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Conserved domains on  [gi|1080384939|gb|OFL72420|]
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hydroxymethylglutaryl-CoA reductase [Corynebacterium sp. HMSC063G05]

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 ...
11-344 3.08e-115

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: 339.91  E-value: 3.08e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  11 YAHVPLSWIGPVRISGNVMNDEVKIPLATYETPLWPSCGRGAKVSRMiEGGITCTFVGEKMTRSVIFTLDSAADAVIARD 90
Cdd:cd00643    67 YVQVPVGVAGPLLINGEYAGGEFYVPMATTEGALVASTNRGCKAINL-SGGATTRVLGDGMTRAPVFRFPSAREAAEFKA 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  91 NILSRYDELKKVVESSSRFAKLVDIHFQIASRLLFVRFDFFSGDASGHNMATLASERLMSYLMEQMPELGYGSISGNYCT 170
Cdd:cd00643   146 WIEENFEAIKEVAESTSRHARLQSIKPYIAGRSVYLRFEYTTGDAMGMNMVTKATEAACDWIEENFPDMEVISLSGNFCT 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 171 DKKTSAVNGILGRGKYVIAEAVIPEPVVRERLRTTAKRLAELNERKNLVGSIMAGSLrSGNAHYANMLLGFYLATGQDAA 250
Cdd:cd00643   226 DKKPSAINWIEGRGKSVVAEATIPREVVKEVLKTTPEALVEVNIAKNLIGSAMAGSG-GFNAHAANIVAAIFIATGQDAA 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 251 NIVEGSQGLTQVEALDDGSVRFSCTLPHLIVGSVGNGKGLDFVEKNLTALGCK-EDREPGENARRLAACCAAIVWCGELS 329
Cdd:cd00643   305 QVVESSNCITTMELTADGDLYISVTMPSLEVGTVGGGTGLPTQRECLELLGCYgAGDEPGANARKLAEIVAATVLAGELS 384
                         330
                  ....*....|....*
gi 1080384939 330 LLAAQTNpGELMEAH 344
Cdd:cd00643   385 LLAALAA-GHLVRSH 398
 
Name Accession Description Interval E-value
HMG-CoA_reductase_classI cd00643
Class I hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); ...
11-344 3.08e-115

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: 339.91  E-value: 3.08e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  11 YAHVPLSWIGPVRISGNVMNDEVKIPLATYETPLWPSCGRGAKVSRMiEGGITCTFVGEKMTRSVIFTLDSAADAVIARD 90
Cdd:cd00643    67 YVQVPVGVAGPLLINGEYAGGEFYVPMATTEGALVASTNRGCKAINL-SGGATTRVLGDGMTRAPVFRFPSAREAAEFKA 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  91 NILSRYDELKKVVESSSRFAKLVDIHFQIASRLLFVRFDFFSGDASGHNMATLASERLMSYLMEQMPELGYGSISGNYCT 170
Cdd:cd00643   146 WIEENFEAIKEVAESTSRHARLQSIKPYIAGRSVYLRFEYTTGDAMGMNMVTKATEAACDWIEENFPDMEVISLSGNFCT 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 171 DKKTSAVNGILGRGKYVIAEAVIPEPVVRERLRTTAKRLAELNERKNLVGSIMAGSLrSGNAHYANMLLGFYLATGQDAA 250
Cdd:cd00643   226 DKKPSAINWIEGRGKSVVAEATIPREVVKEVLKTTPEALVEVNIAKNLIGSAMAGSG-GFNAHAANIVAAIFIATGQDAA 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 251 NIVEGSQGLTQVEALDDGSVRFSCTLPHLIVGSVGNGKGLDFVEKNLTALGCK-EDREPGENARRLAACCAAIVWCGELS 329
Cdd:cd00643   305 QVVESSNCITTMELTADGDLYISVTMPSLEVGTVGGGTGLPTQRECLELLGCYgAGDEPGANARKLAEIVAATVLAGELS 384
                         330
                  ....*....|....*
gi 1080384939 330 LLAAQTNpGELMEAH 344
Cdd:cd00643   385 LLAALAA-GHLVRSH 398
HMG-CoA_red pfam00368
Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of ...
11-344 1.09e-88

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: 270.86  E-value: 1.09e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  11 YAHVPLSWIGPVRISGnvmnDEVKIPLATYETPLWPSCGRGAKVSRMiEGGITCTFVGEKMTRSVIFTLDSAADAVIARD 90
Cdd:pfam00368  40 YVQLPLGVAGPLLING----KDYLVPMATTEGSLVASASRGAKAINA-SGGFTTTVLGDGMTRGPVFLFDSVADAAEAKE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  91 NILSR--YDELKKVVESSSRFAKLVDIHFQIASRLLFVRFDFFSGDASGHNMATLASERLMSYLMEQMPELGYGSISGNY 168
Cdd:pfam00368 115 WIENKenLLEIANAAEPTSRGGGLRDIEVVIAGRMVYLRFLVDTGDAMGANMVNTATEAAAPLIEEEFGGMVLLSILSNL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 169 CTDKKTSAVNGILGRGKYVIAEAVIPEPVVRERLRTTAKRLAELNERKNlVGSIMAGSLrSGNAHYANMLLGFYLATGQD 248
Cdd:pfam00368 195 CTDKKPSAINWIEGRGKSVVAEATIGEEVVKKILKASPEALVDPYRAKN-IGTHNKGII-GGNAHAANGIAAVFLATGQD 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 249 AANIVEGSQGLTQVEALDDGSVRFSCTLPHLIVGSVGNGKGLDFVEKNLTALGCKEDREPGEnarrlaacCAAI----VW 324
Cdd:pfam00368 273 PAAVEESSHAYAALETWEDGDLYGSVTLPSLEVGTVGGGTGLPPQAECLKLLGVKGAGKPRE--------LAEIiaavGL 344
                         330       340
                  ....*....|....*....|
gi 1080384939 325 CGELSLLAAQTNpGELMEAH 344
Cdd:pfam00368 345 AGELSALRALAA-GGIQKGH 363
HMG_CoA_R_NADP TIGR00533
3-hydroxy-3-methylglutaryl Coenzyme A reductase, hydroxymethylglutaryl-CoA reductase (NADP); ...
11-349 2.99e-77

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: 242.86  E-value: 2.99e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  11 YAHVPLSWIGPVRISGNVMNDEVKIPLATYETPLWPSCGRGAKVSRMiEGGITCTFVGEKMTRSVIFTLDSAADAVIARD 90
Cdd:TIGR00533  69 YMQIPLGVAGPLKIDGEYAKGEYYIPLATTEGALVASVNRGCSAITA-GGGATVRVTKDGMTRAPVVRTPSVVRAGACRI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  91 NILSRYDELKKVVESSSRFAKLVDIHFQ-IASRLLFVRFDFFSGDASGHNMATLASERLMSYLMEQMPELGYG--SISGN 167
Cdd:TIGR00533 148 WIDENQNAIKEAAESTTRHGKLQKIQPIcLAGDLLYPRFVTTTGDAMGMNMVTIATEYALKQMVEEYGWEGMEvvAVSGN 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 168 YCTDKKTSAVNGILGRGKYVIAEAVIPEPVVRERLRTTAKRLAELNERKNLVGSIMAGSLrSGNAHYANMLLGFYLATGQ 247
Cdd:TIGR00533 228 YCTDKKPAAINLIEGRGKSIVAEATIPGDVVNKVLKTTVSALVEVNIAKNLIGSAMAGSM-GFNAHYANIIGAIFLATGQ 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 248 DAANIVEGSQGLTQVEAlDDGSVRFSCTLPHLIVGSVGNGKGLDFVEKNLTALGCKEdrepGENARRLAACCAAIVWCGE 327
Cdd:TIGR00533 307 DEAHIVEGSLGITLAEE-VDGDLYFSVSLPDVPVGTVGGGTVLETQGECLDLLGVRG----GNNARQFAEIVGCAVLAGE 381
                         330       340
                  ....*....|....*....|..
gi 1080384939 328 LSLLAAQTnPGELMEAHVSIER 349
Cdd:TIGR00533 382 LSLCGALA-AGHLVQAHMELGR 402
HMG1 COG1257
Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism]; ...
12-290 2.21e-49

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: 170.32  E-value: 2.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  12 AHVPLSWIGPVRISGnvmnDEVKIPLATYETPLWPSCGRGAKVSRMiEGGITCTFVGEKMTRSVIFTldSAADAVIARDN 91
Cdd:COG1257    53 FQLPLGVAGNFLING----KDYLVPMATEEPSVVAAASRGAKLIRE-SGGFKTTVLGDGMIGQPQFV--DVGDARAAREW 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  92 ILSRYDELKKVVES-----SSRFAKLVDIH-FQIASRLLFVRFDFFSGDASGHNMATLASERLMSYLMEQMPELGYGSIS 165
Cdd:COG1257   126 ILENKEEILEAAESadpsmTKRGGGLRDIEvRVLLGNMVVLHLIVDTGDAMGANMVNTATEAVAPWIEELTGGEVLLRIL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 166 GNYCTdkktsavngilgrGKYVIAEAVIPEPVVRERLRTTAKRLAEL-NERKNLVGSIMAGSLrSGNAHYANMLLGFYLA 244
Cdd:COG1257   206 SNYAT-------------GKLVRAEVTIPVEVLGKVLKVSGEEVAEKiVLASNFAGADPYRAA-THNKGIMNGIDAVVIA 271
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1080384939 245 TGQDAANIVEGSQGLT----QVEAL-----DDGSVRFSCTLPhLIVGSVGNGKGL 290
Cdd:COG1257   272 TGNDWRAVEAGAHAYAardgRYESLttwkdEDGDLYGSITLP-LAVGTVGGGTGL 325
 
Name Accession Description Interval E-value
HMG-CoA_reductase_classI cd00643
Class I hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); ...
11-344 3.08e-115

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: 339.91  E-value: 3.08e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  11 YAHVPLSWIGPVRISGNVMNDEVKIPLATYETPLWPSCGRGAKVSRMiEGGITCTFVGEKMTRSVIFTLDSAADAVIARD 90
Cdd:cd00643    67 YVQVPVGVAGPLLINGEYAGGEFYVPMATTEGALVASTNRGCKAINL-SGGATTRVLGDGMTRAPVFRFPSAREAAEFKA 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  91 NILSRYDELKKVVESSSRFAKLVDIHFQIASRLLFVRFDFFSGDASGHNMATLASERLMSYLMEQMPELGYGSISGNYCT 170
Cdd:cd00643   146 WIEENFEAIKEVAESTSRHARLQSIKPYIAGRSVYLRFEYTTGDAMGMNMVTKATEAACDWIEENFPDMEVISLSGNFCT 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 171 DKKTSAVNGILGRGKYVIAEAVIPEPVVRERLRTTAKRLAELNERKNLVGSIMAGSLrSGNAHYANMLLGFYLATGQDAA 250
Cdd:cd00643   226 DKKPSAINWIEGRGKSVVAEATIPREVVKEVLKTTPEALVEVNIAKNLIGSAMAGSG-GFNAHAANIVAAIFIATGQDAA 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 251 NIVEGSQGLTQVEALDDGSVRFSCTLPHLIVGSVGNGKGLDFVEKNLTALGCK-EDREPGENARRLAACCAAIVWCGELS 329
Cdd:cd00643   305 QVVESSNCITTMELTADGDLYISVTMPSLEVGTVGGGTGLPTQRECLELLGCYgAGDEPGANARKLAEIVAATVLAGELS 384
                         330
                  ....*....|....*
gi 1080384939 330 LLAAQTNpGELMEAH 344
Cdd:cd00643   385 LLAALAA-GHLVRSH 398
HMG-CoA_red pfam00368
Hydroxymethylglutaryl-coenzyme A reductase; The HMG-CoA reductases catalyze the conversion of ...
11-344 1.09e-88

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: 270.86  E-value: 1.09e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  11 YAHVPLSWIGPVRISGnvmnDEVKIPLATYETPLWPSCGRGAKVSRMiEGGITCTFVGEKMTRSVIFTLDSAADAVIARD 90
Cdd:pfam00368  40 YVQLPLGVAGPLLING----KDYLVPMATTEGSLVASASRGAKAINA-SGGFTTTVLGDGMTRGPVFLFDSVADAAEAKE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  91 NILSR--YDELKKVVESSSRFAKLVDIHFQIASRLLFVRFDFFSGDASGHNMATLASERLMSYLMEQMPELGYGSISGNY 168
Cdd:pfam00368 115 WIENKenLLEIANAAEPTSRGGGLRDIEVVIAGRMVYLRFLVDTGDAMGANMVNTATEAAAPLIEEEFGGMVLLSILSNL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 169 CTDKKTSAVNGILGRGKYVIAEAVIPEPVVRERLRTTAKRLAELNERKNlVGSIMAGSLrSGNAHYANMLLGFYLATGQD 248
Cdd:pfam00368 195 CTDKKPSAINWIEGRGKSVVAEATIGEEVVKKILKASPEALVDPYRAKN-IGTHNKGII-GGNAHAANGIAAVFLATGQD 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 249 AANIVEGSQGLTQVEALDDGSVRFSCTLPHLIVGSVGNGKGLDFVEKNLTALGCKEDREPGEnarrlaacCAAI----VW 324
Cdd:pfam00368 273 PAAVEESSHAYAALETWEDGDLYGSVTLPSLEVGTVGGGTGLPPQAECLKLLGVKGAGKPRE--------LAEIiaavGL 344
                         330       340
                  ....*....|....*....|
gi 1080384939 325 CGELSLLAAQTNpGELMEAH 344
Cdd:pfam00368 345 AGELSALRALAA-GGIQKGH 363
HMG_CoA_R_NADP TIGR00533
3-hydroxy-3-methylglutaryl Coenzyme A reductase, hydroxymethylglutaryl-CoA reductase (NADP); ...
11-349 2.99e-77

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: 242.86  E-value: 2.99e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  11 YAHVPLSWIGPVRISGNVMNDEVKIPLATYETPLWPSCGRGAKVSRMiEGGITCTFVGEKMTRSVIFTLDSAADAVIARD 90
Cdd:TIGR00533  69 YMQIPLGVAGPLKIDGEYAKGEYYIPLATTEGALVASVNRGCSAITA-GGGATVRVTKDGMTRAPVVRTPSVVRAGACRI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  91 NILSRYDELKKVVESSSRFAKLVDIHFQ-IASRLLFVRFDFFSGDASGHNMATLASERLMSYLMEQMPELGYG--SISGN 167
Cdd:TIGR00533 148 WIDENQNAIKEAAESTTRHGKLQKIQPIcLAGDLLYPRFVTTTGDAMGMNMVTIATEYALKQMVEEYGWEGMEvvAVSGN 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 168 YCTDKKTSAVNGILGRGKYVIAEAVIPEPVVRERLRTTAKRLAELNERKNLVGSIMAGSLrSGNAHYANMLLGFYLATGQ 247
Cdd:TIGR00533 228 YCTDKKPAAINLIEGRGKSIVAEATIPGDVVNKVLKTTVSALVEVNIAKNLIGSAMAGSM-GFNAHYANIIGAIFLATGQ 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 248 DAANIVEGSQGLTQVEAlDDGSVRFSCTLPHLIVGSVGNGKGLDFVEKNLTALGCKEdrepGENARRLAACCAAIVWCGE 327
Cdd:TIGR00533 307 DEAHIVEGSLGITLAEE-VDGDLYFSVSLPDVPVGTVGGGTVLETQGECLDLLGVRG----GNNARQFAEIVGCAVLAGE 381
                         330       340
                  ....*....|....*....|..
gi 1080384939 328 LSLLAAQTnPGELMEAHVSIER 349
Cdd:TIGR00533 382 LSLCGALA-AGHLVQAHMELGR 402
2A060605 TIGR00920
3-hydroxy-3-methylglutaryl-coenzyme A reductase; [Transport and binding proteins, ...
11-351 5.13e-76

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: 250.93  E-value: 5.13e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  11 YAHVPLSWIGPVRISGnvmnDEVKIPLATYETPLWPSCGRGAKvSRMIEGGITCTFVGEKMTRSVIFTLDSAADAVIARD 90
Cdd:TIGR00920 530 YMPIPVGVAGPLLLDG----KEYQVPMATTEGCLVASTNRGCR-ALMLGGGVRSRVLADGMTRGPVVRLPSACRAAEAKA 604
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  91 NILS--RYDELKKVVESSSRFAKLVDIHFQIASRLLFVRFDFFSGDASGHNMATLASERLMSYLMEQMPELGYGSISGNY 168
Cdd:TIGR00920 605 WLEVpeNFAVIKDAFDSTSRFARLKKIHIAMAGRNLYIRFQAKTGDAMGMNMISKGTEQALAELQEHFPDMQILSLSGNY 684
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 169 CTDKKTSAVNGILGRGKYVIAEAVIPEPVVRERLRTTAKRLAELNERKNLVGSIMAGSLRSGNAHYANMLLGFYLATGQD 248
Cdd:TIGR00920 685 CTDKKPAAINWIEGRGKSVVCEATIPAKIVRSVLKTSAEALVDVNINKNLIGSAMAGSIGGFNAHAANIVTAIYIATGQD 764
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 249 AANIVEGSQGLTQVEAL--DDGSVRFSCTLPHLIVGSVGNGKGLDFVEKNLTALGCKEDRE--PGENARRLAACCAAIVW 324
Cdd:TIGR00920 765 AAQNVGSSNCMTLMEAWgpTGEDLYISCTMPSIEIGTVGGGTVLPPQSACLQMLGVRGANAtrPGENAKQLARIVCATVM 844
                         330       340
                  ....*....|....*....|....*..
gi 1080384939 325 CGELSLLAAQTNpGELMEAHVSIERAK 351
Cdd:TIGR00920 845 AGELSLMAALAA-GHLVKSHMRHNRSS 870
HMG1 COG1257
Hydroxymethylglutaryl-CoA reductase [Lipid transport and metabolism]; ...
12-290 2.21e-49

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: 170.32  E-value: 2.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  12 AHVPLSWIGPVRISGnvmnDEVKIPLATYETPLWPSCGRGAKVSRMiEGGITCTFVGEKMTRSVIFTldSAADAVIARDN 91
Cdd:COG1257    53 FQLPLGVAGNFLING----KDYLVPMATEEPSVVAAASRGAKLIRE-SGGFKTTVLGDGMIGQPQFV--DVGDARAAREW 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  92 ILSRYDELKKVVES-----SSRFAKLVDIH-FQIASRLLFVRFDFFSGDASGHNMATLASERLMSYLMEQMPELGYGSIS 165
Cdd:COG1257   126 ILENKEEILEAAESadpsmTKRGGGLRDIEvRVLLGNMVVLHLIVDTGDAMGANMVNTATEAVAPWIEELTGGEVLLRIL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 166 GNYCTdkktsavngilgrGKYVIAEAVIPEPVVRERLRTTAKRLAEL-NERKNLVGSIMAGSLrSGNAHYANMLLGFYLA 244
Cdd:COG1257   206 SNYAT-------------GKLVRAEVTIPVEVLGKVLKVSGEEVAEKiVLASNFAGADPYRAA-THNKGIMNGIDAVVIA 271
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1080384939 245 TGQDAANIVEGSQGLT----QVEAL-----DDGSVRFSCTLPhLIVGSVGNGKGL 290
Cdd:COG1257   272 TGNDWRAVEAGAHAYAardgRYESLttwkdEDGDLYGSITLP-LAVGTVGGGTGL 325
HMG-CoA_reductase cd00365
Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR); Hydroxymethylglutaryl-coenzyme A ...
11-333 2.18e-30

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: 118.93  E-value: 2.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  11 YAHVPLSWIGPVRISGNvmndEVKIPLATYETPLWPSCGRGAKVSRMiEGGITCTFVGEKMTRSVIFTLDSAADAVIARD 90
Cdd:cd00365    50 TFELPYAVASNFQIDGR----DVLVPLVTEEPSIVAAASYMAKLARA-GGGFTTSSSAPLMHAQVQIVLIQDPLNAKLSL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939  91 NiLSRYDELKKVVESSSRF-----AKLVDIHFQIASRLLFVRFDFFSGDASGHNMATLASERLMSYLMEQMPELGYGSIS 165
Cdd:cd00365   125 L-RSGKDEIIELANRKDQLlnslgGGCRDIEVHTFGPMLVAHLIVDVGDAMGANMINTMAEAVAPLMEAYTGGMQVRLRS 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 166 GNYCTdkktsavngilGRGKYVIAEAVIPEPVVRERL---RTTAKRLAELNERKNLVGSIMAGSLrsgNAHYANMLLGFY 242
Cdd:cd00365   204 LSNLT-----------GDGRLARAQARITPQQLETAEfsgEAVIEGILDAYAFKAAVDSYRAATH---NKGIMNGVDPLI 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080384939 243 LATGQDAANIVEGSQG--------LTQVEALDDGSVRFSCTLPhLIVGSVGNG-KGLDFVEKNLTALGCKEDREPGEnar 313
Cdd:cd00365   270 VACGQDWRAVEVGAHAyacrhygsLTTWEKDNNGHLVITLEMS-MPVGLVGGAtKTHPLAQASLRILGVKTAQALAR--- 345
                         330       340
                  ....*....|....*....|
gi 1080384939 314 rlaaCCAAIVWCGELSLLAA 333
Cdd:cd00365   346 ----IAVAVGLAQNLGAMRA 361
 
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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