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Conserved domains on  [gi|521258030|ref|WP_020444595|]
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MULTISPECIES: hydroxymethylglutaryl-CoA synthase [Bacillota]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HMG-CoA-S_prok super family cl33300
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
 7-125 6.48e-26

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.


The actual alignment was detected with superfamily member TIGR01835:

Pssm-ID: 213655 [Multi-domain]  Cd Length: 379  Bit Score: 99.82  E-value: 6.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521258030    7 TVLWNRDVGNIYTGSLYLSLISLLQN-HTFQPEEKVCLFSYGSGAVGEIFSGSIVKGYDKALDKEKHLNMLESREQLSVE 85
Cdd:TIGR01835 264 SIIYNREVGNLYTGSLYLGLASLLENaFEDTTGDKIGLFSYGSGAVAEFFSGTLVAGYRDHLKKERHLALLKNRTNLSYA 343

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 521258030   86 EYETFFNRFDNQEFDFERELTQdPYSKVylySIEDHIRTY 125
Cdd:TIGR01835 344 EYEALFEETLPTDGDQPGEDRG-FFRLA---GINDHKRIY 379
 
Name Accession Description Interval E-value
HMG-CoA-S_prok TIGR01835
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
 7-125 6.48e-26

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: 99.82  E-value: 6.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521258030    7 TVLWNRDVGNIYTGSLYLSLISLLQN-HTFQPEEKVCLFSYGSGAVGEIFSGSIVKGYDKALDKEKHLNMLESREQLSVE 85
Cdd:TIGR01835 264 SIIYNREVGNLYTGSLYLGLASLLENaFEDTTGDKIGLFSYGSGAVAEFFSGTLVAGYRDHLKKERHLALLKNRTNLSYA 343

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 521258030   86 EYETFFNRFDNQEFDFERELTQdPYSKVylySIEDHIRTY 125
Cdd:TIGR01835 344 EYEALFEETLPTDGDQPGEDRG-FFRLA---GINDHKRIY 379
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 7-126 1.48e-24

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: 96.02  E-value: 1.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521258030   7 TVLWNRDVGNIYTGSLYLSLISLLQNHTFQPEEKVCLFSYGSGAVGEIFSGSIVKGYDKALDKEKHLNMLESREQLSVEE 86
Cdd:COG3425  268 SLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGTVTPGIEERLRRPGVEEQLANRRYLSYAE 347

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 521258030  87 YETFFNrfDNQEFDFERELTQDPYskvYLYSIEDHIRTYK 126
Cdd:COG3425  348 YEKLRG--KILPEDAEDVTLPGEF---VLTGIKDHERIYE 382
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 9-57 1.98e-04

"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: 39.34  E-value: 1.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 521258030   9 LWNRDVGNIYTGSLYLSLISLLQNHTFQPEEKVCLFSYGSGAVGEIFSG 57
Cdd:cd00827  276 ILLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFTAEAFVL 324
HMG_CoA_synt_C pfam08540
Hydroxymethylglutaryl-coenzyme A synthase C terminal;
7-88 9.64e-03

Hydroxymethylglutaryl-coenzyme A synthase C terminal;


Pssm-ID: 400722  Cd Length: 280  Bit Score: 34.37  E-value: 9.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521258030    7 TVLWNRDVGNIYTGSLYLSLISLLQNHTFQ--PEEKVCLFSYGSGAVGEIFSGSIV--KGYDKALDKEKHLNM---LESR 79
Cdd:pfam08540 147 SLLVPTNNGNMYTASLYAALASLLSHVSADdlAGKRIGAFSYGSGLAATLFSLRVKqdVSPGSILDIASVLDLgkrLDSR 226


                  ....*....
gi 521258030   80 EQLSVEEYE 88
Cdd:pfam08540 227 ICVTPEEFT 235
 
Name Accession Description Interval E-value
HMG-CoA-S_prok TIGR01835
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
 7-125 6.48e-26

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: 99.82  E-value: 6.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521258030    7 TVLWNRDVGNIYTGSLYLSLISLLQN-HTFQPEEKVCLFSYGSGAVGEIFSGSIVKGYDKALDKEKHLNMLESREQLSVE 85
Cdd:TIGR01835 264 SIIYNREVGNLYTGSLYLGLASLLENaFEDTTGDKIGLFSYGSGAVAEFFSGTLVAGYRDHLKKERHLALLKNRTNLSYA 343

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 521258030   86 EYETFFNRFDNQEFDFERELTQdPYSKVylySIEDHIRTY 125
Cdd:TIGR01835 344 EYEALFEETLPTDGDQPGEDRG-FFRLA---GINDHKRIY 379
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 7-126 1.48e-24

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: 96.02  E-value: 1.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521258030   7 TVLWNRDVGNIYTGSLYLSLISLLQNHTFQPEEKVCLFSYGSGAVGEIFSGSIVKGYDKALDKEKHLNMLESREQLSVEE 86
Cdd:COG3425  268 SLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGTVTPGIEERLRRPGVEEQLANRRYLSYAE 347

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 521258030  87 YETFFNrfDNQEFDFERELTQDPYskvYLYSIEDHIRTYK 126
Cdd:COG3425  348 YEKLRG--KILPEDAEDVTLPGEF---VLTGIKDHERIYE 382
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 9-57 1.98e-04

"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: 39.34  E-value: 1.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 521258030   9 LWNRDVGNIYTGSLYLSLISLLQNHTFQPEEKVCLFSYGSGAVGEIFSG 57
Cdd:cd00827  276 ILLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFTAEAFVL 324
HMG_CoA_synt_C pfam08540
Hydroxymethylglutaryl-coenzyme A synthase C terminal;
7-88 9.64e-03

Hydroxymethylglutaryl-coenzyme A synthase C terminal;


Pssm-ID: 400722  Cd Length: 280  Bit Score: 34.37  E-value: 9.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521258030    7 TVLWNRDVGNIYTGSLYLSLISLLQNHTFQ--PEEKVCLFSYGSGAVGEIFSGSIV--KGYDKALDKEKHLNM---LESR 79
Cdd:pfam08540 147 SLLVPTNNGNMYTASLYAALASLLSHVSADdlAGKRIGAFSYGSGLAATLFSLRVKqdVSPGSILDIASVLDLgkrLDSR 226


                  ....*....
gi 521258030   80 EQLSVEEYE 88
Cdd:pfam08540 227 ICVTPEEFT 235
 
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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