MDHP1_SORBI
ID MDHP1_SORBI Reviewed; 429 AA.
AC P17606; P19796;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Malate dehydrogenase [NADP] 1, chloroplastic;
DE EC=1.1.1.82;
DE AltName: Full=NADP-MDH-1;
DE Flags: Precursor;
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. INRA 450; TISSUE=Leaf;
RX PubMed=2373367; DOI=10.1016/0378-1119(90)90003-a;
RA Luchetta P., Cretin C., Gadal P.;
RT "Structure and characterization of the Sorghum vulgare gene encoding NADP-
RT malate dehydrogenase.";
RL Gene 89:171-177(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Tamaran FNK 140; TISSUE=Leaf;
RX PubMed=2209586; DOI=10.1111/j.1432-1033.1990.tb19227.x;
RA Cretin C., Luchetta P., Joly C., Decottignies P., Lepiniec L., Gadal P.,
RA Sallantin M., Huet J.-C., Pernollet J.-C.;
RT "Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA
RT sequence. Homology with malate dehydrogenase (NAD).";
RL Eur. J. Biochem. 192:299-303(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND SUBUNIT.
RX PubMed=10194350; DOI=10.1021/bi982876c;
RA Johansson K., Ramaswamy S., Saarinen M., Lemaire-Chamley M.,
RA Issakidis-Bourguet E., Miginiac-Maslow M., Eklund H.;
RT "Structural basis for light activation of a chloroplast enzyme: the
RT structure of sorghum NADP-malate dehydrogenase in its oxidized form.";
RL Biochemistry 38:4319-4326(1999).
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, disulfide bridges on
CC the protein must be reduced by thioredoxin which receives electrons
CC from ferredoxin and the electron transport system of photosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10194350}.
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; M31965; AAA34047.1; -; Genomic_DNA.
DR EMBL; X53453; CAA37531.1; -; mRNA.
DR PIR; JH0151; JH0151.
DR PIR; S13588; S13588.
DR RefSeq; XP_002445670.1; XM_002445625.1.
DR PDB; 7MDH; X-ray; 2.40 A; A/B/C/D=55-429.
DR PDBsum; 7MDH; -.
DR AlphaFoldDB; P17606; -.
DR SMR; P17606; -.
DR STRING; 4558.Sb07g023920.1; -.
DR PRIDE; P17606; -.
DR EnsemblPlants; EES15165; EES15165; SORBI_3007G166300.
DR GeneID; 8057802; -.
DR Gramene; EES15165; EES15165; SORBI_3007G166300.
DR KEGG; sbi:8057802; -.
DR eggNOG; KOG1496; Eukaryota.
DR HOGENOM; CLU_040727_3_0_1; -.
DR OMA; GLEINDW; -.
DR OrthoDB; 1118998at2759; -.
DR BRENDA; 1.1.1.82; 5768.
DR SABIO-RK; P17606; -.
DR EvolutionaryTrace; P17606; -.
DR ExpressionAtlas; P17606; baseline and differential.
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 3D-structure; Chloroplast; Disulfide bond; NADP; Oxidoreductase; Plastid;
KW Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 41..429
FT /note="Malate dehydrogenase [NADP] 1, chloroplastic"
FT /id="PRO_0000018647"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 93..99
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 187
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 211..213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT SITE 64
FT /note="Activation of NADP-MDH"
FT SITE 69
FT /note="Activation of NADP-MDH"
FT DISULFID 64..69
FT /note="In oxidized inactive NAD-MDH"
FT DISULFID 405..417
FT /note="In oxidized inactive NAD-MDH"
FT CONFLICT 226..228
FT /note="APD -> PPH (in Ref. 2; CAA37531)"
FT /evidence="ECO:0000305"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:7MDH"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:7MDH"
FT TURN 108..112
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:7MDH"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 180..201
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 239..252
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 294..306
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 321..336
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 360..369
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 386..405
FT /evidence="ECO:0007829|PDB:7MDH"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:7MDH"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:7MDH"
SQ SEQUENCE 429 AA; 46455 MW; 17D9E0A34A67F1FF CRC64;
MGLSTAYSPV GSHLAPAPLG HRRSAQLHRP RRALLATVRC SVDAAKQVQD GVATAEAPAT
RKDCFGVFCT TYDLKAEDKT KSWKKLVNIA VSGAAGMISN HLLFKLASGE VFGQDQPIAL
KLLGSERSFQ ALEGVAMELE DSLYPLLREV SIGIDPYEVF EDVDWALLIG AKPRGPGMER
AALLDINGQI FADQGKALNA VASKNVKVLV VGNPCNTNAL ICLKNAPDIP AKNFHALTRL
DENRAKCQLA LKAGVFYDKV SNVTIWGNHS TTQVPDFLNA KIDGRPVKEV IKDTKWLEEE
FTITVQKRGG ALIQKWGRSS AASTAVSIAD AIKSLVTPTP EGDWFSTGVY TTGNPYGIAE
DIVFSMPCRS KGDGDYELAT DVSMDDFLWE RIKKSEAELL AEKKCVAHLT GEGNAYCDVP
EDTMLPGEV
