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Conserved domains on  [gi|961386535|gb|ALS09148|]
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3-hydroxy-3-methylglutaryl coenzyme A reductase 2, partial [Solanum chacoense]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HMG-CoA_reductase super family cl00205
Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A ...
 1-135 1.61e-78

Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) is a tightly regulated enzyme, which catalyzes the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. In mammals, this is the rate limiting committed step in cholesterol biosynthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. There are two classes of HMGR: class I enzymes which are found predominantly in eukaryotes and contain N-terminal membrane regions and class II enzymes which are found primarily in prokaryotes and are soluble as they lack the membrane region. With the exception of Archaeoglobus fulgidus, most archeae are assigned to class I, based on sequence similarity of the active site, even though they lack membrane regions. Yeast and human HMGR are divergent in their N-terminal regions, but are conserved in their active site. In contrast, human and bacterial HMGR differ in their active site architecture. While the prokaryotic enzyme is a homodimer, the eukaryotic enzyme is a homotetramer.


The actual alignment was detected with superfamily member cd00643:

Pssm-ID: 469656  Cd Length: 403  Bit Score: 237.07  E-value: 1.61e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961386535   1 VSKGVQNVLDYLQNEYPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITEEVVKKVLKTEVSALVELNMLKNLTG 80
Cdd:cd00643  196 VTKATEAACDWIEENFPDMEVISLSGNFCTDKKPSAINWIEGRGKSVVAEATIPREVVKEVLKTTPEALVEVNIAKNLIG 275

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 961386535  81 SAMAGaLGGFNAHASNIVSAVFIATGQDPAQNIESSHCITMMEAVNDGkDLHISV 135
Cdd:cd00643  276 SAMAG-SGGFNAHAANIVAAIFIATGQDAAQVVESSNCITTMELTADG-DLYISV 328
 
Name Accession Description Interval E-value
HMG-CoA_reductase_classI cd00643
Class I hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); ...
 1-135 1.61e-78

Class I hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class I enzyme, homotetramer. Catalyzes the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. In mammals this is the rate limiting committed step in cholesterol biosynthesis. Class I enzymes are found predominantly in eukaryotes and contain N-terminal membrane regions. With the exception of Archaeoglobus fulgidus, most archeae are assigned to class I, based on sequence similarity of the active site, even though they lack membrane regions. Yeast and human HMGR are divergent in their N-terminal regions, but are conserved in their active site. In contrast, human and bacterial HMGR differ in their active site architecture.


Pssm-ID: 153081  Cd Length: 403  Bit Score: 237.07  E-value: 1.61e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961386535   1 VSKGVQNVLDYLQNEYPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITEEVVKKVLKTEVSALVELNMLKNLTG 80
Cdd:cd00643  196 VTKATEAACDWIEENFPDMEVISLSGNFCTDKKPSAINWIEGRGKSVVAEATIPREVVKEVLKTTPEALVEVNIAKNLIG 275

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 961386535  81 SAMAGaLGGFNAHASNIVSAVFIATGQDPAQNIESSHCITMMEAVNDGkDLHISV 135
Cdd:cd00643  276 SAMAG-SGGFNAHAANIVAAIFIATGQDAAQVVESSNCITTMELTADG-DLYISV 328
2A060605 TIGR00920
3-hydroxy-3-methylglutaryl-coenzyme A reductase; [Transport and binding proteins, ...
 1-134 1.26e-69

3-hydroxy-3-methylglutaryl-coenzyme A reductase; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273339 [Multi-domain]  Cd Length: 886  Bit Score: 224.35  E-value: 1.26e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961386535    1 VSKGVQNVLDYLQNEYPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITEEVVKKVLKTEVSALVELNMLKNLTG 80
Cdd:TIGR00920 657 ISKGTEQALAELQEHFPDMQILSLSGNYCTDKKPAAINWIEGRGKSVVCEATIPAKIVRSVLKTSAEALVDVNINKNLIG 736

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 961386535   81 SAMAGALGGFNAHASNIVSAVFIATGQDPAQNIESSHCITMMEAVN-DGKDLHIS 134
Cdd:TIGR00920 737 SAMAGSIGGFNAHAANIVTAIYIATGQDAAQNVGSSNCMTLMEAWGpTGEDLYIS 791
HMG-CoA_red pfam00368
Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of ...
 1-135 2.89e-61

Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of HMG-CoA to mevalonate, which is the rate-limiting step in the synthesis of isoprenoids like cholesterol. Probably because of the critical role of this enzyme in cholesterol homeostasis, mammalian HMG-CoA reductase is heavily regulated at the transcriptional, translational, and post-translational levels.


Pssm-ID: 459786  Cd Length: 368  Bit Score: 191.90  E-value: 2.89e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961386535    1 VSKGVQNVLDYLQNEYPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITEEVVKKVLKTEVSALVELNMLKNLtG 80
Cdd:pfam00368 167 VNTATEAAAPLIEEEFGGMVLLSILSNLCTDKKPSAINWIEGRGKSVVAEATIGEEVVKKILKASPEALVDPYRAKNI-G 245

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 961386535   81 SAMAGALgGFNAHASNIVSAVFIATGQDPAQNIESSHCITMMEAVNDGkDLHISV 135
Cdd:pfam00368 246 THNKGII-GGNAHAANGIAAVFLATGQDPAAVEESSHAYAALETWEDG-DLYGSV 298
HMG1 COG1257
Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism]; ...
 8-135 2.14e-17

Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism]; Hydroxymethylglutaryl-CoA reductase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440869  Cd Length: 409  Bit Score: 76.72  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961386535   8 VLDYLQNEYPDMDVIGISGNFCSdkkpaavnwiegrGKSVVCEAIITEEVVKKVLKTEVSALVEL-NMLKNLTGSAMAGA 86
Cdd:COG1257  188 VAPWIEELTGGEVLLRILSNYAT-------------GKLVRAEVTIPVEVLGKVLKVSGEEVAEKiVLASNFAGADPYRA 254

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 961386535  87 LGgFNAHASNIVSAVFIATGQDPAQNIESSHCIT--------MMEAVNDGKDLHISV 135
Cdd:COG1257  255 AT-HNKGIMNGIDAVVIATGNDWRAVEAGAHAYAardgryesLTTWKDEDGDLYGSI 310
 
Name Accession Description Interval E-value
HMG-CoA_reductase_classI cd00643
Class I hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); ...
 1-135 1.61e-78

Class I hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class I enzyme, homotetramer. Catalyzes the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. In mammals this is the rate limiting committed step in cholesterol biosynthesis. Class I enzymes are found predominantly in eukaryotes and contain N-terminal membrane regions. With the exception of Archaeoglobus fulgidus, most archeae are assigned to class I, based on sequence similarity of the active site, even though they lack membrane regions. Yeast and human HMGR are divergent in their N-terminal regions, but are conserved in their active site. In contrast, human and bacterial HMGR differ in their active site architecture.


Pssm-ID: 153081  Cd Length: 403  Bit Score: 237.07  E-value: 1.61e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961386535   1 VSKGVQNVLDYLQNEYPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITEEVVKKVLKTEVSALVELNMLKNLTG 80
Cdd:cd00643  196 VTKATEAACDWIEENFPDMEVISLSGNFCTDKKPSAINWIEGRGKSVVAEATIPREVVKEVLKTTPEALVEVNIAKNLIG 275

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 961386535  81 SAMAGaLGGFNAHASNIVSAVFIATGQDPAQNIESSHCITMMEAVNDGkDLHISV 135
Cdd:cd00643  276 SAMAG-SGGFNAHAANIVAAIFIATGQDAAQVVESSNCITTMELTADG-DLYISV 328
2A060605 TIGR00920
3-hydroxy-3-methylglutaryl-coenzyme A reductase; [Transport and binding proteins, ...
 1-134 1.26e-69

3-hydroxy-3-methylglutaryl-coenzyme A reductase; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273339 [Multi-domain]  Cd Length: 886  Bit Score: 224.35  E-value: 1.26e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961386535    1 VSKGVQNVLDYLQNEYPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITEEVVKKVLKTEVSALVELNMLKNLTG 80
Cdd:TIGR00920 657 ISKGTEQALAELQEHFPDMQILSLSGNYCTDKKPAAINWIEGRGKSVVCEATIPAKIVRSVLKTSAEALVDVNINKNLIG 736

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 961386535   81 SAMAGALGGFNAHASNIVSAVFIATGQDPAQNIESSHCITMMEAVN-DGKDLHIS 134
Cdd:TIGR00920 737 SAMAGSIGGFNAHAANIVTAIYIATGQDAAQNVGSSNCMTLMEAWGpTGEDLYIS 791
HMG-CoA_red pfam00368
Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of ...
 1-135 2.89e-61

Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of HMG-CoA to mevalonate, which is the rate-limiting step in the synthesis of isoprenoids like cholesterol. Probably because of the critical role of this enzyme in cholesterol homeostasis, mammalian HMG-CoA reductase is heavily regulated at the transcriptional, translational, and post-translational levels.


Pssm-ID: 459786  Cd Length: 368  Bit Score: 191.90  E-value: 2.89e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961386535    1 VSKGVQNVLDYLQNEYPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITEEVVKKVLKTEVSALVELNMLKNLtG 80
Cdd:pfam00368 167 VNTATEAAAPLIEEEFGGMVLLSILSNLCTDKKPSAINWIEGRGKSVVAEATIGEEVVKKILKASPEALVDPYRAKNI-G 245

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 961386535   81 SAMAGALgGFNAHASNIVSAVFIATGQDPAQNIESSHCITMMEAVNDGkDLHISV 135
Cdd:pfam00368 246 THNKGII-GGNAHAANGIAAVFLATGQDPAAVEESSHAYAALETWEDG-DLYGSV 298
HMG_CoA_R_NADP TIGR00533
3-hydroxy-3-methylglutaryl Coenzyme A reductase, hydroxymethylglutaryl-CoA reductase (NADP); ...
 1-135 3.77e-56

3-hydroxy-3-methylglutaryl Coenzyme A reductase, hydroxymethylglutaryl-CoA reductase (NADP); This model represents archaeal examples of the enzyme hydroxymethylglutaryl-CoA reductase (NADP) (EC 1.1.1.34) and the catalytic domain of eukaryotic examples, which also contain a hydrophobic N-terminal domain. This enzyme synthesizes mevalonate, a precursor of isopentenyl pyrophosphate (IPP), a building block for the synthesis of cholesterol, isoprenoids, and other molecules. A related hydroxymethylglutaryl-CoA reductase, typified by an example from Pseudomonas mevalonii, is NAD-dependent and catabolic. [Central intermediary metabolism, Other]


Pssm-ID: 129624  Cd Length: 402  Bit Score: 179.68  E-value: 3.77e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961386535    1 VSKGVQNVLDYLQNEY--PDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITEEVVKKVLKTEVSALVELNMLKNL 78
Cdd:TIGR00533 199 VTIATEYALKQMVEEYgwEGMEVVAVSGNYCTDKKPAAINLIEGRGKSIVAEATIPGDVVNKVLKTTVSALVEVNIAKNL 278

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 961386535   79 TGSAMAGALgGFNAHASNIVSAVFIATGQDPAQNIESSHCITMMEAVnDGkDLHISV 135
Cdd:TIGR00533 279 IGSAMAGSM-GFNAHYANIIGAIFLATGQDEAHIVEGSLGITLAEEV-DG-DLYFSV 332
HMG-CoA_reductase cd00365
Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A ...
 1-134 1.05e-17

Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) is a tightly regulated enzyme, which catalyzes the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. In mammals, this is the rate limiting committed step in cholesterol biosynthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. There are two classes of HMGR: class I enzymes which are found predominantly in eukaryotes and contain N-terminal membrane regions and class II enzymes which are found primarily in prokaryotes and are soluble as they lack the membrane region. With the exception of Archaeoglobus fulgidus, most archeae are assigned to class I, based on sequence similarity of the active site, even though they lack membrane regions. Yeast and human HMGR are divergent in their N-terminal regions, but are conserved in their active site. In contrast, human and bacterial HMGR differ in their active site architecture. While the prokaryotic enzyme is a homodimer, the eukaryotic enzyme is a homotetramer.


Pssm-ID: 153080  Cd Length: 376  Bit Score: 77.72  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961386535   1 VSKGVQNVLDYLQNEYPDMDVIGISGNFCSdkkpaavnwieGRGKSVVCEAIITEEVVKKVL---KTEVSALVELNMLKN 77
Cdd:cd00365  179 INTMAEAVAPLMEAYTGGMQVRLRSLSNLT-----------GDGRLARAQARITPQQLETAEfsgEAVIEGILDAYAFKA 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961386535  78 LTGSAMAGalgGFNAHASNIVSAVFIATGQDPAQNIESSH--------CITMMEAVNDGkDLHIS 134
Cdd:cd00365  248 AVDSYRAA---THNKGIMNGVDPLIVACGQDWRAVEVGAHayacrhygSLTTWEKDNNG-HLVIT 308
HMG1 COG1257
Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism]; ...
 8-135 2.14e-17

Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism]; Hydroxymethylglutaryl-CoA reductase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440869  Cd Length: 409  Bit Score: 76.72  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961386535   8 VLDYLQNEYPDMDVIGISGNFCSdkkpaavnwiegrGKSVVCEAIITEEVVKKVLKTEVSALVEL-NMLKNLTGSAMAGA 86
Cdd:COG1257  188 VAPWIEELTGGEVLLRILSNYAT-------------GKLVRAEVTIPVEVLGKVLKVSGEEVAEKiVLASNFAGADPYRA 254

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 961386535  87 LGgFNAHASNIVSAVFIATGQDPAQNIESSHCIT--------MMEAVNDGKDLHISV 135
Cdd:COG1257  255 AT-HNKGIMNGIDAVVIATGNDWRAVEAGAHAYAardgryesLTTWKDEDGDLYGSI 310
 
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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