[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. B73 Inbred; PubMed=2584183 [NCBI, ExPASy, EBI, Israel, Japan] Rothermel B.A., Nelson T.; "Primary structure of the maize NADP-dependent malic enzyme."; J. Biol. Chem. 264:19587-19592(1989).
[2]	MUTAGENESIS OF ARG-237; ALA-387 AND ALA-392. DOI=10.1074/jbc.M212530200; PubMed=12562758 [NCBI, ExPASy, EBI, Israel, Japan] Detarsio E., Wheeler M.C., Campos-Bermudez V.A., Andreo C.S., Drincovich M.F.; "Maize C4 NADP-malic enzyme. Expression in Escherichia coli and characterization of site-directed mutants at the putative nucleoside-binding sites."; J. Biol. Chem. 278:13757-13764(2003).
[3]	MUTAGENESIS OF LYS-255 AND 435-LYS-LYS-436, AND 3D-STRUCTURE MODELING. DOI=10.1042/BJ20040594; PubMed=15245332 [NCBI, ExPASy, EBI, Israel, Japan] Detarsio E., Andreo C.S., Drincovich M.F.; "Basic residues play key roles in catalysis and NADP(+)-specificity in maize (Zea mays L.) photosynthetic NADP(+)-dependent malic enzyme."; Biochem. J. 382:1025-1030(2004).

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.
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

J05130; AAA33487.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A34482; DEZMMX.

NP_001105313.1; -.

3D structure databases

HSSP

P40927; 1GQ2. [HSSP ENTRY / PDB]

ModBase

P16243.

Organism-specific databases

Gramene

P16243; -.

MaizeGDB

13848; -.

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

P16243.

Genome annotation databases

GeneID

542233; -.

Other

ProtoNet

P16243.

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 62`	`62`	`Chloroplast (Potential).`
`CHAIN`	`63 636`	`574`	`NADP-dependent malic enzyme, chloroplastic.`	`PRO_0000018547`
`NP_BIND`	`380 396`	`17`	`NADP (By similarity).`
`ACT_SITE`	`184 184`		`Proton donor (By similarity).`
`ACT_SITE`	`255 255`		`Proton acceptor (By similarity).`
`METAL`	`327 327`		`Divalent metal cation (By similarity).`
`METAL`	`328 328`		`Divalent metal cation (By similarity).`
`METAL`	`351 351`		`Divalent metal cation (By similarity).`
`BINDING`	`237 237`		`NAD (By similarity).`
`BINDING`	`351 351`		`NAD (By similarity).`
`BINDING`	`492 492`		`NAD (By similarity).`
`SITE`	`351 351`	`1`	`Important for activity (By similarity).`
`MUTAGEN`	`237 237`		`R->L: Decreases Kcat 530-fold. Increases Km for NADP 36-fold and Km for malate 10-fold.`
`MUTAGEN`	`255 255`		`K->I: Increases Km for malate 10-fold, and Km for NADP 15-fold. Decreases Kcat 200-fold.`
`MUTAGEN`	`387 387`		`A->G: Decreases Kcat 48-fold. Increases Km for NADP 4-fold. Increases Km for malate 6-fold.`
`MUTAGEN`	`392 392`		`A->G: No effect on Kcat. Increases Km for NADP 3.5-fold. Increases Km for malate 2.5-fold.`
`MUTAGEN`	`435 436`		`KK->LL: No effect on Kcat and on Km for malate. Increases Km for NADP 9-fold.`

Sequence information

Length: 636 AA [This is the length of the unprocessed precursor]

Molecular weight: 69824 Da [This is the MW of the unprocessed precursor]

CRC64: DF2D36FD4B2682EA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSTRTAAVA ASASPASPWK LGGRSEGGAS CDGCRTYRNT LRRRAAPAKV RALPPRRVDA 

        70         80         90        100        110        120 
VAMVSNAETE TEKEQEEAAA ASEELPVMPW ATSVASGYTL LRDPHHNKGL AFTEEERDGH 

       130        140        150        160        170        180 
YLRGLLPPAV LSQELQIKKF MNTLRQYQTP LQRYIAMMNL QETDERLFYK LLIDNVVELL 

       190        200        210        220        230        240 
PFVYTPTVGE ACQKYGSIFG RPQGLYVSLK DKGKVLEVLR NWPHRNIQVI CVTDGERILG 

       250        260        270        280        290        300 
LGDLGCQGMG IPVGKLALYT ALGGVDPSVC LPITIDVGTN NEFLLNDEFY IGLRQKRATG 

       310        320        330        340        350        360 
EEYDELIEEF MSAVKQFYGE KVLIQFEDFA NHNAFDLLEK YSKSHLVFND DIQGTASVVL 

       370        380        390        400        410        420 
AGLLAALKMV GGTLAEQTYL FLGAGEAGTG IAELIALEIS KQTNAPIEEC RKKVWLVDSK 

       430        440        450        460        470        480 
GLIVDSRKGS LQPFKKPWAH EHEPLKTLYD AVQSIKPTVL IGTSGVGRTF TKEIIEAMSS 

       490        500        510        520        530        540 
FNERPIIFSL SNPTSHSECT AEQAYTWSQG RSIFASGSPF APVEYEGKTF VPGQSNNAYI 

       550        560        570        580        590        600 
FPGLGLGLVI SGAVRVHEDM LLAASKALAD QATQDNFEKG SIFPPFTSIR KISAHIAAAV 

       610        620        630 
AGKAYELGLA TRLPPPSDLV KYAENCMYTP VYRNYR

P16243 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