ID MDHP_MEDSA Reviewed; 437 AA.
AC O48902;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 13-SEP-2023, entry version 124.
DE RecName: Full=Malate dehydrogenase [NADP], chloroplastic;
DE EC=1.1.1.82;
DE AltName: Full=NADP-MDH;
DE Flags: Precursor;
GN Name=MDH1; Synonyms=P1MDH;
OS Medicago sativa (Alfalfa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Saranac; TISSUE=Root nodule;
RX PubMed=9721676; DOI=10.1046/j.1365-313x.1998.00192.x;
RA Miller S.S., Driscoll B.T., Gregerson R.G., Gantt J.S., Vance C.P.;
RT "Alfalfa malate dehydrogenase (MDH): molecular cloning and characterization
RT of five different forms reveals a unique nodule-enhanced MDH.";
RL Plant J. 15:173-184(1998).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000305}.
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DR EMBL; AF020269; AAB99753.1; -; mRNA.
DR AlphaFoldDB; O48902; -.
DR SMR; O48902; -.
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 CDD; cd01338; MDH_choloroplast_like; 1.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR01757; Malate-DH_plant; 1.
DR NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00068; MDH; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Disulfide bond; NADP; Oxidoreductase; Plastid;
KW Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..437
FT /note="Malate dehydrogenase [NADP], chloroplastic"
FT /id="PRO_0000018644"
FT ACT_SITE 277
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 101..107
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 219..221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT SITE 72
FT /note="Activation of NADP-MDH"
FT /evidence="ECO:0000250"
FT SITE 77
FT /note="Activation of NADP-MDH"
FT /evidence="ECO:0000250"
FT DISULFID 72..77
FT /note="In oxidized inactive NAD-MDH"
FT /evidence="ECO:0000250"
FT DISULFID 413..425
FT /note="In oxidized inactive NAD-MDH"
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 47835 MW; 9C7C5377DBA5454A CRC64;
MALTQLNNTC SKTQLHSSSQ LSFLSRTLPR HHHCTLAPLH RTQHARISCS VAPNQVQAPA
VQTQDPKSKP DCYGVFCLTY DLKAEEETKS WKKLITIAVS GAAGMISNHL LFKLASGEVF
GPNQPIALKL LGSERSLQAL EGVAMELEDS LFPLLREVVI SIDPYEVFQD AEWALLIGAK
PRGPGMERAA LLDINGQIFA EQGKALNAVA SRNVKVIVVG NPCNTNALIC LKNAPNIPAK
NFHALTRLDE NRAKCQLALK AGVFYDKVSN MTIWGNHSTT QVPDFLNARI DGLPVKEVIK
DHKWLEEEFT EKVQKRGGAL IQKWGRSSAA STSVSIVDAI RSLIIPTPEG DWFSTGVYTT
GNPYGIAEDI VFSMPCRSKG DGDYELVKDV IFDDYLRQKL AKTEAELLAE KKCVAHLTGE
GIAVCDLPGD TMLPGEM
//
