Reviewed, UniProtKB/Swiss-Prot P11708 (MDHC_PIG)

Names and origin

Protein names

Recommended name:
    Malate dehydrogenase, cytoplasmic
    EC=1.1.1.37
Alternative name(s):
    Cytosolic malate dehydrogenase

Gene names

Name:

MDH1

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	334 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.5
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
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	cytosol Ref.2 Inferred from direct assay. Source: MGI
Molecular function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: EC 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

Initiator methionine

1

1

Removed

Chain

2 – 334

333

Malate dehydrogenase, cytoplasmic

PRO_0000113411

Regions

Nucleotide binding

11 – 17

7

NAD

Nucleotide binding

129 – 131

3

NAD

Sites

Active site

187

1

Proton acceptor

Binding site

92

1

Substrate

Binding site

98

1

Substrate

Binding site

105

1

NAD

Binding site

112

1

NAD

Binding site

131

1

Substrate

Binding site

162

1

Substrate

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.3

Modified residue

210

1

Phosphotyrosine By similarity

Experimental info

Sequence conflict

238

1

R → Q in AAA31072. Ref.2

Secondary structure

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334

Helix Strand Turn

Details...

Beta strand

5 – 11

7

Helix

15 – 18

4

Helix

21 – 25

5

Turn

26 – 30

5

Beta strand

36 – 41

6

Helix

44 – 46

3

Helix

47 – 59

13

Beta strand

65 – 72

8

Helix

74 – 77

4

Turn

78 – 80

3

Beta strand

82 – 86

5

Turn

98 – 101

4

Helix

102 – 119

18

Beta strand

125 – 128

4

Beta strand

130 – 132

3

Helix

133 – 142

10

Helix

149 – 151

3

Beta strand

152 – 154

3

Helix

157 – 171

15

Helix

175 – 177

3

Beta strand

182 – 185

4

Beta strand

192 – 194

3

Beta strand

199 – 201

3

Beta strand

206 – 208

3

Helix

209 – 213

5

Helix

216 – 220

5

Helix

222 – 238

17

Helix

244 – 259

16

Beta strand

267 – 272

6

Beta strand

277 – 279

3

Beta strand

285 – 293

9

Beta strand

296 – 299

4

Helix

307 – 333

27

Sequences

	Sequence		Length	Mass (Da)
	P11708-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 2574A8F3C2DD2C84	FASTA	334	36,454
	10 20 30 40 50 60 MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC 70 80 90 100 110 120 ALPLLKDVIA TDKEEIAFKD LDVAILVGSM PRRDGMERKD LLKANVKIFK CQGAALDKYA 130 140 150 160 170 180 KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKAQIALK LGVTSDDVKN 190 200 210 220 230 240 VIIWGNHSST QYPDVNHAKV KLQAKEVGVY EAVKDDSWLK GEFITTVQQR GAAVIKARKL 250 260 270 280 290 300 SSAMSAAKAI CDHVRDIWFG TPEGEFVSMG IISDGNSYGV PDDLLYSFPV TIKDKTWKIV 310 320 330 EGLPINDFSR EKMDLTAKEL AEEKETAFEF LSSA

References

[1]	"Cloning, sequencing and functional expression of a DNA encoding pig cytosolic malate dehydrogenase: purification and characterization of the recombinant enzyme." Trejo F., Costa M., Gelpi J.L., Busquets M., Clarke A.R., Holbrook J.J., Cortes A. Gene 172:303-308(1996) [PubMed: 8682322] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	"Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase." Joh T., Takeshima H., Tsuzuki T., Setoyama C., Shimada K., Tanase S., Kuramitsu S., Kagamiyama H., Morino Y. J. Biol. Chem. 262:15127-15131(1987) [PubMed: 3312200] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-334.
[3]	"Structure of porcine heart cytoplasmic malate dehydrogenase: combining X-ray diffraction and chemical sequence data in structural studies." Birktoft J.J., Bradshaw R.A., Banaszak L.J. Biochemistry 26:2722-2734(1987) [PubMed: 3606987] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), PARTIAL PROTEIN SEQUENCE.
[4]	"Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution." Birktoft J.J., Rhodes G., Banaszak L.J. Biochemistry 28:6065-6081(1989) [PubMed: 2775751] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]	"Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD." Chapman A.D., Cortes A., Dafforn T.R., Clarke A.R., Brady R.L. J. Mol. Biol. 285:703-712(1999) [PubMed: 10075524] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBLGenBankDDBJ

U44846 mRNA. Translation: AAC48610.1.
M29463 mRNA. Translation: AAA31072.1.

PIR

A32472. JC4876.

RefSeq

NP_999039.1.

UniGene

Ssc.11103

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4MDH	X-ray	2.50	A/B	2-334	[»]
5MDH	X-ray	2.40	A/B	2-334	[»]

ModBase

Search...

Genome annotation databases

GeneID

396894.

KEGG

ssc:396894.

Phylogenomic databases

HOVERGEN

P11708.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13033.

BRENDA

1.1.1.37. 249.

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.
IPR011274. Malate_DH_NAD-dep_euk.
IPR010945. Malate_DH_SF1.
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

PTHR23382. MDH_SF1. 1 hit.

Pfam

PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000102. Lac_mal_DH. 1 hit.

ProDom

PD003052. Mal_dehydrog. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01759. MalateDH-SF1. 1 hit.
TIGR01758. MDH_euk_cyt. 1 hit.

PROSITE

PS00068. MDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

BindingDB

P11708.

Entry information

Entry name

MDHC_PIG

Accession

Primary (citable) accession number: P11708
Secondary accession number(s): Q29560

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 98 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)