NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|516456528|ref|WP_017845368|]
View 

MULTISPECIES: ketoacyl-ACP synthase III [Pseudomonas]

Protein Classification

ketoacyl-ACP synthase III( domain architecture ID 10093604)

beta-ketoacyl-[acyl-carrier-protein] synthase 3 initiates the elongation in type II fatty acid synthase by specifically using acetyl-CoA over acyl-CoA

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
1-306 7.23e-93

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: 278.27  E-value: 7.23e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   1 MIGIKSIASYVPADGIDNYAQGAKFAKDEEFIIGKIGSAFLPRKEAGQETSDLCVEAVNALFANNpQLKRESIDALIVVT 80
Cdd:cd00830    1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDA-GIDADDIDLIIVAT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  81 QNGDEeGLPHTAAIVQDKLGLPtHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTTMLFG 160
Cdd:cd00830   80 STPDY-LFPATACLVQARLGAK-NAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 161 DAATATWMGE-DASWLLGKAKFGTDGSGAPHLKVS--------------DGVFFMNGRQVFNFALLKVPAHLHALLDESD 225
Cdd:cd00830  158 DGAGAVVLEAtEEDPGILDSVLGSDGSGADLLTIPaggsrspfedaeggDPYLVMDGREVFKFAVRLMPESIEEALEKAG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 226 LKADDIDAFCIHQGSAAIVDAVARRFEdAPVDKFIKDMVETGNTVSSSIPLLLEKHALDSTWK---RVAISGFGVGLSWG 302
Cdd:cd00830  238 LTPDDIDWFVPHQANLRIIEAVAKRLG-LPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKkgdLVLLLGFGAGLTWG 316

                 ....
gi 516456528 303 SAIL 306
Cdd:cd00830  317 AALL 320
 
Name Accession Description Interval E-value
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
1-306 7.23e-93

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: 278.27  E-value: 7.23e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   1 MIGIKSIASYVPADGIDNYAQGAKFAKDEEFIIGKIGSAFLPRKEAGQETSDLCVEAVNALFANNpQLKRESIDALIVVT 80
Cdd:cd00830    1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDA-GIDADDIDLIIVAT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  81 QNGDEeGLPHTAAIVQDKLGLPtHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTTMLFG 160
Cdd:cd00830   80 STPDY-LFPATACLVQARLGAK-NAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 161 DAATATWMGE-DASWLLGKAKFGTDGSGAPHLKVS--------------DGVFFMNGRQVFNFALLKVPAHLHALLDESD 225
Cdd:cd00830  158 DGAGAVVLEAtEEDPGILDSVLGSDGSGADLLTIPaggsrspfedaeggDPYLVMDGREVFKFAVRLMPESIEEALEKAG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 226 LKADDIDAFCIHQGSAAIVDAVARRFEdAPVDKFIKDMVETGNTVSSSIPLLLEKHALDSTWK---RVAISGFGVGLSWG 302
Cdd:cd00830  238 LTPDDIDWFVPHQANLRIIEAVAKRLG-LPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKkgdLVLLLGFGAGLTWG 316

                 ....
gi 516456528 303 SAIL 306
Cdd:cd00830  317 AALL 320
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
2-306 1.08e-81

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: 250.03  E-value: 1.08e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   2 IGIKSIASYVPADGIDNYAQGAKFAKDEEFIIGKIGSAFLPRKEAGQETSDLCVEAVNALFANnPQLKRESIDALIVVTQ 81
Cdd:COG0332    3 VRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEA-AGIDPEDIDLIIVATV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  82 NGDEEgLPHTAAIVQDKLGLpTHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTTMLFGD 161
Cdd:COG0332   82 TPDYL-FPSTACLVQHKLGA-KNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 162 AATATWMG--EDASWLLGkAKFGTDGSGAPHLKVSDG--------------VFFMNGRQVFNFALLKVPAHLHALLDESD 225
Cdd:COG0332  160 GAGAVVLEasEEGPGILG-SVLGSDGSGADLLVVPAGgsrnppspvdegdhYLRMDGREVFKFAVRNLPEVIREALEKAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 226 LKADDIDAFCIHQGSAAIVDAVARRFEdAPVDKFIKDMVETGNTVSSSIPLLLEkHALDS----TWKRVAISGFGVGLSW 301
Cdd:COG0332  239 LTLDDIDWFIPHQANLRIIEAVAKRLG-LPEEKVVVNIDRYGNTSAASIPLALD-EALREgrikPGDLVLLAGFGAGLTW 316

                 ....*
gi 516456528 302 GSAIL 306
Cdd:COG0332  317 GAAVL 321
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
2-306 5.56e-65

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 206.85  E-value: 5.56e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   2 IGIKSIASYVPADGIDNyaqgAKFAK----DEEFIIGKIGSAFLPRKEAGQETSDLCVEA-VNALfaNNPQLKRESIDAL 76
Cdd:PRK09352   4 AKILGTGSYLPERVVTN----DDLEKmvdtSDEWIVTRTGIKERRIAAPDETTSDLATEAaKKAL--EAAGIDPEDIDLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  77 IVVTQNGDEeGLPHTAAIVQDKLGLpTHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTT 156
Cdd:PRK09352  78 IVATTTPDY-AFPSTACLVQARLGA-KNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTC 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 157 MLFGDAATATWMGEDASWLLGKAKFGTDGSGAPHLKVSDGV---------FFMNGRQVFNFALLKVPAHLHALLDESDLK 227
Cdd:PRK09352 156 VLFGDGAGAVVLGASEEPGILSTHLGSDGSYGDLLYLPGGGsrgpaspgyLRMEGREVFKFAVRELAKVAREALEAAGLT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 228 ADDIDAFCIHQGSAAIVDAVARRFeDAPVDKFIKDMVETGNTVSSSIPLLL----EKHALDSTwKRVAISGFGVGLSWGS 303
Cdd:PRK09352 236 PEDIDWLVPHQANLRIIDATAKKL-GLPMEKVVVTVDKYGNTSAASIPLALdeavRDGRIKRG-DLVLLEGFGGGLTWGA 313

                 ...
gi 516456528 304 AIL 306
Cdd:PRK09352 314 ALV 316
fabH TIGR00747
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ...
3-307 6.59e-46

3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273249 [Multi-domain]  Cd Length: 318  Bit Score: 157.54  E-value: 6.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528    3 GIKSIASYVPADGIDNyAQGAKFAK-DEEFIIGKIGsaFLPRKEAGQE--TSDLCVEAV-NALfaNNPQLKRESIDaLIV 78
Cdd:TIGR00747   4 GILGTGSYLPEKVLTN-ADLEKMVDtSDEWIVTRTG--IKERRIAADDetSSTMGFEAAkRAI--ENAGISKDDID-LII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   79 VTQNGDEEGLPHTAAIVQDKLGLpTHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTTML 158
Cdd:TIGR00747  78 VATTTPDHAFPSAACMVQAYLGI-KGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  159 FGDAATATWMGE-DASWLLGKAKFGTDGSGAPHLKVSDGV---------FFMNGRQVFNFALLKVPAHLHALLDESDLKA 228
Cdd:TIGR00747 157 FGDGAGAVVLGEsEDPGGIISTHLGADGTQGEALYLPAGGrptsgpspfITMEGNEVFKHAVRKMGDVVEETLEANGLDP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  229 DDIDAFCIHQGSAAIVDAVARRFEdAPVDKFIKDMVETGNTVSSSIPL----LLEKHALDSTwKRVAISGFGVGLSWGSA 304
Cdd:TIGR00747 237 EDIDWFVPHQANLRIIEALAKRLE-LDMSQVVKTVHKYGNTSAASIPLaldeLLRTGRIKPG-DLLLLVAFGGGLTWGAA 314

                  ...
gi 516456528  305 ILY 307
Cdd:TIGR00747 315 LVR 317
ACP_syn_III_C pfam08541
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ...
221-306 1.38e-24

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: 94.88  E-value: 1.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  221 LDESDLKADDIDAFCIHQGSAAIVDAVARRFEdAPVDKFIKDMVETGNTVSSSIPLLLEkHALDS----TWKRVAISGFG 296
Cdd:pfam08541   1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLG-LPPEKVVVNLDEYGNTSAASIPLALD-EAVEEgklkPGDLVLLVGFG 78
                          90
                  ....*....|
gi 516456528  297 VGLSWGSAIL 306
Cdd:pfam08541  79 AGLTWGAALL 88
 
Name Accession Description Interval E-value
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
1-306 7.23e-93

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: 278.27  E-value: 7.23e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   1 MIGIKSIASYVPADGIDNYAQGAKFAKDEEFIIGKIGSAFLPRKEAGQETSDLCVEAVNALFANNpQLKRESIDALIVVT 80
Cdd:cd00830    1 NARILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGETTSDLAVEAAKKALEDA-GIDADDIDLIIVAT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  81 QNGDEeGLPHTAAIVQDKLGLPtHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTTMLFG 160
Cdd:cd00830   80 STPDY-LFPATACLVQARLGAK-NAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILDWTDRSTAVLFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 161 DAATATWMGE-DASWLLGKAKFGTDGSGAPHLKVS--------------DGVFFMNGRQVFNFALLKVPAHLHALLDESD 225
Cdd:cd00830  158 DGAGAVVLEAtEEDPGILDSVLGSDGSGADLLTIPaggsrspfedaeggDPYLVMDGREVFKFAVRLMPESIEEALEKAG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 226 LKADDIDAFCIHQGSAAIVDAVARRFEdAPVDKFIKDMVETGNTVSSSIPLLLEKHALDSTWK---RVAISGFGVGLSWG 302
Cdd:cd00830  238 LTPDDIDWFVPHQANLRIIEAVAKRLG-LPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKkgdLVLLLGFGAGLTWG 316

                 ....
gi 516456528 303 SAIL 306
Cdd:cd00830  317 AALL 320
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
2-306 1.08e-81

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: 250.03  E-value: 1.08e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   2 IGIKSIASYVPADGIDNYAQGAKFAKDEEFIIGKIGSAFLPRKEAGQETSDLCVEAVNALFANnPQLKRESIDALIVVTQ 81
Cdd:COG0332    3 VRILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRIAAPDETTSDLAVEAARKALEA-AGIDPEDIDLIIVATV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  82 NGDEEgLPHTAAIVQDKLGLpTHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTTMLFGD 161
Cdd:COG0332   82 TPDYL-FPSTACLVQHKLGA-KNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSRIVDWTDRSTCVLFGD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 162 AATATWMG--EDASWLLGkAKFGTDGSGAPHLKVSDG--------------VFFMNGRQVFNFALLKVPAHLHALLDESD 225
Cdd:COG0332  160 GAGAVVLEasEEGPGILG-SVLGSDGSGADLLVVPAGgsrnppspvdegdhYLRMDGREVFKFAVRNLPEVIREALEKAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 226 LKADDIDAFCIHQGSAAIVDAVARRFEdAPVDKFIKDMVETGNTVSSSIPLLLEkHALDS----TWKRVAISGFGVGLSW 301
Cdd:COG0332  239 LTLDDIDWFIPHQANLRIIEAVAKRLG-LPEEKVVVNIDRYGNTSAASIPLALD-EALREgrikPGDLVLLAGFGAGLTW 316

                 ....*
gi 516456528 302 GSAIL 306
Cdd:COG0332  317 GAAVL 321
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
2-306 5.56e-65

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 206.85  E-value: 5.56e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   2 IGIKSIASYVPADGIDNyaqgAKFAK----DEEFIIGKIGSAFLPRKEAGQETSDLCVEA-VNALfaNNPQLKRESIDAL 76
Cdd:PRK09352   4 AKILGTGSYLPERVVTN----DDLEKmvdtSDEWIVTRTGIKERRIAAPDETTSDLATEAaKKAL--EAAGIDPEDIDLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  77 IVVTQNGDEeGLPHTAAIVQDKLGLpTHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTT 156
Cdd:PRK09352  78 IVATTTPDY-AFPSTACLVQARLGA-KNAAAFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRIVDWTDRSTC 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 157 MLFGDAATATWMGEDASWLLGKAKFGTDGSGAPHLKVSDGV---------FFMNGRQVFNFALLKVPAHLHALLDESDLK 227
Cdd:PRK09352 156 VLFGDGAGAVVLGASEEPGILSTHLGSDGSYGDLLYLPGGGsrgpaspgyLRMEGREVFKFAVRELAKVAREALEAAGLT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 228 ADDIDAFCIHQGSAAIVDAVARRFeDAPVDKFIKDMVETGNTVSSSIPLLL----EKHALDSTwKRVAISGFGVGLSWGS 303
Cdd:PRK09352 236 PEDIDWLVPHQANLRIIDATAKKL-GLPMEKVVVTVDKYGNTSAASIPLALdeavRDGRIKRG-DLVLLEGFGGGLTWGA 313

                 ...
gi 516456528 304 AIL 306
Cdd:PRK09352 314 ALV 316
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
47-306 1.74e-50

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


Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 169.66  E-value: 1.74e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  47 GQETSDLCVEAV-NALfaNNPQLKRESIDALIVVTQNGDEEgLPHTAAIVQDKLGLPtHVAAFDLSLGCSGYVYGIYAMK 125
Cdd:PRK12879  50 EEYTSDLAIKAAeRAL--ARAGLDAEDIDLIIVATTTPDYL-FPSTASQVQARLGIP-NAAAFDINAACAGFLYGLETAN 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 126 GFMEATGLKNGLLITADPYSKIVDPEDRNTTMLFGDAATATWMGEDASWL-LGKAKFGTDGSGAPHLKVS---------- 194
Cdd:PRK12879 126 GLITSGLYKKVLVIGAERLSKVTDYTDRTTCILFGDGAGAVVLEATENEPgFIDYVLGTDGDGGDILYRTglgttmdrda 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 195 ---DGVFFMNGRQVFNFALLKVPAHLHALLDESDLKADDIDAFCIHQGSAAIVDAVARRFeDAPVDKFIKDMVETGNTVS 271
Cdd:PRK12879 206 lsgDGYIVQNGREVFKWAVRTMPKGARQVLEKAGLTKDDIDWVIPHQANLRIIESLCEKL-GIPMEKTLVSVEYYGNTSA 284
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 516456528 272 SSIPLllekhALDSTWKRVAIS--------GFGVGLSWGSAIL 306
Cdd:PRK12879 285 ATIPL-----ALDLALEQGKIKpgdtlllyGFGAGLTWAALLV 322
fabH TIGR00747
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ...
3-307 6.59e-46

3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273249 [Multi-domain]  Cd Length: 318  Bit Score: 157.54  E-value: 6.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528    3 GIKSIASYVPADGIDNyAQGAKFAK-DEEFIIGKIGsaFLPRKEAGQE--TSDLCVEAV-NALfaNNPQLKRESIDaLIV 78
Cdd:TIGR00747   4 GILGTGSYLPEKVLTN-ADLEKMVDtSDEWIVTRTG--IKERRIAADDetSSTMGFEAAkRAI--ENAGISKDDID-LII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   79 VTQNGDEEGLPHTAAIVQDKLGLpTHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTTML 158
Cdd:TIGR00747  78 VATTTPDHAFPSAACMVQAYLGI-KGIPAFDLSAACAGFIYALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTDRGTCVL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  159 FGDAATATWMGE-DASWLLGKAKFGTDGSGAPHLKVSDGV---------FFMNGRQVFNFALLKVPAHLHALLDESDLKA 228
Cdd:TIGR00747 157 FGDGAGAVVLGEsEDPGGIISTHLGADGTQGEALYLPAGGrptsgpspfITMEGNEVFKHAVRKMGDVVEETLEANGLDP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  229 DDIDAFCIHQGSAAIVDAVARRFEdAPVDKFIKDMVETGNTVSSSIPL----LLEKHALDSTwKRVAISGFGVGLSWGSA 304
Cdd:TIGR00747 237 EDIDWFVPHQANLRIIEALAKRLE-LDMSQVVKTVHKYGNTSAASIPLaldeLLRTGRIKPG-DLLLLVAFGGGLTWGAA 314

                  ...
gi 516456528  305 ILY 307
Cdd:TIGR00747 315 LVR 317
PLN02326 PLN02326
3-oxoacyl-[acyl-carrier-protein] synthase III
67-306 1.26e-43

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


Pssm-ID: 215185  Cd Length: 379  Bit Score: 153.35  E-value: 1.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  67 QLKRESIDALIVVTQNGDEegLPHTAAIVQDKLGLpTHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSK 146
Cdd:PLN02326 112 GVDPEDVDLVLLCTSSPDD--LFGSAPQVQAALGC-TNALAFDLTAACSGFVLGLVTAARFIRGGGYKNVLVIGADALSR 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 147 IVDPEDRNTTMLFGDAATATWM---GEDASWLLGKAkFGTDGSGAPHLKV--------------SDGVFF---------- 199
Cdd:PLN02326 189 YVDWTDRGTCILFGDGAGAVVLqacDDDEDGLLGFD-MHSDGNGHKHLHAtfkgedddssggntNGVGDFppkkasysci 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 200 -MNGRQVFNFALLKVPAHLHALLDESDLKADDIDAFCIHQGSAAIVDAVARRFeDAPVDKFIKDMVETGNTVSSSIPLLL 278
Cdd:PLN02326 268 qMNGKEVFKFAVRCVPQVIESALQKAGLTAESIDWLLLHQANQRIIDAVAQRL-GIPPEKVISNLANYGNTSAASIPLAL 346
                        250       260       270
                 ....*....|....*....|....*....|.
gi 516456528 279 EKHALDSTWKR---VAISGFGVGLSWGSAIL 306
Cdd:PLN02326 347 DEAVRSGKVKKgdvIATAGFGAGLTWGSAIV 377
fabH CHL00203
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
4-306 3.86e-43

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


Pssm-ID: 164577 [Multi-domain]  Cd Length: 326  Bit Score: 150.87  E-value: 3.86e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   4 IKSIASYVPADGIDNYAQGAKFAKDEEFIIGKIGsaFLPRKEAGQETS--DLCVEAVN-ALFANNpqLKRESIDALIVVT 80
Cdd:CHL00203   5 ILSTGSSVPNFSVENQQFEDIIETSDHWISTRTG--IKKRHLAPSSTSltKLAAEAANkALDKAH--MDPLEIDLIILAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  81 QNGDEegLPHTAAIVQDKLGLPTHVAaFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTTMLFG 160
Cdd:CHL00203  81 STPDD--LFGSASQLQAEIGATRAVA-FDITAACSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTCILFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 161 DAATATWMGEDASWLLGKAKFGTDGSGAPHL---------------KVSDGVF---FMNGRQVFNFALLKVPAHLHALLD 222
Cdd:CHL00203 158 DGAGAAIIGASYENSILGFKLCTDGKLNSHLqlmnkpvnnqsfgttKLPQGQYqsiSMNGKEVYKFAVFQVPAVIIKCLN 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 223 ESDLKADDIDAFCIHQGSAAIVDAVARRFEdAPVDKFIKDMVETGNTVSSSIPLllekhALDSTWKR--------VAISG 294
Cdd:CHL00203 238 ALNISIDEVDWFILHQANKRILEAIANRLS-VPNSKMITNLEKYGNTSAASIPL-----ALDEAIQNnkiqpgqiIVLSG 311
                        330
                 ....*....|..
gi 516456528 295 FGVGLSWGSAIL 306
Cdd:CHL00203 312 FGAGLTWGAIVL 323
PRK12880 PRK12880
beta-ketoacyl-ACP synthase III;
51-306 4.10e-35

beta-ketoacyl-ACP synthase III;


Pssm-ID: 171793  Cd Length: 353  Bit Score: 130.09  E-value: 4.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  51 SDLCVEAVNALFaNNPQLKRESIDALIVVTQNGDEeGLPHTAAIVQDKLGLPTHVAAFDLSLGCSGYVYGIYAMKGFMEa 130
Cdd:PRK12880  61 SDLGKHAANTLL-QGLNIDKNSLDALIVVTQSPDF-FMPSTACYLHQLLNLSSKTIAFDLGQACAGYLYGLFVAHSLIQ- 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 131 TGLKNGLLITADPYSKIVDPEDRNTTMLFGDAATATwmgedaswLLGKAKF-------GTDGSGAPHLKVSDGVF----- 198
Cdd:PRK12880 138 SGLGKILLICGDTLSKFIHPKNMNLAPIFGDGVSAT--------LIEKTDFneaffelGSDGKYFDKLIIPKGAMripka 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 199 --------------------FMNGRQVFNFALLKVPAHLHALLDESDLKADDIDAFCIHQGSAAIVDAVAR--RFEDAPV 256
Cdd:PRK12880 210 difnddslmqteefrqlenlYMDGANIFNMALECEPKSFKEILEFSKVDEKDIAFHLFHQSNAYLVDCIKEelKLNDDKV 289
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 516456528 257 DKFIkdMVETGNTVSSSIPLLLEKHALDSTWKrVAISGFGVGLSWGSAIL 306
Cdd:PRK12880 290 PNFI--MEKYANLSACSLPALLCELDTPKEFK-ASLSAFGAGLSWGSAVL 336
PRK05963 PRK05963
beta-ketoacyl-ACP synthase III;
10-306 2.32e-29

beta-ketoacyl-ACP synthase III;


Pssm-ID: 180328 [Multi-domain]  Cd Length: 326  Bit Score: 114.05  E-value: 2.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  10 YVPADGIDNYAQGAKFAKDEEFIIGKIGSAFLPRKEAGQETSDLCVEAVNALFANnPQLKRESIDALIVVTQNGDEEgLP 89
Cdd:PRK05963  12 AVPDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETLSDLAASAGDMALSD-AGIERSDIALTLLATSTPDHL-LP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  90 HTAAIVQDKLGLPtHVAAFDLSLGCSGYVYGIYAMKGFMEATGlKNGLLITADPYSKIVDPEDRNTTMLFGDAATATWMG 169
Cdd:PRK05963  90 PSAPLLAHRLGLQ-NSGAIDLAGACAGFLYALVLADGFVRAQG-KPVLVVAANILSRRINMAERASAVLFADAAGAVVLA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 170 ---EDASWLLGkAKFGTDGSG---------------APHLKVSDGVFFM-NGRQVFNFALLKVPAHLHALLDESDLKADD 230
Cdd:PRK05963 168 psaKANSGVLG-SQLISDGSHydlikipaggsarpfAPERDASEFLMTMqDGRAVFTEAVRMMSGASQNVLASAAMTPQD 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 231 IDAFCIHQGSAAIVDAVARRFEDAPvDKFIKDMVETGNTVSSSIPLLL----EKHALDSTwKRVAISGFGVGLSWGSAIL 306
Cdd:PRK05963 247 IDRFFPHQANARIVDKVCETIGIPR-AKAASTLETYGNSSAATIPLSLslanLEQPLREG-ERLLFAAAGAGMTGGAVVM 324
ACP_syn_III_C pfam08541
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ...
221-306 1.38e-24

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: 94.88  E-value: 1.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  221 LDESDLKADDIDAFCIHQGSAAIVDAVARRFEdAPVDKFIKDMVETGNTVSSSIPLLLEkHALDS----TWKRVAISGFG 296
Cdd:pfam08541   1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLG-LPPEKVVVNLDEYGNTSAASIPLALD-EAVEEgklkPGDLVLLVGFG 78
                          90
                  ....*....|
gi 516456528  297 VGLSWGSAIL 306
Cdd:pfam08541  79 AGLTWGAALL 88
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
108-185 2.62e-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: 88.34  E-value: 2.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  108 FDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTTMLFGDAATATWMG--EDASWLLGKAKFGTDG 185
Cdd:pfam08545   1 FDINAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEatDEPGARILDSVLGSDG 80
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
1-306 9.80e-20

"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: 87.49  E-value: 9.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   1 MIGIKSIASYVPADGIDN--YAQGAKFAKDEEFIigKIGSaflpRKEAGQETS--DLCVEAVNALFANNpQLKRESIDAL 76
Cdd:cd00827    1 DVGIEAIGAYLPRYRVDNeeLAEGLGVDPGKYTT--GIGQ----RHMAGDDEDvpTMAVEAARRALERA-GIDPDDIGLL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  77 IVVTQNGDEEGLPHtAAIVQDKLGLpTHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTT 156
Cdd:cd00827   74 IVATESPIDKGKSA-ATYLAELLGL-TNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDEGSALEP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 157 MlFGDAATA---------TWMGEDASWLLGKAKFGTDGSGAPHLKVSDGVFF---------MNGRQVFNFALLKVPAHLH 218
Cdd:cd00827  152 T-LGDGAAAmlvsrnpgiLAAGIVSTHSTSDPGYDFSPYPVMDGGYPKPCKLayairltaePAGRAVFEAAHKLIAKVVR 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 219 ALLDESDLKaDDIDAFCIHQGSAAIVDAVARRFEDAPVDKFIKDMV----ETGNTVSSSIPLLLEkHALDS----TWKRV 290
Cdd:cd00827  231 KALDRAGLS-EDIDYFVPHQPNGKKILEAVAKKLGGPPEKASQTRWillrRVGNMYAASILLGLA-SLLESgklkAGDRV 308
                        330
                 ....*....|....*.
gi 516456528 291 AISGFGVGLSWGSAIL 306
Cdd:cd00827  309 LLFSYGSGFTAEAFVL 324
PRK07204 PRK07204
beta-ketoacyl-ACP synthase III;
2-306 1.18e-19

beta-ketoacyl-ACP synthase III;


Pssm-ID: 235964  Cd Length: 329  Bit Score: 87.58  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   2 IGIKSIASYVPADGIDNYAQGAKFAKDEEFIIGKigSAFLPRKEAGQETSDLcVEAVNALFA-NNPQLKRESIDALIVVT 80
Cdd:PRK07204   5 ISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKK--SGVKTRHFVDGETSSY-MGAEAAKKAvEDAKLTLDDIDCIICAS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  81 QNGdEEGLPHTAAIVQDKLGLP-THVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKIVDPEDRNTTMLF 159
Cdd:PRK07204  82 GTI-QQAIPCTASLIQEQLGLQhSGIPCFDINSTCLSFITALDTISYAIECGRYKRVLIISSEISSVGLNWGQNESCILF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 160 GDAATATWM--GEDASWLLGkAKFGTDGSGAPHLKV-----------------SDGVFFMNGRQVFNFALLKVPAHLHAL 220
Cdd:PRK07204 161 GDGAAAVVItkGDHSSRILA-SHMETYSSGAHLSEIrgggtmihpreyseerkEDFLFDMNGRAIFKLSSKYLMKFIDKL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 221 LDESDLKADDIDAFCIHQGSAAIVDAVARRFeDAPVDKFIKDMVETGNTVSSSIPLLLEkHALDST----WKRVAISGFG 296
Cdd:PRK07204 240 LMDAGYTLADIDLIVPHQASGPAMRLIRKKL-GVDEERFVTIFEDHGNMIAASIPVALF-EAIKQKkvqrGNKILLLGTS 317
                        330
                 ....*....|
gi 516456528 297 VGLSWGSAIL 306
Cdd:PRK07204 318 AGLSIGGILL 327
PRK07515 PRK07515
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
68-306 4.99e-15

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


Pssm-ID: 236037  Cd Length: 372  Bit Score: 74.53  E-value: 4.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  68 LKRESIDALIVVTQNgDEEGLPHTAAIVQDKLGlpTHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADPYSKI 147
Cdd:PRK07515 112 RTAEDIDAVIVACSN-MQRAYPAMAIEIQQALG--IEGFAFDMNVACSSATFGIQTAANAIRSGSARRVLVVNPEICSGH 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 148 VDPEDRNTTMLFGDAATATWMGEDA------SW-LLG-----------KAKFG----TDGSGAPhlkVSDGVFFMNGRQV 205
Cdd:PRK07515 189 LNFRDRDSHFIFGDVATAVIVERADtatsagGFeILGtrlftqfsnniRNNFGflnrADPEGIG---ARDKLFVQEGRKV 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 206 FNFALLKVPAHLHALLDESDLKADDIDAFCIHQGSAAIVDAVARRF-------EDAPVdkfIKDmvETGNTVSSSIPLLL 278
Cdd:PRK07515 266 FKEVCPMVAEHIVEHLAENGLTPADVKRFWLHQANINMNQLIGKKVlgrdatpEEAPV---ILD--EYANTSSAGSIIAF 340
                        250       260
                 ....*....|....*....|....*....
gi 516456528 279 EKHALDSTWKRVA-ISGFGVGLSWGSAIL 306
Cdd:PRK07515 341 HKHSDDLAAGDLGvICSFGAGYSIGSVIV 369
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
49-300 5.30e-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: 71.49  E-value: 5.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  49 ETSDLCVEAVNALFANNPQLKREsIDALIVVTQNG-DEEGLphTAAIVQdKLGLPTHVAAFDLS-LGCSGYVYGIYAMKG 126
Cdd:cd00831   84 EARELAEEAARGALDEAGLRPSD-IDHLVVNTSTGnPTPSL--DAMLIN-RLGLRPDVKRYNLGgMGCSAGAIALDLAKD 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 127 FMEATGLKNGLLITADPYSKIVDPEDRNTTM----LFGDAATATWMGEDASWLLGKAKFG----------TDGSGAPHLK 192
Cdd:cd00831  160 LLEANPGARVLVVSTELCSLWYRGPDHRSMLvgnaLFGDGAAAVLLSNDPRDRRRERPLFelvraastllPDSEDAMGWH 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 193 VSDGVFFMN-GRQVFNFALLKVPAHLHALLDE--SDLKADDIDAFCIHQGSAAIVDAVARRFEDAPVDKFIKDMV--ETG 267
Cdd:cd00831  240 LGEEGLTFVlSRDVPRLVEKNLERVLRKLLARlgIGLFKLAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMVlrRYG 319
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 516456528 268 NTVSSSIPLLLEKHALDSTWK---RVAISGFGVGLS 300
Cdd:cd00831  320 NMSSSSVLYVLAYMEAKGRVKrgdRGLLIAFGPGFT 355
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
1-298 1.12e-10

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: 61.73  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   1 MIGIKSIASYVP-----------ADGIDNyaqgAKFAKDeefiIGKIGSAFLPrkeAGQETSDLCVEAVNALFANNpQLK 69
Cdd:COG3425    2 KVGIDAIGFYIPryrldleelaeARGVDP----EKYTKG----LGQEEKSVPP---PDEDAVTMAANAARRALDRA-GID 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  70 RESIDALIVVTQNGDEEGLPhTAAIVQDKLGLPTHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLLITADpYSKIvd 149
Cdd:COG3425   70 PSDIGAVYVGTESGPDASKP-IATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASD-IARY-- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 150 peDRNTT--MLFGDAATATWMGED---ASWLLGKAKFGTDgsgaphlkVSDgvFFM-NGRQvfnFAL----LKVPAHLHA 219
Cdd:COG3425  146 --GPGSAgeYTQGAGAVAMLVGADpriAEIEGGSGSYTTD--------VMD--FWRpNGSD---YPLvdgrFSEPAYLDH 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 220 L-------LDESDLKADDIDAFCIHQGSAAIVDAVAR---RFEDAPVDKFIKDMVET--------GNTVSSSIPL----L 277
Cdd:COG3425  211 LeeavkdyKEKTGLKPDDFDYFVFHQPFGKMPKKAAKklgRKAGREIQEDFEEQVEPsliysrriGNTYTGSLYLglasL 290
                        330       340
                 ....*....|....*....|.
gi 516456528 278 LEkHALDSTWKRVAISGFGVG 298
Cdd:COG3425  291 LD-NAKDLPGDRIGLFSYGSG 310
PRK09258 PRK09258
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
45-299 1.71e-09

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


Pssm-ID: 181732  Cd Length: 338  Bit Score: 57.97  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  45 EAGQETSDLCVEAVNALFANNpQLKRESIDALI--VVTQNGDEeglPHTAAIVQDKLGLPTHVAAFDLSLGCSGYVYGIY 122
Cdd:PRK09258  56 PEGTQLSDGAIAAGRKALAEA-GIDPSDIGLLIntSVCRDYLE---PATACRVHHNLGLPKSCANFDVSNACLGFLNGML 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 123 AMKGFMEATGLKNGLLITADPYSKIVDP------EDRNTTMLFGDA-ATATWMGEDASWLLGKAKFGTDGS---GAPHLK 192
Cdd:PRK09258 132 DAANMIELGQIDYALVVSGESAREIVEAtidrllAPETTREDFAQSfATLTLGSGAAAAVLTRGSLHPRGHrllGGVTRA 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 193 VSD-------GVFFM--NGRQVFNFALLKVPAHLHALLDESDLKADDIDAFCIHQGSAAIVDAVARRFEDAPVdkfiKDM 263
Cdd:PRK09258 212 ATEhhelcqgGRDGMrtDAVGLLKEGVELAVDTWEAFLAQLGWAVEQVDRVICHQVGAAHTRAILKALGIDPE----KVF 287
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 516456528 264 V---ETGNTVSSSIPLLL----EKHALdSTWKRVAISGFGVGL 299
Cdd:PRK09258 288 TtfpTLGNMGPASLPITLamaaEEGFL-KPGDRVALLGIGSGL 329
PRK06840 PRK06840
3-oxoacyl-ACP synthase;
1-186 7.97e-08

3-oxoacyl-ACP synthase;


Pssm-ID: 235872  Cd Length: 339  Bit Score: 53.09  E-value: 7.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528   1 MIGIKSIASYVPadgiDNYAQGAKFAKD----EEFIIGKIGSAFLPRKEAGQETSDLCVEAVNALFANnPQLKRESIDAL 76
Cdd:PRK06840   4 NVGIVGTGVYLP----KDVMTAEEIAEKtgipEEVVIEKFGIYEKPVPGPEDHTSDMAIAAAKPALKQ-AGVDPAAIDVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  77 IVVTQNGDEEGLPHTAAIVQDKLGLpTHVAAFDLSLGCSGYVYGIYAMKGFMEATG-LKNGLLITADPYSKIVDPEDRNT 155
Cdd:PRK06840  79 IYIGSEHKDYPVWSSAPKIQHEIGA-KNAWAFDIMAVCASFPIALKVAKDLLYSDPsIENVLLVGGYRNSDLVDYDNPRT 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 516456528 156 TMLF--GDAATATWMGEDA--SWLLGKAkFGTDGS 186
Cdd:PRK06840 158 RFMFnfAAGGSAALLKKDAgkNRILGSA-IITDGS 191
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
89-306 3.96e-05

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: 44.55  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528  89 PHTAAIVQDKLGLptHVAAFDLSLGCSGYVYGIYAMKGFMEATGLKNGLL----ITADPYSKIVDP-------------- 150
Cdd:cd00825   73 PGASGQIATPLGI--HGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAggseELAAPMDCEFDAmgalstpekasrtf 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 151 EDRNTTMLFGDAATATWMGEDASWLLGKA--KFGTDGSGAPHLKVSDGVFFMNGRQVfnfallkVPAHLHALlDESDLKA 228
Cdd:cd00825  151 DAAADGFVFGDGAGALVVEELEHALARGAhiYAEIVGTAATIDGAGMGAFAPSAEGL-------ARAAKEAL-AVAGLTV 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516456528 229 DDIDAFCIHQGSAAIVDAVARRF---EDAPVDKFIK-DMVETGNTVSSSIPLLLEK--------------------HALD 284
Cdd:cd00825  223 WDIDYLVAHGTGTPIGDVKELKLlrsEFGDKSPAVSaTKAMTGNLSSAAVVLAVDEavlmlehgfippsihieeldEAGL 302
                        250       260       270
                 ....*....|....*....|....*....|
gi 516456528 285 STWKR--------VAISGFGVGLSWGSAIL 306
Cdd:cd00825  303 NIVTEttprelrtALLNGFGLGGTNATLVL 332
 
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