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P33163 (MDH_THEAL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 48. 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
OrganismThermoleophilum album
Taxonomic identifier29539 [NCBI]
Taxonomic lineageBacteriaActinobacteriaThermoleophiliaThermoleophilalesThermoleophilaceaeThermoleophilum

Protein attributes

Sequence length23 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.

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 – ›23›23Malate dehydrogenase
PRO_0000113397

Experimental info

Non-terminal residue231

Sequences

Sequence LengthMass (Da)Tools
P33163 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 9B48F8218EF4F125

FASTA232,544
        10         20 
MSILPLVHAM ANVRGDIEYL TEA 

« Hide

References

[1]"Characterization of the malate dehydrogenase from Thermoleophilum album NM."
Novotny J.F. Jr., Perry J.J.
Arch. Microbiol. 154:304-307(1990)
Cited for: PROTEIN SEQUENCE.
Strain: NM.

Cross-references

Sequence databases

PIRA60689.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameMDH_THEAL
AccessionPrimary (citable) accession number: P33163
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 48 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