ID A0A0E0IU06_ORYNI Unreviewed; 397 AA.
AC A0A0E0IU06;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA10G14580.1};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA10G14580.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA10G14580.1};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA10G14580.1}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA10G14580.1};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC Evidence={ECO:0000256|RuleBase:RU003405};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000256|ARBA:ARBA00009613}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0E0IU06; -.
DR STRING; 4536.A0A0E0IU06; -.
DR EnsemblPlants; ONIVA10G14580.1; ONIVA10G14580.1; ONIVA10G14580.
DR Gramene; ONIVA10G14580.1; ONIVA10G14580.1; ONIVA10G14580.
DR eggNOG; KOG1496; Eukaryota.
DR HOGENOM; CLU_040727_2_0_1; -.
DR OMA; TKGMERG; -.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd01336; MDH_cytoplasmic_cytosolic; 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; IPR001557; L-lactate/malate_DH.
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; IPR011274; Malate_DH_NAD-dep_euk.
DR InterPro; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR NCBIfam; TIGR01758; MDH_euk_cyt; 1.
DR PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23382:SF3; MALATE DEHYDROGENASE, CYTOPLASMIC; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 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 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000102-3, ECO:0000256|RuleBase:RU003405};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU003405}.
FT DOMAIN 71..218
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 222..390
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 253
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 77..83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 195..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 397 AA; 42466 MW; 77CFC8D0838609F5 CRC64;
MGRGAPTWEQ RGFSGLPVAA RLNNGHPFPP LSQNSPKRAA SPLLLPNPYA SRTFSKLPLP
PPSAPMAKEP MRVLVTGAAG QIGYALVPMI ARGVMLGADQ PVILHMLDIP PATESLNGLK
MELVDAAFPL LKGIVATTDV VEACTGVNVA VMVGGFPRKE GMERKDVMSK NVSIYKSQAS
ALEAHAAPNC KVLVVANPAN TNALILKEFA PSIPEKNITC LTRLDHNRAL GQISEKLNVQ
VTDVKNAIIW GNHSSTQYPD VNHATVKTPS GEKPVRELVA DDEWLNTEFI STVQQRGAAI
IKARKQSSAL SAASSACDHI RDWVLGTPEG TFVSMGVYSD GSYGVPAGLI YSFPVTCSGG
EWTIVQGLPI DEFSRKKMDA TAQELSEEKT LAYSCLN
//