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P19979

- MDH_MICGL

UniProt

P19979 - MDH_MICGL

Protein

Malate dehydrogenase

Gene

mdh

Organism
Microtetraspora glauca
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalyzes the reversible oxidation of malate to oxaloacetate.By similarity

    Catalytic activityi

    (S)-malate + NAD+ = oxaloacetate + NADH.PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi8 – 147NADBy similarity

    GO - Molecular functioni

    1. L-malate dehydrogenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase (EC:1.1.1.37)
    Gene namesi
    Name:mdh
    OrganismiMicrotetraspora glauca
    Taxonomic identifieri1996 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeStreptosporangiaceaeMicrotetraspora

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›20›20Malate dehydrogenasePRO_0000113377Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LDH/MDH superfamily. MDH type 2 family.Curated

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    P19979-1 [UniParc]FASTAAdd to Basket

    « Hide

    TVKVTVTGAA GQIGYALLFR                                    20
    Length:20
    Mass (Da):2,065
    Last modified:February 1, 1991 - v1
    Checksum:i740129BE59D01EBE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei20 – 201

    Sequence databases

    PIRiS04958.

    Cross-referencesi

    Sequence databases

    PIRi S04958.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification and N-terminal amino-acid sequences of bacterial malate dehydrogenases from six actinomycetales strains and from Phenylobacterium immobile, strain E."
      Rommel T.O., Hund H.-K., Speth A.R., Lingens F.
      Biol. Chem. Hoppe-Seyler 370:763-768(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiMDH_MICGL
    AccessioniPrimary (citable) accession number: P19979
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 60 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

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3