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Malate dehydrogenase [NADP], chloroplastic (EC 1.1.1.82) (NADP-MDH)

 MDHP_PEA                Reviewed;         441 AA.
P21528;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
25-OCT-2017, entry version 119.
RecName: Full=Malate dehydrogenase [NADP], chloroplastic;
EC=1.1.1.82;
AltName: Full=NADP-MDH;
Flags: Precursor;
Pisum sativum (Garden pea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Pisum.
NCBI_TaxID=3888;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8223554; DOI=10.1111/j.1432-1033.1993.tb18233.x;
Reng W., Riessland R., Scheibe R., Jaenicke R.;
"Cloning, site-specific mutagenesis, expression and characterization
of full-length chloroplast NADP-malate dehydrogenase from Pisum
sativum.";
Eur. J. Biochem. 217:189-197(1993).
[2]
PROTEIN SEQUENCE OF 65-441, AND DISULFIDE BOND.
STRAIN=cv. Kleine Rheinlaenderin;
PubMed=1986782; DOI=10.1016/0167-4838(91)90212-I;
Scheibe R., Kampfenkel K., Wessels R., Tripier D.;
"Primary structure and analysis of the location of the regulatory
disulfide bond of pea chloroplast NADP-malate dehydrogenase.";
Biochim. Biophys. Acta 1076:1-8(1991).
[3]
PARTIAL PROTEIN SEQUENCE.
PubMed=3665938; DOI=10.1111/j.1432-1033.1987.tb13466.x;
Fickenscher K., Scheibe R., Marcus F.;
"Amino acid sequence similarity between malate dehydrogenases (NAD)
and pea chloroplast malate dehydrogenase (NADP).";
Eur. J. Biochem. 168:653-658(1987).
[4]
PROTEIN SEQUENCE OF 59-74 AND 92-112, AND SUBUNIT.
STRAIN=cv. Kleine Rheinlaenderin;
PubMed=1472542; DOI=10.1016/0304-4165(92)90098-F;
Kampfenkel K.;
"Limited proteolysis of NADP-malate dehydrogenase from pea chloroplast
by aminopeptidase K yields monomers. Evidence of proteolytic
degradation of NADP-malate dehydrogenase during purification from
pea.";
Biochim. Biophys. Acta 1156:71-77(1992).
-!- 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, disulfide
bridges on the protein must be reduced by thioredoxin which
receives electrons from ferredoxin and the electron transport
system of photosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1472542}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast.
-!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
{ECO:0000305}.
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EMBL; X74507; CAA52614.1; -; mRNA.
PIR; S38346; S38346.
ProteinModelPortal; P21528; -.
SMR; P21528; -.
IntAct; P21528; 1.
MINT; MINT-2584130; -.
PRIDE; P21528; -.
SABIO-RK; P21528; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
Gene3D; 3.90.110.10; -; 1.
InterPro; IPR022383; Lactate/malate_DH_C.
InterPro; IPR001236; Lactate/malate_DH_N.
InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
InterPro; IPR001252; Malate_DH_AS.
InterPro; IPR011273; Malate_DH_NADP-dep_pln.
InterPro; IPR010945; Malate_DH_type2.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR23382; PTHR23382; 1.
Pfam; PF02866; Ldh_1_C; 1.
Pfam; PF00056; Ldh_1_N; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF56327; SSF56327; 1.
TIGRFAMs; TIGR01757; Malate-DH_plant; 1.
TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
PROSITE; PS00068; MDH; 1.
1: Evidence at protein level;
Chloroplast; Direct protein sequencing; Disulfide bond; NADP;
Oxidoreductase; Plastid; Transit peptide.
TRANSIT 1 58 Chloroplast.
{ECO:0000269|PubMed:1472542}.
CHAIN 59 441 Malate dehydrogenase [NADP],
chloroplastic.
/FTId=PRO_0000018646.
NP_BIND 105 111 NADP. {ECO:0000250}.
NP_BIND 223 225 NADP. {ECO:0000250}.
ACT_SITE 281 281 Proton acceptor. {ECO:0000250}.
BINDING 186 186 Substrate. {ECO:0000255|PROSITE-
ProRule:PRU10004}.
BINDING 192 192 Substrate. {ECO:0000255|PROSITE-
ProRule:PRU10004}.
BINDING 199 199 NADP. {ECO:0000250}.
BINDING 206 206 NAD. {ECO:0000250}.
BINDING 225 225 Substrate. {ECO:0000255|PROSITE-
ProRule:PRU10004}.
BINDING 256 256 Substrate. {ECO:0000255|PROSITE-
ProRule:PRU10004}.
SITE 76 76 Activation of NADP-MDH.
SITE 81 81 Activation of NADP-MDH.
DISULFID 76 81 In oxidized inactive NAD-MDH.
{ECO:0000269|PubMed:1986782}.
DISULFID 417 429 In oxidized inactive NAD-MDH.
{ECO:0000250}.
CONFLICT 90 90 E -> T (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 234 234 C -> M (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 287 287 P -> K (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 294 294 I -> L (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 297 297 L -> I (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 366 366 N -> V (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 377 377 S -> G (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 441 AA; 48264 MW; 613747E6357C325B CRC64;
MALTQLNSTC SKPQLHSSSQ LSFLSRTRTR TLPRHYHSTF APLHRTQHAR ISCSVAPNQV
QVPAAQTQDP KGKPDCYGVF CLTYDLKAEE ETKSWKKLIN IAVSGAAGMI SNHLLFKLAS
GEVFGPDQPI ALKLLGSERS IQALEGVAME LEDSLFPLLR EVVISIDPYE VFQDAEWALL
IGAKPRGPGV ERAALLDING QIFAEQGKAL NAVASRNAKV IVVGNPCNTN ALICLKNAPN
IPAKNFHALT RLDENRAKCQ LALKAGVFYD KVSNMTIWGN HSTTQVPDFL NARIDGLPVK
EVIKDNKWLE EEFTEKVQKR GGVLIQKWGR SSAASTSVSI VDAIRSLITP TPEGDWFSSG
VYTNGNPYGI AEDIVFSMPC RSKGDGDYEL VNDVIFDDYL RQKLAKTEAE LLAEKKCVAH
LTGEGIAVCD LPGDTMLPGE M


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