[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Leaf; DOI=10.1016/0014-5793(90)81063-T; PubMed=2226841 [NCBI, ExPASy, EBI, Israel, Japan] Boersch D., Westhoff P.; "Primary structure of NADP-dependent malic enzyme in the dicotyledonous C4 plant Flaveria trinervia."; FEBS Lett. 273:111-115(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 461-648. TISSUE=Leaf; DOI=10.1007/BF00040632; PubMed=1883995 [NCBI, ExPASy, EBI, Israel, Japan] Rajeevan M.S., Bassett C.L., Hughes D.W.; "Isolation and characterization of cDNA clones for NADP-malic enzyme from leaves of Flaveria: transcript abundance distinguishes C3, C3-C4 and C4 photosynthetic types."; Plant Mol. Biol. 17:371-383(1991).

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

X57142; CAA40421.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M59416; AAB19243.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S12893; S12893.

3D structure databases

HSSP

P40927; 1GQ2. [HSSP ENTRY / PDB]

ModBase

P22178.

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

P22178.

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 ?61`		`Chloroplast.`
`CHAIN`	`?62 648`		`NADP-dependent malic enzyme, chloroplastic.`	`PRO_0000018546`
`NP_BIND`	`392 408`	`17`	`NADP (By similarity).`
`ACT_SITE`	`195 195`		`Proton donor (By similarity).`
`ACT_SITE`	`266 266`		`Proton acceptor (By similarity).`
`METAL`	`339 339`		`Divalent metal cation (By similarity).`
`METAL`	`340 340`		`Divalent metal cation (By similarity).`
`METAL`	`363 363`		`Divalent metal cation (By similarity).`
`BINDING`	`248 248`		`NAD (By similarity).`
`BINDING`	`363 363`		`NAD (By similarity).`
`BINDING`	`504 504`		`NAD (By similarity).`
`SITE`	`363 363`	`1`	`Important for activity (By similarity).`
`CONFLICT`	`580 580`		`P -> L (in Ref. 2; AAB19243).`

Sequence information

Length: 648 AA [This is the length of the unprocessed precursor]

Molecular weight: 71470 Da [This is the MW of the unprocessed precursor]

CRC64: A03D8E8D704D8842 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MISLNSSFLE RSSVTGGSRT QSQSLRLSAR RPVVTSMLNS NSLPERNVSV SVDSAVRDVN 

        70         80         90        100        110        120 
APVAVEVDRS VGEKPFAAVG GGVEDMYGED TATEDHYITP WSVSVASGYS LLRDPHHNKG 

       130        140        150        160        170        180 
LAFTEKERDA HFLRGLLPPV VVNHDLQVKK MMHNIRQYQV PLQRYQAMMD LQQRNERLFY 

       190        200        210        220        230        240 
KLLIENVEEL LPIVYTPTVG EACQKYGSIF ENSQGLFISL KDKGRILEIL KNWPHKKIQV 

       250        260        270        280        290        300 
IVVTDGERIL GLGDLGCQGM GIPVGKLALY TALGGVRPSA CLPITIDVGT NNEKLLNDDE 

       310        320        330        340        350        360 
FYIGLKQKRA AGQEYAELMN EFMSAVKQNY GENLLIQFED FANHNAFDLL EKYRTTHLVF 

       370        380        390        400        410        420 
NDDIQGTASV VLGGLISALK LVGGSLADQK FLFLGAGEAG TGIAELIALE ISKQTNIPLE 

       430        440        450        460        470        480 
ESRKKVWLVD SKGLIVRSRL DSLQHFKKPW AHDHEPVNEF LDAIKTIRPT VLIGSSGTGQ 

       490        500        510        520        530        540 
TFTKEVVETM SSLNEKPIIL ALSNPTSQSE CTAEQAYTWS EGRAIFASGS PFKPVEYNGK 

       550        560        570        580        590        600 
LYVSGQANNA YIFPGFGLGL IISGAIRVHD DMLLAASEAP AEQVTQEHFD KGLIFPPFTS 

       610        620        630        640 
IRKISAHIAA KVAAKAYELG LASRLPQPEN LVAYAESCMY SPKYRIYR

P22178 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