SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P19980

- MDH_PHEIM

UniProt

P19980 - MDH_PHEIM

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Malate dehydrogenase
Gene
mdh
Organism
Phenylobacterium immobile
Status
Reviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

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 bindingi11 – 177NAD By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

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
OrganismiPhenylobacterium immobile
Taxonomic identifieri21 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaePhenylobacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›25›25Malate dehydrogenase
PRO_0000113385Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

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

Sequencei

Sequence statusi: Fragment.

P19980-1 [UniParc]FASTAAdd to Basket

« Hide

SKTPIRVAVT GAAGNIGYHL LFRIA                              25
Length:25
Mass (Da):2,626
Last modified:February 1, 1991 - v1
Checksum:iC8D81E008825845C
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei25 – 251

Sequence databases

PIRiS07574.

Cross-referencesi

Sequence databases

PIRi S07574.

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.
    Strain: E.

Entry informationi

Entry nameiMDH_PHEIM
AccessioniPrimary (citable) accession number: P19980
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: February 19, 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

Similar proteinsi