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 30-NOV-2016, entry version 132.
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=Cytsolic 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; Magnoliophyta; eudicotyledons; Gunneridae;
OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC 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;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA Stitt M., 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
CC reaction involved in central metabolism and redox homeostasis
CC between organelle compartments. {ECO:0000305|PubMed:20876337}.
CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC {ECO:0000255|PROSITE-ProRule:PRU10004}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with 14-3-3-like
CC proteins 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}.
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 UniGene; At.27775; -.
DR ProteinModelPortal; P57106; -.
DR SMR; P57106; -.
DR BioGrid; 19601; 3.
DR MINT; MINT-8062783; -.
DR STRING; 3702.AT5G43330.1; -.
DR iPTMnet; P57106; -.
DR PaxDb; P57106; -.
DR PRIDE; P57106; -.
DR EnsemblPlants; AT5G43330.1; AT5G43330.1; AT5G43330.
DR GeneID; 834351; -.
DR Gramene; AT5G43330.1; AT5G43330.1; AT5G43330.
DR KEGG; ath:AT5G43330; -.
DR TAIR; AT5G43330; -.
DR eggNOG; KOG1496; Eukaryota.
DR eggNOG; COG0039; LUCA.
DR HOGENOM; HOG000220953; -.
DR InParanoid; P57106; -.
DR KO; K00025; -.
DR OMA; ACFDAVK; -.
DR OrthoDB; EOG09360G1U; -.
DR PhylomeDB; P57106; -.
DR Reactome; R-ATH-70263; Gluconeogenesis.
DR PRO; PR:P57106; -.
DR Proteomes; UP000006548; Chromosome 5.
DR Genevisible; P57106; AT.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 3.40.50.720; -; 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; IPR016040; NAD(P)-bd_dom.
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 Complete proteome; Cytoplasm; Isopeptide bond; NAD; Oxidoreductase;
KW Reference proteome; Tricarboxylic acid cycle; Ubl conjugation.
FT CHAIN 1 332 Malate dehydrogenase 2, cytoplasmic.
FT /FTId=PRO_0000113413.
FT NP_BIND 12 18 NAD. {ECO:0000250|UniProtKB:P11708}.
FT NP_BIND 130 132 NAD. {ECO:0000250|UniProtKB:P11708}.
FT ACT_SITE 188 188 Proton acceptor.
FT {ECO:0000250|UniProtKB:P11708}.
FT BINDING 43 43 NAD. {ECO:0000250|UniProtKB:P11708}.
FT BINDING 93 93 Substrate.
FT {ECO:0000250|UniProtKB:P11708}.
FT BINDING 99 99 Substrate.
FT {ECO:0000250|UniProtKB:P11708}.
FT BINDING 106 106 NAD. {ECO:0000250|UniProtKB:P11708}.
FT BINDING 113 113 NAD. {ECO:0000250|UniProtKB:P11708}.
FT BINDING 132 132 Substrate.
FT {ECO:0000250|UniProtKB:P11708}.
FT BINDING 163 163 Substrate.
FT {ECO:0000250|UniProtKB:P11708}.
FT CROSSLNK 119 119 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT {ECO:0000250|UniProtKB:P93819}.
FT CONFLICT 4 4 E -> K (in Ref. 4; AAM65532).
FT {ECO:0000305}.
FT CONFLICT 205 205 V -> S (in Ref. 4; AAM65532).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 6 153 ipfam:Ldh_1_N [T]
FT MYHIT 157 327 ipfam:Ldh_1_C [T]
FT MYHIT 156 168 ipat:MDH [T]
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
//
|
