P19982 (MDH_STRAR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Malate dehydrogenase
EC=1.1.1.37

Gene names

Name:

mdh

Organism

Streptomyces atratus

Taxonomic identifier

1893 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	31 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01517
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule 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	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›31	›31	Malate dehydrogenase HAMAP-Rule MF_01517		PRO_0000113392
Regions
	Nucleotide binding	11 – 17	7	NAD By similarity
Experimental info
	Non-terminal residue	31	1

Sequences

	Sequence		Length	Mass (Da)
	P19982 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 2973FDBDA2ACCE3A	FASTA	31	3,155
	10 20 30 TRTPVNVTVT GAAGQIGYAL LFRIASGHLL G

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.

Cross-references

Sequence databases
PIR	S04960.
3D structure databases
ProteinModelPortal	P19982.
SMR	P19982. Positions 2-31.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_01517. Malate_dehydrog_2.
InterPro	IPR016040. NAD(P)-bd_dom. [Graphical view]
PROSITE	PS00068. MDH. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDH_STRAR

Accession

Primary (citable) accession number: P19982

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	April 3, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program