NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Saranac;
TISSUE=Root nodule;
PubMed=9721676 [NCBI, ExPASy, EBI, Israel, Japan]
Miller S.S., Driscoll B.T., Gregerson R.G., Gantt J.S., Vance C.P.;
"Alfalfa malate dehydrogenase (MDH): molecular cloning and characterization of five different forms reveals a unique nodule-enhanced MDH.";
Plant J. 15:173-184(1998).

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 (By similarity).
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 (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

AF020269; AAB99753.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P46489; 1CIV. [HSSP ENTRY / PDB]

SMR

O48902; 69-434.

ModBase

O48902.

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 49`	`49`	`Chloroplast (Potential).`
`CHAIN`	`50 437`	`388`	`Malate dehydrogenase [NADP], chloroplastic.`	`PRO_0000018644`
`NP_BIND`	`101 107`	`7`	`NADP (By similarity).`
`NP_BIND`	`219 221`	`3`	`NADP (By similarity).`
`ACT_SITE`	`277 277`		`Proton acceptor (By similarity).`
`BINDING`	`182 182`		`Substrate (By similarity).`
`BINDING`	`188 188`		`Substrate (By similarity).`
`BINDING`	`195 195`		`NADP (By similarity).`
`BINDING`	`202 202`		`NAD (By similarity).`
`BINDING`	`221 221`		`Substrate (By similarity).`
`BINDING`	`252 252`		`Substrate (By similarity).`
`SITE`	`72 72`	`1`	`Activation of NADP-MDH (By similarity).`
`SITE`	`77 77`	`1`	`Activation of NADP-MDH (By similarity).`
`DISULFID`	`72 77`		`In oxidized inactive NAD-MDH (By similarity).`
`DISULFID`	`413 425`		`In oxidized inactive NAD-MDH (By similarity).`

Sequence information

Length: 437 AA [This is the length of the unprocessed precursor]

Molecular weight: 47835 Da [This is the MW of the unprocessed precursor]

CRC64: 9C7C5377DBA5454A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALTQLNNTC SKTQLHSSSQ LSFLSRTLPR HHHCTLAPLH RTQHARISCS VAPNQVQAPA 

        70         80         90        100        110        120 
VQTQDPKSKP DCYGVFCLTY DLKAEEETKS WKKLITIAVS GAAGMISNHL LFKLASGEVF 

       130        140        150        160        170        180 
GPNQPIALKL LGSERSLQAL EGVAMELEDS LFPLLREVVI SIDPYEVFQD AEWALLIGAK 

       190        200        210        220        230        240 
PRGPGMERAA LLDINGQIFA EQGKALNAVA SRNVKVIVVG NPCNTNALIC LKNAPNIPAK 

       250        260        270        280        290        300 
NFHALTRLDE NRAKCQLALK AGVFYDKVSN MTIWGNHSTT QVPDFLNARI DGLPVKEVIK 

       310        320        330        340        350        360 
DHKWLEEEFT EKVQKRGGAL IQKWGRSSAA STSVSIVDAI RSLIIPTPEG DWFSTGVYTT 

       370        380        390        400        410        420 
GNPYGIAEDI VFSMPCRSKG DGDYELVKDV IFDDYLRQKL AKTEAELLAE KKCVAHLTGE 

       430 
GIAVCDLPGD TMLPGEM

O48902 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