NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. INRA 450;
TISSUE=Leaf;
DOI=10.1007/BF00260642; PubMed=1896015 [NCBI, ExPASy, EBI, Israel, Japan]
Luchetta P., Cretin C., Gadal P.;
"Organization and expression of the two homologous genes encoding the NADP-malate dehydrogenase in Sorghum vulgare leaves.";
Mol. Gen. Genet. 228:473-481(1991).

Comments

FUNCTION: The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells.
CATALYTIC ACTIVITY: (S)-malate + NADP⁺ = oxaloacetate + NADPH.
ENZYME REGULATION: Chloroplast NADP-MDH is activated upon illumination. In order to be enzymatically active, disulfides bridges on the protein must be reduced by thioredoxin which receives electrons from ferredoxin and the electron transport system of photosynthesis.
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast.
SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 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

X54404; CAA38270.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S55884; AAB19835.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S17781; S17781.
S20743; S20743.

3D structure databases

HSSP

P17606; 7MDH. [HSSP ENTRY / PDB]

SMR

P37229; 66-429.

ModBase

P37229.

Organism-specific databases

Gramene

P37229; -.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0046554;	Molecular function: malate dehydrogenase (NADP+) activity (inferred from electronic annotation from InterPro).
GO:0005975;	Biological process: carbohydrate metabolic process (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

IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
IPR001252; Malate_DHase_AS.
IPR011273; Malate_DHase_NADP-dep_pln.
IPR010945; Malate_DHase_SF1.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.110.10; lact_mal_DH; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR23382; MDH_SF1; 1.

Pfam

PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.

ProDom

PD003052; Mal_dehydrog; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01757; Malate-DH_plant; 1.
TIGR01759; MalateDH-SF1; 1.

PS00068; MDH; 1.

Other

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

Keywords

Chloroplast; NADP; Oxidoreductase; Plastid; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 40`	`40`	`Chloroplast (By similarity).`
`CHAIN`	`41 432`	`392`	`Malate dehydrogenase [NADP] 2, chloroplastic.`	`PRO_0000018648`
`NP_BIND`	`96 102`	`7`	`NADP (By similarity).`
`NP_BIND`	`214 216`	`3`	`NADP (By similarity).`
`ACT_SITE`	`272 272`		`Proton acceptor (By similarity).`
`BINDING`	`177 177`		`Substrate (By similarity).`
`BINDING`	`183 183`		`Substrate (By similarity).`
`BINDING`	`190 190`		`NADP (By similarity).`
`BINDING`	`197 197`		`NAD (By similarity).`
`BINDING`	`216 216`		`Substrate (By similarity).`
`BINDING`	`247 247`		`Substrate (By similarity).`
`SITE`	`67 67`	`1`	`Activation of NADP-MDH.`
`SITE`	`72 72`	`1`	`Activation of NADP-MDH.`
`DISULFID`	`67 72`		`In oxidized inactive NAD-MDH.`
`DISULFID`	`408 420`		`In oxidized inactive NAD-MDH (By similarity).`

Sequence information

Length: 432 AA [This is the length of the unprocessed precursor]

Molecular weight: 46640 Da [This is the MW of the unprocessed precursor]

CRC64: 94CAB78C824DB5AA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGLSTAYSPA GSGLVPAPLA RAARRRSVQV RRPRLATVRC SVVDAAKQVQ DGVATAVGGG 

        70         80         90        100        110        120 
AASGNECFGV FCNIYDLKAE DKTKSWKKLV TIAVSGAAGM ISNHLLFKLA SGEVFGQDQP 

       130        140        150        160        170        180 
IALKLLGSER SFQALEGVRM ELEDSLYPLL REVSIGIGPY EVFQDVDWAL LIGAKPRGPG 

       190        200        210        220        230        240 
MERAALLDIN GQIFADQGKA LNAVASRNVK VLVVGNPCNT NALICLKNTP NIPAKNFHAL 

       250        260        270        280        290        300 
TRLDENRAKC QIALKAGVFY DKVSNVTIWG NHSTTQVPDF LNAKIDGRPV KEIIQDTKWL 

       310        320        330        340        350        360 
EEEFTMTVQK RGGVLIQKWG RSSAASTAVS IVDAIKSLVT PTPEGEWFST GVYTTGNPYG 

       370        380        390        400        410        420 
IAEDIVFSMP CRSKGDGDYE LATDVSMDDF LWERIKKSEA ELLAEKKCVA HLTGEGDAFC 

       430 
DLPEDTMLPG EN

P37229 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