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P80542

- MDH_BREDI

UniProt

P80542 - MDH_BREDI

Protein

Malate dehydrogenase

Gene

mdh

Organism
Brevundimonas diminuta (Pseudomonas diminuta)
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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi9 – 146NADBy 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
    OrganismiBrevundimonas diminuta (Pseudomonas diminuta)
    Taxonomic identifieri293 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeBrevundimonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›19›19Malate dehydrogenasePRO_0000113440Add
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LDH/MDH superfamily. MDH type 3 family.Curated

    Sequencei

    Sequence statusi: Fragment.

    P80542-1 [UniParc]FASTAAdd to Basket

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    AXAKIALIGA GMIGGTLAA                                     19
    Length:19
    Mass (Da):1,710
    Last modified:February 1, 1996 - v1
    Checksum:i3E643277AB542F23
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei19 – 191

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas species are the first reported MDHs in Proteobacteria which resemble lactate dehydrogenases in primary structure."
      Charnock C.
      J. Bacteriol. 179:4066-4070(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Strain: ATCC 11568 / DSM 7234 / JCM 2788 / NCIB 9393 / NCTC 8545.

    Entry informationi

    Entry nameiMDH_BREDI
    AccessioniPrimary (citable) accession number: P80542
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 45 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