[1]	NUCLEOTIDE SEQUENCE [MRNA]. Achenbach P., Steinbrenner H., Reindl G., Seissler J.; "Cloning of rat cytosolic malate dehydrogenase."; Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Pituitary; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PROTEIN SEQUENCE OF 7-32; 80-92; 126-157; 171-199; 206-230; 239-255; 299-310 AND 319-334, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord; Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.; Submitted (JUL-2007) to UniProtKB.
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 251-284. Earley S.; "Partial sequence of rat malate dehydrogenase (MDH) mRNA."; Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: (S)-malate + NAD⁺ = oxaloacetate + NADH.
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF093773; AAC64180.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC059124; AAH59124.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF075574; AAC26799.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_150238.1; -.

UniGene

Rn.13492

3D structure databases

HSSP

P11708; 4MDH. [HSSP ENTRY / PDB]

SMR

O88989; 1-333, 2-334.

ModBase

O88989.

PTM databases

PhosphoSite

O88989; -.

Organism-specific databases

RGD

3072; Mdh1.

Gene expression databases

ArrayExpress

O88989; -.

GermOnline

ENSRNOG00000008103; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0030060;	Molecular function: L-malate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from InterPro).
GO:0006108;	Biological process: malate metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.
IPR011274; Malate_DHase_NAD-dep_euk.
IPR010945; Malate_DHase_SF1.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.110.10; lact_mal_DH; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR23382; MDH_SF1; 1.

Pfam

PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000102; Lac_mal_DH; 1.

ProDom

PD003052; Mal_dehydrog; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

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

PROSITE

PS00068; MDH; 1.

Proteomics databases

PRIDE

O88989; -.

Genome annotation databases

Ensembl

ENSRNOG00000008103; Rattus norvegicus. [Contig view]

GeneID

24551; -.

KEGG

rno:24551; -.

NMPDR

fig|10116.3.peg.10844; -.

Phylogenomic databases

HOVERGEN

O88989; -.

Other

603654; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 334`	`333`	`Malate dehydrogenase, cytoplasmic.`	`PRO_0000226737`
`NP_BIND`	`11 17`	`7`	`NAD (By similarity).`
`NP_BIND`	`129 131`	`3`	`NAD (By similarity).`
`ACT_SITE`	`187 187`		`Proton acceptor (By similarity).`
`BINDING`	`92 92`		`Substrate (By similarity).`
`BINDING`	`98 98`		`Substrate (By similarity).`
`BINDING`	`105 105`		`NAD (By similarity).`
`BINDING`	`112 112`		`NAD (By similarity).`
`BINDING`	`131 131`		`Substrate (By similarity).`
`BINDING`	`162 162`		`Substrate (By similarity).`
`MOD_RES`	`2 2`		`N-acetylserine (By similarity).`
`MOD_RES`	`210 210`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`251 251`		`S -> A (in Ref. 4; AAC26799).`
`CONFLICT`	`276 276`		`N -> D (in Ref. 2; AAH59124).`

Sequence information

Length: 334 AA [This is the length of the unprocessed precursor]

Molecular weight: 36483 Da [This is the MW of the unprocessed precursor]

CRC64: 8F6778722A607B3C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC 

        70         80         90        100        110        120 
ALPLLQDVIA TDKEEVAFKD LDVAVLVGSM PRREGMERKD LLKANVKIFK SQGAALEKYA 

       130        140        150        160        170        180 
KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKSQIALK LGVTADDVKN 

       190        200        210        220        230        240 
VIIWGNHSST QYPDVNHAKV KLQGKEVGVY EALKDDSWLK GEFITTVQQR GAAVIKARKL 

       250        260        270        280        290        300 
SSAMSAAKAI SDHIRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV 

       310        320        330 
EGLPINDFSR EKMDLTAKEL TEEKETAFEF LSSA

O88989 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools