[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0166-6851(93)90040-5; PubMed=8366891 [NCBI, ExPASy, EBI, Israel, Japan] Rodrigues J.J., Ferreira H.B., Zaha A.; "Molecular cloning and characterization of an Echinococcus granulosus cDNA encoding malate dehydrogenase."; Mol. Biochem. Parasitol. 60:157-160(1993).
[2]	SEQUENCE REVISION. Rodrigues J.J.; Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: (S)-malate + NAD⁺ = oxaloacetate + NADH.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
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

L08894; AAC28239.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T09228; T09228.

3D structure databases

HSSP

P11708; 4MDH. [HSSP ENTRY / PDB]

ModBase

Q04820.

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.

PS00068; MDH; 1.

Other

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

Keywords

Cytoplasm; NAD; Oxidoreductase; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 332`	`332`	`Malate dehydrogenase, cytoplasmic.`	`PRO_0000113408`
`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).`

Sequence information

Length: 332 AA [This is the length of the unprocessed precursor]

Molecular weight: 36651 Da [This is the MW of the unprocessed precursor]

CRC64: 0EACE29A26F565E2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPGPLRVLIT GAAGQIAYNL SNMVANGNLF GKDQQIILHL LDIPEAKTVL DGVVMELQDC 

        70         80         90        100        110        120 
AFTVLAGIVP THCLKEAFTD IDVALMVGAM PRKQGMERRD LLSSNVKIFK EQGEALDKYA 

       130        140        150        160        170        180 
KKTVKVLVVG NPANTNCLIM SKYAPSIPKE NFTALTRLDH NRAIYQVAAK AGVPNTCVKN 

       190        200        210        220        230        240 
VCIWGNHSNK QFPDLSHAVV TKDGKQHPAK ELINDEKWVK EVFIPCVQNR GAAVIGLRKL 

       250        260        270        280        290        300 
SRAASAAKAI VDQMRDWWFG TKEGEWVSMS VYSTGDHYGA PKDIYFSFPV TIKDGHYKVV 

       310        320        330 
DGLSMDEWSR SLFNLSADEL VDEREVALAS FK

Q04820 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