[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3041415 [NCBI, ExPASy, EBI, Israel, Japan] Walter M.H., Grima-Pettenati J., Grand C., Boudet A.M., Lamb C.J.; "Cinnamyl-alcohol dehydrogenase, a molecular marker specific for lignin synthesis: cDNA cloning and mRNA induction by fungal elicitor."; Proc. Natl. Acad. Sci. U.S.A. 85:5546-5550(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Processor; TISSUE=Leaf; PubMed=7925425 [NCBI, ExPASy, EBI, Israel, Japan] Walter M.H., Grima-Pettenati J., Feuillet C.; "Characterization of a bean (Phaseolus vulgaris L.) malic-enzyme gene."; Eur. J. Biochem. 224:999-1009(1994).
[3]	SIMILARITY TO MALIC ENZYMES. DOI=10.1007/BF00019173; PubMed=2103472 [NCBI, ExPASy, EBI, Israel, Japan] Walter M.H., Grima-Pettenati J., Grand C., Boudet A.M., Lamb C.J.; "Extensive sequence similarity of the bean CAD4 (cinnamyl-alcohol dehydrogenase) to a maize malic enzyme."; Plant Mol. Biol. 15:525-526(1990).

Comments

CATALYTIC ACTIVITY: (S)-malate + NADP⁺ = pyruvate + CO₂ + NADPH.
COFACTOR: Divalent metal cations. Prefers magnesium or manganese (By similarity).
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Potential).
INDUCTION: By fungal elicitor.
SIMILARITY: Belongs to the malic enzymes family.
CAUTION: Was originally (PubMed:3041415) thought to be a cinnamyl-alcohol dehydrogenase.

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

J03825; AAA19575.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X80051; CAA56354.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S48198; DEFBC.

3D structure databases

HSSP

P40927; 1GQ2. [HSSP ENTRY / PDB]

ModBase

P12628.

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.

Other

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

Keywords

Cytoplasm; Metal-binding; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 589`	`589`	`NADP-dependent malic enzyme.`	`PRO_0000160201`
`NP_BIND`	`333 349`	`17`	`NADP (By similarity).`
`ACT_SITE`	`137 137`		`Proton donor (By similarity).`
`ACT_SITE`	`208 208`		`Proton acceptor (By similarity).`
`METAL`	`280 280`		`Divalent metal cation (By similarity).`
`METAL`	`281 281`		`Divalent metal cation (By similarity).`
`METAL`	`304 304`		`Divalent metal cation (By similarity).`
`BINDING`	`190 190`		`NAD (By similarity).`
`BINDING`	`304 304`		`NAD (By similarity).`
`BINDING`	`445 445`		`NAD (By similarity).`
`SITE`	`304 304`	`1`	`Important for activity (By similarity).`
`CONFLICT`	`16 16`		`K -> N (in Ref. 2; CAA56354).`
`CONFLICT`	`130 130`		`A -> E (in Ref. 2; CAA56354).`
`CONFLICT`	`258 259`		`TF -> EL (in Ref. 2; CAA56354).`
`CONFLICT`	`350 350`		`V -> L (in Ref. 2; CAA56354).`
`CONFLICT`	`567 567`		`K -> P (in Ref. 2; CAA56354).`

Sequence information

Length: 589 AA [This is the length of the unprocessed precursor]

Molecular weight: 64932 Da [This is the MW of the unprocessed precursor]

CRC64: 9BFADDB2699BAC1E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSISLKENG GEVSVKKDYS NGGGVRDLYG EDSATEDHLI TPWTFSVASG CSLLRDPRYN 

        70         80         90        100        110        120 
KGLAFTEGER DAHYLRGLLP PSVFNQELQE KRLMHNLRQY EVPLHRYMAL MDLQERNERL 

       130        140        150        160        170        180 
FYKLLIDNVA ELLPVVYTPT VGEACQKYGS IFRRPQGLYI SLKEKGKILE VLKNWPEKSI 

       190        200        210        220        230        240 
QVIVVTDGER ILGLGDLGCQ GMGIPVGKLS LYTALGGVRP SSCLPVTIDV GTNNEKLLND 

       250        260        270        280        290        300 
EFYIGLRQRR ATGQEYATFL DEFMRAVKQN YGEKVLVQFE DFANHNAFDL LEKYSSSHLV 

       310        320        330        340        350        360 
FNDDIQGTAS VVLAGLLASL KLVGGTLADH TFLFLGAGEA GTGIAELIAV EVSKQTKAPV 

       370        380        390        400        410        420 
EETRKKIWLV DSKGLIVSSR LESLQQFKKP WAHEHEPVKG LLEAVKAIKP TVLIGSSGAG 

       430        440        450        460        470        480 
KTFTKEVVET MASLNEKPLI LALSNPTSQS ECTAEEAYTW SKGRAIFASG SPFDPVEYEG 

       490        500        510        520        530        540 
KLFVPGQANN AYIFPGFGLG LIMSGAIRVR DEMLLAASEA LAAQVSEENY DKGLIYPPFT 

       550        560        570        580 
NIRKISANIA AKVAAKAYDL GLASHLKRPK DLVKYAESCM YSPGYRSYR

P12628 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