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Reviewed, UniProtKB/Swiss-Prot P19977 (MDH_ACTMI)

Last modified January 19, 2010. Version 47. 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
OrganismActinoplanes missouriensis
Taxonomic identifier1866 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeActinoplanes

Protein attributes

Sequence length22 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP MF_01517

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP MF_01517

Subunit structure

Homodimer By similarity. HAMAP MF_01517

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 – ›22›22Malate dehydrogenase HAMAP MF_01517
PRO_0000113345

Regions

Nucleotide binding9 – 157NAD By similarity

Experimental info

Non-terminal residue221

Sequences

Sequence LengthMass (Da)Tools
P19977-1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 9D64079BC962A76E

FASTA222,262
        10         20 
AEPNVTVTGA AGQIGYALLF RI 

« 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: 2775496] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRS04959.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.37. 1587.

Family and domain databases

HAMAPMF_01517. Malate_dehydrog_2.
[Tree]
PROSITEPS00068. MDH. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_ACTMI
AccessionPrimary (citable) accession number: P19977
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: January 19, 2010
This is version 47 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