MDHP_SPIOL
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 03-AUG-2022, entry version 115.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; 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(1995).
RN [2]
RP PROTEIN SEQUENCE OF 46-84, AND MUTAGENESIS.
RX 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 the
CC photosynthesis C4 cycle, which allows plants to circumvent the problem
CC of photorespiration. In C4 plants, NADP-MDH activity acts to convert
CC oxaloacetate to malate in chloroplasts of mesophyll cells for transport
CC to the bundle sheath cells.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate;
CC Xref=Rhea:RHEA:10824, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.82;
CC -!- ACTIVITY REGULATION: Chloroplast NADP-MDH is activated upon
CC illumination. In order to be enzymatically active, disulfides bridges
CC on the protein must be reduced by thioredoxin which receives electrons
CC from ferredoxin and the electron transport system of photosynthesis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- DOMAIN: Removal of amino acids 57 to 76 results in the formation of
CC active monomers, a shift of the pH optimum from 8 to 7, the loss of
CC oxaloacetate inhibition and an increased maximal velocity.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000305}.
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DR EMBL; X84020; CAA58848.1; -; mRNA.
DR PIR; S52268; S52268.
DR AlphaFoldDB; P52426; -.
DR SMR; P52426; -.
DR PRIDE; P52426; -.
DR BioCyc; MetaCyc:MON-17409; -.
DR SABIO-RK; P52426; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR Gene3D; 3.90.110.10; -; 1.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
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_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23382; PTHR23382; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 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
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:8476924"
FT CHAIN 46..435
FT /note="Malate dehydrogenase [NADP], chloroplastic"
FT /id="PRO_0000018649"
FT ACT_SITE 274
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 98..104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 216..218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT SITE 69
FT /note="Activation of NADP-MDH"
FT /evidence="ECO:0000250"
FT SITE 74
FT /note="Activation of NADP-MDH"
FT /evidence="ECO:0000250"
FT DISULFID 69..74
FT /note="In oxidized inactive NAD-MDH"
FT /evidence="ECO:0000250"
FT DISULFID 410..422
FT /note="In oxidized inactive NAD-MDH"
FT /evidence="ECO:0000250"
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
