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Conserved domains on  [gi|504377723|ref|WP_014564825|]
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hydroxymethylglutaryl-CoA synthase [Lactobacillus delbrueckii]

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 1.12e-167

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: 473.90  E-value: 1.12e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   1 MDIGIDQIGFYTPNKFVDMVDLANARNQDPNKFLIGIGQDRMAVADKTQDAVSMGINATAEYLD--QVDLEQLGLLIFAT 78
Cdd:COG3425    1 MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDraGIDPSDIGAVYVGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  79 ESGIDQSKSASLFVKEALNLPARIRTFEIKEACFALTASLQVARDYVRAHPHHSAMIIGSDIARYGLATAGEVTQGAGAI 158
Cdd:COG3425   81 ESGPDASKPIATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIARYGPGSAGEYTQGAGAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 159 SMLIKENPAIIALEDGHTSHSENINDFWRPNNLATAVVDGHYSRDVYLDFFKSTFKPFLAEKQLQVSDFAGICYHLPYTK 238
Cdd:COG3425  161 AMLVGADPRIAEIEGGSGSYTTDVMDFWRPNGSDYPLVDGRFSEPAYLDHLEEAVKDYKEKTGLKPDDFDYFVFHQPFGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 239 MGYKAHKIAIEGQDDETVKRLSDNFQLSAKYSRQVGNIYTASLYMSVLSLLENGDLEAGDRIGFFSYGSGAMAEFFSGKV 318
Cdd:COG3425  241 MPKKAAKKLGRKAGREIQEDFEEQVEPSLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGTV 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504377723 319 VAGYQKRLRPALHARMLKERIRIGVGQYEDIFTEGLEALPENVEFTsdanhGTWYLAGQEGYVRQYK 385
Cdd:COG3425  321 TPGIEERLRRPGVEEQLANRRYLSYAEYEKLRGKILPEDAEDVTLP-----GEFVLTGIKDHERIYE 382
 
Name Accession Description Interval E-value
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 1-385 1.12e-167

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: 473.90  E-value: 1.12e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   1 MDIGIDQIGFYTPNKFVDMVDLANARNQDPNKFLIGIGQDRMAVADKTQDAVSMGINATAEYLD--QVDLEQLGLLIFAT 78
Cdd:COG3425    1 MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDraGIDPSDIGAVYVGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  79 ESGIDQSKSASLFVKEALNLPARIRTFEIKEACFALTASLQVARDYVRAHPHHSAMIIGSDIARYGLATAGEVTQGAGAI 158
Cdd:COG3425   81 ESGPDASKPIATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIARYGPGSAGEYTQGAGAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 159 SMLIKENPAIIALEDGHTSHSENINDFWRPNNLATAVVDGHYSRDVYLDFFKSTFKPFLAEKQLQVSDFAGICYHLPYTK 238
Cdd:COG3425  161 AMLVGADPRIAEIEGGSGSYTTDVMDFWRPNGSDYPLVDGRFSEPAYLDHLEEAVKDYKEKTGLKPDDFDYFVFHQPFGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 239 MGYKAHKIAIEGQDDETVKRLSDNFQLSAKYSRQVGNIYTASLYMSVLSLLENGDLEAGDRIGFFSYGSGAMAEFFSGKV 318
Cdd:COG3425  241 MPKKAAKKLGRKAGREIQEDFEEQVEPSLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGTV 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504377723 319 VAGYQKRLRPALHARMLKERIRIGVGQYEDIFTEGLEALPENVEFTsdanhGTWYLAGQEGYVRQYK 385
Cdd:COG3425  321 TPGIEERLRRPGVEEQLANRRYLSYAEYEKLRGKILPEDAEDVTLP-----GEFVLTGIKDHERIYE 382
HMG-CoA-S_prok TIGR01835
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
 3-384 6.39e-137

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: 395.66  E-value: 6.39e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723    3 IGIDQIGFYTPNKFVDMVDLANARNQDPNKFLIGIGQDRMAVADKTQDAVSMGINATAEYLDQVDLEQLGLLIFATESGI 82
Cdd:TIGR01835   1 IGIDKISFFTPQNYLDMTALAEARGVDPEKFHIGIGQKKMAVPPIDEDIVTMAASAAKPILDRNDKQKIDMVIFGTESGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   83 DQSKSASLFVKEALNLPARIRTFEIKEACFALTASLQVARDYVRAHPHHSAMIIGSDIARYGLATAGEVTQGAGAISMLI 162
Cdd:TIGR01835  81 DQSKAAAVYVHGLLGLQPFCRSFELKQACYGATAALQMAKGHVALSPDRKVLVIASDIAKYGLESPGEPTQGAGAVAMLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  163 KENPAIIALEDGHTSHSENINDFWRPNNLATAVVDGHYSRDVYLDFFKSTFKPFLAEKQLQVSDFAGICYHLPYTKMGYK 242
Cdd:TIGR01835 161 SADPKLLAINEDSVLYTDDIMDFWRPNYSTTALVDGQYSNEQYLNAFENAWNDYAKRTGLSLADFAAFCFHVPFTKMGLK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  243 AHKIAIEGQDDETVKRLSDNFQLSAKYSRQVGNIYTASLYMSVLSLLENG-DLEAGDRIGFFSYGSGAMAEFFSGKVVAG 321
Cdd:TIGR01835 241 ALRHILKKNYEDEDESVQNAYLESIIYNREVGNLYTGSLYLGLASLLENAfEDTTGDKIGLFSYGSGAVAEFFSGTLVAG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504377723  322 YQKRLRPALHARMLKERIRIGVGQYEDIFTeglEALPENVEFTSDANhGTWYLAGQEGYVRQY 384
Cdd:TIGR01835 321 YRDHLKKERHLALLKNRTNLSYAEYEALFE---ETLPTDGDQPGEDR-GFFRLAGINDHKRIY 379
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 2-316 3.17e-69

"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: 220.77  E-value: 3.17e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   2 DIGIDQIGFYTPNKFVDMVDLANARNQDPNKFLIGIGQDRMAVADKtqDAVSMGINATAEYLD--QVDLEQLGLLIFATE 79
Cdd:cd00827    1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMAGDDE--DVPTMAVEAARRALEraGIDPDDIGLLIVATE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  80 SGIDQSKSASLFVKEALNLPaRIRTFEIKEACFALTASLQVARDYVRAHPHHSAMIIGSDIARYGL--ATAGEVTQGAGA 157
Cdd:cd00827   79 SPIDKGKSAATYLAELLGLT-NAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLdeGSALEPTLGDGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 158 ISMLIKENPAIIALE----DGHTSHSENIN-----DFWRPNNLATAV---VDGHYSRDVYLDFFKSTFKPFLAEKQLQVS 225
Cdd:cd00827  158 AAMLVSRNPGILAAGivstHSTSDPGYDFSpypvmDGGYPKPCKLAYairLTAEPAGRAVFEAAHKLIAKVVRKALDRAG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 226 DFAGICYHLPYTKMGYKAHKIAIEGQDDETVKRLSDNFqlsaKYSRQVGNIYTASLYMSVLSLLENGDLEAGDRIGFFSY 305
Cdd:cd00827  238 LSEDIDYFVPHQPNGKKILEAVAKKLGGPPEKASQTRW----ILLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSY 313

                        330
                 ....*....|.
gi 504377723 306 GSGAMAEFFSG 316
Cdd:cd00827  314 GSGFTAEAFVL 324
PLN02577 PLN02577
hydroxymethylglutaryl-CoA synthase
 2-387 5.44e-44

hydroxymethylglutaryl-CoA synthase


Pssm-ID: 178189 [Multi-domain]  Cd Length: 459  Bit Score: 158.37  E-value: 5.44e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   2 DIGIDQIGFYTPNKFVDMVDLANARNQDPNKFLIGIGQDRMAVADKTQDAVSMGINATAEYLDQ--VDLEQLGLLIFATE 79
Cdd:PLN02577   4 NVGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEKynIDPKQIGRLEVGSE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  80 SGIDQSKSASLFV----KEALNLParIRTFEIKEACFALTASLQVARDYV--RAHPHHSAMIIGSDIARYGLATAgEVTQ 153
Cdd:PLN02577  84 TVIDKSKSIKTFLmqlfEESGNTD--IEGVDSTNACYGGTAALLNCVNWVesSSWDGRYGLVVAADSAVYAEGPA-RPTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 154 GAGAISMLIKENpAIIALEDGH-TSHSENINDFWRPnNLAT--AVVDGHYSRDVYLDFFKSTFKPFLAE------KQLQV 224
Cdd:PLN02577 161 GAGAVAMLVGPN-APIVFESKYrGSHMAHVYDFYKP-DLASeyPVVDGKLSQTCYLMALDSCYKRFCEKyeklegKQFSI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 225 SDFAGICYHLPYTKMGYK----------AHKIAIEGQD-------------DETV--KRLSDNFQLSAKY---------- 269
Cdd:PLN02577 239 SDADYFVFHAPYNKLVQKsfarlvyndfQRNASSVDEDakeklapfaglssDESYqnRDLEKVSQQVAKPlydakvqptt 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 270 --SRQVGNIYTASLYMSVLSLLEN-GDLEAGDRIGFFSYGSGAMAEFFSGKVVAGyQKRLRPALHARMLK--ERIRIGVG 344
Cdd:PLN02577 319 liPKQVGNMYTASLYAALASLVHNkHSELAGKRILMFSYGSGLTATMFSLRLHEG-QHPFSLSNIAKVMDvsEKLKSRHE 397

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504377723 345 QYEDIFTEGLE-------ALP-ENVEFTSDANHGTWYLAG-QEGYVRQYKQK 387
Cdd:PLN02577 398 VSPEKFVETLKlmehrygAKDfVPSKDVSLLAPGTYYLTEvDSLYRRFYDRK 449
HMG_CoA_synt_C pfam08540
Hydroxymethylglutaryl-coenzyme A synthase C terminal;
169-387 1.51e-18

Hydroxymethylglutaryl-coenzyme A synthase C terminal;


Pssm-ID: 400722  Cd Length: 280  Bit Score: 84.83  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  169 IALEDG-HTSHSENINDFWRPNNLAT-AVVDGHYSRDVYLDFFKSTFKPFLAEKQLQVS---------DFAGICYHLPYT 237
Cdd:pfam08540   1 IVFDRGlRGSHMEHAYDFYKPDLTSEyPVVDGKLSLSCYLKALDRCYKNYRKKINRITKdgdkifglnDFDYMIFHSPTC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  238 KMGYKA----------------------HKIAIEG----QDDETVKRLSDNFQLSAK------------YSRQVGNIYTA 279
Cdd:pfam08540  81 KLVQKSlarllyndflsnpssdkfngvdEKLTAFGgltlDESYTDKDLEKAFMKLSKpffkkkvqpsllVPTNNGNMYTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  280 SLYMSVLSLLEN--GDLEAGDRIGFFSYGSGAMAEFFSGKVVAGYQKRLRPALHARM-LKERIRIGVGQYEDIFTEGLEA 356
Cdd:pfam08540 161 SLYAALASLLSHvsADDLAGKRIGAFSYGSGLAATLFSLRVKQDVSPGSILDIASVLdLGKRLDSRICVTPEEFTEAMEL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 504377723  357 -----LPENVEFTSDANH---GTWYLAG-QEGYVRQYKQK 387
Cdd:pfam08540 241 reqahLKKNFKPQGSIDSlfpGTYYLTNvDDKFRRSYARK 280
 
Name Accession Description Interval E-value
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 1-385 1.12e-167

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: 473.90  E-value: 1.12e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   1 MDIGIDQIGFYTPNKFVDMVDLANARNQDPNKFLIGIGQDRMAVADKTQDAVSMGINATAEYLD--QVDLEQLGLLIFAT 78
Cdd:COG3425    1 MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDraGIDPSDIGAVYVGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  79 ESGIDQSKSASLFVKEALNLPARIRTFEIKEACFALTASLQVARDYVRAHPHHSAMIIGSDIARYGLATAGEVTQGAGAI 158
Cdd:COG3425   81 ESGPDASKPIATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIARYGPGSAGEYTQGAGAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 159 SMLIKENPAIIALEDGHTSHSENINDFWRPNNLATAVVDGHYSRDVYLDFFKSTFKPFLAEKQLQVSDFAGICYHLPYTK 238
Cdd:COG3425  161 AMLVGADPRIAEIEGGSGSYTTDVMDFWRPNGSDYPLVDGRFSEPAYLDHLEEAVKDYKEKTGLKPDDFDYFVFHQPFGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 239 MGYKAHKIAIEGQDDETVKRLSDNFQLSAKYSRQVGNIYTASLYMSVLSLLENGDLEAGDRIGFFSYGSGAMAEFFSGKV 318
Cdd:COG3425  241 MPKKAAKKLGRKAGREIQEDFEEQVEPSLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGTV 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504377723 319 VAGYQKRLRPALHARMLKERIRIGVGQYEDIFTEGLEALPENVEFTsdanhGTWYLAGQEGYVRQYK 385
Cdd:COG3425  321 TPGIEERLRRPGVEEQLANRRYLSYAEYEKLRGKILPEDAEDVTLP-----GEFVLTGIKDHERIYE 382
HMG-CoA-S_prok TIGR01835
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
 3-384 6.39e-137

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: 395.66  E-value: 6.39e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723    3 IGIDQIGFYTPNKFVDMVDLANARNQDPNKFLIGIGQDRMAVADKTQDAVSMGINATAEYLDQVDLEQLGLLIFATESGI 82
Cdd:TIGR01835   1 IGIDKISFFTPQNYLDMTALAEARGVDPEKFHIGIGQKKMAVPPIDEDIVTMAASAAKPILDRNDKQKIDMVIFGTESGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   83 DQSKSASLFVKEALNLPARIRTFEIKEACFALTASLQVARDYVRAHPHHSAMIIGSDIARYGLATAGEVTQGAGAISMLI 162
Cdd:TIGR01835  81 DQSKAAAVYVHGLLGLQPFCRSFELKQACYGATAALQMAKGHVALSPDRKVLVIASDIAKYGLESPGEPTQGAGAVAMLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  163 KENPAIIALEDGHTSHSENINDFWRPNNLATAVVDGHYSRDVYLDFFKSTFKPFLAEKQLQVSDFAGICYHLPYTKMGYK 242
Cdd:TIGR01835 161 SADPKLLAINEDSVLYTDDIMDFWRPNYSTTALVDGQYSNEQYLNAFENAWNDYAKRTGLSLADFAAFCFHVPFTKMGLK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  243 AHKIAIEGQDDETVKRLSDNFQLSAKYSRQVGNIYTASLYMSVLSLLENG-DLEAGDRIGFFSYGSGAMAEFFSGKVVAG 321
Cdd:TIGR01835 241 ALRHILKKNYEDEDESVQNAYLESIIYNREVGNLYTGSLYLGLASLLENAfEDTTGDKIGLFSYGSGAVAEFFSGTLVAG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504377723  322 YQKRLRPALHARMLKERIRIGVGQYEDIFTeglEALPENVEFTSDANhGTWYLAGQEGYVRQY 384
Cdd:TIGR01835 321 YRDHLKKERHLALLKNRTNLSYAEYEALFE---ETLPTDGDQPGEDR-GFFRLAGINDHKRIY 379
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 2-316 3.17e-69

"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: 220.77  E-value: 3.17e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   2 DIGIDQIGFYTPNKFVDMVDLANARNQDPNKFLIGIGQDRMAVADKtqDAVSMGINATAEYLD--QVDLEQLGLLIFATE 79
Cdd:cd00827    1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMAGDDE--DVPTMAVEAARRALEraGIDPDDIGLLIVATE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  80 SGIDQSKSASLFVKEALNLPaRIRTFEIKEACFALTASLQVARDYVRAHPHHSAMIIGSDIARYGL--ATAGEVTQGAGA 157
Cdd:cd00827   79 SPIDKGKSAATYLAELLGLT-NAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLdeGSALEPTLGDGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 158 ISMLIKENPAIIALE----DGHTSHSENIN-----DFWRPNNLATAV---VDGHYSRDVYLDFFKSTFKPFLAEKQLQVS 225
Cdd:cd00827  158 AAMLVSRNPGILAAGivstHSTSDPGYDFSpypvmDGGYPKPCKLAYairLTAEPAGRAVFEAAHKLIAKVVRKALDRAG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 226 DFAGICYHLPYTKMGYKAHKIAIEGQDDETVKRLSDNFqlsaKYSRQVGNIYTASLYMSVLSLLENGDLEAGDRIGFFSY 305
Cdd:cd00827  238 LSEDIDYFVPHQPNGKKILEAVAKKLGGPPEKASQTRW----ILLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSY 313

                        330
                 ....*....|.
gi 504377723 306 GSGAMAEFFSG 316
Cdd:cd00827  314 GSGFTAEAFVL 324
HMG-CoA-S_euk TIGR01833
3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA ...
 2-387 7.00e-46

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: 163.40  E-value: 7.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723    2 DIGIDQIGFYTPNKFVDMVDLANARNQDPNKFLIGIGQDRMAVADKTQDAVSMGINATAEYLD--QVDLEQLGLLIFATE 79
Cdd:TIGR01833   4 DVGILALEIYFPSQYVDQAELEKYDGVSAGKYTIGLGQTKMGFCTDREDINSLCLTVVSKLMEryNIDYDQIGRLEVGTE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   80 SGIDQSKSA-----SLFvKEALNlpARIRTFEIKEACFALTASLQVARDYVRAHP--HHSAMIIGSDIARYGLATAgEVT 152
Cdd:TIGR01833  84 TIIDKSKSVktvlmQLF-EESGN--TDVEGIDTTNACYGGTAALFNAINWIESSSwdGRYALVVAGDIAVYAKGNA-RPT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  153 QGAGAISMLIKENpAIIALEDG-HTSHSENINDFWRPnNLAT--AVVDGHYSRDVYLDFFKSTFKPFL--AEKQLQVS-- 225
Cdd:TIGR01833 160 GGAGAVAMLIGPN-APIVFERGlRGSHMQHAYDFYKP-DLASeyPVVDGKLSIQCYLSALDRCYKSYCkkIEKQWGKSgs 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  226 -------DFAGICYHLPYTKMGYKA---------------HKIAIEGQDDE----------TVKRLSDNFQLSAK----- 268
Cdd:TIGR01833 238 drkftldDFDYMIFHSPYCKLVQKSlarllyndflrnpssTDTSLYEGLEAlsglkledtyTDRDLEKAFMKASKelfdk 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  269 -------YSRQVGNIYTASLYMSVLSLL---ENGDLeAGDRIGFFSYGSGAMAEFFSGKVV------AGYQKRLRPALHA 332
Cdd:TIGR01833 318 ktkpsllVPTQVGNMYTASLYGCLASLLsskSAQEL-AGKRVGMFSYGSGLAASMFSLRVSqdaspgSALDKLIASLSDL 396

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504377723  333 R-MLKERIRIGVGQYEDIFtEGLEALPENVEFTSDAN-----HGTWYLAG-QEGYVRQYKQK 387
Cdd:TIGR01833 397 KnRLDSRHCVAPEEFEETM-ELREQAHHKKNFTPQGSidslfPGTWYLERvDSKHRRSYARK 457
PLN02577 PLN02577
hydroxymethylglutaryl-CoA synthase
 2-387 5.44e-44

hydroxymethylglutaryl-CoA synthase


Pssm-ID: 178189 [Multi-domain]  Cd Length: 459  Bit Score: 158.37  E-value: 5.44e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   2 DIGIDQIGFYTPNKFVDMVDLANARNQDPNKFLIGIGQDRMAVADKTQDAVSMGINATAEYLDQ--VDLEQLGLLIFATE 79
Cdd:PLN02577   4 NVGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEKynIDPKQIGRLEVGSE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  80 SGIDQSKSASLFV----KEALNLParIRTFEIKEACFALTASLQVARDYV--RAHPHHSAMIIGSDIARYGLATAgEVTQ 153
Cdd:PLN02577  84 TVIDKSKSIKTFLmqlfEESGNTD--IEGVDSTNACYGGTAALLNCVNWVesSSWDGRYGLVVAADSAVYAEGPA-RPTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 154 GAGAISMLIKENpAIIALEDGH-TSHSENINDFWRPnNLAT--AVVDGHYSRDVYLDFFKSTFKPFLAE------KQLQV 224
Cdd:PLN02577 161 GAGAVAMLVGPN-APIVFESKYrGSHMAHVYDFYKP-DLASeyPVVDGKLSQTCYLMALDSCYKRFCEKyeklegKQFSI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 225 SDFAGICYHLPYTKMGYK----------AHKIAIEGQD-------------DETV--KRLSDNFQLSAKY---------- 269
Cdd:PLN02577 239 SDADYFVFHAPYNKLVQKsfarlvyndfQRNASSVDEDakeklapfaglssDESYqnRDLEKVSQQVAKPlydakvqptt 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 270 --SRQVGNIYTASLYMSVLSLLEN-GDLEAGDRIGFFSYGSGAMAEFFSGKVVAGyQKRLRPALHARMLK--ERIRIGVG 344
Cdd:PLN02577 319 liPKQVGNMYTASLYAALASLVHNkHSELAGKRILMFSYGSGLTATMFSLRLHEG-QHPFSLSNIAKVMDvsEKLKSRHE 397

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504377723 345 QYEDIFTEGLE-------ALP-ENVEFTSDANHGTWYLAG-QEGYVRQYKQK 387
Cdd:PLN02577 398 VSPEKFVETLKlmehrygAKDfVPSKDVSLLAPGTYYLTEvDSLYRRFYDRK 449
PRK04262 PRK04262
hypothetical protein; Provisional
 1-346 1.69e-19

hypothetical protein; Provisional


Pssm-ID: 235266 [Multi-domain]  Cd Length: 347  Bit Score: 88.42  E-value: 1.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   1 MDIGIDQIGFYTPNKFVDMVDLANARNQDPNKFLIGIGQDRMAVADKTQDAVSMGINATAEYLD--QVDLEQLGLLIFAT 78
Cdd:PRK04262   1 MMVGIVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKraGIDPKEIGAVYVGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  79 ESGIDQSKSASLFVKEALNLPARIRTFEIKEACFALTASLQVARDYVRAHPHHSAMIIGSDIARYGLATAGEVTQGAGAI 158
Cdd:PRK04262  81 ESHPYAVKPTATIVAEALGATPDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGADTAQGAPGDALEYTAAAGGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 159 SMLI-KENPaiIALEDGHTSHSENINDFWRPnnlatavvDG-HYSR--------DVYLDFFKSTFKPFLAEKQLQVSDFA 228
Cdd:PRK04262 161 AFIIgKEEV--IAEIEATYSYTTDTPDFWRR--------EGePYPRhggrftgePAYFKHIISAAKGLMEKLGLKPSDYD 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 229 GICYHLPYTKMGYKAHKIAieGQDDETVKrlsdnfqlSAKYSRQVGNIYTASLYMSVLSLLENGdlEAGDRIGFFSYGSG 308
Cdd:PRK04262 231 YAVFHQPNGKFPLRVAKML--GFTKEQVK--------PGLLTPYIGNTYSGSALLGLAAVLDVA--KPGDRILVVSFGSG 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 504377723 309 AMAEFFSGKV---VAGYQKRLRPAlhARMLKERIRIGVGQY 346
Cdd:PRK04262 299 AGSDAFSITVtdaIEEKRDLAPTV--EDYLERKKYIDYAVY 337
HMG_CoA_synt_C pfam08540
Hydroxymethylglutaryl-coenzyme A synthase C terminal;
169-387 1.51e-18

Hydroxymethylglutaryl-coenzyme A synthase C terminal;


Pssm-ID: 400722  Cd Length: 280  Bit Score: 84.83  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  169 IALEDG-HTSHSENINDFWRPNNLAT-AVVDGHYSRDVYLDFFKSTFKPFLAEKQLQVS---------DFAGICYHLPYT 237
Cdd:pfam08540   1 IVFDRGlRGSHMEHAYDFYKPDLTSEyPVVDGKLSLSCYLKALDRCYKNYRKKINRITKdgdkifglnDFDYMIFHSPTC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  238 KMGYKA----------------------HKIAIEG----QDDETVKRLSDNFQLSAK------------YSRQVGNIYTA 279
Cdd:pfam08540  81 KLVQKSlarllyndflsnpssdkfngvdEKLTAFGgltlDESYTDKDLEKAFMKLSKpffkkkvqpsllVPTNNGNMYTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  280 SLYMSVLSLLEN--GDLEAGDRIGFFSYGSGAMAEFFSGKVVAGYQKRLRPALHARM-LKERIRIGVGQYEDIFTEGLEA 356
Cdd:pfam08540 161 SLYAALASLLSHvsADDLAGKRIGAFSYGSGLAATLFSLRVKQDVSPGSILDIASVLdLGKRLDSRICVTPEEFTEAMEL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 504377723  357 -----LPENVEFTSDANH---GTWYLAG-QEGYVRQYKQK 387
Cdd:pfam08540 241 reqahLKKNFKPQGSIDSlfpGTYYLTNvDDKFRRSYARK 280
HMG_CoA_synt_N pfam01154
Hydroxymethylglutaryl-coenzyme A synthase N terminal;
2-165 4.24e-16

Hydroxymethylglutaryl-coenzyme A synthase N terminal;


Pssm-ID: 307348 [Multi-domain]  Cd Length: 173  Bit Score: 75.35  E-value: 4.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723    2 DIGIDQIGFYTPNKFVDMVDLANARNQDPNKFLIGIGQDRMAVADKTQDAVSMGINATAEYLD--QVDLEQLGLLIFATE 79
Cdd:pfam01154   3 DVGILALEIYFPAQYVDQTELEKFDGVEAGKYTIGLGQTRMGFCSDREDINSLCLTVVQKLMEryNLPWDKIGRLEVGTE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   80 SGIDQSKSA-----SLFvKEALNlpARIRTFEIKEACFALTASLQVARDYVRAHP--HHSAMIIGSDIARYGLATAgEVT 152
Cdd:pfam01154  83 TIIDKSKSVksvlmQLF-QESGN--TDIEGIDTTNACYGGTAALFNAANWIESSSwdGRYALVVCGDIAIYPSGNA-RPT 158

                         170
                  ....*....|...
gi 504377723  153 QGAGAISMLIKEN 165
Cdd:pfam01154 159 GGAGAVAMLIGPK 171
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 3-308 1.88e-10

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: 61.40  E-value: 1.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   3 IGIDQIGFYTPNKFVDmvdlanarNQDPNKFL----------IGIGQDRMAVADKTqdAVSMGINATAEYLDQ--VDLEQ 70
Cdd:cd00830    2 ARILGIGSYLPERVVT--------NDELEKRLdtsdewirtrTGIRERRIADPGET--TSDLAVEAAKKALEDagIDADD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  71 LGLLIFATESGIDQSKSASLFVKEALNLPaRIRTFEIKEACFALTASLQVARDYVRAHPHHSAMIIGSDIARYGL----- 145
Cdd:cd00830   72 IDLIIVATSTPDYLFPATACLVQARLGAK-NAAAFDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLSRILdwtdr 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 146 ATAGEVTQGAGAisMLI---KENPAIIALE---DGHTSHSENINDFWRPNNLATAVVDGHY----SRDVYLDFFKS---T 212
Cdd:cd00830  151 STAVLFGDGAGA--VVLeatEEDPGILDSVlgsDGSGADLLTIPAGGSRSPFEDAEGGDPYlvmdGREVFKFAVRLmpeS 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 213 FKPFLAEKQLQVSDfagICYHLPYT-----------KMGYKAHKIAIegqddetvkrlsdNFQlsakysrQVGNIYTASL 281
Cdd:cd00830  229 IEEALEKAGLTPDD---IDWFVPHQanlriieavakRLGLPEEKVVV-------------NLD-------RYGNTSAASI 285

                        330       340
                 ....*....|....*....|....*..
gi 504377723 282 YMSVLSLLENGDLEAGDRIGFFSYGSG 308
Cdd:cd00830  286 PLALDEAIEEGKLKKGDLVLLLGFGAG 312
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 1-308 2.61e-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: 2.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   1 MDIGIDQIGFYTPNKFVDMVDLAnARNQDPNKFLI---GIGQDRmaVADKTQDAVSMGINATAEYLDQ--VDLEQLGLLI 75
Cdd:COG0332    1 RNVRILGTGSYLPERVVTNDDLE-KRLDTSDEWIEertGIRERR--IAAPDETTSDLAVEAARKALEAagIDPEDIDLII 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  76 FATESGIDQSKSASLFVKEALNLPaRIRTFEIKEAC--FaLTAsLQVARDYVRAHPHHSAMIIGSDIARYGL-----ATA 148
Cdd:COG0332   78 VATVTPDYLFPSTACLVQHKLGAK-NAAAFDINAACsgF-VYA-LSVAAALIRSGQAKNVLVVGAETLSRIVdwtdrSTC 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 149 geVTQGAGAISMLI---KENPAIIALE---DGHTSHSENINDFWRPNNLATAVVDGHY----SRDVY---LDFFKSTFKP 215
Cdd:COG0332  155 --VLFGDGAGAVVLeasEEGPGILGSVlgsDGSGADLLVVPAGGSRNPPSPVDEGDHYlrmdGREVFkfaVRNLPEVIRE 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 216 FLAEKQLQVSDFAGICYH---LPYTKMGYKAHKIAIEgqddetvkRLSDNFQlsaKYsrqvGNIYTASLYMSVLSLLENG 292
Cdd:COG0332  233 ALEKAGLTLDDIDWFIPHqanLRIIEAVAKRLGLPEE--------KVVVNID---RY----GNTSAASIPLALDEALREG 297

                        330
                 ....*....|....*.
gi 504377723 293 DLEAGDRIGFFSYGSG 308
Cdd:COG0332  298 RIKPGDLVLLAGFGAG 313
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
1-139 4.07e-04

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 41.98  E-value: 4.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   1 MDIGIDQIGFYTPNKFVDmvdlanarNQDPNKFL------I----GIGQDRMAVADKTqdAVSMGINATAEYLDQ--VDL 68
Cdd:PRK09352   2 MYAKILGTGSYLPERVVT--------NDDLEKMVdtsdewIvtrtGIKERRIAAPDET--TSDLATEAAKKALEAagIDP 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504377723  69 EQLGLLIFATESGIDQSKSASLFVKEALNL---PArirtFEIKEAC----FALTaslqVARDYVRAHPHHSAMIIGSD 139
Cdd:PRK09352  72 EDIDLIIVATTTPDYAFPSTACLVQARLGAknaAA----FDLSAACsgfvYALS----TADQFIRSGAYKNVLVIGAE 141
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
 29-129 5.73e-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: 41.44  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  29 DPNKFLIGIGQDRMAVADKtqDAVSMGINATAEYLDQ--VDLEQLGLLIFATESGIDqSKSASLFVKEALNLPARIRTFE 106
Cdd:cd00831   65 APRPEMSPSLDERNDIALE--EARELAEEAARGALDEagLRPSDIDHLVVNTSTGNP-TPSLDAMLINRLGLRPDVKRYN 141

                         90       100
                 ....*....|....*....|....
gi 504377723 107 IKE-ACFALTASLQVARDYVRAHP 129
Cdd:cd00831  142 LGGmGCSAGAIALDLAKDLLEANP 165
PRK06840 PRK06840
3-oxoacyl-ACP synthase;
1-204 2.36e-03

3-oxoacyl-ACP synthase;


Pssm-ID: 235872  Cd Length: 339  Bit Score: 39.60  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723   1 MDIGIDQIGFYTPNKFVDMVDLANARNQDPN----KFliGIGQDRmaVADKTQDAVSMGINATAEYLDQ--VDLEQLGLL 74
Cdd:PRK06840   3 MNVGIVGTGVYLPKDVMTAEEIAEKTGIPEEvvieKF--GIYEKP--VPGPEDHTSDMAIAAAKPALKQagVDPAAIDVV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  75 IFATESGID-QSKSASLFVKEALNLpARIRTFEIKEACFALTASLQVARDYVRAHPH-HSAMIIG----SDIARYG-LAT 147
Cdd:PRK06840  79 IYIGSEHKDyPVWSSAPKIQHEIGA-KNAWAFDIMAVCASFPIALKVAKDLLYSDPSiENVLLVGgyrnSDLVDYDnPRT 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504377723 148 AGEVTQGAGAISMLIKENPAIIALedghtshsenindfwrpnnLATAV-VDGHYSRDV 204
Cdd:PRK06840 158 RFMFNFAAGGSAALLKKDAGKNRI-------------------LGSAIiTDGSFSEDV 196
PRK09258 PRK09258
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 66-312 8.71e-03

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


Pssm-ID: 181732  Cd Length: 338  Bit Score: 37.94  E-value: 8.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723  66 VDLEQLGLLIFATESGIDQSKSASLFVKEALNLPARIRTFEIKEACFA-LTASLQVArdyvrahphhsAMIIGSDIaRYG 144
Cdd:PRK09258  78 IDPSDIGLLINTSVCRDYLEPATACRVHHNLGLPKSCANFDVSNACLGfLNGMLDAA-----------NMIELGQI-DYA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 145 LATAGE-----------------------------VTQGAGAISMLI---KENPAIIALEDG----HTSHSE-NINDFWR 187
Cdd:PRK09258 146 LVVSGEsareiveatidrllapettredfaqsfatLTLGSGAAAAVLtrgSLHPRGHRLLGGvtraATEHHElCQGGRDG 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504377723 188 PNNLATAVVDGHysrdvyLDFFKSTFKPFLAEKQLQVSDFAGICYH---LPYTKMGYKAHKIAIEgQDDETVKRLsdnfq 264
Cdd:PRK09258 226 MRTDAVGLLKEG------VELAVDTWEAFLAQLGWAVEQVDRVICHqvgAAHTRAILKALGIDPE-KVFTTFPTL----- 293

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504377723 265 lsakysrqvGNIYTASLYMSVLSLLENGDLEAGDRIGFFSYGSG---AMAE 312
Cdd:PRK09258 294 ---------GNMGPASLPITLAMAAEEGFLKPGDRVALLGIGSGlncSMLE 335
 
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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