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Conserved domains on  [gi|1853433212|gb|QKQ07521|]
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hydroxymethylglutaryl-CoA synthase [Staphylococcus saprophyticus]

Protein Classification

hydroxymethylglutaryl-CoA synthase family protein( domain architecture ID 11465766)

hydroxymethylglutaryl-CoA synthase family protein, similar to Haloferax volcanii hydroxymethylglutaryl-CoA synthase (HMG-CoA synthase) which catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA, and Bacillus subtilis 3-hydroxy-3-methylglutaryl-ACP synthase PksG which catalyzes the condensation between the acetyl group attached to acyl-carrier-protein AcpK and a beta-ketothioester polyketide intermediate in a reaction analogous to that catalyzed by HMG-CoA synthase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 1-385 5.18e-171

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: 482.37  E-value: 5.18e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212   1 MTVGIDQINFYVPRFYVDMAKLAESRQVDPNKYLLGIGQTEMSVSPMSQDIVSMGANAAKAIVTDE--DKKQISMVIVAT 78
Cdd:COG3425     1 MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDRAgiDPSDIGAVYVGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  79 ESAIDSAKASAVQIHNLLGIQPFARCIEMKEACYAATPAIQLAKDYLAQRPDEKVLVIASDTARYGLHSGGEPTQGAGAV 158
Cdd:COG3425    81 ESGPDASKPIATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIARYGPGSAGEYTQGAGAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 159 AMMISQNPRILELNDDAVAFTEDVYDFWRPSGQAYPLVDGALSKDAYIRSFQESWQEYARRHNKSLADFKSLCFHVPFTK 238
Cdd:COG3425   161 AMLVGADPRIAEIEGGSGSYTTDVMDFWRPNGSDYPLVDGRFSEPAYLDHLEEAVKDYKEKTGLKPDDFDYFVFHQPFGK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 239 MGKKALDSILtDDIDAETKERLTSGYDAATYYNRYVGNIYTGSLYLSLISLLETHDLSANDTIGLFSYGSGSVGEFFSGK 318
Cdd:COG3425   241 MPKKAAKKLG-RKAGREIQEDFEEQVEPSLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGT 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1853433212 319 IVEGYQDVLDIQGHKDLLNNREEISVETYESFFNrfdnlEFDHETELENEKNTIFYLESINDHIRNY 385
Cdd:COG3425   320 VTPGIEERLRRPGVEEQLANRRYLSYAEYEKLRG-----KILPEDAEDVTLPGEFVLTGIKDHERIY 381
 
Name Accession Description Interval E-value
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 1-385 5.18e-171

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: 482.37  E-value: 5.18e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212   1 MTVGIDQINFYVPRFYVDMAKLAESRQVDPNKYLLGIGQTEMSVSPMSQDIVSMGANAAKAIVTDE--DKKQISMVIVAT 78
Cdd:COG3425     1 MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDRAgiDPSDIGAVYVGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  79 ESAIDSAKASAVQIHNLLGIQPFARCIEMKEACYAATPAIQLAKDYLAQRPDEKVLVIASDTARYGLHSGGEPTQGAGAV 158
Cdd:COG3425    81 ESGPDASKPIATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIARYGPGSAGEYTQGAGAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 159 AMMISQNPRILELNDDAVAFTEDVYDFWRPSGQAYPLVDGALSKDAYIRSFQESWQEYARRHNKSLADFKSLCFHVPFTK 238
Cdd:COG3425   161 AMLVGADPRIAEIEGGSGSYTTDVMDFWRPNGSDYPLVDGRFSEPAYLDHLEEAVKDYKEKTGLKPDDFDYFVFHQPFGK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 239 MGKKALDSILtDDIDAETKERLTSGYDAATYYNRYVGNIYTGSLYLSLISLLETHDLSANDTIGLFSYGSGSVGEFFSGK 318
Cdd:COG3425   241 MPKKAAKKLG-RKAGREIQEDFEEQVEPSLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGT 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1853433212 319 IVEGYQDVLDIQGHKDLLNNREEISVETYESFFNrfdnlEFDHETELENEKNTIFYLESINDHIRNY 385
Cdd:COG3425   320 VTPGIEERLRRPGVEEQLANRRYLSYAEYEKLRG-----KILPEDAEDVTLPGEFVLTGIKDHERIY 381
HMG-CoA-S_prok TIGR01835
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
 3-385 3.10e-165

3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of hydroxymethylglutaryl-CoA (HMG-CoA) synthases is found in a limited spectrum of mostly gram-positive bacteria which make isopentenyl pyrophosphate (IPP) via the mevalonate pathway. This pathway is found primarily in eukaryotes and archaea, but the bacterial homologs are distinct, having aparrently diverged after being laterally transferred from an early eukaryote. HMG-CoA synthase is the first step in the pathway and joins acetyl-CoA with acetoacetyl-CoA with the release of one molecule of CoA. The Borellia sequence may have resulted from a separate lateral transfer event.


Pssm-ID: 213655 [Multi-domain]  Cd Length: 379  Bit Score: 467.69  E-value: 3.10e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212   3 VGIDQINFYVPRFYVDMAKLAESRQVDPNKYLLGIGQTEMSVSPMSQDIVSMGANAAKAIVTDEDKKQISMVIVATESAI 82
Cdd:TIGR01835   1 IGIDKISFFTPQNYLDMTALAEARGVDPEKFHIGIGQKKMAVPPIDEDIVTMAASAAKPILDRNDKQKIDMVIFGTESGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  83 DSAKASAVQIHNLLGIQPFARCIEMKEACYAATPAIQLAKDYLAQRPDEKVLVIASDTARYGLHSGGEPTQGAGAVAMMI 162
Cdd:TIGR01835  81 DQSKAAAVYVHGLLGLQPFCRSFELKQACYGATAALQMAKGHVALSPDRKVLVIASDIAKYGLESPGEPTQGAGAVAMLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 163 SQNPRILELNDDAVAFTEDVYDFWRPSGQAYPLVDGALSKDAYIRSFQESWQEYARRHNKSLADFKSLCFHVPFTKMGKK 242
Cdd:TIGR01835 161 SADPKLLAINEDSVLYTDDIMDFWRPNYSTTALVDGQYSNEQYLNAFENAWNDYAKRTGLSLADFAAFCFHVPFTKMGLK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 243 ALDSILtDDIDAETKERLTSGYDAATYYNRYVGNIYTGSLYLSLISLLE-THDLSANDTIGLFSYGSGSVGEFFSGKIVE 321
Cdd:TIGR01835 241 ALRHIL-KKNYEDEDESVQNAYLESIIYNREVGNLYTGSLYLGLASLLEnAFEDTTGDKIGLFSYGSGAVAEFFSGTLVA 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1853433212 322 GYQDVLDIQGHKDLLNNREEISVETYESFFNRFDNLEFDHETELENEkntiFYLESINDHIRNY 385
Cdd:TIGR01835 320 GYRDHLKKERHLALLKNRTNLSYAEYEALFEETLPTDGDQPGEDRGF----FRLAGINDHKRIY 379
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 2-317 3.10e-72

"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: 228.47  E-value: 3.10e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212   2 TVGIDQINFYVPRFYVDMAKLAESRQVDPNKYLLGIGQTEM-----SVSPMSQDIVSMGANAAKaivtdEDKKQISMVIV 76
Cdd:cd00827     1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMagddeDVPTMAVEAARRALERAG-----IDPDDIGLLIV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  77 ATESAIDSAKASAVQIHNLLGIQpFARCIEMKEACYAATPAIQLAKDYLAQRPDEKVLVIASDTARYGLH--SGGEPTQG 154
Cdd:cd00827    76 ATESPIDKGKSAATYLAELLGLT-NAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDegSALEPTLG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 155 AGAVAMMISQNPRILELNDDAVAFTED---------VYDFWRPSGQAYPLVDGALSKDAYIRSFQESWQEYARRHNKSLA 225
Cdd:cd00827   155 DGAAAMLVSRNPGILAAGIVSTHSTSDpgydfspypVMDGGYPKPCKLAYAIRLTAEPAGRAVFEAAHKLIAKVVRKALD 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 226 DFKS---LCFHVPFTKMGKKALDSILTDDIDAETKERLTSGYdaatyYNRYVGNIYTGSLYLSLISLLETHDLSANDTIG 302
Cdd:cd00827   235 RAGLsedIDYFVPHQPNGKKILEAVAKKLGGPPEKASQTRWI-----LLRRVGNMYAASILLGLASLLESGKLKAGDRVL 309

                         330
                  ....*....|....*
gi 1853433212 303 LFSYGSGSVGEFFSG 317
Cdd:cd00827   310 LFSYGSGFTAEAFVL 324
PLN02577 PLN02577
hydroxymethylglutaryl-CoA synthase
 3-383 1.62e-37

hydroxymethylglutaryl-CoA synthase


Pssm-ID: 178189 [Multi-domain]  Cd Length: 459  Bit Score: 141.03  E-value: 1.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212   3 VGIDQINFYVPRFYVDMAKLAESRQVDPNKYLLGIGQTEMSVSPMSQDIVSMGANAAKAIVT--DEDKKQISMVIVATES 80
Cdd:PLN02577    5 VGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEkyNIDPKQIGRLEVGSET 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  81 AIDSAKAsavqIHNLLgIQPFARC----IE---MKEACYAATPAIQLAKDYLAQRP-DEKV-LVIASDTARYGlHSGGEP 151
Cdd:PLN02577   85 VIDKSKS----IKTFL-MQLFEESgntdIEgvdSTNACYGGTAALLNCVNWVESSSwDGRYgLVVAADSAVYA-EGPARP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 152 TQGAGAVAMMISQN-PRILELNDDAvAFTEDVYDFWRPSGQA-YPLVDGALSKDAYIRSFQESWQEYARRHNK------S 223
Cdd:PLN02577  159 TGGAGAVAMLVGPNaPIVFESKYRG-SHMAHVYDFYKPDLASeYPVVDGKLSQTCYLMALDSCYKRFCEKYEKlegkqfS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 224 LADFKSLCFHVPFTKMGKKAL--------------------------------DSILTDDIDAETKERLTSGYDA----A 267
Cdd:PLN02577  238 ISDADYFVFHAPYNKLVQKSFarlvyndfqrnassvdedakeklapfaglssdESYQNRDLEKVSQQVAKPLYDAkvqpT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 268 TYYNRYVGNIYTGSL-YLSLISLLETHDLSANDTIGLFSYGSGSVGEFFSGKIVEGYQ--DVLDIQGHKDL---LNNREE 341
Cdd:PLN02577  318 TLIPKQVGNMYTASLyAALASLVHNKHSELAGKRILMFSYGSGLTATMFSLRLHEGQHpfSLSNIAKVMDVsekLKSRHE 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1853433212 342 IS----VETYESFFNRFDNLEFDHETELENEKNTIFYLESINDHIR 383
Cdd:PLN02577  398 VSpekfVETLKLMEHRYGAKDFVPSKDVSLLAPGTYYLTEVDSLYR 443
HMG_CoA_synt_C pfam08540
Hydroxymethylglutaryl-coenzyme A synthase C terminal;
178-385 7.49e-17

Hydroxymethylglutaryl-coenzyme A synthase C terminal;


Pssm-ID: 400722  Cd Length: 280  Bit Score: 79.83  E-value: 7.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 178 FTEDVYDFWRPS-GQAYPLVDGALSKDAYIRSFQESWQEYARRHNK---------SLADFKSLCFHVPFTKMGKKALDSI 247
Cdd:pfam08540  11 HMEHAYDFYKPDlTSEYPVVDGKLSLSCYLKALDRCYKNYRKKINRitkdgdkifGLNDFDYMIFHSPTCKLVQKSLARL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 248 LTDD------------IDAETKERLTSGYD-------------------------AATYYNRYVGNIYTGSLYLSLIS-- 288
Cdd:pfam08540  91 LYNDflsnpssdkfngVDEKLTAFGGLTLDesytdkdlekafmklskpffkkkvqPSLLVPTNNGNMYTASLYAALASll 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 289 LLETHDLSANDTIGLFSYGSGSVGEFFSGKIVegyQDV-----LDIQGHKDL---LNNREEISVETYESFFNRFDNL--- 357
Cdd:pfam08540 171 SHVSADDLAGKRIGAFSYGSGLAATLFSLRVK---QDVspgsiLDIASVLDLgkrLDSRICVTPEEFTEAMELREQAhlk 247

                         250       260       270
                  ....*....|....*....|....*....|
gi 1853433212 358 -EFDHETELENEKNTIFYLESIND-HIRNY 385
Cdd:pfam08540 248 kNFKPQGSIDSLFPGTYYLTNVDDkFRRSY 277
 
Name Accession Description Interval E-value
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 1-385 5.18e-171

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: 482.37  E-value: 5.18e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212   1 MTVGIDQINFYVPRFYVDMAKLAESRQVDPNKYLLGIGQTEMSVSPMSQDIVSMGANAAKAIVTDE--DKKQISMVIVAT 78
Cdd:COG3425     1 MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDRAgiDPSDIGAVYVGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  79 ESAIDSAKASAVQIHNLLGIQPFARCIEMKEACYAATPAIQLAKDYLAQRPDEKVLVIASDTARYGLHSGGEPTQGAGAV 158
Cdd:COG3425    81 ESGPDASKPIATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIARYGPGSAGEYTQGAGAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 159 AMMISQNPRILELNDDAVAFTEDVYDFWRPSGQAYPLVDGALSKDAYIRSFQESWQEYARRHNKSLADFKSLCFHVPFTK 238
Cdd:COG3425   161 AMLVGADPRIAEIEGGSGSYTTDVMDFWRPNGSDYPLVDGRFSEPAYLDHLEEAVKDYKEKTGLKPDDFDYFVFHQPFGK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 239 MGKKALDSILtDDIDAETKERLTSGYDAATYYNRYVGNIYTGSLYLSLISLLETHDLSANDTIGLFSYGSGSVGEFFSGK 318
Cdd:COG3425   241 MPKKAAKKLG-RKAGREIQEDFEEQVEPSLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGT 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1853433212 319 IVEGYQDVLDIQGHKDLLNNREEISVETYESFFNrfdnlEFDHETELENEKNTIFYLESINDHIRNY 385
Cdd:COG3425   320 VTPGIEERLRRPGVEEQLANRRYLSYAEYEKLRG-----KILPEDAEDVTLPGEFVLTGIKDHERIY 381
HMG-CoA-S_prok TIGR01835
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
 3-385 3.10e-165

3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of hydroxymethylglutaryl-CoA (HMG-CoA) synthases is found in a limited spectrum of mostly gram-positive bacteria which make isopentenyl pyrophosphate (IPP) via the mevalonate pathway. This pathway is found primarily in eukaryotes and archaea, but the bacterial homologs are distinct, having aparrently diverged after being laterally transferred from an early eukaryote. HMG-CoA synthase is the first step in the pathway and joins acetyl-CoA with acetoacetyl-CoA with the release of one molecule of CoA. The Borellia sequence may have resulted from a separate lateral transfer event.


Pssm-ID: 213655 [Multi-domain]  Cd Length: 379  Bit Score: 467.69  E-value: 3.10e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212   3 VGIDQINFYVPRFYVDMAKLAESRQVDPNKYLLGIGQTEMSVSPMSQDIVSMGANAAKAIVTDEDKKQISMVIVATESAI 82
Cdd:TIGR01835   1 IGIDKISFFTPQNYLDMTALAEARGVDPEKFHIGIGQKKMAVPPIDEDIVTMAASAAKPILDRNDKQKIDMVIFGTESGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  83 DSAKASAVQIHNLLGIQPFARCIEMKEACYAATPAIQLAKDYLAQRPDEKVLVIASDTARYGLHSGGEPTQGAGAVAMMI 162
Cdd:TIGR01835  81 DQSKAAAVYVHGLLGLQPFCRSFELKQACYGATAALQMAKGHVALSPDRKVLVIASDIAKYGLESPGEPTQGAGAVAMLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 163 SQNPRILELNDDAVAFTEDVYDFWRPSGQAYPLVDGALSKDAYIRSFQESWQEYARRHNKSLADFKSLCFHVPFTKMGKK 242
Cdd:TIGR01835 161 SADPKLLAINEDSVLYTDDIMDFWRPNYSTTALVDGQYSNEQYLNAFENAWNDYAKRTGLSLADFAAFCFHVPFTKMGLK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 243 ALDSILtDDIDAETKERLTSGYDAATYYNRYVGNIYTGSLYLSLISLLE-THDLSANDTIGLFSYGSGSVGEFFSGKIVE 321
Cdd:TIGR01835 241 ALRHIL-KKNYEDEDESVQNAYLESIIYNREVGNLYTGSLYLGLASLLEnAFEDTTGDKIGLFSYGSGAVAEFFSGTLVA 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1853433212 322 GYQDVLDIQGHKDLLNNREEISVETYESFFNRFDNLEFDHETELENEkntiFYLESINDHIRNY 385
Cdd:TIGR01835 320 GYRDHLKKERHLALLKNRTNLSYAEYEALFEETLPTDGDQPGEDRGF----FRLAGINDHKRIY 379
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 2-317 3.10e-72

"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: 228.47  E-value: 3.10e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212   2 TVGIDQINFYVPRFYVDMAKLAESRQVDPNKYLLGIGQTEM-----SVSPMSQDIVSMGANAAKaivtdEDKKQISMVIV 76
Cdd:cd00827     1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMagddeDVPTMAVEAARRALERAG-----IDPDDIGLLIV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  77 ATESAIDSAKASAVQIHNLLGIQpFARCIEMKEACYAATPAIQLAKDYLAQRPDEKVLVIASDTARYGLH--SGGEPTQG 154
Cdd:cd00827    76 ATESPIDKGKSAATYLAELLGLT-NAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLDegSALEPTLG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 155 AGAVAMMISQNPRILELNDDAVAFTED---------VYDFWRPSGQAYPLVDGALSKDAYIRSFQESWQEYARRHNKSLA 225
Cdd:cd00827   155 DGAAAMLVSRNPGILAAGIVSTHSTSDpgydfspypVMDGGYPKPCKLAYAIRLTAEPAGRAVFEAAHKLIAKVVRKALD 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 226 DFKS---LCFHVPFTKMGKKALDSILTDDIDAETKERLTSGYdaatyYNRYVGNIYTGSLYLSLISLLETHDLSANDTIG 302
Cdd:cd00827   235 RAGLsedIDYFVPHQPNGKKILEAVAKKLGGPPEKASQTRWI-----LLRRVGNMYAASILLGLASLLESGKLKAGDRVL 309

                         330
                  ....*....|....*
gi 1853433212 303 LFSYGSGSVGEFFSG 317
Cdd:cd00827   310 LFSYGSGFTAEAFVL 324
PLN02577 PLN02577
hydroxymethylglutaryl-CoA synthase
 3-383 1.62e-37

hydroxymethylglutaryl-CoA synthase


Pssm-ID: 178189 [Multi-domain]  Cd Length: 459  Bit Score: 141.03  E-value: 1.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212   3 VGIDQINFYVPRFYVDMAKLAESRQVDPNKYLLGIGQTEMSVSPMSQDIVSMGANAAKAIVT--DEDKKQISMVIVATES 80
Cdd:PLN02577    5 VGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEkyNIDPKQIGRLEVGSET 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  81 AIDSAKAsavqIHNLLgIQPFARC----IE---MKEACYAATPAIQLAKDYLAQRP-DEKV-LVIASDTARYGlHSGGEP 151
Cdd:PLN02577   85 VIDKSKS----IKTFL-MQLFEESgntdIEgvdSTNACYGGTAALLNCVNWVESSSwDGRYgLVVAADSAVYA-EGPARP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 152 TQGAGAVAMMISQN-PRILELNDDAvAFTEDVYDFWRPSGQA-YPLVDGALSKDAYIRSFQESWQEYARRHNK------S 223
Cdd:PLN02577  159 TGGAGAVAMLVGPNaPIVFESKYRG-SHMAHVYDFYKPDLASeYPVVDGKLSQTCYLMALDSCYKRFCEKYEKlegkqfS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 224 LADFKSLCFHVPFTKMGKKAL--------------------------------DSILTDDIDAETKERLTSGYDA----A 267
Cdd:PLN02577  238 ISDADYFVFHAPYNKLVQKSFarlvyndfqrnassvdedakeklapfaglssdESYQNRDLEKVSQQVAKPLYDAkvqpT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 268 TYYNRYVGNIYTGSL-YLSLISLLETHDLSANDTIGLFSYGSGSVGEFFSGKIVEGYQ--DVLDIQGHKDL---LNNREE 341
Cdd:PLN02577  318 TLIPKQVGNMYTASLyAALASLVHNKHSELAGKRILMFSYGSGLTATMFSLRLHEGQHpfSLSNIAKVMDVsekLKSRHE 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1853433212 342 IS----VETYESFFNRFDNLEFDHETELENEKNTIFYLESINDHIR 383
Cdd:PLN02577  398 VSpekfVETLKLMEHRYGAKDFVPSKDVSLLAPGTYYLTEVDSLYR 443
HMG-CoA-S_euk TIGR01833
3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA ...
 3-385 2.88e-36

3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA synthase is the first step of isopentenyl pyrophosphate (IPP) biosynthesis via the mevalonate pathway. This pathway is found mainly in eukaryotes, but also in archaea and some bacteria. This model is specific for eukaryotes.


Pssm-ID: 273826 [Multi-domain]  Cd Length: 457  Bit Score: 137.59  E-value: 2.88e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212   3 VGIDQINFYVPRFYVDMAKLAESRQVDPNKYLLGIGQTEMSVSPMSQDIVSMGANAAKAIVTDE--DKKQISMVIVATES 80
Cdd:TIGR01833   5 VGILALEIYFPSQYVDQAELEKYDGVSAGKYTIGLGQTKMGFCTDREDINSLCLTVVSKLMERYniDYDQIGRLEVGTET 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  81 AIDSAKAsavqIHNLLgIQPFARC-------IEMKEACYAATPAIQLAKDYLAQRP-DEK-VLVIASDTARYGlHSGGEP 151
Cdd:TIGR01833  85 IIDKSKS----VKTVL-MQLFEESgntdvegIDTTNACYGGTAALFNAINWIESSSwDGRyALVVAGDIAVYA-KGNARP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 152 TQGAGAVAMMISQN-PRILELNDDAvAFTEDVYDFWRPS-GQAYPLVDGALSKDAYIRSFQESWQEYARR-HNK------ 222
Cdd:TIGR01833 159 TGGAGAVAMLIGPNaPIVFERGLRG-SHMQHAYDFYKPDlASEYPVVDGKLSIQCYLSALDRCYKSYCKKiEKQwgksgs 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 223 ----SLADFKSLCFHVPFTKMGKKALDSILTDDIDAETKERLTSGYDA----------ATYYNR---------------- 272
Cdd:TIGR01833 238 drkfTLDDFDYMIFHSPYCKLVQKSLARLLYNDFLRNPSSTDTSLYEGlealsglkleDTYTDRdlekafmkaskelfdk 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 273 ----------YVGNIYTGSLYLSLISLLETHDLS--ANDTIGLFSYGSGSVGEFFSGKIVE----GYQDVLDIQGHKDL- 335
Cdd:TIGR01833 318 ktkpsllvptQVGNMYTASLYGCLASLLSSKSAQelAGKRVGMFSYGSGLAASMFSLRVSQdaspGSALDKLIASLSDLk 397

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1853433212 336 --LNNREEISVETYEsffnrfDNLEFDHETEL------ENEKNTIF----YLESIND-HIRNY 385
Cdd:TIGR01833 398 nrLDSRHCVAPEEFE------ETMELREQAHHkknftpQGSIDSLFpgtwYLERVDSkHRRSY 454
PRK04262 PRK04262
hypothetical protein; Provisional
 1-238 9.95e-26

hypothetical protein; Provisional


Pssm-ID: 235266 [Multi-domain]  Cd Length: 347  Bit Score: 106.14  E-value: 9.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212   1 MTVGIDQINFYVPRFYVDMAKLAESRQVDPNKYLLGIGQTEMSVSPMSQDIVSMGANAAK-AIVTDE-DKKQISMVIVAT 78
Cdd:PRK04262    1 MMVGIVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARnALKRAGiDPKEIGAVYVGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  79 ESAIDSAKASAVQIHNLLGIQPFARCIEMKEACYAATPAIQLAKDYLAQRPDEKVLVIASDTARyglhsgGEP------T 152
Cdd:PRK04262   81 ESHPYAVKPTATIVAEALGATPDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGADTAQ------GAPgdaleyT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 153 QGAGAVAMMISQNPRILELNdDAVAFTEDVYDFWRPSGQAYPLVDGALSKD-AYIRSFQESWQEYARRHNKSLADFKSLC 231
Cdd:PRK04262  155 AAAGGAAFIIGKEEVIAEIE-ATYSYTTDTPDFWRREGEPYPRHGGRFTGEpAYFKHIISAAKGLMEKLGLKPSDYDYAV 233


                  ....*..
gi 1853433212 232 FHVPFTK 238
Cdd:PRK04262  234 FHQPNGK 240
HMG_CoA_synt_C pfam08540
Hydroxymethylglutaryl-coenzyme A synthase C terminal;
178-385 7.49e-17

Hydroxymethylglutaryl-coenzyme A synthase C terminal;


Pssm-ID: 400722  Cd Length: 280  Bit Score: 79.83  E-value: 7.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 178 FTEDVYDFWRPS-GQAYPLVDGALSKDAYIRSFQESWQEYARRHNK---------SLADFKSLCFHVPFTKMGKKALDSI 247
Cdd:pfam08540  11 HMEHAYDFYKPDlTSEYPVVDGKLSLSCYLKALDRCYKNYRKKINRitkdgdkifGLNDFDYMIFHSPTCKLVQKSLARL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 248 LTDD------------IDAETKERLTSGYD-------------------------AATYYNRYVGNIYTGSLYLSLIS-- 288
Cdd:pfam08540  91 LYNDflsnpssdkfngVDEKLTAFGGLTLDesytdkdlekafmklskpffkkkvqPSLLVPTNNGNMYTASLYAALASll 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 289 LLETHDLSANDTIGLFSYGSGSVGEFFSGKIVegyQDV-----LDIQGHKDL---LNNREEISVETYESFFNRFDNL--- 357
Cdd:pfam08540 171 SHVSADDLAGKRIGAFSYGSGLAATLFSLRVK---QDVspgsiLDIASVLDLgkrLDSRICVTPEEFTEAMELREQAhlk 247

                         250       260       270
                  ....*....|....*....|....*....|
gi 1853433212 358 -EFDHETELENEKNTIFYLESIND-HIRNY 385
Cdd:pfam08540 248 kNFKPQGSIDSLFPGTYYLTNVDDkFRRSY 277
HMG_CoA_synt_N pfam01154
Hydroxymethylglutaryl-coenzyme A synthase N terminal;
3-165 6.95e-16

Hydroxymethylglutaryl-coenzyme A synthase N terminal;


Pssm-ID: 307348 [Multi-domain]  Cd Length: 173  Bit Score: 74.96  E-value: 6.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212   3 VGIDQINFYVPRFYVDMAKLAESRQVDPNKYLLGIGQTEMSVSPMSQDIVSMGANAAKAIV--TDEDKKQISMVIVATES 80
Cdd:pfam01154   4 VGILALEIYFPAQYVDQTELEKFDGVEAGKYTIGLGQTRMGFCSDREDINSLCLTVVQKLMerYNLPWDKIGRLEVGTET 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  81 AIDSAKASAVQIHNLLGIQPFA--RCIEMKEACYAATPAIQLAKDYLAQRP--DEKVLVIASDTARYGlHSGGEPTQGAG 156
Cdd:pfam01154  84 IIDKSKSVKSVLMQLFQESGNTdiEGIDTTNACYGGTAALFNAANWIESSSwdGRYALVVCGDIAIYP-SGNARPTGGAG 162


                  ....*....
gi 1853433212 157 AVAMMISQN 165
Cdd:pfam01154 163 AVAMLIGPK 171
PRK07515 PRK07515
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 54-136 6.59e-05

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


Pssm-ID: 236037  Cd Length: 372  Bit Score: 44.48  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  54 MGANAAK-----AIVTDEDkkqISMVIVATESAIDSAKASAVQIHNLLGIQPFArcIEMKEACYAATPAIQLAKDYLAQR 128
Cdd:PRK07515   98 MGVAAARqalarAGRTAED---IDAVIVACSNMQRAYPAMAIEIQQALGIEGFA--FDMNVACSSATFGIQTAANAIRSG 172


                  ....*...
gi 1853433212 129 PDEKVLVI 136
Cdd:PRK07515  173 SARRVLVV 180
Chal_sti_synt_N pfam00195
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ...
 51-166 6.76e-05

Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in this N-terminal domain.


Pssm-ID: 395142  Cd Length: 225  Bit Score: 43.69  E-value: 6.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  51 IVSMGANAAKAIVTD--EDKKQISMVIVATESAIDSAKASaVQIHNLLGIQPFARCIEM-KEACYAATPAIQLAKDYLAQ 127
Cdd:pfam00195  99 VPELGAEAALKAIKEwgQPKSKITHLVFCTTSGVRMPGAD-YQLAKLLGLRPSVKRVMLyFQGCYGGATVLRTAKDIAEN 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1853433212 128 RPDEKVLVIASDTARYGLHSG---------GEPTQGAGAVAMMISQNP 166
Cdd:pfam00195 178 NPGARVLVVCSEITVLGFRGPskdrldslvGAALFGDGAAAVIIGADP 225
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 53-309 1.20e-04

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: 43.56  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  53 SMGANAAKAIVTDE--DKKQISMVIVATESAIDSAKASAVQIHNLLGIQPfARCIEMKEAC----YAatpaIQLAKDYLA 126
Cdd:COG0332    53 DLAVEAARKALEAAgiDPEDIDLIIVATVTPDYLFPSTACLVQHKLGAKN-AAAFDINAACsgfvYA----LSVAAALIR 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 127 QRPDEKVLVIASDTARYGLHsggePTQ-------GAGAVAMMIS---QNPRILelndDAVAFTE-DVYDFWR-PSGQAYP 194
Cdd:COG0332   128 SGQAKNVLVVGAETLSRIVD----WTDrstcvlfGDGAGAVVLEaseEGPGIL----GSVLGSDgSGADLLVvPAGGSRN 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 195 LVDGALSKDAYI------------RSFQESWQEYARRHNKSLADFKSLCFHvpftKMGKKALDSILtddidaetkERLts 262
Cdd:COG0332   200 PPSPVDEGDHYLrmdgrevfkfavRNLPEVIREALEKAGLTLDDIDWFIPH----QANLRIIEAVA---------KRL-- 264

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1853433212 263 GYDAA---TYYNRYvGNI---------YTGSlylslisllETHDLSANDTIGLFSYGSG 309
Cdd:COG0332   265 GLPEEkvvVNIDRY-GNTsaasiplalDEAL---------REGRIKPGDLVLLAGFGAG 313
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 52-140 2.44e-04

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: 42.53  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  52 VSMGANAAKAIVTDE--DKKQISMVIVATESAIDSAKASAVQIHNLLGIQPfARCIEMKEACYAATPAIQLAKDYLAQRP 129
Cdd:cd00830    51 SDLAVEAAKKALEDAgiDADDIDLIIVATSTPDYLFPATACLVQARLGAKN-AAAFDINAACSGFLYGLSTAAGLIRSGG 129

                          90
                  ....*....|.
gi 1853433212 130 DEKVLVIASDT 140
Cdd:cd00830   130 AKNVLVVGAET 140
PLN03173 PLN03173
chalcone synthase; Provisional
 50-166 4.28e-04

chalcone synthase; Provisional


Pssm-ID: 178717 [Multi-domain]  Cd Length: 391  Bit Score: 41.99  E-value: 4.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  50 DIVSMGANAAKAIVTD--EDKKQISMVIVATESAIDSAKASaVQIHNLLGIQP-FARCIEMKEACYAATPAIQLAKDYLA 126
Cdd:PLN03173  101 EVPKLGKEAAAKAIKEwgQPKSKITHLVFCTTSGVDMPGAD-YQLTKLLGLRSsVKRFMMYQQGCFAGGTVLRLAKDLAE 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1853433212 127 QRPDEKVLVIASDTARYGLHSG---------GEPTQGAGAVAMMISQNP 166
Cdd:PLN03173  180 NNKGARVLVVCSEITAVTFRGPsdthldslvGQALFGDGAAAIIIGSDP 228
PLN03172 PLN03172
chalcone synthase family protein; Provisional
 58-166 5.34e-04

chalcone synthase family protein; Provisional


Pssm-ID: 178716  Cd Length: 393  Bit Score: 41.96  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  58 AAKAIVT-DEDKKQISMVIVATESAIDSAKASaVQIHNLLGIQPFARCIEM-KEACYAATPAIQLAKDYLAQRPDEKVLV 135
Cdd:PLN03172  110 AAKAIKEwGQPKSKITHLVFCTTSGVDMPGAD-YQLTKLLGLKPSVKRFMMyQQGCFAGGTVLRLAKDLAENNAGSRVLV 188

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1853433212 136 IASDTARYGLHSG---------GEPTQGAGAVAMMISQNP 166
Cdd:PLN03172  189 VCSEITAVTFRGPsdthldslvGQALFGDGAAAVIIGADP 228
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
 111-233 8.38e-04

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: 41.06  E-value: 8.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 111 CYAATPAIQLAKDYLAQRPDEKVLVIASDTAryGLHSGGEPTQ---------GAGAVAMMISQNPRilelnddAVAFTED 181
Cdd:cd00831   147 CSAGAIALDLAKDLLEANPGARVLVVSTELC--SLWYRGPDHRsmlvgnalfGDGAAAVLLSNDPR-------DRRRERP 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212 182 VYDFWRPSGQAYP----LVDGALSKDA-----------YIRSFQESWQEYARRHNK---SLADFKSLCFH 233
Cdd:cd00831   218 LFELVRAASTLLPdsedAMGWHLGEEGltfvlsrdvprLVEKNLERVLRKLLARLGiglFKLAFDHWCVH 287
PLN03170 PLN03170
chalcone synthase; Provisional
 49-166 1.71e-03

chalcone synthase; Provisional


Pssm-ID: 178714 [Multi-domain]  Cd Length: 401  Bit Score: 40.08  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  49 QDIV-----SMGANAAKAIVTD--EDKKQISMVIVATESAIDSAKASaVQIHNLLGIQP-FARCIEMKEACYAATPAIQL 120
Cdd:PLN03170   99 QDIVvvevpKLGKAAAQKAIKEwgQPKSKITHLVFCTTSGVDMPGAD-YQLTKMLGLRPsVNRLMMYQQGCFAGGTVLRV 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1853433212 121 AKDYLAQRPDEKVLVIASDTARYGLHSG---------GEPTQGAGAVAMMISQNP 166
Cdd:PLN03170  178 AKDLAENNRGARVLVVCSEITAVTFRGPseshldsmvGQALFGDGAAAVIVGADP 232
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
52-140 3.16e-03

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 39.29  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1853433212  52 VSMGANAA-KAI-VTDEDKKQISMVIVATESAIDSAKASAVQIHNLLGIQ-PFArcIEMKEAC----YaatpAIQLAKDY 124
Cdd:PRK09352   53 SDLATEAAkKALeAAGIDPEDIDLIIVATTTPDYAFPSTACLVQARLGAKnAAA--FDLSAACsgfvY----ALSTADQF 126

                          90
                  ....*....|....*.
gi 1853433212 125 LAQRPDEKVLVIASDT 140
Cdd:PRK09352  127 IRSGAYKNVLVIGAEK 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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