MDHC2_ARATH
ID MDHC2_ARATH Reviewed; 332 AA.
AC P57106; Q8LA78; Q9LSX3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Malate dehydrogenase 2, cytoplasmic {ECO:0000305};
DE EC=1.1.1.37;
DE AltName: Full=Cytosolic NAD-dependent malate dehydrogenase 2 {ECO:0000305};
DE Short=cNAD-MDH2 {ECO:0000303|PubMed:20876337};
DE AltName: Full=Cytosolic malate dehydrogenase 2 {ECO:0000303|PubMed:20876337};
DE Short=Cytosolic MDH2 {ECO:0000305};
GN Name=MDH2; OrderedLocusNames=At5g43330; ORFNames=MWF20.2;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
RN [6]
RP INTERACTION WITH GRF1; GRF3 AND GRF8.
RX PubMed=22104211; DOI=10.1186/1752-0509-5-192;
RA Diaz C., Kusano M., Sulpice R., Araki M., Redestig H., Saito K., Stitt M.,
RA Shin R.;
RT "Determining novel functions of Arabidopsis 14-3-3 proteins in central
RT metabolic processes.";
RL BMC Syst. Biol. 5:192-192(2011).
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:0000255|PROSITE-ProRule:PRU10004};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with 14-3-3-like proteins
CC GRF1 GRF3 and GRF8 (PubMed:22104211). {ECO:0000250,
CC ECO:0000269|PubMed:22104211}.
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; AB025638; BAA97412.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94946.1; -; Genomic_DNA.
DR EMBL; AY072137; AAL59959.1; -; mRNA.
DR EMBL; AY091220; AAM14159.1; -; mRNA.
DR EMBL; AY087986; AAM65532.1; -; mRNA.
DR RefSeq; NP_199147.1; NM_123699.4.
DR AlphaFoldDB; P57106; -.
DR SMR; P57106; -.
DR BioGRID; 19601; 9.
DR STRING; 3702.AT5G43330.1; -.
DR iPTMnet; P57106; -.
DR PaxDb; P57106; -.
DR PRIDE; P57106; -.
DR ProteomicsDB; 238335; -.
DR EnsemblPlants; AT5G43330.1; AT5G43330.1; AT5G43330.
DR GeneID; 834351; -.
DR Gramene; AT5G43330.1; AT5G43330.1; AT5G43330.
DR KEGG; ath:AT5G43330; -.
DR Araport; AT5G43330; -.
DR TAIR; locus:2176441; AT5G43330.
DR eggNOG; KOG1496; Eukaryota.
DR HOGENOM; CLU_040727_2_0_1; -.
DR InParanoid; P57106; -.
DR OMA; TKGMERG; -.
DR OrthoDB; 1118998at2759; -.
DR PhylomeDB; P57106; -.
DR PRO; PR:P57106; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P57106; baseline and differential.
DR Genevisible; P57106; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; NAD; Oxidoreductase; Reference proteome;
KW Tricarboxylic acid cycle; Ubl conjugation.
FT CHAIN 1..332
FT /note="Malate dehydrogenase 2, cytoplasmic"
FT /id="PRO_0000113413"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 16..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 43
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 99
FT /ligand="oxaloacetate"
FT /ligand_id="ChEBI:CHEBI:16452"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 132
FT /ligand="oxaloacetate"
FT /ligand_id="ChEBI:CHEBI:16452"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 163
FT /ligand="oxaloacetate"
FT /ligand_id="ChEBI:CHEBI:16452"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 188
FT /ligand="oxaloacetate"
FT /ligand_id="ChEBI:CHEBI:16452"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT BINDING 243
FT /ligand="oxaloacetate"
FT /ligand_id="ChEBI:CHEBI:16452"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P93819"
FT CONFLICT 4
FT /note="E -> K (in Ref. 4; AAM65532)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="V -> S (in Ref. 4; AAM65532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 35675 MW; 76BF976943179FA7 CRC64;
MAKEPVRVLV TGAAGQIGYA LVPMIARGIM LGADQPVILH MLDIPFAAEA LNGVKMELVD
AAFPLLKGVV ATTDAVEACT GVNVAVMVGG FPRKEGMERK DVMSKNVSIY KSQASALEKH
AAPNCKVLVV ANPANTNALI LKEFAPSIPE KNITCLTRLD HNRALGQVSE RLSVPVSDVK
NVIIWGNHSS TQYPDVNHAT VKTSVGEKPV RELVKNDEWL NGEFISTVQQ RGAAIIKARK
LSSALSAASS ACDHIRDWVV GTPEGTFVSM GVYSDGSYNV PAGLIYSFPV TCRNGEWTIV
QGLPIDDASR KKMDLTAEEL KEEKDLAYSC LS
