ID   MDHP_SPIOL              Reviewed;         435 AA.
AC   P52426;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 70.
DE   RecName: Full=Malate dehydrogenase [NADP], chloroplastic;
DE            EC=1.1.1.82;
DE   AltName: Full=NADP-MDH;
DE   Flags: Precursor;
GN   Name=MDH;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   Caryophyllales; Amaranthaceae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf mesophyll;
RA   Harnecker J., Scheibe R., von Schaewen A.;
RT   "Full-length cDNA sequence for chloroplast NADP-dependent malate
RT   dehydrogenase from spinach (Spinacia oleracea L.).";
RL   (er) Plant Gene Register PGR95-106.
RN   [2]
RP   PROTEIN SEQUENCE OF 46-84, AND MUTAGENESIS.
RX   MEDLINE=93237315; PubMed=8476924; DOI=10.1016/0167-4838(93)90272-S;
RA   Ocheretina O., Harnecker J., Rother T., Schmid R., Scheibe R.;
RT   "Effects of N-terminal truncations upon chloroplast NADP-malate
RT   dehydrogenases from pea and spinach.";
RL   Biochim. Biophys. Acta 1163:10-16(1993).
CC   -!- FUNCTION: The chloroplastic, NADP-dependent form is essential for
CC       the photosynthesis C4 cycle, which allows plants to circumvent the
CC       problem of photorespiration. In C4 plants, NADP-MDH activity acts
CC       to convert oxaloacetate to malate in chloroplasts of mesophyll
CC       cells for transport to the bundle sheath cells.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NADP(+) = oxaloacetate + NADPH.
CC   -!- ENZYME REGULATION: Chloroplast NADP-MDH is activated upon
CC       illumination. In order to be enzymatically active, disulfides
CC       bridges on the protein must be reduced by thioredoxin which
CC       receives electrons from ferredoxin and the electron transport
CC       system of photosynthesis (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- DOMAIN: Removal of amino acids 57 to 76 results in the formation
CC       of active monomers, a shift of the pH optimum from 8 to 7, the
CC       loss of oxaloacetate inhibition and an increased maximal velocity.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X84020; CAA58848.1; -; mRNA.
DR   PIR; S52268; S52268.
DR   HSSP; P46489; 1CIV.
DR   SMR; P52426; 66-432.
DR   BRENDA; 1.1.1.82; 286.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001236; Lactate/malate_DH.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DH_AS.
DR   InterPro; IPR011273; Malate_DH_NADP-dep_pln.
DR   InterPro; IPR010945; Malate_DH_SF1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR23382; MDH_SF1; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   ProDom; PD003052; Mal_dehydrog; 1.
DR   TIGRFAMs; TIGR01757; Malate-DH_plant; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Disulfide bond; NADP;
KW   Oxidoreductase; Plastid; Transit peptide.
FT   TRANSIT       1     45       Chloroplast.
FT   CHAIN        46    435       Malate dehydrogenase [NADP],
FT                                chloroplastic.
FT                                /FTId=PRO_0000018649.
FT   NP_BIND      98    104       NADP (By similarity).
FT   NP_BIND     216    218       NADP (By similarity).
FT   ACT_SITE    274    274       Proton acceptor (By similarity).
FT   BINDING     179    179       Substrate (By similarity).
FT   BINDING     185    185       Substrate (By similarity).
FT   BINDING     192    192       NADP (By similarity).
FT   BINDING     199    199       NAD (By similarity).
FT   BINDING     218    218       Substrate (By similarity).
FT   BINDING     249    249       Substrate (By similarity).
FT   SITE         69     69       Activation of NADP-MDH (By similarity).
FT   SITE         74     74       Activation of NADP-MDH (By similarity).
FT   DISULFID     69     74       In oxidized inactive NAD-MDH (By
FT                                similarity).
FT   DISULFID    410    422       In oxidized inactive NAD-MDH (By
FT                                similarity).
SQ   SEQUENCE   435 AA;  47488 MW;  D68AA5D3ED7946A9 CRC64;
     MAVAELSPCY QTQIVKPPHL SWLSNNHKLN LLGLPKASRI TEICCSLAPN QVQTPVAVPT
     GAQSIKPECY GVFCWTYDLK KEEETRSWKK MITIAISGAA GTISNHLLFK LASGVVFGPD
     QPIALKLLGS EKSFHALEGV AMELEDSLYP LLREVSIGID PYEVFEDAEW ALLIGAKPRG
     PGMERADLLD INGKIYAEQG KALNAVASPN VKVIVVGNPC NTNALICLKN PPNIPAKNFH
     SLTRLDENRA KCQLALKAGV FYDKVSNVTI WGNHSTTQVP DFVNAQIGGV PVKEVIKAQK
     WLEEEFTEKV RKRGGVLIQK WGRSSAASTA VSIVDAINPL ITPTPPGDWF PSGVYTNGNP
     YGIAEDLIYS MPCRSKGDGD YELVKDVIFD DYLRKRIKTS EEELLAEKRC TAHLTGEGIA
     VCDLPAGDTM LPGEM
//