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P13702

- MVAA_PSEMV

UniProt

P13702 - MVAA_PSEMV

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
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    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 PublicationPROSITE-ProRule annotation

    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

    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. 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 – 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.
    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

    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: October 1, 2014
    This is version 102 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