[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. INRA 450; TISSUE=Leaf; DOI=10.1016/0378-1119(90)90003-A; PubMed=2373367 [NCBI, ExPASy, EBI, Israel, Japan] Luchetta P., Cretin C., Gadal P.; "Structure and characterization of the Sorghum vulgare gene encoding NADP-malate dehydrogenase."; Gene 89:171-177(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Tamaran FNK 140; TISSUE=Leaf; PubMed=2209586 [NCBI, ExPASy, EBI, Israel, Japan] Cretin C., Luchetta P., Joly C., Decottignies P., Lepiniec L., Gadal P., Sallantin M., Huet J.-C., Pernollet J.-C.; "Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA sequence. Homology with malate dehydrogenase (NAD)."; Eur. J. Biochem. 192:299-303(1990).
[3]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND SUBUNIT. DOI=10.1021/bi982876c; PubMed=10194350 [NCBI, ExPASy, EBI, Israel, Japan] Johansson K., Ramaswamy S., Saarinen M., Lemaire-Chamley M., Issakidis-Bourguet E., Miginiac-Maslow M., Eklund H.; "Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form."; Biochemistry 38:4319-4326(1999).

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.
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

M31965; AAA34047.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X53453; CAA37531.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JH0151; JH0151.
S13588; S13588.

3D structure databases

PDB

7MDH; X-ray; 2.40 A; A/B/C/D=55-429.

[ExPASy / RCSB / EBI]

PDBsum

7MDH; -.

ModBase

P17606.

Organism-specific databases

Gramene

P17606; -.

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

3D-structure; Chloroplast; NADP; Oxidoreductase; Plastid; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 40`	`40`	`Chloroplast (By similarity).`
`CHAIN`	`41 429`	`389`	`Malate dehydrogenase [NADP] 1, chloroplastic.`	`PRO_0000018647`
`NP_BIND`	`93 99`	`7`	`NADP (By similarity).`
`NP_BIND`	`211 213`	`3`	`NADP (By similarity).`
`ACT_SITE`	`269 269`		`Proton acceptor (By similarity).`
`BINDING`	`174 174`		`Substrate (By similarity).`
`BINDING`	`180 180`		`Substrate (By similarity).`
`BINDING`	`187 187`		`NADP (By similarity).`
`BINDING`	`194 194`		`NADP (By similarity).`
`BINDING`	`213 213`		`Substrate (By similarity).`
`BINDING`	`244 244`		`Substrate (By similarity).`
`SITE`	`64 64`	`1`	`Activation of NADP-MDH.`
`SITE`	`69 69`	`1`	`Activation of NADP-MDH.`
`DISULFID`	`64 69`		`In oxidized inactive NAD-MDH.`
`DISULFID`	`405 417`		`In oxidized inactive NAD-MDH.`
`CONFLICT`	`226 228`		`APD -> PPH (in Ref. 2; CAA37531).`
`HELIX`	`66 68`	`3`
`STRAND`	`87 92`	`6`
`TURN`	`93 95`	`3`
`HELIX`	`97 107`	`11`
`TURN`	`108 112`	`5`
`STRAND`	`118 123`	`6`
`HELIX`	`126 128`	`3`
`HELIX`	`129 140`	`12`
`STRAND`	`147 154`	`8`
`HELIX`	`156 159`	`4`
`TURN`	`160 162`	`3`
`STRAND`	`164 168`	`5`
`HELIX`	`180 201`	`22`
`STRAND`	`207 210`	`4`
`STRAND`	`212 214`	`3`
`HELIX`	`215 224`	`10`
`HELIX`	`231 233`	`3`
`STRAND`	`234 236`	`3`
`HELIX`	`239 252`	`14`
`HELIX`	`257 259`	`3`
`STRAND`	`264 267`	`4`
`STRAND`	`274 276`	`3`
`HELIX`	`287 289`	`3`
`HELIX`	`294 306`	`13`
`HELIX`	`308 315`	`8`
`HELIX`	`321 336`	`16`
`STRAND`	`345 350`	`6`
`STRAND`	`360 369`	`10`
`STRAND`	`372 374`	`3`
`HELIX`	`386 405`	`20`
`HELIX`	`407 410`	`4`
`STRAND`	`412 414`	`3`

Sequence information

Length: 429 AA [This is the length of the unprocessed precursor]

Molecular weight: 46455 Da [This is the MW of the unprocessed precursor]

CRC64: 17D9E0A34A67F1FF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGLSTAYSPV GSHLAPAPLG HRRSAQLHRP RRALLATVRC SVDAAKQVQD GVATAEAPAT 

        70         80         90        100        110        120 
RKDCFGVFCT TYDLKAEDKT KSWKKLVNIA VSGAAGMISN HLLFKLASGE VFGQDQPIAL 

       130        140        150        160        170        180 
KLLGSERSFQ ALEGVAMELE DSLYPLLREV SIGIDPYEVF EDVDWALLIG AKPRGPGMER 

       190        200        210        220        230        240 
AALLDINGQI FADQGKALNA VASKNVKVLV VGNPCNTNAL ICLKNAPDIP AKNFHALTRL 

       250        260        270        280        290        300 
DENRAKCQLA LKAGVFYDKV SNVTIWGNHS TTQVPDFLNA KIDGRPVKEV IKDTKWLEEE 

       310        320        330        340        350        360 
FTITVQKRGG ALIQKWGRSS AASTAVSIAD AIKSLVTPTP EGDWFSTGVY TTGNPYGIAE 

       370        380        390        400        410        420 
DIVFSMPCRS KGDGDYELAT DVSMDDFLWE RIKKSEAELL AEKKCVAHLT GEGNAYCDVP 


EDTMLPGEV

P17606 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