NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Callus;
DOI=10.1007/BF00014450; PubMed=8204833 [NCBI, ExPASy, EBI, Israel, Japan]
Fushimi T., Umeda M., Shimazaki T., Kato A., Toriyama K., Uchimiya H.;
"Nucleotide sequence of a rice cDNA similar to a maize NADP-dependent malic enzyme.";
Plant Mol. Biol. 24:965-967(1994).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
DOI=10.1038/nature01184; PubMed=12447438 [NCBI, ExPASy, EBI, Israel, Japan]
Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y., Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H., Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M., Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S., Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H., Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S., Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y., Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S., Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
"The genome sequence and structure of rice chromosome 1.";
Nature 420:312-316(2002).

Comments

FUNCTION: The chloroplastic ME isoform decarboxylates malate shuttled from neighboring mesophyll cells. The CO(2) released is then refixed by ribulose-bisphosphate carboxylase. This pathway eliminates the photorespiratory loss of CO(2) that occurs in most plants.
CATALYTIC ACTIVITY: (S)-malate + NADP⁺ = pyruvate + CO₂ + NADPH.
COFACTOR: Divalent metal cations. Prefers magnesium or manganese (By similarity).
PATHWAY: Photosynthesis; C4 acid pathway .
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast.
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

D16499; BAA03949.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP002816; BAB03427.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP002836; BAB07934.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S46499; S46499.

NP_001042257.1; -.

3D structure databases

HSSP

P40927; 1GQ2. [HSSP ENTRY / PDB]

ModBase

P43279.

Organism-specific databases

Gramene

P43279; -.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0004473;	Molecular function: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) 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

P43279.

Genome annotation databases

GeneID

4326769; -.

KEGG

osa:4326769; -.

Other

UniRef

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

Keywords

Chloroplast; Metal-binding; NAD; NADP; Oxidoreductase; Plastid; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 49`	`49`	`Chloroplast (Potential).`
`CHAIN`	`50 639`	`590`	`NADP-dependent malic enzyme, chloroplastic.`	`PRO_0000018548`
`NP_BIND`	`383 399`	`17`	`NADP (By similarity).`
`ACT_SITE`	`187 187`		`Proton donor (By similarity).`
`ACT_SITE`	`258 258`		`Proton acceptor (By similarity).`
`METAL`	`330 330`		`Divalent metal cation (By similarity).`
`METAL`	`331 331`		`Divalent metal cation (By similarity).`
`METAL`	`354 354`		`Divalent metal cation (By similarity).`
`BINDING`	`240 240`		`NAD (By similarity).`
`BINDING`	`354 354`		`NAD (By similarity).`
`BINDING`	`495 495`		`NAD (By similarity).`
`SITE`	`354 354`	`1`	`Important for activity (By similarity).`
`CONFLICT`	`45 45`		`Missing (in Ref. 1; BAA03949).`
`CONFLICT`	`50 52`		`AAA -> TPV (in Ref. 1; BAA03949).`
`CONFLICT`	`494 494`		`S -> A (in Ref. 1; BAA03949).`
`CONFLICT`	`602 602`		`S -> T (in Ref. 1; BAA03949).`

Sequence information

Length: 639 AA [This is the length of the unprocessed precursor]

Molecular weight: 69866 Da [This is the MW of the unprocessed precursor]

CRC64: A12C763D31D8D25D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSARAAATA AAAAASPLWK RGEGGSSGSG SGCTSCREVR RRAAAVRVRA AAPRRVEAVA 

        70         80         90        100        110        120 
MESAAETEKK EEVAAAGGGV EDMATEEVPV TPWAFSVASG YTLLRDPHHN KGLAFSEKER 

       130        140        150        160        170        180 
DAHYLRGLLP PAVVSQDLQV KKIMHNLRQY SVPLQRYMAM MDLQERNERL FYKLLIDNVE 

       190        200        210        220        230        240 
ELLPVVYTPT VGEACQKYGS IFRQPQGLYV SLKDKGKVLD VLRNWPERNI QVIVVTDGER 

       250        260        270        280        290        300 
ILGLGDLGCQ GMGIPVGKLS LYTALGGVRP SACLPITIDV GTNNEQLLND EFYIGLRQRR 

       310        320        330        340        350        360 
ATGKEYHELM EEFMSAVKQI YGEKVLIQFE DFANHNAFDL LAKYSKSHLV FNDDIQGTAS 

       370        380        390        400        410        420 
VVLAGLLSSL KVVGGTLAEH TYLFLGAGEA GTGIAELIAL EISKQTKAPI EECRKKVWLL 

       430        440        450        460        470        480 
DSKGLIVNSR KESLQAFKKP WAHEHEPVTT LLDAVQSIKP TVLIGTSGVG KTFTKEVIEA 

       490        500        510        520        530        540 
MASFNERPVI FSLSNPTSHS ECTAEEAYNW SQGRAVFASG SPFDPVEYNG KIHVPGQSNN 

       550        560        570        580        590        600 
AYIFPGFGLG VVISGAVRVH EDMLLAASET LADQATQENF EKGSIFPPFT NIRKISARIA 

       610        620        630 
ASVAAKAYEL GLATRLPQPR DLEKYAESCM YTPVYRSYR

P43279 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