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P80037 (MDH_HELGE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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
OrganismHeliobacterium gestii
Taxonomic identifier2699 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesHeliobacteriaceaeHeliobacterium

Protein attributes

Sequence length30 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.

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 3 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 – ›30›30Malate dehydrogenase
PRO_0000113455

Regions

Nucleotide binding9 – 146NAD By similarity

Experimental info

Non-terminal residue301

Sequences

Sequence LengthMass (Da)Tools
P80037 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 958743720AACF319

FASTA302,910
        10         20         30 
MTKKITIIGA GNVGATAAXX AASKDLGDIV 

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References

[1]"Malate dehydrogenase from Chlorobium vibrioforme, Chlorobium tepidum, and Heliobacterium gestii: purification, characterization, and investigation of dinucleotide binding by dehydrogenases by use of empirical methods of protein sequence analysis."
Charnock C.B., Refseth U.H., Strevaag R.
J. Bacteriol. 174:1307-1313(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR016040. NAD(P)-bd_dom.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_HELGE
AccessionPrimary (citable) accession number: P80037
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: February 19, 2014
This is version 59 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