Reviewed, UniProtKB/Swiss-Prot P16243 (MAOC_MAIZE)

Names and origin

Protein names

Recommended name:
    NADP-dependent malic enzyme, chloroplastic
      Short name=NADP-ME
    EC=1.1.1.40

Gene names

Name:	MOD1
Synonyms:	ME1

Organism

Zea mays (Maize)

Taxonomic identifier

4577 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACCAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length	636 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The chloroplastic ME isoform decarboxylates malate shuttled from neighboring mesophyll cells. The CO2 released is then refixed by ribulose-bisphosphate carboxylase. This pathway eliminates the photorespiratory loss of CO2 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 structure	Homotetramer.
Subcellular location	Plastid › chloroplast.
Sequence similarities	Belongs to the malic enzymes family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Metal-binding NAD NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	malate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 62	62	Chloroplast Potential
	Chain	63 – 636	574	NADP-dependent malic enzyme, chloroplastic		PRO_0000018547
Regions
	Nucleotide binding	380 – 396	17	NADP By similarity
Sites
	Active site	184	1	Proton donor By similarity
	Active site	255	1	Proton acceptor By similarity
	Metal binding	327	1	Divalent metal cation By similarity
	Metal binding	328	1	Divalent metal cation By similarity
	Metal binding	351	1	Divalent metal cation By similarity
	Binding site	237	1	NAD By similarity
	Binding site	351	1	NAD By similarity
	Binding site	492	1	NAD By similarity
	Site	351	1	Important for activity By similarity
Experimental info
	Mutagenesis	237	1	R → L: Decreases Kcat 530-fold. Increases Km for NADP 36-fold and Km for malate 10-fold. Ref.2
	Mutagenesis	255	1	K → I: Increases Km for malate 10-fold, and Km for NADP 15-fold. Decreases Kcat 200-fold. Ref.3
	Mutagenesis	387	1	A → G: Decreases Kcat 48-fold. Increases Km for NADP 4-fold. Increases Km for malate 6-fold. Ref.2
	Mutagenesis	392	1	A → G: No effect on Kcat. Increases Km for NADP 3.5-fold. Increases Km for malate 2.5-fold. Ref.2
	Mutagenesis	435 – 436	2	KK → LL: No effect on Kcat and on Km for malate. Increases Km for NADP 9-fold.

Sequences

	Sequence		Length	Mass (Da)
	P16243-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: DF2D36FD4B2682EA	FASTA	636	69,824
	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

References

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05130 mRNA. Translation: AAA33487.1.
PIR	DEZMMX. A34482.
RefSeq	NP_001105313.1.
UniGene	Zm.15
3D structure databases
SMR	P16243. Positions 96-636.
ModBase	Search...
Genome annotation databases
GeneID	542233.
KEGG	zma:542233.
Organism-specific databases
Gramene	P16243.
MaizeGDB	13848.
Enzyme and pathway databases
BRENDA	1.1.1.40. 289.
Family and domain databases
InterPro	IPR015884. Malic_enzyme_CS. IPR012301. Malic_N. IPR012302. Malic_NAD_bd. IPR001891. Malic_OxRdtase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00390. malic. 1 hit. PF03949. Malic_M. 1 hit. [Graphical view]
PRINTS	PR00072. MALOXRDTASE.
PROSITE	PS00331. MALIC_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MAOC_MAIZE

Accession

Primary (citable) accession number: P16243

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	January 19, 2010
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)