Reviewed, UniProtKB/Swiss-Prot P19977 (MDH_ACTMI)

Names and origin

Protein names

Recommended name:
    Malate dehydrogenase
    EC=1.1.1.37

Gene names

Name:

mdh

Organism

Actinoplanes missouriensis

Taxonomic identifier

1866 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micromonosporineae › Micromonosporaceae › Actinoplanes

Protein attributes

Sequence length	22 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reversible oxidation of malate to oxaloacetate By similarity.
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP MF_01517
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Molecular function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›22	›22	Malate dehydrogenase HAMAP MF_01517		PRO_0000113345
Regions
	Nucleotide binding	9 – 15	7	NAD By similarity
Experimental info
	Non-terminal residue	22	1

Sequences

	Sequence		Length	Mass (Da)
	P19977-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 9D64079BC962A76E	FASTA	22	2,262
	10 20 AEPNVTVTGA AGQIGYALLF RI

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
PIR	S04959.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.37. 1587.
Family and domain databases
HAMAP	MF_01517. [Tree]
InterPro	IPR001236. Lactate/malate_DH. IPR001252. Malate_DH_AS. [Graphical view]
Pfam	PF00056. Ldh_1_N. 1 hit. [Graphical view]
PROSITE	PS00068. MDH. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDH_ACTMI

Accession

Primary (citable) accession number: P19977

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)