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.

P19983

- MDH_STRRS

UniProt

P19983 - MDH_STRRS

(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
Streptosporangium roseum
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
OrganismiStreptosporangium roseum
Taxonomic identifieri2001 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeStreptosporangiaceaeStreptosporangium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›24›24Malate dehydrogenasePRO_0000113395Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0039.

Family and domain databases

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

Sequencei

Sequence statusi: Fragment.

P19983-1 [UniParc]FASTAAdd to Basket

« Hide

AQTPVKVTVT GAAGQIGYAL LFRI                               24
Length:24
Mass (Da):2,475
Last modified:February 1, 1991 - v1
Checksum:iD8350129B9587C19
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei24 – 241

Sequence databases

PIRiS04956.

Cross-referencesi

Sequence databases

PIRi S04956.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0039.

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_STRRS
AccessioniPrimary (citable) accession number: P19983
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: February 19, 2014
This is version 63 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