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P13702

- MVAA_PSEMV

UniProt

P13702 - MVAA_PSEMV

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Protein

3-hydroxy-3-methylglutaryl-coenzyme A reductase

Gene
mvaA
Organism
Pseudomonas mevalonii
Status
Reviewed - 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.

Pathwayi

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 donor1 Publication

GO - Molecular functioni

  1. coenzyme binding Source: InterPro
  2. hydroxymethylglutaryl-CoA reductase (NADPH) activity Source: InterPro
  3. hydroxymethylglutaryl-CoA reductase activity Source: UniProtKB-EC

GO - Biological processi

  1. coenzyme A metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11829.
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.
Mutagenesisi83 – 831E → Q: Greatly reduced activity.
Mutagenesisi183 – 1831D → A or N: Reduced activity.
Mutagenesisi381 – 3811H → A, N, Q or K: Reduced activity.

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 – 123
Helixi15 – 2612
Helixi30 – 378
Helixi44 – 507
Beta strandi51 – 6515
Beta strandi77 – 804
Beta strandi82 – 854
Helixi86 – 9813
Turni99 – 1013
Beta strandi103 – 1075
Beta strandi111 – 12010
Helixi124 – 13310
Helixi135 – 14410
Helixi147 – 1515
Beta strandi155 – 16410
Beta strandi172 – 1809
Helixi187 – 20519
Beta strandi208 – 2147
Beta strandi221 – 2299
Helixi231 – 2344
Beta strandi237 – 2393
Helixi241 – 25717
Helixi259 – 27921
Helixi284 – 29512
Turni296 – 2983
Beta strandi304 – 3096
Beta strandi315 – 3228
Beta strandi327 – 3293
Turni330 – 3345
Helixi336 – 34510
Helixi350 – 37425
Helixi378 – 39316
Turni398 – 4003
Helixi405 – 4084
Turni409 – 4113
Helixi415 – 4206

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP13702.

Family & Domainsi

Sequence similaritiesi

Belongs to the HMG-CoA reductase family.

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

MSLDSRLPAF RNLSPAARLD HIGQLLGLSH DDVSLLANAG ALPMDIANGM    50
IENVIGTFEL PYAVASNFQI NGRDVLVPLV VEEPSIVAAA SYMAKLARAN 100
GGFTTSSSAP LMHAQVQIVG IQDPLNARLS LLRRKDEIIE LANRKDQLLN 150
SLGGGCRDIE VHTFADTPRG PMLVAHLIVD VRDAMGANTV NTMAEAVAPL 200
MEAITGGQVR LRILSNLADL RLARAQVRIT PQQLETAEFS GEAVIEGILD 250
AYAFAAVDPY RAATHNKGIM NGIDPLIVAT GNDWRAVEAG AHAYACRSGH 300
YGSLTTWEKD NNGHLVGTLE MPMPVGLVGG ATKTHPLAQL SLRILGVKTA 350
QALAEIAVAV GLAQNLGAMR ALATEGIQRG HMALHARNIA VVAGARGDEV 400
DWVARQLVEY HDVRADRAVA LLKQKRGQ 428
Length:428
Mass (Da):45,590
Last modified:January 1, 1990 - v1
Checksum:i3302701FE6E1B1F3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M24015 Genomic DNA. Translation: AAA25837.1.
M29727 Genomic DNA. No translation available.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M24015 Genomic DNA. Translation: AAA25837.1 .
M29727 Genomic DNA. No translation available.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QAX X-ray 2.80 A/B 1-428 [» ]
1QAY X-ray 2.80 A/B 1-428 [» ]
1R31 X-ray 2.10 A/B 1-428 [» ]
1R7I X-ray 2.21 A/B 1-428 [» ]
1T02 X-ray 2.60 A/B 1-428 [» ]
4I4B X-ray 1.70 A/B 1-428 [» ]
4I56 X-ray 1.50 A/B 1-428 [» ]
4I64 X-ray 1.75 A/B 1-428 [» ]
4I6A X-ray 1.85 A/B 1-428 [» ]
4I6W X-ray 1.66 A/B 1-428 [» ]
4I6Y X-ray 1.45 A/B 1-428 [» ]
ProteinModelPortali P13702.
SMRi P13702. Positions 4-428.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00257 ; UER00367 .
BioCyci MetaCyc:MONOMER-11829.
SABIO-RK P13702.

Miscellaneous databases

EvolutionaryTracei P13702.

Family and domain databases

Gene3Di 3.30.70.420. 1 hit.
3.90.770.10. 2 hits.
InterProi IPR002202. 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 ]
PANTHERi PTHR10572. PTHR10572. 1 hit.
Pfami PF00368. HMG-CoA_red. 1 hit.
[Graphical view ]
SUPFAMi SSF55035. SSF55035. 1 hit.
SSF56542. SSF56542. 2 hits.
TIGRFAMsi TIGR00532. HMG_CoA_R_NAD. 1 hit.
PROSITEi PS00066. 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 ]
ProtoNeti Search...

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: September 3, 2014
This is version 101 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

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