[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Leaf; Trevanion S.J., Ashton A.R.; Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
[2]	CRYSTALLIZATION. DOI=10.1107/S0907444997015655; PubMed=9761865 [NCBI, ExPASy, EBI, Israel, Japan] Macpherson K.H., Ashton A.R., Carr P.D., Trevanion S.J., Verger D., Ollis D.L.; "Crystallization and preliminary crystallographic studies of chloroplast NADP-dependent malate dehydrogenase from Flaveria bidentis."; Acta Crystallogr. D 54:654-656(1998).
[3]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT. TISSUE=Leaf; DOI=10.1016/S0969-2126(99)80058-6; PubMed=10196131 [NCBI, ExPASy, EBI, Israel, Japan] Carr P.D., Verger D., Ashton A.R., Ollis D.L.; "Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction."; Structure 7:461-475(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

L40958; AAA63907.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1CIV; X-ray; 2.80 A; A=69-453.

[ExPASy / RCSB / EBI]

PDBsum

1CIV; -.

ModBase

P46489.

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 68`	`68`	`Chloroplast.`
`CHAIN`	`69 453`	`385`	`Malate dehydrogenase [NADP], chloroplastic.`	`PRO_0000018642`
`NP_BIND`	`117 123`	`7`	`NADP.`
`NP_BIND`	`235 237`	`3`	`NADP.`
`ACT_SITE`	`293 293`		`Proton acceptor (By similarity).`
`BINDING`	`198 198`		`Substrate (By similarity).`
`BINDING`	`204 204`		`Substrate (By similarity).`
`BINDING`	`211 211`		`NADP (By similarity).`
`BINDING`	`218 218`		`NADP.`
`BINDING`	`237 237`		`Substrate (By similarity).`
`BINDING`	`268 268`		`Substrate (By similarity).`
`SITE`	`88 88`	`1`	`Activation of NADP-MDH (By similarity).`
`SITE`	`93 93`	`1`	`Activation of NADP-MDH (By similarity).`
`DISULFID`	`88 93`		`In oxidized inactive NAD-MDH.`
`DISULFID`	`429 441`		`In oxidized inactive NAD-MDH.`
`TURN`	`90 93`	`4`
`STRAND`	`101 103`	`3`
`STRAND`	`111 116`	`6`
`TURN`	`117 119`	`3`
`HELIX`	`121 131`	`11`
`TURN`	`132 136`	`5`
`STRAND`	`142 147`	`6`
`HELIX`	`150 152`	`3`
`HELIX`	`153 164`	`12`
`TURN`	`165 167`	`3`
`STRAND`	`171 178`	`8`
`HELIX`	`180 183`	`4`
`TURN`	`184 186`	`3`
`STRAND`	`188 192`	`5`
`HELIX`	`204 225`	`22`
`STRAND`	`231 234`	`4`
`STRAND`	`236 238`	`3`
`HELIX`	`239 248`	`10`
`HELIX`	`255 257`	`3`
`STRAND`	`258 260`	`3`
`HELIX`	`263 277`	`15`
`STRAND`	`283 285`	`3`
`STRAND`	`288 291`	`4`
`STRAND`	`298 300`	`3`
`HELIX`	`311 313`	`3`
`HELIX`	`318 323`	`6`
`HELIX`	`325 329`	`5`
`HELIX`	`332 338`	`7`
`HELIX`	`345 360`	`16`
`STRAND`	`369 374`	`6`
`STRAND`	`384 393`	`10`
`STRAND`	`395 398`	`4`
`HELIX`	`410 429`	`20`
`TURN`	`430 435`	`6`

Sequence information

Length: 453 AA [This is the length of the unprocessed precursor]

Molecular weight: 49515 Da [This is the MW of the unprocessed precursor]

CRC64: 7CD3A0F9F2A7B539 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVVKLSPWA NYSSSKSEIK SSSSSSSSKS SLSAYVINVS SSPRLSFYNP YPRRLHHQRL 

        70         80         90        100        110        120 
SSPASIRCSV TSSDQIQAPL PAKQKPECFG VFCLTYDLKA EEETKSWKKI INVAVSGAAG 

       130        140        150        160        170        180 
MISNHLLFKL ASGEVFGPDQ PISLKLLGSE RSFAALEGVA MELEDSLYPL LRQVSIGIDP 

       190        200        210        220        230        240 
YEIFQDAEWA LLIGAKPRGP GMERADLLDI NGQIFAEQGK ALNAVASPNV KVMVVGNPCN 

       250        260        270        280        290        300 
TNALICLKNA PNIPPKNFHA LTRLDENRAK CQLALKAGVF YDKVSNVTIW GNHSTTQVPD 

       310        320        330        340        350        360 
FLNAKIHGIP VTEVIRDRKW LEDEFTNMVQ TRGGVLIKKW GRSSAASTAV SIVDAIRSLV 

       370        380        390        400        410        420 
TPTPEGDWFS TGVYTNGNPY GIAEDIVFSM PCRSKGDGDY EFVKDVIFDD YLSKKIKKSE 

       430        440        450 
DELLAEKKCV AHLTGEGIAV CDLPEDTMLP GEM

P46489 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