Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P13702 (MVAA_PSEMV) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-hydroxy-3-methylglutaryl-coenzyme A reductase

Short name=HMG-CoA reductase
EC=1.1.1.88
Gene names
Name:mvaA
OrganismPseudomonas mevalonii
Taxonomic identifier32044 [NCBI]
Taxonomic lineageBacteriaProteobacteria

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Metabolic intermediate metabolism; (R)-mevalonate degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1.

Subunit structure

Homotetramer.

Induction

Coinduction with mevalonate transport system.

Sequence similarities

Belongs to the HMG-CoA reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4284283-hydroxy-3-methylglutaryl-coenzyme A reductase
PRO_0000114467

Sites

Active site831Charge relay system
Active site2671Charge relay system
Active site2831Charge relay system
Active site3811Proton donor Ref.4

Experimental info

Mutagenesis521E → Q: No loss of activity.
Mutagenesis831E → Q: Greatly reduced activity.
Mutagenesis1831D → A or N: Reduced activity.
Mutagenesis3811H → A, N, Q or K: Reduced activity.

Secondary structure

................................................................... 428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13702 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 3302701FE6E1B1F3

FASTA42845,590
        10         20         30         40         50         60 
MSLDSRLPAF RNLSPAARLD HIGQLLGLSH DDVSLLANAG ALPMDIANGM IENVIGTFEL 

        70         80         90        100        110        120 
PYAVASNFQI NGRDVLVPLV VEEPSIVAAA SYMAKLARAN GGFTTSSSAP LMHAQVQIVG 

       130        140        150        160        170        180 
IQDPLNARLS LLRRKDEIIE LANRKDQLLN SLGGGCRDIE VHTFADTPRG PMLVAHLIVD 

       190        200        210        220        230        240 
VRDAMGANTV NTMAEAVAPL MEAITGGQVR LRILSNLADL RLARAQVRIT PQQLETAEFS 

       250        260        270        280        290        300 
GEAVIEGILD AYAFAAVDPY RAATHNKGIM NGIDPLIVAT GNDWRAVEAG AHAYACRSGH 

       310        320        330        340        350        360 
YGSLTTWEKD NNGHLVGTLE MPMPVGLVGG ATKTHPLAQL SLRILGVKTA QALAEIAVAV 

       370        380        390        400        410        420 
GLAQNLGAMR ALATEGIQRG HMALHARNIA VVAGARGDEV DWVARQLVEY HDVRADRAVA 


LLKQKRGQ 

« Hide

References

[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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24015 Genomic DNA. Translation: AAA25837.1.
M29727 Genomic DNA. No translation available.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP13702.
SMRP13702. Positions 4-428.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11829.
SABIO-RKP13702.
UniPathwayUPA00257; UER00367.

Family and domain databases

Gene3D3.30.70.420. 1 hit.
3.90.770.10. 2 hits.
InterProIPR002202. 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.
IPR009029. HMG_CoA_Rdtase_sub-bd.
[Graphical view]
PANTHERPTHR10572. PTHR10572. 1 hit.
PfamPF00368. HMG-CoA_red. 1 hit.
[Graphical view]
SUPFAMSSF55035. SSF55035. 1 hit.
SSF56542. SSF56542. 2 hits.
TIGRFAMsTIGR00532. HMG_CoA_R_NAD. 1 hit.
PROSITEPS00066. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP13702.

Entry information

Entry nameMVAA_PSEMV
AccessionPrimary (citable) accession number: P13702
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 13, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways