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P80537 (MDH_BURCE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malate dehydrogenase

EC=1.1.1.37
Gene names
Name:mdh
OrganismBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifier292 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length21 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity.

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH.

Subunit structure

Homodimer By similarity.

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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›21›21Malate dehydrogenase
PRO_0000113352

Regions

Nucleotide binding11 – 177NAD By similarity

Experimental info

Non-terminal residue211

Sequences

Sequence LengthMass (Da)Tools
P80537 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9B8F1B1106197111

FASTA212,085
        10         20 
AKPAKRVAVT GAAGQIAYSL L 

« Hide

References

[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 25416 / DSM 7288 / JCM 5964 / NBRC 14074 / NCTC 10743.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameMDH_BURCE
AccessionPrimary (citable) accession number: P80537
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
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