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Reviewed, UniProtKB/Swiss-Prot P80540 (MDH_ACIDE)

Last modified November 4, 2008. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Malate dehydrogenase
    EC=1.1.1.37
Gene names
Name: mdh
OrganismAcidovorax delafieldii
Taxonomic identifier47920 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length17 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
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 processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

tricarboxylic acid cycle

Inferred from electronic annotation. Source: HAMAP

   Molecular functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›17›17Malate dehydrogenase
PRO_0000113344

Regions

Nucleotide binding11 – 177NAD By similarity

Experimental info

Non-terminal residue171

Sequences

Sequence LengthMass (Da)Tools
P80540-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 110E8111A516909E

FASTA171,663
        10 
XKKPVRVAVT GAAGQIG 

« 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: 9190829] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: CCUG 12929.

Cross-references

3D structure databases

ModBaseSearch...

Family and domain databases

HAMAPMF_01517.
[Tree]
InterProIPR001252. Malate_DHase_AS.
[Graphical view]
PROSITEPS00068. MDH. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_ACIDE
AccessionPrimary (citable) accession number: P80540
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 4, 2008
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents