[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3805042 [NCBI, ExPASy, EBI, Israel, Japan] Bagchi S., Wise L.S., Brown M.L., Bregman D., Sul H.S., Rubin C.S.; "Structure and expression of murine malic enzyme mRNA. Differentiation-dependent accumulation of two forms of malic enzyme mRNA in 3T3-L1 cells."; J. Biol. Chem. 262:1558-1565(1987).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=3541755 [NCBI, ExPASy, EBI, Israel, Japan] Bagchi S., Wise L.S., Brown M.L., Sul H.S., Bregman D.B., Rubin C.S.; "Regulation and structure of murine malic enzyme mRNA."; Ann. N. Y. Acad. Sci. 478:77-92(1986).
[3]	PROTEIN SEQUENCE OF 428-445, AND MASS SPECTROMETRY. TISSUE=Hippocampus; Lubec G., Klug S.; Submitted (MAR-2007) to UniProtKB.

Comments

CATALYTIC ACTIVITY: (S)-malate + NADP⁺ = pyruvate + CO₂ + NADPH.
COFACTOR: Divalent metal cations. Prefers magnesium or manganese (By similarity).
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
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

J02652; AAA39727.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26756; AAA39489.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A26683; DEMSMX.

UniGene

Mm.148155

3D structure databases

HSSP

P40927; 1GQ2. [HSSP ENTRY / PDB]

2D gel databases

P06801; -.

P06801; -.

Organism-specific databases

MGI

MGI:97043; Me1.

Gene expression databases

ArrayExpress

P06801; -.

CleanEx

MM_ME1; -.

GermOnline

ENSMUSG00000032418; Mus musculus.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from sequence or structural similarity from UniProtKB).
GO:0005625;	Cellular component: soluble fraction (inferred from direct assay from MGI).
GO:0004473;	Molecular function: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) activity (inferred from sequence or structural similarity from UniProtKB).
GO:0030145;	Molecular function: manganese ion binding (inferred from sequence or structural similarity from UniProtKB).
GO:0006108;	Biological process: malate metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0009725;	Biological process: response to hormone stimulus (inferred from sequence or structural similarity from UniProtKB).
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.

BLOCKS

P06801.

Genome annotation databases

Ensembl

ENSMUSG00000032418; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

P06801; -.

HOVERGEN

P06801; -.

Other

Me1; Mus musculus.

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

Keywords

Cytoplasm; Direct protein sequencing; Metal-binding; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 572`	`572`	`NADP-dependent malic enzyme.`	`PRO_0000160193`
`NP_BIND`	`301 318`	`18`	`NADP (By similarity).`
`ACT_SITE`	`102 102`		`Proton donor (By similarity).`
`ACT_SITE`	`173 173`		`Proton acceptor (By similarity).`
`METAL`	`245 245`		`Divalent metal cation (By similarity).`
`METAL`	`246 246`		`Divalent metal cation (By similarity).`
`METAL`	`269 269`		`Divalent metal cation (By similarity).`
`BINDING`	`155 155`		`NADP (By similarity).`
`BINDING`	`269 269`		`NADP (By similarity).`
`SITE`	`269 269`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 572 AA [This is the length of the unprocessed precursor]

Molecular weight: 63999 Da [This is the MW of the unprocessed precursor]

CRC64: 86B1761D04C2B51E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEPRAPRRRH THQRGYLLTR DPHLNKDLAF TLEERQQLNI HGLLPPCIIS QELQVLRIIK 

        70         80         90        100        110        120 
NFERLNSDFD RYLLLMDLQD RNEKLFYSVL MSDVEKFMPI VYTPTVGLAC QQYSLAFRKP 

       130        140        150        160        170        180 
RGLFISIHDK GHIASVLNAW PEDVVKAIVV TDGERILGLG DLGCNGMGIP VGKLALYTAC 

       190        200        210        220        230        240 
GGVNPQQCLP ITLDVGTENE ELLKDPLYIG LRHRRVRGPE YDAFLDEFME AASSKYGMNC 

       250        260        270        280        290        300 
LIQFEDFANR NAFRLLNKYR NKYCTFNDDI QGTASVAVAG LLAALRITKN KLSDQTVLFQ 

       310        320        330        340        350        360 
GAGEAALGIA HLVVMAMEKE GLSKENARKK IWLVDSKGLI VKGRASLTEE KEVFAHEHEE 

       370        380        390        400        410        420 
MKNLEAIVQK IKPTALIGVA AIGGAFTEQI LKDMAAFNER PIIFALSSPT SKAECSADEC 

       430        440        450        460        470        480 
YKVTKGRAIF ASGSPFDPVT LPDGRTLFPG QGNNSYVFPG VALGVVACGL RHIDDKVFLT 

       490        500        510        520        530        540 
TREVISQQVS DKHLQEGRLY PPLNTIRGVS LKIAVKIVQD AYKEKMATVY PEPQNKEEFV 

       550        560        570 
SSQMYSTNYD QILPDCYPWP AEVQKIQTKV NQ

P06801 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