Reviewed, UniProtKB/Swiss-Prot P00346 (MDHM_PIG)

Names and origin

Protein names

Recommended name:
    Malate dehydrogenase, mitochondrial
    EC=1.1.1.37

Gene names

Name:

MDH2

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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.

General annotation (Comments)

Catalytic activity	(S)-malate + NAD(+) = oxaloacetate + NADH.
Subunit structure	Homodimer. Ref.4
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 1 family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
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: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: InterPro 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

Transit peptide

1 – 24

24

Mitochondrion Ref.2

Chain

25 – 338

314

Malate dehydrogenase, mitochondrial

PRO_0000018630

Regions

Nucleotide binding

31 – 37

7

NAD By similarity

Nucleotide binding

140 – 142

3

NAD By similarity

Sites

Active site

200

1

Proton acceptor

Binding site

57

1

NAD By similarity

Binding site

104

1

Substrate

Binding site

110

1

Substrate

Binding site

117

1

NAD By similarity

Binding site

142

1

Substrate

Binding site

176

1

Substrate

Binding site

251

1

NAD By similarity

Amino acid modifications

Modified residue

56

1

Phosphotyrosine By similarity

Modified residue

157

1

N6-acetyllysine By similarity

Modified residue

239

1

N6-acetyllysine By similarity

Modified residue

314

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

120

1

I → M in AAA31071. Ref.3

Sequence conflict

126

1

A → V in AAA31071. Ref.3

Sequence conflict

150

1

I → M in AAA31071. Ref.3

Sequence conflict

304

1

G → R in AAA31071. Ref.3

Sequence conflict

337

1

M → T in AAA31071. Ref.3

Secondary structure

1

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338

Helix Strand Turn

Details...

Beta strand

26 – 31

6

Helix

37 – 45

9

Beta strand

51 – 60

10

Helix

61 – 68

8

Beta strand

71 – 74

4

Beta strand

76 – 82

7

Helix

83 – 85

3

Helix

86 – 90

5

Beta strand

94 – 98

5

Helix

110 – 113

4

Helix

114 – 131

18

Beta strand

135 – 139

5

Helix

144 – 157

14

Beta strand

165 – 168

4

Helix

171 – 184

14

Helix

189 – 191

3

Beta strand

196 – 198

3

Helix

202 – 204

3

Beta strand

205 – 207

3

Helix

209 – 211

3

Helix

220 – 241

22

Helix

249 – 267

19

Beta strand

273 – 279

7

Beta strand

282 – 295

14

Beta strand

298 – 302

5

Helix

310 – 334

25

Sequences

	Sequence		Length	Mass (Da)
	P00346-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: B0435E87383D0B1E	FASTA	338	35,596
	10 20 30 40 50 60 MLSALARPAG AALRRSFSTS XQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH 70 80 90 100 110 120 TPGVAADLSH IETRATVKGY LGPEQLPDCL KGCDVVVIPA GVPRKPGMTR DDLFNTNATI 130 140 150 160 170 180 VATLTAACAQ HCPDAMICII SNPVNSTIPI TAEVFKKHGV YNPNKIFGVT TLDIVRANAF 190 200 210 220 230 240 VAELKGLDPA RVSVPVIGGH AGKTIIPLIS QCTPKVDFPQ DQLSTLTGRI QEAGTEVVKA 250 260 270 280 290 300 KAGAGSATLS MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETDCPYFST PLLLGKKGIE 310 320 330 KNLGIGKISP FEEKMIAEAI PELKASIKKG EEFVKNMK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones." Winteroe A.K., Fredholm M., Davies W. Mamm. Genome 7:509-517(1996) [PubMed: 8672129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-40. Tissue: Small intestine.
[2]	"Amino acid sequence homology among the 2-hydroxy acid dehydrogenases: mitochondrial and cytoplasmic malate dehydrogenases form a homologous system with lactate dehydrogenase." Birktoft J.J., Fernley R.T., Bradshaw R.A., Banaszak L.J. Proc. Natl. Acad. Sci. U.S.A. 79:6166-6170(1982) [PubMed: 6959107] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-338.
[3]	"Cloning and sequence analysis of cDNAs encoding mammalian mitochondrial malate dehydrogenase." Joh T., Takeshima H., Tsuzuki T., Shimada K., Tanase S., Morino Y. Biochemistry 26:2515-2520(1987) [PubMed: 3038184] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-338.
[4]	"Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases." Gleason W.B., Fu Z., Birktoft J.J., Banaszak L.J. Biochemistry 33:2078-2088(1994) [PubMed: 8117664] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT. Tissue: Heart.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z81157 mRNA. Translation: CAB03545.1.
M16427 mRNA. Translation: AAA31071.1.

PIR

DEPGMM. A00355.

UniGene

Ssc.12417

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MLD	X-ray	1.83	A/B/C/D	25-338	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P00346. 1 interaction.

Phylogenomic databases

HOVERGEN

P00346.

Family and domain databases

InterPro

IPR001557. L-lactate/malate_DHase.
IPR001236. Lactate/malate_DHase.
IPR015955. Lactate_DHase/Glyco_Ohase_4_C.
IPR001252. Malate_DHase_AS.
IPR010097. Malate_DHase_NAD-dep_euk_g_bac.
IPR016040. NAD(P)-bd.
[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

BindingDB

P00346.

LinkHub

P00346.

Entry information

Entry name

MDHM_PIG

Accession

Primary (citable) accession number: P00346
Secondary accession number(s): Q95308

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1997
Last modified:	December 16, 2008
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)