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 24-JAN-2024, entry version 174. 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}. 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 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.Q9ZP05; -. DR iPTMnet; Q9ZP05; -. DR MetOSite; Q9ZP05; -. DR PaxDb; 3702-AT5G09660-4; -. 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 TAIR; AT5G09660; PMDH2. DR eggNOG; KOG1494; Eukaryota. DR HOGENOM; CLU_047181_0_2_1; -. DR InParanoid; Q9ZP05; -. DR PhylomeDB; Q9ZP05; -. DR BioCyc; ARA:AT5G09660-MONOMER; -. DR BioCyc; MetaCyc:AT5G09660-MONOMER; -. DR PRO; PR:Q9ZP05; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q9ZP05; baseline and differential. 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; 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; IPR010097; Malate_DH_type1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01772; MDH_euk_gproteo; 1. DR PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1. DR PANTHER; PTHR11540:SF52; MALATE DEHYDROGENASE 2, PEROXISOMAL; 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. DR Genevisible; Q9ZP05; AT. 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 //