NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=cv. Desiree;
TISSUE=Leaf;
PubMed=8106447 [NCBI, ExPASy, EBI, Israel, Japan]
Winning B.M., Bourguignon J., Leaver C.J.;
"Plant mitochondrial NAD+-dependent malic enzyme. cDNA cloning, deduced primary structure of the 59- and 62-kDa subunits, import, gene complexity and expression analysis.";
J. Biol. Chem. 269:4780-4786(1994).

Comments

CATALYTIC ACTIVITY: (S)-malate + NAD⁺ = pyruvate + CO₂ + NADH.
COFACTOR: Divalent metal cations. Prefers magnesium or manganese (By similarity).
SUBUNIT: Heterodimer of two related subunits.
SUBCELLULAR LOCATION: Mitochondrion matrix.
SIMILARITY: Belongs to the malic enzymes 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

Z23002; CAA80547.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A53318; A53318.

3D structure databases

HSSP

P27443; 1LLQ. [HSSP ENTRY / PDB]

ModBase

P37225.

Protein-protein interaction databases

IntAct

P37225; -.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004471;	Molecular function: malate dehydrogenase (decarboxylating) activity (inferred from electronic annotation from EC).
GO:0046872;	Molecular function: metal ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051287;	Molecular function: NAD binding (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).
QuickGo view.

Family and domain databases

InterPro

IPR015884; Malic_enzyme_CS.
IPR012301; Malic_N.
IPR012302; Malic_NAD_bd.
IPR001891; Malic_OxRdtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

Pfam

PF00390; malic; 1.
PF03949; Malic_M; 1.
Pfam graphical view of domain structure.

PRINTS

PR00072; MALOXRDTASE.

PROSITE

PS00331; MALIC_ENZYMES; 1.

ProtoNet

P37225.

Other

UniRef

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

Keywords

Direct protein sequencing; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 18`	`18`	`Mitochondrion.`
`CHAIN`	`19 601`	`583`	`NAD-dependent malic enzyme 59 kDa isoform, mitochondrial.`	`PRO_0000018544`
`ACT_SITE`	`129 129`		`Proton donor (By similarity).`
`ACT_SITE`	`200 200`		`Proton acceptor (By similarity).`
`METAL`	`271 271`		`Divalent metal cation (By similarity).`
`METAL`	`272 272`		`Divalent metal cation (By similarity).`
`METAL`	`295 295`		`Divalent metal cation (By similarity).`
`BINDING`	`182 182`		`NAD (By similarity).`
`BINDING`	`295 295`		`NAD (By similarity).`
`BINDING`	`444 444`		`NAD (By similarity).`
`SITE`	`295 295`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 601 AA [This is the length of the unprocessed precursor]

Molecular weight: 66272 Da [This is the MW of the unprocessed precursor]

CRC64: D6C2A128CC9E971C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MWRVARSAAS TFRRTRRLST AISAPCIVHK RGADILHDPW FNKDTGFPMT ERDRLGLRGL 

        70         80         90        100        110        120 
LPPRVISFEQ QYDRFMESFR SLEKNTEGQP DSVVSLAKWR ILNRLHDRNE TLYYRVLIDN 

       130        140        150        160        170        180 
IKDFAPIIYT PTVGLVCQNY SGLFRRPRGM YFSAKDKGEM MSMIFNWPST QVDMIVLTDG 

       190        200        210        220        230        240 
SRILGLGDLG VQGIGIPIGK LDMYVAAAGI NPQRVLPVML DVGTNNQKLL EDPLYLGLRQ 

       250        260        270        280        290        300 
PRLEGEEYLS IVDEFVEAVH ARWPKAVVQF EDFQAKWAFE TLDRYRKKFC MFNDDIQGTA 

       310        320        330        340        350        360 
GVALAGLLGT VRAQGRPLTD FANQKIVVVG AGSAGLGVLK MALQAVSRMT GPSADPHFFL 

       370        380        390        400        410        420 
LDKNGLITKD RKDIDPAALP FAKAHHEIEG LGLQEGAGLA EVVKKVKPHV LLGLSGVGGI 

       430        440        450        460        470        480 
FHEEVLRAMK ESDSVRPAIF AMSNPTNNAE CCPVDAFKLA GEDIVFASGS PFANVDLGNG 

       490        500        510        520        530        540 
KIGHVNQANN MYLFPGIGLG ALLSGARNIS DTMLEAAAEC LASYMSDDEI NRGILYPSID 

       550        560        570        580        590        600 
DIRDITAEVG AAVLRAAVAE DLAEGHGDVG VKELQHMSKE ETIEHVRQNM WYPVYGPLVH 


E

P37225 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