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Protein

3-hydroxy-3-methylglutaryl-coenzyme A reductase

Gene

mvaA

Organism
Pseudomonas mevalonii
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

P.mevalonii can use mevalonate as sole carbon source. With this enzyme mevalonate is deacetylated to HMG-CoA.

Catalytic activityi

(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH.

Pathway: (R)-mevalonate degradation

This protein is involved in step 1 of the subpathway that synthesizes (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate.
Proteins known to be involved in this subpathway in this organism are:
  1. 3-hydroxy-3-methylglutaryl-coenzyme A reductase (mvaA)
This subpathway is part of the pathway (R)-mevalonate degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate, the pathway (R)-mevalonate degradation and in Metabolic intermediate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei83 – 831Charge relay system
Active sitei267 – 2671Charge relay system
Active sitei283 – 2831Charge relay system
Active sitei381 – 3811Proton donorPROSITE-ProRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11829.
BRENDAi1.1.1.88. 5143.
SABIO-RKP13702.
UniPathwayiUPA00257; UER00367.

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxy-3-methylglutaryl-coenzyme A reductase (EC:1.1.1.88)
Short name:
HMG-CoA reductase
Gene namesi
Name:mvaA
OrganismiPseudomonas mevalonii
Taxonomic identifieri32044 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521E → Q: No loss of activity. 1 Publication
Mutagenesisi83 – 831E → Q: Greatly reduced activity. 1 Publication
Mutagenesisi183 – 1831D → A or N: Reduced activity. 1 Publication
Mutagenesisi381 – 3811H → A, N, Q or K: Reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4284283-hydroxy-3-methylglutaryl-coenzyme A reductasePRO_0000114467Add
BLAST

Expressioni

Inductioni

Coinduction with mevalonate transport system.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
428
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123Combined sources
Helixi15 – 2612Combined sources
Helixi30 – 378Combined sources
Helixi44 – 507Combined sources
Beta strandi51 – 6515Combined sources
Beta strandi77 – 804Combined sources
Beta strandi82 – 854Combined sources
Helixi86 – 9813Combined sources
Turni99 – 1013Combined sources
Beta strandi103 – 1075Combined sources
Beta strandi111 – 12010Combined sources
Helixi124 – 13310Combined sources
Helixi135 – 14410Combined sources
Helixi147 – 1515Combined sources
Beta strandi155 – 16410Combined sources
Beta strandi172 – 1809Combined sources
Helixi187 – 20519Combined sources
Beta strandi208 – 2147Combined sources
Beta strandi221 – 2299Combined sources
Helixi231 – 2344Combined sources
Beta strandi237 – 2393Combined sources
Helixi241 – 25717Combined sources
Helixi259 – 27921Combined sources
Helixi284 – 29512Combined sources
Turni296 – 2983Combined sources
Beta strandi304 – 3096Combined sources
Beta strandi315 – 3228Combined sources
Beta strandi327 – 3293Combined sources
Turni330 – 3345Combined sources
Helixi336 – 34510Combined sources
Helixi350 – 37425Combined sources
Helixi378 – 39316Combined sources
Turni398 – 4003Combined sources
Helixi405 – 4084Combined sources
Turni409 – 4113Combined sources
Helixi415 – 4206Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QAXX-ray2.80A/B1-428[»]
1QAYX-ray2.80A/B1-428[»]
1R31X-ray2.10A/B1-428[»]
1R7IX-ray2.21A/B1-428[»]
1T02X-ray2.60A/B1-428[»]
4I4BX-ray1.70A/B1-428[»]
4I56X-ray1.50A/B1-428[»]
4I64X-ray1.75A/B1-428[»]
4I6AX-ray1.85A/B1-428[»]
4I6WX-ray1.66A/B1-428[»]
4I6YX-ray1.45A/B1-428[»]
ProteinModelPortaliP13702.
SMRiP13702. Positions 4-428.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13702.

Family & Domainsi

Sequence similaritiesi

Belongs to the HMG-CoA reductase family.Curated

Family and domain databases

Gene3Di3.30.70.420. 1 hit.
3.90.770.10. 2 hits.
InterProiIPR002202. HMG_CoA_Rdtase.
IPR004553. HMG_CoA_Rdtase_bac-typ.
IPR023074. HMG_CoA_Rdtase_cat.
IPR023076. HMG_CoA_Rdtase_CS.
IPR009023. HMG_CoA_Rdtase_NAD(P)-bd_dom.
IPR009029. HMG_CoA_Rdtase_sub-bd_dom.
[Graphical view]
PANTHERiPTHR10572. PTHR10572. 1 hit.
PfamiPF00368. HMG-CoA_red. 1 hit.
[Graphical view]
SUPFAMiSSF55035. SSF55035. 1 hit.
SSF56542. SSF56542. 2 hits.
TIGRFAMsiTIGR00532. HMG_CoA_R_NAD. 1 hit.
PROSITEiPS00066. HMG_COA_REDUCTASE_1. 1 hit.
PS00318. HMG_COA_REDUCTASE_2. 1 hit.
PS01192. HMG_COA_REDUCTASE_3. 1 hit.
PS50065. HMG_COA_REDUCTASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13702-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLDSRLPAF RNLSPAARLD HIGQLLGLSH DDVSLLANAG ALPMDIANGM
60 70 80 90 100
IENVIGTFEL PYAVASNFQI NGRDVLVPLV VEEPSIVAAA SYMAKLARAN
110 120 130 140 150
GGFTTSSSAP LMHAQVQIVG IQDPLNARLS LLRRKDEIIE LANRKDQLLN
160 170 180 190 200
SLGGGCRDIE VHTFADTPRG PMLVAHLIVD VRDAMGANTV NTMAEAVAPL
210 220 230 240 250
MEAITGGQVR LRILSNLADL RLARAQVRIT PQQLETAEFS GEAVIEGILD
260 270 280 290 300
AYAFAAVDPY RAATHNKGIM NGIDPLIVAT GNDWRAVEAG AHAYACRSGH
310 320 330 340 350
YGSLTTWEKD NNGHLVGTLE MPMPVGLVGG ATKTHPLAQL SLRILGVKTA
360 370 380 390 400
QALAEIAVAV GLAQNLGAMR ALATEGIQRG HMALHARNIA VVAGARGDEV
410 420
DWVARQLVEY HDVRADRAVA LLKQKRGQ
Length:428
Mass (Da):45,590
Last modified:January 1, 1990 - v1
Checksum:i3302701FE6E1B1F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24015 Genomic DNA. Translation: AAA25837.1.
M29727 Genomic DNA. No translation available.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24015 Genomic DNA. Translation: AAA25837.1.
M29727 Genomic DNA. No translation available.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QAXX-ray2.80A/B1-428[»]
1QAYX-ray2.80A/B1-428[»]
1R31X-ray2.10A/B1-428[»]
1R7IX-ray2.21A/B1-428[»]
1T02X-ray2.60A/B1-428[»]
4I4BX-ray1.70A/B1-428[»]
4I56X-ray1.50A/B1-428[»]
4I64X-ray1.75A/B1-428[»]
4I6AX-ray1.85A/B1-428[»]
4I6WX-ray1.66A/B1-428[»]
4I6YX-ray1.45A/B1-428[»]
ProteinModelPortaliP13702.
SMRiP13702. Positions 4-428.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00257; UER00367.
BioCyciMetaCyc:MONOMER-11829.
BRENDAi1.1.1.88. 5143.
SABIO-RKP13702.

Miscellaneous databases

EvolutionaryTraceiP13702.

Family and domain databases

Gene3Di3.30.70.420. 1 hit.
3.90.770.10. 2 hits.
InterProiIPR002202. HMG_CoA_Rdtase.
IPR004553. HMG_CoA_Rdtase_bac-typ.
IPR023074. HMG_CoA_Rdtase_cat.
IPR023076. HMG_CoA_Rdtase_CS.
IPR009023. HMG_CoA_Rdtase_NAD(P)-bd_dom.
IPR009029. HMG_CoA_Rdtase_sub-bd_dom.
[Graphical view]
PANTHERiPTHR10572. PTHR10572. 1 hit.
PfamiPF00368. HMG-CoA_red. 1 hit.
[Graphical view]
SUPFAMiSSF55035. SSF55035. 1 hit.
SSF56542. SSF56542. 2 hits.
TIGRFAMsiTIGR00532. HMG_CoA_R_NAD. 1 hit.
PROSITEiPS00066. HMG_COA_REDUCTASE_1. 1 hit.
PS00318. HMG_COA_REDUCTASE_2. 1 hit.
PS01192. HMG_COA_REDUCTASE_3. 1 hit.
PS50065. HMG_COA_REDUCTASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase."
    Beach M.J., Rodwell V.W.
    J. Bacteriol. 171:2994-3001(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "(S)-3-hydroxy-3-methylglutaryl coenzyme A reductase, a product of the mva operon of Pseudomonas mevalonii, is regulated at the transcriptional level."
    Wang Y., Beach M.J., Rodwell V.W.
    J. Bacteriol. 171:5567-5571(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
  3. "Identification of the principal catalytically important acidic residue of 3-hydroxy-3-methylglutaryl coenzyme A reductase."
    Wang Y., Darnay B.G., Rodwell V.W.
    J. Biol. Chem. 265:21634-21641(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  4. "Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase."
    Darnay B.G., Wang Y., Rodwell V.W.
    J. Biol. Chem. 267:15064-15070(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE HIS-381.
  5. "Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase."
    Tabernero L., Bochar D.A., Rodwell V.W., Stauffacher C.V.
    Proc. Natl. Acad. Sci. U.S.A. 96:7167-7171(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiMVAA_PSEMV
AccessioniPrimary (citable) accession number: P13702
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 27, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.