MDHC3_ARATH
ID MDHC3_ARATH Reviewed; 339 AA.
AC Q9FJU0;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Malate dehydrogenase 3, cytoplasmic {ECO:0000305};
DE EC=1.1.1.37 {ECO:0000305};
DE AltName: Full=Cytosolic NAD-dependent malate dehydrogenase 3 {ECO:0000305};
DE Short=cNAD-MDH3 {ECO:0000303|PubMed:20876337};
DE AltName: Full=Cytosolic malate dehydrogenase 3 {ECO:0000303|PubMed:20876337};
DE Short=Cytosolic MDH3 {ECO:0000305};
GN Name=MDH3 {ECO:0000305};
GN OrderedLocusNames=At5g56720 {ECO:0000312|Araport:AT5G56720};
GN ORFNames=MIK19.17 {ECO:0000312|EMBL:BAB09890.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20876337; DOI=10.1104/pp.110.161612;
RA Tomaz T., Bagard M., Pracharoenwattana I., Linden P., Lee C.P.,
RA Carroll A.J., Stroeher E., Smith S.M., Gardestroem P., Millar A.H.;
RT "Mitochondrial malate dehydrogenase lowers leaf respiration and alters
RT photorespiration and plant growth in Arabidopsis.";
RL Plant Physiol. 154:1143-1157(2010).
CC -!- FUNCTION: Catalyzes a reversible NAD-dependent dehydrogenase reaction
CC involved in central metabolism and redox homeostasis between organelle
CC compartments. {ECO:0000305|PubMed:20876337}.
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:0000305};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves at low levels.
CC {ECO:0000269|PubMed:20876337}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000305}.
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DR EMBL; AB013392; BAB09890.1; -; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q9FJU0; -.
DR SMR; Q9FJU0; -.
DR STRING; 3702.AT5G56720.1; -.
DR PaxDb; Q9FJU0; -.
DR PeptideAtlas; Q9FJU0; -.
DR PRIDE; Q9FJU0; -.
DR EnsemblPlants; AT5G56720.1; AT5G56720.1; AT5G56720.
DR Gramene; AT5G56720.1; AT5G56720.1; AT5G56720.
DR Araport; AT5G56720; -.
DR TAIR; locus:2165066; AT5G56720.
DR eggNOG; KOG1496; Eukaryota.
DR HOGENOM; CLU_040727_2_0_1; -.
DR InParanoid; Q9FJU0; -.
DR PhylomeDB; Q9FJU0; -.
DR PRO; PR:Q9FJU0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJU0; baseline and differential.
DR GO; GO:0016020; C:membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd01336; MDH_cytoplasmic_cytosolic; 1.
DR Gene3D; 3.90.110.10; -; 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 PANTHER; PTHR23382; PTHR23382; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR TIGRFAMs; TIGR01758; MDH_euk_cyt; 1.
DR PROSITE; PS00068; MDH; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; NAD; Oxidoreductase; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..339
FT /note="Malate dehydrogenase 3, cytoplasmic"
FT /id="PRO_0000438326"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 22..23
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 49
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 105
FT /ligand="oxaloacetate"
FT /ligand_id="ChEBI:CHEBI:16452"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 138
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 138
FT /ligand="oxaloacetate"
FT /ligand_id="ChEBI:CHEBI:16452"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 169
FT /ligand="oxaloacetate"
FT /ligand_id="ChEBI:CHEBI:16452"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 194
FT /ligand="oxaloacetate"
FT /ligand_id="ChEBI:CHEBI:16452"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 249
FT /ligand="oxaloacetate"
FT /ligand_id="ChEBI:CHEBI:16452"
FT /evidence="ECO:0000250|UniProtKB:P93819"
SQ SEQUENCE 339 AA; 36870 MW; D2209D9FA86E1C8E CRC64;
MCNLLNIEKD PIRVLITGAA GNIGYAIAPM IARGIMLGPD QPMILHLLDI EPASSSLEAV
KMELQDSAFP LLKGVIATTN VVEACKDVNI VIMIGGFPRI AGMERKDVMS KNVVIYKAQA
SALERYASDD CKVLVVANPA NTNALILKEF APSIPEENIT CLTRLDHNRA LAQLADKLSV
PVSSVKNVIV WGNHSSTQYP DTNHATVSTK TGDRPLKELV TDHNWLKNEF IVEVQQRGAA
VLRARKQSSA FSAAGAACDH IRDWFLGTPK GTWVSMGVCS DGSYGIPPGL VYSFPVICEK
GSWKIVQGLS IDEFSREKMD DSARELAEEK DLAYSCLNV
