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P19980 (MDH_PHEIM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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
OrganismPhenylobacterium immobile
Taxonomic identifier21 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaePhenylobacterium

Protein attributes

Sequence length25 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 – ›25›25Malate dehydrogenase
PRO_0000113385

Regions

Nucleotide binding11 – 177NAD By similarity

Experimental info

Non-terminal residue251

Sequences

Sequence LengthMass (Da)Tools
P19980 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: C8D81E008825845C

FASTA252,626
        10         20 
SKTPIRVAVT GAAGNIGYHL LFRIA 

« 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.
Strain: E.

Cross-references

Sequence databases

PIRS07574.

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_PHEIM
AccessionPrimary (citable) accession number: P19980
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: February 19, 2014
This is version 60 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