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P19978 (MDH_KIBAR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Malate dehydrogenase
EC=1.1.1.37
Gene names
Name:mdh
OrganismKibdelosporangium aridum
Taxonomic identifier2030 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Kibdelosporangium

Protein attributes

Sequence length20 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01517

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01517

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01517

Sequence similarities

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

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processtricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›20›20Malate dehydrogenase HAMAP-Rule MF_01517
PRO_0000113370

Regions

Nucleotide binding11 – 177NAD By similarity

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P19978 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 79587E6F58C00AC9

FASTA201,989
        10         20 
TRTPVNVTVT GAAGQIGYAL

« Hide

References

[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.

Cross-references

Sequence databases

PIRS04961.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01517. Malate_dehydrog_2.
PROSITEPS00068. MDH. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_KIBAR
AccessionPrimary (citable) accession number: P19978
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 3, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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