGGSgsyttdvmdfwrpNG 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 199 SDatfYEVATGRWRLPenptgeakprLYFSLFSDgqnkmasfvptnvpiAMRRALEKAGLGSDDIDYFVFHQPAPFLVK- 277
Cdd:COG3425 193 SD---YPLVDGRFSEP----------AYLDHLEE---------------AVKDYKEKTGLKPDDFDYFVFHQPFGKMPKk 244
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596195 278 --------AWAEGIGARPEQYQLTM------GDTGvmiSVSIPYTLMTGLREGKIRPGDRIVMAG 328
Cdd:COG3425 245 aakklgrkAGREIQEDFEEQVEPSLiysrriGNTY---TGSLYLGLASLLDNAKDLPGDRIGLFS 306
PRK12880 PRK12880
beta-ketoacyl-ACP synthase III;
3-276 9.70e-11

beta-ketoacyl-ACP synthase III;


Pssm-ID: 171793  Cd Length: 353  Bit Score: 62.29  E-value: 9.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195    3 KVKLAAITCELPARSYENDD---PVFAAVPDLSESWWQFWGVNRRGYFDPRNGENEfsLVVRAAERLLRSSDTAPDSVDM 79
Cdd:PRK12880   7 KAKISGICVSVPEHKICIDDeleSVFSNDIKTLKRMKKVIGLNTRYICDENTCVSD--LGKHAANTLLQGLNIDKNSLDA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   80 LICSASSPimtdagdvlpDLrgrLYPRMANVLSKQLGLS-RALPLDSQMECASFLLNLRLAASMIRQGKAeKVLVVCSEY 158
Cdd:PRK12880  85 LIVVTQSP----------DF---FMPSTACYLHQLLNLSsKTIAFDLGQACAGYLYGLFVAHSLIQSGLG-KILLICGDT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  159 ISNLLDFTS-RTSTLFADGCAVALLTRGDDDSC--DLLasaehSDATFYE---VATGRWRLPE-NPTGEAKP------RL 225
Cdd:PRK12880 151 LSKFIHPKNmNLAPIFGDGVSATLIEKTDFNEAffELG-----SDGKYFDkliIPKGAMRIPKaDIFNDDSLmqteefRQ 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15596195  226 YFSLFSDGQNKMASFVPTNvPIAMRRALEKAGLGSDDIDYFVFHQPAPFLV 276
Cdd:PRK12880 226 LENLYMDGANIFNMALECE-PKSFKEILEFSKVDEKDIAFHLFHQSNAYLV 275
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
101-318 4.16e-09

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: 57.26  E-value: 4.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 101 GRLYPRMANVLSKQLGLSrALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSEYISNLLD---------------- 164
Cdd:cd00825  69 KAMFPGASGQIATPLGIH-GPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDcefdamgalstpekas 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 165 --FTSR-TSTLFADGCAVALLTRGDddscDLLASAEHSDATFYEVATGrwrlpenptgeakprlyfslfSDGQNkMASFV 241
Cdd:cd00825 148 rtFDAAaDGFVFGDGAGALVVEELE----HALARGAHIYAEIVGTAAT---------------------IDGAG-MGAFA 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 242 P--TNVPIAMRRALEKAGLGSDDIDYFVFHQPA-----PFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLR 314
Cdd:cd00825 202 PsaEGLARAAKEALAVAGLTVWDIDYLVAHGTGtpigdVKELKLLRSEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVL 281

                ....
gi 15596195 315 EGKI 318
Cdd:cd00825 282 MLEH 285
PRK07515 PRK07515
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
60-187 5.93e-09

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


Pssm-ID: 236037  Cd Length: 372  Bit Score: 56.81  E-value: 5.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   60 VRAAERLLRSSDTAPDSVDMLICSASSpiMTdagdvlpdlrgRLYPRMANVLSKQLGLsRALPLDSQMECASFLLNLRLA 139
Cdd:PRK07515 100 VAAARQALARAGRTAEDIDAVIVACSN--MQ-----------RAYPAMAIEIQQALGI-EGFAFDMNVACSSATFGIQTA 165
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15596195  140 ASMIRQGKAEKVLVVCSEYISNLLDFTSRTST-LFADGCAVALLTRGDD 187
Cdd:PRK07515 166 ANAIRSGSARRVLVVNPEICSGHLNFRDRDSHfIFGDVATAVIVERADT 214
PRK09258 PRK09258
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
59-332 1.25e-08

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


Pssm-ID: 181732  Cd Length: 338  Bit Score: 55.66  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195   59 VVRAAERLLRSSDTAPDSVDMLI-CSASspimtdagdvlpdlRGRLYPRMANVLSKQLGLSR-ALPLDSQMECASFLLNL 136
Cdd:PRK09258  65 AIAAGRKALAEAGIDPSDIGLLInTSVC--------------RDYLEPATACRVHHNLGLPKsCANFDVSNACLGFLNGM 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  137 RLAASMIRQGKAEKVLVVCSEYISNLLDFT-----SRTSTL------FA-----DGCAVALLTRGDD--DSCDLLASAEH 198
Cdd:PRK09258 131 LDAANMIELGQIDYALVVSGESAREIVEATidrllAPETTRedfaqsFAtltlgSGAAAAVLTRGSLhpRGHRLLGGVTR 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  199 SDATFYEVAtgRWRLPenptgeakprlyfSLFSDGQNKMASFVPTNVpIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKA 278
Cdd:PRK09258 211 AATEHHELC--QGGRD-------------GMRTDAVGLLKEGVELAV-DTWEAFLAQLGWAVEQVDRVICHQVGAAHTRA 274
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15596195  279 WAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLREGKIRPGDRIVMAGAATG 332
Cdd:PRK09258 275 ILKALGIDPEKVFTTFPTLGNMGPASLPITLAMAAEEGFLKPGDRVALLGIGSG 328
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
103-335 7.50e-08

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: 52.83  E-value: 7.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 103 LYPRMANVLSKQLGLSRALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSEYIsnlldftsrtstLFADGCAVALL 182
Cdd:cd00327  42 EFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF------------VFGDGAAAAVV 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 183 TRGDD---DSCDLLASAEHSDATFyevatgrwrlpENPTGEAKPrlyfslfsdgqnkmasfVPTNVPIAMRRALEKAGLG 259
Cdd:cd00327 110 ESEEHalrRGAHPQAEIVSTAATF-----------DGASMVPAV-----------------SGEGLARAARKALEGAGLT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 260 SDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQL-----TMGDTGVMISVSIPYTLMTGLREGKIR---PGDRIVMAGAAT 331
Cdd:cd00327 162 PSDIDYVEAHGTGTPIGDAVELALGLDPDGVRSpavsaTLIMTGHPLGAAGLAILDELLLMLEHEfipPTPREPRTVLLL 241

                ....
gi 15596195 332 GWGF 335
Cdd:cd00327 242 GFGL 245
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
129-283 2.36e-06

"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: 48.97  E-value: 2.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 129 CASFLLNLRLAASMIRQGKAEKVLVVCSEYISNLLDF-----------------------TSRTSTLFADGCAVALLTRG 185
Cdd:cd00828 162 CATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSgfanmgalstaeeepeemsrpfdETRDGFVEAEGAGVLVLERA 241
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 186 DDdscdllasAEHSDATFYEVATGRwrlpenptgeakprlyfSLFSDGQNKMASFVPTNVPIAMRRALEKAGLGSDDIDY 265
Cdd:cd00828 242 EL--------ALARGAPIYGRVAGT-----------------ASTTDGAGRSVPAGGKGIARAIRTALAKAGLSLDDLDV 296
                       170
                ....*....|....*....
gi 15596195 266 FVFHQPA-PFLVKAWAEGI 283
Cdd:cd00828 297 ISAHGTStPANDVAESRAI 315
PRK04262 PRK04262
hypothetical protein; Provisional
248-334 3.53e-06

hypothetical protein; Provisional


Pssm-ID: 235266 [Multi-domain]  Cd Length: 347  Bit Score: 48.36  E-value: 3.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  248 AMRRALEKAGLGSDDIDYFVFHQP-APFLVKAwAEGIGARPEQYQ--LTMGDTGVMISVSIPYTLMTGLREGKirPGDRI 324
Cdd:PRK04262 214 AAKGLMEKLGLKPSDYDYAVFHQPnGKFPLRV-AKMLGFTKEQVKpgLLTPYIGNTYSGSALLGLAAVLDVAK--PGDRI 290
                         90
                 ....*....|
gi 15596195  325 VMAGAATGWG 334
Cdd:PRK04262 291 LVVSFGSGAG 300
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
47-284 1.46e-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: 43.41  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195  47 FDPRNGENEFSLVVRAAERLLRSSDTAPDSVDMLICSASSPIMTDAGdvlpdlrgrlyprMANVLSKQLGLSRALPLDSQ 126
Cdd:cd00829   8 FGRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSF-------------PGALIAEYLGLLGKPATRVE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 127 MECASFLLNLRLAASMIRQGKAEKVLVVCSEYISNL---LDFTSRTSTLFADGCAV----------ALLTR------GDD 187
Cdd:cd00829  75 AAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVptgDEAGGRASDLEWEGPEPpggltppalyALAARrymhryGTT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596195 188 DscDLLA---------SAEHSDATFY------EVATGRW-----------------------------RLPENP-----T 218
Cdd:cd00829 155 R--EDLAkvavknhrnAARNPYAQFRkpitveDVLNSRMiadplrlldccpvsdgaaavvlaseerarELTDRPvwilgV 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596195 219 GEAKPRLYFSLFSDGQNKMASFvptnvpIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIG 284
Cdd:cd00829 233 GAASDTPSLSERDDFLSLDAAR------LAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLG 292
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH