Reviewed, UniProtKB/Swiss-Prot Q7X3X5 (MDH_MORS2)

Names and origin

Protein names

Recommended name:
    Malate dehydrogenase
    EC=1.1.1.37

Gene names

Name:

mdh

Organism

Moritella sp. (strain 2D2)

Taxonomic identifier

215801 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Moritellaceae › Moritella

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reversible oxidation of malate to oxaloacetate. HAMAP MF_01516
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. Ref.1
Subunit structure	Homodimer By similarity. HAMAP MF_01516
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 1 family.
Biophysicochemical properties	pH dependence: Optimum pH is 9.5-10.0 for malate dehydrogenation, and 7.5-8.0 for oxaloacetate reduction. HAMAP MF_01516 Temperature dependence: Optimum temperature is 40 degrees Celsius.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: InterPro malate metabolic process Inferred from electronic annotation. Source: InterPro 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 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 – 312	312	Malate dehydrogenase HAMAP MF_01516		PRO_0000113315
Regions
	Nucleotide binding	7 – 13	7	NAD By similarity
	Nucleotide binding	117 – 119	3	NAD By similarity
Sites
	Active site	177	1	Proton acceptor By similarity
	Binding site	34	1	NAD By similarity
	Binding site	81	1	Substrate By similarity
	Binding site	87	1	Substrate By similarity
	Binding site	94	1	NAD By similarity
	Binding site	119	1	Substrate By similarity
	Binding site	153	1	Substrate By similarity
	Binding site	227	1	NAD By similarity
Experimental info
	Mutagenesis	229	1	H → Q: Decreases the thermal stability. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q7X3X5-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: DA8A42A7C8F5DB1B	FASTA	312	31,941
	10 20 30 40 50 60 MKVAVLGAAG GIGQALALLL KTQLPAGSEL SLYDIAPVTP GVAVDLSHIP TDVTITGFSG 70 80 90 100 110 120 IDPTAALVGA DVVLISAGVA RKPGMDRSDL FNINAGIIKN LASKCAEVCP TACIGIITNP 130 140 150 160 170 180 VNTTVPIAAE VLKQAGVYDK RKLFGITTLD VIRSETFVSA LKGISLADVA VPVIGGHSGA 190 200 210 220 230 240 TILPLLSQVK GVEFTAEEIA TLTTRIQNAG TEVVEAKAGG GSATLSMGHA AARFGLSLVR 250 260 270 280 290 300 ALQGEKGIVE CTYVDGGSEH ATFFAQPVLL GKNGVEEVLA YGDLSDFETN ARDAMLEELK 310 ANITLGEEFV AG

References

[1]

"Differences in malate dehydrogenases from the obligately piezophilic deep-sea bacterium Moritella sp. strain 2D2 and the psychrophilic bacterium Moritella sp. strain 5710." Saito R., Nakayama A. FEMS Microbiol. Lett. 233:165-172(2004) [PubMed: 15043884] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-229.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB097559 Genomic DNA. Translation: BAC77301.1.
3D structure databases
SMR	Q7X3X5. Positions 1-310.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.37. 276002.
Family and domain databases
HAMAP	MF_01516. Malate_dehydrog_1. [Tree]
InterPro	IPR001557. L-lactate/malate_DH. IPR001236. Lactate/malate_DH. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR001252. Malate_DH_AS. IPR010097. Malate_DH_NAD-dep_euk/g-bac. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR11540:SF1. MDH_euk_g_bac. 1 hit.
Pfam	PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view]
PIRSF	PIRSF000102. Lac_mal_DH. 1 hit.
TIGRFAMs	TIGR01772. MDH_euk_gproteo. 1 hit.
PROSITE	PS00068. MDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDH_MORS2

Accession

Primary (citable) accession number: Q7X3X5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 39 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)