Malate dehydrogenase, mitochondrial precursor

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Names and origin

Protein names

Recommended name:
Malate dehydrogenase, mitochondrial
EC=1.1.1.37

Gene names

Name:

MDH2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	(S)-malate + NAD⁺ = oxaloacetate + NADH.
Subunit structure	Homodimer. Ref.7
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 1 family.

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Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: InterPro malate metabolic process Inferred from direct assay. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from Experiment. Source: Reactome
Molecular function	L-malate dehydrogenase activity Inferred from direct assay. Source: UniProtKB binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 24

24

Mitochondrion By similarity

Chain

25 – 338

314

Malate dehydrogenase, mitochondrial

PRO_0000018628

Regions

Nucleotide binding

31 – 37

7

NAD

Nucleotide binding

140 – 142

3

NAD

Sites

Active site

200

1

Proton acceptor By similarity

Binding site

57

1

NAD

Binding site

104

1

Substrate

Binding site

110

1

Substrate

Binding site

117

1

NAD

Binding site

142

1

Substrate

Binding site

176

1

Substrate

Binding site

251

1

NAD

Amino acid modifications

Modified residue

56

1

Phosphotyrosine Ref.5

Modified residue

157

1

N6-acetyllysine By similarity

Modified residue

239

1

N6-acetyllysine By similarity

Modified residue

314

1

N6-acetyllysine By similarity

Natural variations

Natural variant

9

1

A → V: dbSNP rs17849553. Ref.1 Ref.4

VAR_047787

Secondary structure

1

.

338

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P40926-1 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: AAB9F5E5B2FBC8CA
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FASTA

338

35,503

        10         20         30         40         50         60 
MLSALARPAS AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH 

        70         80         90        100        110        120 
TPGVAADLSH IETKAAVKGY LGPEQLPDCL KGCDVVVIPA GVPRKPGMTR DDLFNTNATI 

       130        140        150        160        170        180 
VATLTAACAQ HCPEAMICVI ANPVNSTIPI TAEVFKKHGV YNPNKIFGVT TLDIVRANTF 

       190        200        210        220        230        240 
VAELKGLDPA RVNVPVIGGH AGKTIIPLIS QCTPKVDFPQ DQLTALTGRI QEAGTEVVKA 

       250        260        270        280        290        300 
KAGAGSATLS MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETECTYFST PLLLGKKGIE 

       310        320        330 
KNLGIGKVSS FEEKMISDAI PELKASIKKG EDFVKTLK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human homolog of mouse and pig MDH mRNA." Hu G. Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-9.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney and Tongue.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-9. Tissue: Lung.
[5]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-56, MASS SPECTROMETRY.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"Crystal structure of human malate dehydrogenase type 2." Structural genomics consortium (SGC) Submitted (MAR-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 20-338 IN COMPLEX WITH NAD AND SUBSTRATE, SUBUNIT.
+	Additional computationally mapped references.

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Web resources

Wikipedia

Malate dehydrogenase entry

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Cross-references

Sequence databases

AF047470 mRNA. Translation: AAC03787.1.
AK290779 mRNA. Translation: BAF83468.1.
AK316587 mRNA. Translation: BAG38175.1.
CH471220 Genomic DNA. Translation: EAW71796.1.
BC001917 mRNA. Translation: AAH01917.1.

IPI

IPI00291006.

RefSeq

NP_005909.2.

UniGene

Hs.520967

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DFD	X-ray	1.90	A/B/C/D	20-338	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P40926. 3 interactions.

PTM databases

PhosphoSite

P40926.

2-D gel databases

DOSAC-COBS-2DPAGE

P40926.

REPRODUCTION-2DPAGE

IPI00291006.
P40926.

Proteomic databases

PRIDE

P40926.

Genome annotation databases

Ensembl

ENSG00000146701. Homo sapiens. [Contig view]

GeneID

4191.

KEGG

hsa:4191.

Organism-specific databases

GeneCards

GC07P075515.

H-InvDB

HIX0006786.

HGNC

HGNC:6971. MDH2.

MIM

154100. gene.

PharmGKB

PA30716.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P40926.

HOVERGEN

P40926.

OMA

P40926. VRSEETE.

Enzyme and pathway databases

BRENDA

1.1.1.37. 247.

Reactome

REACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpress

P40926.

Bgee

P40926.

CleanEx

HS_MDH2.

Family and domain databases

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...

Other Resources

DrugBank

DB00157. NADH.

NextBio

16514.

SOURCE

Search...

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Entry information

Entry name

MDHM_HUMAN

Accession

Primary (citable) accession number: P40926
Secondary accession number(s): A8K414, B2RE78, O43682

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	November 25, 2008
Last modified:	June 16, 2009
This is version 99 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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