P48364 (MDH_MORS5) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Malate dehydrogenase
EC=1.1.1.37

Gene names

Name:

mdh

Organism

Moritella sp. (strain 5710)

Taxonomic identifier

246794 [NCBI]

Taxonomic lineage

cellular organisms › 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-Rule MF_01516
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. Ref.2
Subunit structure	Homodimer By similarity.
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-Rule MF_01516 Temperature dependence: Optimum temperature is 35 degrees Celsius.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro malate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Molecular_function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP 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 – 312	312	Malate dehydrogenase HAMAP-Rule MF_01516		PRO_0000113316
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	Q → H: Increases the thermal stability. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P48364 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 2C4A3253E5B5D2E6	FASTA	312	31,985
	10 20 30 40 50 60 MKVAVLGAAG GIGQALALLL KTQLPAGSDL SLYDIAPVTP GVAVDLSHIP TDVTIAGFAG 70 80 90 100 110 120 MDPTDALVGA DVVLISAGVA RKPGMDRSDL FNINAGIIKN LAGKCAEVCP NACIGIITNP 130 140 150 160 170 180 VNTTVPIAAE VLKQAGVYDK RKLFGITTLD VIRSETFVSA LKGISLADVE VPVIGGHSGV 190 200 210 220 230 240 TILPLLSQVK GVEFTAEEVV ALTARIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR 250 260 270 280 290 300 ALQGEKGIVE CTYVDGGSEH ATFFAQPVLL GKNGVEEVLA YGELSEFETN ARDAMLEELK 310 ANITLGEEFV AG

References

[1]	"Characterization of malate dehydrogenase from deep-sea psychrophilic Vibrio sp. strain no. 5710 and cloning of its gene." Ohkuma M., Ohtoko K., Takada N., Hamamoto T., Usami R., Kudo T., Horikoshi K. FEMS Microbiol. Lett. 137:247-252(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-229.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D78194 Genomic DNA. Translation: BAA11301.1.
3D structure databases
ProteinModelPortal	P48364.
SMR	P48364. Positions 1-310.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.40.50.720. 1 hit. 3.90.110.10. 1 hit.
HAMAP	MF_01516. Malate_dehydrog_1.
InterPro	IPR001557. L-lactate/malate_DH. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR001252. Malate_DH_AS. IPR010097. Malate_DH_type1. IPR023958. Malate_DH_type1_bac. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11540. PTHR11540. 1 hit.
Pfam	PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view]
PIRSF	PIRSF000102. Lac_mal_DH. 1 hit.
SUPFAM	SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMs	TIGR01772. MDH_euk_gproteo. 1 hit.
PROSITE	PS00068. MDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDH_MORS5

Accession

Primary (citable) accession number: P48364

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program