MDHX2_ARATH
ID MDHX2_ARATH Reviewed; 354 AA.
AC Q9ZP05; Q93ZA7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Malate dehydrogenase 2, peroxisomal {ECO:0000305};
DE EC=1.1.1.37;
DE AltName: Full=Microbody NAD-dependent malate dehydrogenase {ECO:0000303|PubMed:9774405};
DE Short=mbNAD-MDH {ECO:0000303|PubMed:9774405};
DE AltName: Full=Peroxisomal NAD-dependent malate dehydrogenase 2 {ECO:0000305};
DE Short=pxNAD-MDH2 {ECO:0000303|PubMed:20876337};
DE AltName: Full=Peroxisomal malate dehydrogenase 2 {ECO:0000303|PubMed:20876337};
DE Short=Peroxisomal MDH2 {ECO:0000305};
GN Name=PMDH2 {ECO:0000303|PubMed:17376163}; OrderedLocusNames=At5g09660;
GN ORFNames=F17I14_150, MTH16.8;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9774405; DOI=10.1074/jbc.273.43.27927;
RA Berkemeyer M., Scheibe R., Ocheretina O.;
RT "A novel, non-redox-regulated NAD-dependent malate dehydrogenase from
RT chloroplasts of Arabidopsis thaliana L.";
RL J. Biol. Chem. 273:27927-27933(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17376163; DOI=10.1111/j.1365-313x.2007.03055.x;
RA Pracharoenwattana I., Cornah J.E., Smith S.M.;
RT "Arabidopsis peroxisomal malate dehydrogenase functions in beta-oxidation
RT but not in the glyoxylate cycle.";
RL Plant J. 50:381-390(2007).
RN [8]
RP FUNCTION.
RX PubMed=18685043; DOI=10.1104/pp.108.122622;
RA Cousins A.B., Pracharoenwattana I., Zhou W., Smith S.M., Badger M.R.;
RT "Peroxisomal malate dehydrogenase is not essential for photorespiration in
RT Arabidopsis but its absence causes an increase in the stoichiometry of
RT photorespiratory CO2 release.";
RL Plant Physiol. 148:786-795(2008).
RN [9]
RP FUNCTION.
RX PubMed=19812894; DOI=10.1007/s11103-009-9554-2;
RA Pracharoenwattana I., Zhou W., Smith S.M.;
RT "Fatty acid beta-oxidation in germinating Arabidopsis seeds is supported by
RT peroxisomal hydroxypyruvate reductase when malate dehydrogenase is
RT absent.";
RL Plant Mol. Biol. 72:101-109(2010).
RN [10]
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 (Probable). Peroxisomal NAD-dependent malate dehydrogenase
CC involved in fatty acid beta-oxidation. Reoxidizes NADH from the beta-
CC oxidation and provides NAD for the conversion of fatty acyl-CoA to
CC acetyl-CoA. Does not participate directly in the glyoxylate cycle
CC (PubMed:17376163, PubMed:19812894). Required for maintenance of
CC photosynthetic rates under photorespiratory conditions, and carbon flow
CC during photorespiration. Supplies NADH reductant to the peroxisomal
CC hydroxypyruvate reductase (HPR), which reduces hydroxypyruvate into
CC glycerate in the photorespiratory cycle (PubMed:18685043).
CC {ECO:0000269|PubMed:17376163, ECO:0000269|PubMed:18685043,
CC ECO:0000269|PubMed:19812894, 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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17376163}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9ZP05-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves.
CC {ECO:0000269|PubMed:20876337}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutant plants pmdh1 and pmdh2 show seedling
CC growth arrest 5 days after seed imbibition.
CC {ECO:0000269|PubMed:17376163}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000305}.
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DR EMBL; AJ131206; CAA10321.1; -; mRNA.
DR EMBL; AB020752; BAB09521.1; -; Genomic_DNA.
DR EMBL; AL353994; CAB89364.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91422.1; -; Genomic_DNA.
DR EMBL; AF428373; AAL16303.1; -; mRNA.
DR EMBL; AY037252; AAK59853.1; -; mRNA.
DR EMBL; AY057682; AAL15313.1; -; mRNA.
DR EMBL; AY077653; AAL76131.1; -; mRNA.
DR PIR; PA0040; PA0040.
DR PIR; T49932; T49932.
DR RefSeq; NP_196528.1; NM_121003.4. [Q9ZP05-1]
DR AlphaFoldDB; Q9ZP05; -.
DR SMR; Q9ZP05; -.
DR BioGRID; 16103; 1.
DR STRING; 3702.AT5G09660.4; -.
DR MetOSite; Q9ZP05; -.
DR PaxDb; Q9ZP05; -.
DR PRIDE; Q9ZP05; -.
DR ProteomicsDB; 238770; -. [Q9ZP05-1]
DR EnsemblPlants; AT5G09660.1; AT5G09660.1; AT5G09660. [Q9ZP05-1]
DR GeneID; 830825; -.
DR Gramene; AT5G09660.1; AT5G09660.1; AT5G09660. [Q9ZP05-1]
DR KEGG; ath:AT5G09660; -.
DR Araport; AT5G09660; -.
DR eggNOG; KOG1494; Eukaryota.
DR HOGENOM; CLU_047181_0_2_1; -.
DR InParanoid; Q9ZP05; -.
DR PhylomeDB; Q9ZP05; -.
DR BioCyc; ARA:AT5G09660-MON; -.
DR BioCyc; MetaCyc:AT5G09660-MON; -.
DR PRO; PR:Q9ZP05; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ZP05; baseline and differential.
DR Genevisible; Q9ZP05; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0031998; P:regulation of fatty acid beta-oxidation; IMP:UniProtKB.
DR GO; GO:0080093; P:regulation of photorespiration; IMP:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 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; IPR010097; Malate_DH_type1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; TIGR01772; MDH_euk_gproteo; 1.
DR PROSITE; PS00068; MDH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glyoxylate bypass; NAD; Oxidoreductase; Peroxisome;
KW Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..354
FT /note="Malate dehydrogenase 2, peroxisomal"
FT /id="PRO_0000018634"
FT REGION 10..18
FT /note="Peroxisomal targeting signal PTS2"
FT /evidence="ECO:0000305|PubMed:17376163"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 49..55
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT BINDING 75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 135
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT BINDING 158..160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11708"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40926"
FT CONFLICT 166
FT /note="V -> I (in Ref. 5; AAL15313)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 37369 MW; AC56EAC7AB025288 CRC64;
MEFRGDANQR IARISAHLTP QMEAKNSVIG RENCRAKGGN PGFKVAILGA AGGIGQSLSL
LMKMNPLVSL LHLYDVVNAP GVTADVSHMD TGAVVRGFLG AKQLEDALTG MDLVIIPAGI
PRKPGMTRDD LFKINAGIVK TLCEGVAKCC PNAIVNLISN PVNSTVPIAA EVFKKAGTYD
PKKLLGVTTL DVARANTFVA EVLGLDPREV DVPVVGGHAG VTILPLLSQV KPPSSFTPQE
IEYLTNRIQN GGTEVVEAKA GAGSATLSMA YAAAKFADAC LRGLRGDANV VECSFVASQV
TELAFFATKV RLGRTGAEEV YQLGPLNEYE RIGLEKAKDE LAGSIQKGVE FIRK
