[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Leaf, and Root; Cushman J.C.; "Molecular cloning and expression of chloroplast NADP-malate dehydrogenase during Crassulacean acid metabolism induction by salt stress."; Photosyn. Res. 35:15-27(1993).

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.
INDUCTION: Expression decreases transiently in the leaves after salt stress and then increases to levels greater than two-fold higher than in unstressed plants.
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

X63727; CAA45270.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S33066; S33066.

3D structure databases

HSSP

P46489; 1CIV. [HSSP ENTRY / PDB]

SMR

Q05145; 72-438.

ModBase

Q05145.

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 51`	`51`	`Chloroplast (Potential).`
`CHAIN`	`52 441`	`390`	`Malate dehydrogenase [NADP], chloroplastic.`	`PRO_0000018645`
`NP_BIND`	`104 110`	`7`	`NADP (By similarity).`
`NP_BIND`	`222 224`	`3`	`NADP (By similarity).`
`ACT_SITE`	`280 280`		`Proton acceptor (By similarity).`
`BINDING`	`185 185`		`Substrate (By similarity).`
`BINDING`	`191 191`		`Substrate (By similarity).`
`BINDING`	`198 198`		`NADP (By similarity).`
`BINDING`	`205 205`		`NAD (By similarity).`
`BINDING`	`224 224`		`Substrate (By similarity).`
`BINDING`	`255 255`		`Substrate (By similarity).`
`SITE`	`75 75`	`1`	`Activation of NADP-MDH (By similarity).`
`SITE`	`80 80`	`1`	`Activation of NADP-MDH (By similarity).`
`DISULFID`	`75 80`		`In oxidized inactive NAD-MDH (By similarity).`
`DISULFID`	`416 428`		`In oxidized inactive NAD-MDH (By similarity).`

Sequence information

Length: 441 AA [This is the length of the unprocessed precursor]

Molecular weight: 48004 Da [This is the MW of the unprocessed precursor]

CRC64: 77AFB169F1488FA7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVAELSPSY KTQLKTCQQL SSSLSTRLSD HRKFSLRLLP RPVSVRGGIR CSVAPNQVQA 

        70         80         90        100        110        120 
PVAVPAEGQT GKPECYGIFC LTYDLKAEEE TKTWKKMITI AVSGAAGMIS NHLLFKLASG 

       130        140        150        160        170        180 
EVFGPDQPIA LKLLGSERSF NALEGVAMEL EDSLYPLLRA VSIGIDPYDI FQDAEWALLI 

       190        200        210        220        230        240 
GAKPRGPGME RADLLDINGQ IFAEQGKALN AVASRNVKVI VVGNPCNTNA LICLKNAPNI 

       250        260        270        280        290        300 
PAKNFHGLTR LDENRAKCQL ALKAGVFYDK VSNMTIWGNH STTQVPDFLN AKIDGLPVKT 

       310        320        330        340        350        360 
VIKDHKWLEE EFTVMIQKRG GALIQKWGRS SAASTAVSIA DAIKSLVTPT PEGDWFSSAV 

       370        380        390        400        410        420 
YTNGNPYGIA EDLVFSMPCR SKGDGDYELV KDVVFDDYLR QRIKKSEEEL LAEKRCTAHL 

       430        440 
TGEGVAVCDL PAGDTMLPGE M

Q05145 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