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Conserved domains on  [gi|920604465|ref|WP_053015941|]
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hydroxymethylglutaryl-CoA synthase [Staphylococcus haemolyticus]

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]; ...
 1-384 2.30e-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: 483.14  E-value: 2.30e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   1 MSIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVSQDIVSMGANAAKDIIT--DDDKKHIGMVIVAT 78
Cdd:COG3425    1 MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDraGIDPSDIGAVYVGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  79 ESAIDNAKAAAVQIHNLLGIQPFARCFEMKEACYAATPAIQLAKDYIEKRPNEKVLVIASDTARYGIQSGGEPTQGAGAV 158
Cdd:COG3425   81 ESGPDASKPIATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIARYGPGSAGEYTQGAGAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 159 AMLISNNPSILELNDDAVAYTEDVYDFWRPTGHKYPLVAGALSKDAYIKSFQESWNEYARREDKTLSDFESLCFHVPFTK 238
Cdd:COG3425  161 AMLVGADPRIAEIEGGSGSYTTDVMDFWRPNGSDYPLVDGRFSEPAYLDHLEEAVKDYKEKTGLKPDDFDYFVFHQPFGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 239 MGKKALDSIINDADETTQERLTSGYEDAVYYNRYVGNIYTGSLYLSLISLLENRSLKGGQTIGLFSYGSGSVGEFFSATL 318
Cdd:COG3425  241 MPKKAAKKLGRKAGREIQEDFEEQVEPSLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGTV 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 920604465 319 VEGYEKQLDIEGHKALLNERQEVSVEGYESFFKRFDDLEFDHATEQTDddksiYYLENIQDDIRQY 384
Cdd:COG3425  321 TPGIEERLRRPGVEEQLANRRYLSYAEYEKLRGKILPEDAEDVTLPGE-----FVLTGIKDHERIY 381
 
Name Accession Description Interval E-value
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 1-384 2.30e-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: 483.14  E-value: 2.30e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   1 MSIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVSQDIVSMGANAAKDIIT--DDDKKHIGMVIVAT 78
Cdd:COG3425    1 MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDraGIDPSDIGAVYVGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  79 ESAIDNAKAAAVQIHNLLGIQPFARCFEMKEACYAATPAIQLAKDYIEKRPNEKVLVIASDTARYGIQSGGEPTQGAGAV 158
Cdd:COG3425   81 ESGPDASKPIATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIARYGPGSAGEYTQGAGAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 159 AMLISNNPSILELNDDAVAYTEDVYDFWRPTGHKYPLVAGALSKDAYIKSFQESWNEYARREDKTLSDFESLCFHVPFTK 238
Cdd:COG3425  161 AMLVGADPRIAEIEGGSGSYTTDVMDFWRPNGSDYPLVDGRFSEPAYLDHLEEAVKDYKEKTGLKPDDFDYFVFHQPFGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 239 MGKKALDSIINDADETTQERLTSGYEDAVYYNRYVGNIYTGSLYLSLISLLENRSLKGGQTIGLFSYGSGSVGEFFSATL 318
Cdd:COG3425  241 MPKKAAKKLGRKAGREIQEDFEEQVEPSLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGTV 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 920604465 319 VEGYEKQLDIEGHKALLNERQEVSVEGYESFFKRFDDLEFDHATEQTDddksiYYLENIQDDIRQY 384
Cdd:COG3425  321 TPGIEERLRRPGVEEQLANRRYLSYAEYEKLRGKILPEDAEDVTLPGE-----FVLTGIKDHERIY 381
HMG-CoA-S_prok TIGR01835
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
 3-384 2.00e-169

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: 478.09  E-value: 2.00e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465    3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVSQDIVSMGANAAKDIITDDDKKHIGMVIVATESAI 82
Cdd:TIGR01835   1 IGIDKISFFTPQNYLDMTALAEARGVDPEKFHIGIGQKKMAVPPIDEDIVTMAASAAKPILDRNDKQKIDMVIFGTESGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   83 DNAKAAAVQIHNLLGIQPFARCFEMKEACYAATPAIQLAKDYIEKRPNEKVLVIASDTARYGIQSGGEPTQGAGAVAMLI 162
Cdd:TIGR01835  81 DQSKAAAVYVHGLLGLQPFCRSFELKQACYGATAALQMAKGHVALSPDRKVLVIASDIAKYGLESPGEPTQGAGAVAMLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  163 SNNPSILELNDDAVAYTEDVYDFWRPTGHKYPLVAGALSKDAYIKSFQESWNEYARREDKTLSDFESLCFHVPFTKMGKK 242
Cdd:TIGR01835 161 SADPKLLAINEDSVLYTDDIMDFWRPNYSTTALVDGQYSNEQYLNAFENAWNDYAKRTGLSLADFAAFCFHVPFTKMGLK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  243 ALDSIINDADETTQERLTSGYEDAVYYNRYVGNIYTGSLYLSLISLLEN-RSLKGGQTIGLFSYGSGSVGEFFSATLVEG 321
Cdd:TIGR01835 241 ALRHILKKNYEDEDESVQNAYLESIIYNREVGNLYTGSLYLGLASLLENaFEDTTGDKIGLFSYGSGAVAEFFSGTLVAG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 920604465  322 YEKQLDIEGHKALLNERQEVSVEGYESFFKRFDDLEFDhateQTDDDKSIYYLENIQDDIRQY 384
Cdd:TIGR01835 321 YRDHLKKERHLALLKNRTNLSYAEYEALFEETLPTDGD----QPGEDRGFFRLAGINDHKRIY 379
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 2-316 8.81e-76

"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: 237.72  E-value: 8.81e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   2 SIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVsqDIVSMGANAAKDII--TDDDKKHIGMVIVATE 79
Cdd:cd00827    1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMAGDDE--DVPTMAVEAARRALerAGIDPDDIGLLIVATE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  80 SAIDNAKAAAVQIHNLLGIQpFARCFEMKEACYAATPAIQLAKDYIEKRPNEKVLVIASDTARYGI--QSGGEPTQGAGA 157
Cdd:cd00827   79 SPIDKGKSAATYLAELLGLT-NAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLdeGSALEPTLGDGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 158 VAMLISNNPSILELNDDAVAYTED---------VYDFWRPTGHKYPLVAGALSKDAYIKSFQESWNEYARREDKTLSDF- 227
Cdd:cd00827  158 AAMLVSRNPGILAAGIVSTHSTSDpgydfspypVMDGGYPKPCKLAYAIRLTAEPAGRAVFEAAHKLIAKVVRKALDRAg 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 228 --ESLCFHVPFTKMGKKALDSIINDADETTQERLTSGYedavYYNRYVGNIYTGSLYLSLISLLENRSLKGGQTIGLFSY 305
Cdd:cd00827  238 lsEDIDYFVPHQPNGKKILEAVAKKLGGPPEKASQTRW----ILLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSY 313

                        330
                 ....*....|.
gi 920604465 306 GSGSVGEFFSA 316
Cdd:cd00827  314 GSGFTAEAFVL 324
PLN02577 PLN02577
hydroxymethylglutaryl-CoA synthase
 2-321 3.36e-37

hydroxymethylglutaryl-CoA synthase


Pssm-ID: 178189 [Multi-domain]  Cd Length: 459  Bit Score: 139.88  E-value: 3.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   2 SIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVSQDIVSMGANAAKDIIT--DDDKKHIGMVIVATE 79
Cdd:PLN02577   4 NVGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEkyNIDPKQIGRLEVGSE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  80 SAIDNAKAaavqIHNLLgIQPFARC-------FEMKEACYAATPAIQLAKDYIEKRP--NEKVLVIASDTARYGiQSGGE 150
Cdd:PLN02577  84 TVIDKSKS----IKTFL-MQLFEESgntdiegVDSTNACYGGTAALLNCVNWVESSSwdGRYGLVVAADSAVYA-EGPAR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 151 PTQGAGAVAMLIS-NNPSILELNDDAvAYTEDVYDFWRPTG-HKYPLVAGALSKDAYIKSFQESWNEYARREDK------ 222
Cdd:PLN02577 158 PTGGAGAVAMLVGpNAPIVFESKYRG-SHMAHVYDFYKPDLaSEYPVVDGKLSQTCYLMALDSCYKRFCEKYEKlegkqf 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 223 TLSDFESLCFHVPFTKMGKKAL------DSIIN--DADETTQERLT-----SGYE------------------------D 265
Cdd:PLN02577 237 SISDADYFVFHAPYNKLVQKSFarlvynDFQRNasSVDEDAKEKLApfaglSSDEsyqnrdlekvsqqvakplydakvqP 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 920604465 266 AVYYNRYVGNIYTGSLYLSLISLLEN-RSLKGGQTIGLFSYGSGSVGEFFSATLVEG 321
Cdd:PLN02577 317 TTLIPKQVGNMYTASLYAALASLVHNkHSELAGKRILMFSYGSGLTATMFSLRLHEG 373
HMG_CoA_synt_N pfam01154
Hydroxymethylglutaryl-coenzyme A synthase N terminal;
3-165 2.42e-18

Hydroxymethylglutaryl-coenzyme A synthase N terminal;


Pssm-ID: 307348 [Multi-domain]  Cd Length: 173  Bit Score: 81.90  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465    3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVSQDIVSMGANAAKDIITDD--DKKHIGMVIVATES 80
Cdd:pfam01154   4 VGILALEIYFPAQYVDQTELEKFDGVEAGKYTIGLGQTRMGFCSDREDINSLCLTVVQKLMERYnlPWDKIGRLEVGTET 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   81 AIDNAKAAAVQIHNLLGIQPFA--RCFEMKEACYAATPAIQLAKDYIEKRP--NEKVLVIASDTARYGiQSGGEPTQGAG 156
Cdd:pfam01154  84 IIDKSKSVKSVLMQLFQESGNTdiEGIDTTNACYGGTAALFNAANWIESSSwdGRYALVVCGDIAIYP-SGNARPTGGAG 162


                  ....*....
gi 920604465  157 AVAMLISNN 165
Cdd:pfam01154 163 AVAMLIGPK 171
 
Name Accession Description Interval E-value
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 1-384 2.30e-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: 483.14  E-value: 2.30e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   1 MSIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVSQDIVSMGANAAKDIIT--DDDKKHIGMVIVAT 78
Cdd:COG3425    1 MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDraGIDPSDIGAVYVGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  79 ESAIDNAKAAAVQIHNLLGIQPFARCFEMKEACYAATPAIQLAKDYIEKRPNEKVLVIASDTARYGIQSGGEPTQGAGAV 158
Cdd:COG3425   81 ESGPDASKPIATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIARYGPGSAGEYTQGAGAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 159 AMLISNNPSILELNDDAVAYTEDVYDFWRPTGHKYPLVAGALSKDAYIKSFQESWNEYARREDKTLSDFESLCFHVPFTK 238
Cdd:COG3425  161 AMLVGADPRIAEIEGGSGSYTTDVMDFWRPNGSDYPLVDGRFSEPAYLDHLEEAVKDYKEKTGLKPDDFDYFVFHQPFGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 239 MGKKALDSIINDADETTQERLTSGYEDAVYYNRYVGNIYTGSLYLSLISLLENRSLKGGQTIGLFSYGSGSVGEFFSATL 318
Cdd:COG3425  241 MPKKAAKKLGRKAGREIQEDFEEQVEPSLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGTV 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 920604465 319 VEGYEKQLDIEGHKALLNERQEVSVEGYESFFKRFDDLEFDHATEQTDddksiYYLENIQDDIRQY 384
Cdd:COG3425  321 TPGIEERLRRPGVEEQLANRRYLSYAEYEKLRGKILPEDAEDVTLPGE-----FVLTGIKDHERIY 381
HMG-CoA-S_prok TIGR01835
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
 3-384 2.00e-169

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: 478.09  E-value: 2.00e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465    3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVSQDIVSMGANAAKDIITDDDKKHIGMVIVATESAI 82
Cdd:TIGR01835   1 IGIDKISFFTPQNYLDMTALAEARGVDPEKFHIGIGQKKMAVPPIDEDIVTMAASAAKPILDRNDKQKIDMVIFGTESGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   83 DNAKAAAVQIHNLLGIQPFARCFEMKEACYAATPAIQLAKDYIEKRPNEKVLVIASDTARYGIQSGGEPTQGAGAVAMLI 162
Cdd:TIGR01835  81 DQSKAAAVYVHGLLGLQPFCRSFELKQACYGATAALQMAKGHVALSPDRKVLVIASDIAKYGLESPGEPTQGAGAVAMLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  163 SNNPSILELNDDAVAYTEDVYDFWRPTGHKYPLVAGALSKDAYIKSFQESWNEYARREDKTLSDFESLCFHVPFTKMGKK 242
Cdd:TIGR01835 161 SADPKLLAINEDSVLYTDDIMDFWRPNYSTTALVDGQYSNEQYLNAFENAWNDYAKRTGLSLADFAAFCFHVPFTKMGLK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  243 ALDSIINDADETTQERLTSGYEDAVYYNRYVGNIYTGSLYLSLISLLEN-RSLKGGQTIGLFSYGSGSVGEFFSATLVEG 321
Cdd:TIGR01835 241 ALRHILKKNYEDEDESVQNAYLESIIYNREVGNLYTGSLYLGLASLLENaFEDTTGDKIGLFSYGSGAVAEFFSGTLVAG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 920604465  322 YEKQLDIEGHKALLNERQEVSVEGYESFFKRFDDLEFDhateQTDDDKSIYYLENIQDDIRQY 384
Cdd:TIGR01835 321 YRDHLKKERHLALLKNRTNLSYAEYEALFEETLPTDGD----QPGEDRGFFRLAGINDHKRIY 379
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 2-316 8.81e-76

"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: 237.72  E-value: 8.81e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   2 SIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVsqDIVSMGANAAKDII--TDDDKKHIGMVIVATE 79
Cdd:cd00827    1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMAGDDE--DVPTMAVEAARRALerAGIDPDDIGLLIVATE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  80 SAIDNAKAAAVQIHNLLGIQpFARCFEMKEACYAATPAIQLAKDYIEKRPNEKVLVIASDTARYGI--QSGGEPTQGAGA 157
Cdd:cd00827   79 SPIDKGKSAATYLAELLGLT-NAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLdeGSALEPTLGDGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 158 VAMLISNNPSILELNDDAVAYTED---------VYDFWRPTGHKYPLVAGALSKDAYIKSFQESWNEYARREDKTLSDF- 227
Cdd:cd00827  158 AAMLVSRNPGILAAGIVSTHSTSDpgydfspypVMDGGYPKPCKLAYAIRLTAEPAGRAVFEAAHKLIAKVVRKALDRAg 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 228 --ESLCFHVPFTKMGKKALDSIINDADETTQERLTSGYedavYYNRYVGNIYTGSLYLSLISLLENRSLKGGQTIGLFSY 305
Cdd:cd00827  238 lsEDIDYFVPHQPNGKKILEAVAKKLGGPPEKASQTRW----ILLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSY 313

                        330
                 ....*....|.
gi 920604465 306 GSGSVGEFFSA 316
Cdd:cd00827  314 GSGFTAEAFVL 324
HMG-CoA-S_euk TIGR01833
3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA ...
 3-383 2.11e-38

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: 143.37  E-value: 2.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465    3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVSQDIVSMGANAAKDIITDD--DKKHIGMVIVATES 80
Cdd:TIGR01833   5 VGILALEIYFPSQYVDQAELEKYDGVSAGKYTIGLGQTKMGFCTDREDINSLCLTVVSKLMERYniDYDQIGRLEVGTET 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   81 AIDNAKAaavqIHNLLgIQPFARC-------FEMKEACYAATPAIQLAKDYIEKRP--NEKVLVIASDTARYGiQSGGEP 151
Cdd:TIGR01833  85 IIDKSKS----VKTVL-MQLFEESgntdvegIDTTNACYGGTAALFNAINWIESSSwdGRYALVVAGDIAVYA-KGNARP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  152 TQGAGAVAMLI-SNNPSILELNDDAvAYTEDVYDFWRPT-GHKYPLVAGALSKDAYIKS-----------FQESWNEYAR 218
Cdd:TIGR01833 159 TGGAGAVAMLIgPNAPIVFERGLRG-SHMQHAYDFYKPDlASEYPVVDGKLSIQCYLSAldrcyksyckkIEKQWGKSGS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  219 REDKTLSDFESLCFHVPFTKMGKKALDSII-ND---ADETTQERLTSGYE-------DAVYYNR---------------- 271
Cdd:TIGR01833 238 DRKFTLDDFDYMIFHSPYCKLVQKSLARLLyNDflrNPSSTDTSLYEGLEalsglklEDTYTDRdlekafmkaskelfdk 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  272 ----------YVGNIYTGSLYLSLI---SLLENRSLKgGQTIGLFSYGSGSVGEFFS----------ATLVEGYEKQLDI 328
Cdd:TIGR01833 318 ktkpsllvptQVGNMYTASLYGCLAsllSSKSAQELA-GKRVGMFSYGSGLAASMFSlrvsqdaspgSALDKLIASLSDL 396

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 920604465  329 eghKALLNERQEVSVEGYESFFKRFDD--LEFDHATEQTDDD--KSIYYLENIQDDIRQ 383
Cdd:TIGR01833 397 ---KNRLDSRHCVAPEEFEETMELREQahHKKNFTPQGSIDSlfPGTWYLERVDSKHRR 452
PLN02577 PLN02577
hydroxymethylglutaryl-CoA synthase
 2-321 3.36e-37

hydroxymethylglutaryl-CoA synthase


Pssm-ID: 178189 [Multi-domain]  Cd Length: 459  Bit Score: 139.88  E-value: 3.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   2 SIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVSQDIVSMGANAAKDIIT--DDDKKHIGMVIVATE 79
Cdd:PLN02577   4 NVGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEkyNIDPKQIGRLEVGSE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  80 SAIDNAKAaavqIHNLLgIQPFARC-------FEMKEACYAATPAIQLAKDYIEKRP--NEKVLVIASDTARYGiQSGGE 150
Cdd:PLN02577  84 TVIDKSKS----IKTFL-MQLFEESgntdiegVDSTNACYGGTAALLNCVNWVESSSwdGRYGLVVAADSAVYA-EGPAR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 151 PTQGAGAVAMLIS-NNPSILELNDDAvAYTEDVYDFWRPTG-HKYPLVAGALSKDAYIKSFQESWNEYARREDK------ 222
Cdd:PLN02577 158 PTGGAGAVAMLVGpNAPIVFESKYRG-SHMAHVYDFYKPDLaSEYPVVDGKLSQTCYLMALDSCYKRFCEKYEKlegkqf 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 223 TLSDFESLCFHVPFTKMGKKAL------DSIIN--DADETTQERLT-----SGYE------------------------D 265
Cdd:PLN02577 237 SISDADYFVFHAPYNKLVQKSFarlvynDFQRNasSVDEDAKEKLApfaglSSDEsyqnrdlekvsqqvakplydakvqP 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 920604465 266 AVYYNRYVGNIYTGSLYLSLISLLEN-RSLKGGQTIGLFSYGSGSVGEFFSATLVEG 321
Cdd:PLN02577 317 TTLIPKQVGNMYTASLYAALASLVHNkHSELAGKRILMFSYGSGLTATMFSLRLHEG 373
PRK04262 PRK04262
hypothetical protein; Provisional
 1-323 3.03e-26

hypothetical protein; Provisional


Pssm-ID: 235266 [Multi-domain]  Cd Length: 347  Bit Score: 107.68  E-value: 3.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   1 MSIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVSQDIVSMGANAAKDIITDD--DKKHIGMVIVAT 78
Cdd:PRK04262   1 MMVGIVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAgiDPKEIGAVYVGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  79 ESAIDNAKAAAVQIHNLLGIQPFARCFEMKEACYAATPAIQLAKDYIEKRPNEKVLVIASDTARygiqsgGEP------T 152
Cdd:PRK04262  81 ESHPYAVKPTATIVAEALGATPDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGADTAQ------GAPgdaleyT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 153 QGAGAVAMLISNNPSILELNDdAVAYTEDVYDFWRPTGHKYPLVAGALSKD-AYIKSFQESWNEYARREDKTLSDFESLC 231
Cdd:PRK04262 155 AAAGGAAFIIGKEEVIAEIEA-TYSYTTDTPDFWRREGEPYPRHGGRFTGEpAYFKHIISAAKGLMEKLGLKPSDYDYAV 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465 232 FHVPFTKMGKKAlDSIINDADETTQERLTSGyedavyynrYVGNIYTGSLYLSLISLLENRslKGGQTIGLFSYGSGSVG 311
Cdd:PRK04262 234 FHQPNGKFPLRV-AKMLGFTKEQVKPGLLTP---------YIGNTYSGSALLGLAAVLDVA--KPGDRILVVSFGSGAGS 301

                        330
                 ....*....|..
gi 920604465 312 EFFSATLVEGYE 323
Cdd:PRK04262 302 DAFSITVTDAIE 313
HMG_CoA_synt_N pfam01154
Hydroxymethylglutaryl-coenzyme A synthase N terminal;
3-165 2.42e-18

Hydroxymethylglutaryl-coenzyme A synthase N terminal;


Pssm-ID: 307348 [Multi-domain]  Cd Length: 173  Bit Score: 81.90  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465    3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTQMAVSPVSQDIVSMGANAAKDIITDD--DKKHIGMVIVATES 80
Cdd:pfam01154   4 VGILALEIYFPAQYVDQTELEKFDGVEAGKYTIGLGQTRMGFCSDREDINSLCLTVVQKLMERYnlPWDKIGRLEVGTET 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   81 AIDNAKAAAVQIHNLLGIQPFA--RCFEMKEACYAATPAIQLAKDYIEKRP--NEKVLVIASDTARYGiQSGGEPTQGAG 156
Cdd:pfam01154  84 IIDKSKSVKSVLMQLFQESGNTdiEGIDTTNACYGGTAALFNAANWIESSSwdGRYALVVCGDIAIYP-SGNARPTGGAG 162


                  ....*....
gi 920604465  157 AVAMLISNN 165
Cdd:pfam01154 163 AVAMLIGPK 171
HMG_CoA_synt_C pfam08540
Hydroxymethylglutaryl-coenzyme A synthase C terminal;
178-382 1.25e-12

Hydroxymethylglutaryl-coenzyme A synthase C terminal;


Pssm-ID: 400722  Cd Length: 280  Bit Score: 67.50  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  178 YTEDVYDFWRPT-GHKYPLVAGALSKDAYIKSFQESWNEYARREDK---------TLSDFESLCFHVPFTKMGKKAL--- 244
Cdd:pfam08540  11 HMEHAYDFYKPDlTSEYPVVDGKLSLSCYLKALDRCYKNYRKKINRitkdgdkifGLNDFDYMIFHSPTCKLVQKSLarl 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  245 ---DS-------IINDADETTQERLTSGYED-------------------------AVYYNRYVGNIYTGSLYLSLISLL 289
Cdd:pfam08540  91 lynDFlsnpssdKFNGVDEKLTAFGGLTLDEsytdkdlekafmklskpffkkkvqpSLLVPTNNGNMYTASLYAALASLL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  290 ENRS---LKgGQTIGLFSYGSGSVGEFFSATLVE--GYEKQLDIEGHKAL---LNERQEVSVEGYESFFKRFDDL----E 357
Cdd:pfam08540 171 SHVSaddLA-GKRIGAFSYGSGLAATLFSLRVKQdvSPGSILDIASVLDLgkrLDSRICVTPEEFTEAMELREQAhlkkN 249

                         250       260
                  ....*....|....*....|....*
gi 920604465  358 FDHATEQTDDDKSIYYLENIQDDIR 382
Cdd:pfam08540 250 FKPQGSIDSLFPGTYYLTNVDDKFR 274
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 53-169 3.44e-08

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: 54.73  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  53 SMGANAAKDIITD--DDKKHIGMVIVATESAIDNAKAAAVQIHNLLGIQPfARCFEMKEAC----YaatpAIQLAKDYIE 126
Cdd:COG0332   53 DLAVEAARKALEAagIDPEDIDLIIVATVTPDYLFPSTACLVQHKLGAKN-AAAFDINAACsgfvY----ALSVAAALIR 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 920604465 127 KRPNEKVLVIASDTARYGIqsggEPTQ-------GAGAVAMLIS---NNPSIL 169
Cdd:COG0332  128 SGQAKNVLVVGAETLSRIV----DWTDrstcvlfGDGAGAVVLEaseEGPGIL 176
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 52-140 3.33e-07

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: 51.39  E-value: 3.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  52 VSMGANAAKDIITD--DDKKHIGMVIVATESAIDNAKAAAVQIHNLLGIQPfARCFEMKEACYAATPAIQLAKDYIEKRP 129
Cdd:cd00830   51 SDLAVEAAKKALEDagIDADDIDLIIVATSTPDYLFPATACLVQARLGAKN-AAAFDINAACSGFLYGLSTAAGLIRSGG 129

                         90
                 ....*....|.
gi 920604465 130 NEKVLVIASDT 140
Cdd:cd00830  130 AKNVLVVGAET 140
PRK07515 PRK07515
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 54-136 6.27e-07

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


Pssm-ID: 236037  Cd Length: 372  Bit Score: 51.03  E-value: 6.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  54 MGANAAKDIITDDDKK--HIGMVIVATESAIDNAKAAAVQIHNLLGIQPFArcFEMKEACYAATPAIQLAKDYIEKRPNE 131
Cdd:PRK07515  98 MGVAAARQALARAGRTaeDIDAVIVACSNMQRAYPAMAIEIQQALGIEGFA--FDMNVACSSATFGIQTAANAIRSGSAR 175


                 ....*
gi 920604465 132 KVLVI 136
Cdd:PRK07515 176 RVLVV 180
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
52-140 2.90e-06

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 48.53  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  52 VSMGANAAKDIITDD--DKKHIGMVIVATESAIDNAKAAAVQIHNLLGIQ-PFArcFEMKEAC----YaatpAIQLAKDY 124
Cdd:PRK09352  53 SDLATEAAKKALEAAgiDPEDIDLIIVATTTPDYAFPSTACLVQARLGAKnAAA--FDLSAACsgfvY----ALSTADQF 126

                         90
                 ....*....|....*.
gi 920604465 125 IEKRPNEKVLVIASDT 140
Cdd:PRK09352 127 IRSGAYKNVLVIGAEK 142
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 8-140 4.37e-06

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


Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 47.94  E-value: 4.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   8 INFYVPKYYVDMAKLAeaRQVDPNKFLI----GIGQTQMAvsPVSQDIVSMGANAAKDIITDDDK--KHIGMVIVATESA 81
Cdd:PRK12879  10 IGTYVPPRVLTNDDLE--TFIDTSDEWIvqrtGIKERRIA--HVEEYTSDLAIKAAERALARAGLdaEDIDLIIVATTTP 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 920604465  82 IDNAKAAAVQIHNLLGIqPFARCFEMKEACYAATPAIQLAKDYIEKRPNEKVLVIASDT 140
Cdd:PRK12879  86 DYLFPSTASQVQARLGI-PNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAER 143
Chal_sti_synt_N pfam00195
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ...
 47-166 1.26e-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: 46.00  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465   47 VSQDIVSMGANAAKDIITD--DDKKHIGMVIVATESAIDnAKAAAVQIHNLLGIQPFARCFEM-KEACYAATPAIQLAKD 123
Cdd:pfam00195  95 ANAEVPELGAEAALKAIKEwgQPKSKITHLVFCTTSGVR-MPGADYQLAKLLGLRPSVKRVMLyFQGCYGGATVLRTAKD 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 920604465  124 YIEKRPNEKVLVIASDTARYGIQSG---------GEPTQGAGAVAMLISNNP 166
Cdd:pfam00195 174 IAENNPGARVLVVCSEITVLGFRGPskdrldslvGAALFGDGAAAVIIGADP 225
PLN03173 PLN03173
chalcone synthase; Provisional
 50-168 2.53e-05

chalcone synthase; Provisional


Pssm-ID: 178717 [Multi-domain]  Cd Length: 391  Bit Score: 45.84  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  50 DIVSMGANAAKDIITD--DDKKHIGMVIVATESAIDnAKAAAVQIHNLLGIQPFARCFEM-KEACYAATPAIQLAKDYIE 126
Cdd:PLN03173 101 EVPKLGKEAAAKAIKEwgQPKSKITHLVFCTTSGVD-MPGADYQLTKLLGLRSSVKRFMMyQQGCFAGGTVLRLAKDLAE 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 920604465 127 KRPNEKVLVIASDTARYGIQSG---------GEPTQGAGAVAMLISNNPSI 168
Cdd:PLN03173 180 NNKGARVLVVCSEITAVTFRGPsdthldslvGQALFGDGAAAIIIGSDPVL 230
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
 54-167 6.08e-05

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: 44.52  E-value: 6.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  54 MGANAAKDII--TDDDKKHIGMVIVATESAIDnAKAAAVQIHNLLGIQPFAR---CFEMkeACYAATPAIQLAKDYIEKR 128
Cdd:cd00831   88 LAEEAARGALdeAGLRPSDIDHLVVNTSTGNP-TPSLDAMLINRLGLRPDVKrynLGGM--GCSAGAIALDLAKDLLEAN 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 920604465 129 PNEKVLVIASDTARYGIQsgGEPTQ---------GAGAVAMLISNNPS 167
Cdd:cd00831  165 PGARVLVVSTELCSLWYR--GPDHRsmlvgnalfGDGAAAVLLSNDPR 210
PLN03172 PLN03172
chalcone synthase family protein; Provisional
 50-166 1.65e-04

chalcone synthase family protein; Provisional


Pssm-ID: 178716  Cd Length: 393  Bit Score: 43.50  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  50 DIVSMGANAAKDIITD--DDKKHIGMVIVATESAIDnAKAAAVQIHNLLGIQPFARCFEM-KEACYAATPAIQLAKDYIE 126
Cdd:PLN03172 101 EVPKLGKEAAAKAIKEwgQPKSKITHLVFCTTSGVD-MPGADYQLTKLLGLKPSVKRFMMyQQGCFAGGTVLRLAKDLAE 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 920604465 127 KRPNEKVLVIASDTARYGIQSG---------GEPTQGAGAVAMLISNNP 166
Cdd:PLN03172 180 NNAGSRVLVVCSEITAVTFRGPsdthldslvGQALFGDGAAAVIIGADP 228
fabH CHL00203
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
 36-179 4.50e-04

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


Pssm-ID: 164577 [Multi-domain]  Cd Length: 326  Bit Score: 41.85  E-value: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  36 GIGQTQMAvsPVSQDIVSMGANAAKDIItddDKKH-----IGMVIVATeSAIDNAKAAAVQIHNLLGIQPfARCFEMKEA 110
Cdd:CHL00203  38 GIKKRHLA--PSSTSLTKLAAEAANKAL---DKAHmdpleIDLIILAT-STPDDLFGSASQLQAEIGATR-AVAFDITAA 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 920604465 111 CYAATPAIQLAKDYIEKRPNEKVLVIASDTARYGIQSGGEPT-----QGAGAVAMLISNNPSIL--ELNDDAVAYT 179
Cdd:CHL00203 111 CSGFILALVTATQFIQNGSYKNILVVGADTLSKWIDWSDRKTcilfgDGAGAAIIGASYENSILgfKLCTDGKLNS 186
PLN03170 PLN03170
chalcone synthase; Provisional
 49-166 8.16e-04

chalcone synthase; Provisional


Pssm-ID: 178714 [Multi-domain]  Cd Length: 401  Bit Score: 41.24  E-value: 8.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  49 QDIV-----SMGANAAKDIITD--DDKKHIGMVIVATESAIDnAKAAAVQIHNLLGIQP-FARCFEMKEACYAATPAIQL 120
Cdd:PLN03170  99 QDIVvvevpKLGKAAAQKAIKEwgQPKSKITHLVFCTTSGVD-MPGADYQLTKMLGLRPsVNRLMMYQQGCFAGGTVLRV 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 920604465 121 AKDYIEKRPNEKVLVIASD----TARYGIQSG-----GEPTQGAGAVAMLISNNP 166
Cdd:PLN03170 178 AKDLAENNRGARVLVVCSEitavTFRGPSESHldsmvGQALFGDGAAAVIVGADP 232
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 35-225 3.07e-03

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: 39.16  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  35 IGIGQTQMAVSPVSQDIVSMGANAAKDiitdddKKHIGMVIVATESAIDNAK---------------------AAAVQIH 93
Cdd:cd00825    7 LGSYVSILGFEAAERAIADAGLSREYQ------KNPIVGVVVGTGGGSPRFQvfgadamravgpyvvtkamfpGASGQIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  94 NLLGIQpfARCFEMKEACYAATPAIQLAKDYIEKRPNEKVLVIASD--TARYGI--QSGGEPTQGAGAVAMLISNNPSIL 169
Cdd:cd00825   81 TPLGIH--GPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEelAAPMDCefDAMGALSTPEKASRTFDAAADGFV 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 920604465 170 ELNDDAVAYTEDVYDFWRPTGHKYPLVAG-ALSKD-AYIKSFQESWNEYARREDKTLS 225
Cdd:cd00825  159 FGDGAGALVVEELEHALARGAHIYAEIVGtAATIDgAGMGAFAPSAEGLARAAKEALA 216
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 55-158 8.79e-03

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: 37.42  E-value: 8.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920604465  55 GANAAKDIITD--DDKKHIGMVIVATESAIDNAKAAAVQIHNLLGIqPFARCFEMKEACYAATPAIQLAKDYIEKRPNEK 132
Cdd:cd00327   11 GFEAAEQAIADagLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGI-SGGPAYSVNQACATGLTALALAVQQVQNGKADI 89

                         90       100
                 ....*....|....*....|....*.
gi 920604465 133 VLVIASDTARYGiqsggeptQGAGAV 158
Cdd:cd00327   90 VLAGGSEEFVFG--------DGAAAA 107
 
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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