[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Leaf mesophyll; Harnecker J., Scheibe R., von Schaewen A.; "Full-length cDNA sequence for chloroplast NADP-dependent malate dehydrogenase from spinach (Spinacia oleracea L.)."; (er) Plant Gene Register PGR95-106.
[2]	PROTEIN SEQUENCE OF 46-84, AND MUTAGENESIS. DOI=10.1016/0167-4838(93)90272-S; PubMed=8476924 [NCBI, ExPASy, EBI, Israel, Japan] Ocheretina O., Harnecker J., Rother T., Schmid R., Scheibe R.; "Effects of N-terminal truncations upon chloroplast NADP-malate dehydrogenases from pea and spinach."; Biochim. Biophys. Acta 1163:10-16(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 (By similarity).
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Plastid, chloroplast.
DOMAIN: Removal of amino acids 57 to 76 results in the formation of active monomers, a shift of the pH optimum from 8 to 7, the loss of oxaloacetate inhibition and an increased maximal velocity.
SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.

Copyright

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Cross-references

Sequence databases

EMBL

X84020; CAA58848.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S52268; S52268.

3D structure databases

HSSP

P46489; 1CIV. [HSSP ENTRY / PDB]

SMR

P52426; 66-432.

ModBase

P52426.

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.

PROSITE

PS00068; MDH; 1.

Other

ProtoNet

P52426.

UniRef

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

Keywords

Chloroplast; Direct protein sequencing; NADP; Oxidoreductase; Plastid; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 45`	`45`	`Chloroplast.`
`CHAIN`	`46 435`	`390`	`Malate dehydrogenase [NADP], chloroplastic.`	`PRO_0000018649`
`NP_BIND`	`98 104`	`7`	`NADP (By similarity).`
`NP_BIND`	`216 218`	`3`	`NADP (By similarity).`
`ACT_SITE`	`274 274`		`Proton acceptor (By similarity).`
`BINDING`	`179 179`		`Substrate (By similarity).`
`BINDING`	`185 185`		`Substrate (By similarity).`
`BINDING`	`192 192`		`NADP (By similarity).`
`BINDING`	`199 199`		`NAD (By similarity).`
`BINDING`	`218 218`		`Substrate (By similarity).`
`BINDING`	`249 249`		`Substrate (By similarity).`
`SITE`	`69 69`	`1`	`Activation of NADP-MDH (By similarity).`
`SITE`	`74 74`	`1`	`Activation of NADP-MDH (By similarity).`
`DISULFID`	`69 74`		`In oxidized inactive NAD-MDH (By similarity).`
`DISULFID`	`410 422`		`In oxidized inactive NAD-MDH (By similarity).`

Sequence information

Length: 435 AA [This is the length of the unprocessed precursor]

Molecular weight: 47488 Da [This is the MW of the unprocessed precursor]

CRC64: D68AA5D3ED7946A9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVAELSPCY QTQIVKPPHL SWLSNNHKLN LLGLPKASRI TEICCSLAPN QVQTPVAVPT 

        70         80         90        100        110        120 
GAQSIKPECY GVFCWTYDLK KEEETRSWKK MITIAISGAA GTISNHLLFK LASGVVFGPD 

       130        140        150        160        170        180 
QPIALKLLGS EKSFHALEGV AMELEDSLYP LLREVSIGID PYEVFEDAEW ALLIGAKPRG 

       190        200        210        220        230        240 
PGMERADLLD INGKIYAEQG KALNAVASPN VKVIVVGNPC NTNALICLKN PPNIPAKNFH 

       250        260        270        280        290        300 
SLTRLDENRA KCQLALKAGV FYDKVSNVTI WGNHSTTQVP DFVNAQIGGV PVKEVIKAQK 

       310        320        330        340        350        360 
WLEEEFTEKV RKRGGVLIQK WGRSSAASTA VSIVDAINPL ITPTPPGDWF PSGVYTNGNP 

       370        380        390        400        410        420 
YGIAEDLIYS MPCRSKGDGD YELVKDVIFD DYLRKRIKTS EEELLAEKRC TAHLTGEGIA 

       430 
VCDLPAGDTM LPGEM

P52426 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