ID MDHP_ARATH Reviewed; 403 AA. AC Q9SN86; O81844; DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 147. DE RecName: Full=Malate dehydrogenase, chloroplastic {ECO:0000305}; DE EC=1.1.1.37; DE AltName: Full=Chloroplastic malate dehydrogenase {ECO:0000303|PubMed:20876337}; DE Short=Chloroplastic MDH {ECO:0000305}; DE Short=cpNAD-MDH {ECO:0000303|PubMed:20876337}; DE AltName: Full=Plastidic NAD-dependent malate dehydrogenase {ECO:0000305}; DE Short=pNAD-MDH {ECO:0000305}; DE Flags: Precursor; GN OrderedLocusNames=At3g47520; ORFNames=F1P2.70; 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], AND SUBCELLULAR LOCATION. RC STRAIN=cv. Columbia; TISSUE=Leaf; 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=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; RL Nature 408:820-822(2000). RN [3] 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 [4] 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC STRAIN=cv. Wassilewskija; RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200; RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., RA Garin J., Joyard J., Rolland N.; RT "Proteomics of the chloroplast envelope membranes from Arabidopsis RT thaliana."; RL Mol. Cell. Proteomics 2:325-345(2003). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=cv. Landsberg erecta; RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200; RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.; RT "Multidimensional protein identification technology (MudPIT) analysis of RT ubiquitinated proteins in plants."; RL Mol. Cell. Proteomics 6:601-610(2007). RN [7] 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 [8] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, RP AND DISRUPTION PHENOTYPE. RX PubMed=24198233; DOI=10.1093/mp/sst151; RA Selinski J., Koenig N., Wellmeyer B., Hanke G.T., Linke V., Neuhaus H.E., RA Scheibe R.; RT "The plastid-localized NAD-dependent malate dehydrogenase is crucial for RT energy homeostasis in developing Arabidopsis thaliana seeds."; RL Mol. Plant 7:170-186(2014). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION RP PHENOTYPE. RX PubMed=24453164; DOI=10.1104/pp.113.233866; RA Beeler S., Liu H.C., Stadler M., Schreier T., Eicke S., Lue W.L., RA Truernit E., Zeeman S.C., Chen J., Koetting O.; RT "Plastidial NAD-dependent malate dehydrogenase is critical for embryo RT development and heterotrophic metabolism in Arabidopsis."; RL Plant Physiol. 164:1175-1190(2014). CC -!- FUNCTION: Catalyzes a reversible NAD-dependent dehydrogenase reaction CC involved in central metabolism and redox homeostasis between organelle CC compartments (Probable). Plays a key role in the metabolism of dark CC chloroplasts and non-green plastids. Essential for embryo viability CC (PubMed:24198233, PubMed:24453164). Plays an essential role in CC heterotrophic metabolism in embryos, and autotrophic metabolism in CC photosynthetic tissues as well (PubMed:24453164). CC {ECO:0000269|PubMed:24198233, ECO:0000269|PubMed:24453164, CC 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: Plastid, chloroplast stroma CC {ECO:0000269|PubMed:12766230, ECO:0000269|PubMed:24198233, CC ECO:0000269|PubMed:24453164, ECO:0000269|PubMed:9774405}. CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves (PubMed:20876337). CC Expressed in meristematic regions of roots and shoots, cotyledons, CC young leaves, trichomes, stamen, pollen, tapetum, gynoecium and ovules CC (PubMed:24198233). {ECO:0000269|PubMed:20876337, CC ECO:0000269|PubMed:24198233}. CC -!- DEVELOPMENTAL STAGE: During pollen development, expressed in mature CC pollen grains and early in pollen-tube growth. Not expressed in CC immature pollen grains and fully grown pollen tubes (PubMed:24198233). CC During embryo development, expressed from the heart stage to mature CC embryo. Not expressed at the beginning of embryo development up to the CC globular stage (PubMed:24198233, PubMed:24453164). CC {ECO:0000269|PubMed:24198233, ECO:0000269|PubMed:24453164}. CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous due to embryo CC development arrest at globular stage. {ECO:0000269|PubMed:24198233, CC ECO:0000269|PubMed:24453164}. 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; Y13987; CAA74320.1; -; mRNA. DR EMBL; AL132955; CAB61978.1; -; Genomic_DNA. DR EMBL; CP002686; AEE78292.1; -; Genomic_DNA. DR EMBL; AY128281; AAM91090.1; -; mRNA. DR EMBL; BT000621; AAN18188.1; -; mRNA. DR PIR; T45712; T45712. DR PIR; T51862; T51862. DR RefSeq; NP_190336.1; NM_114620.3. DR AlphaFoldDB; Q9SN86; -. DR SMR; Q9SN86; -. DR BioGRID; 9226; 4. DR STRING; 3702.Q9SN86; -. DR iPTMnet; Q9SN86; -. DR PaxDb; 3702-AT3G47520-1; -. DR ProteomicsDB; 239049; -. DR EnsemblPlants; AT3G47520.1; AT3G47520.1; AT3G47520. DR GeneID; 823906; -. DR Gramene; AT3G47520.1; AT3G47520.1; AT3G47520. DR KEGG; ath:AT3G47520; -. DR Araport; AT3G47520; -. DR TAIR; AT3G47520; MDH. DR eggNOG; KOG1494; Eukaryota. DR HOGENOM; CLU_047181_0_0_1; -. DR InParanoid; Q9SN86; -. DR OMA; CIVECAY; -. DR OrthoDB; 5059897at2759; -. DR PhylomeDB; Q9SN86; -. DR BioCyc; ARA:AT3G47520-MONOMER; -. DR BioCyc; MetaCyc:AT3G47520-MONOMER; -. DR BRENDA; 1.1.1.37; 399. DR PRO; PR:Q9SN86; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9SN86; baseline and differential. DR GO; GO:0048046; C:apoplast; HDA:TAIR. DR GO; GO:0009507; C:chloroplast; IDA:TAIR. DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR. DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR. DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0005739; C:mitochondrion; HDA:TAIR. DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR. DR GO; GO:0009536; C:plastid; HDA:TAIR. DR GO; GO:0009532; C:plastid stroma; IDA:TAIR. DR GO; GO:0010319; C:stromule; IDA:TAIR. DR GO; GO:0062091; C:Ycf2/FtsHi complex; IDA:TAIR. DR GO; GO:0016464; F:chloroplast protein-transporting ATPase activity; IDA:TAIR. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IDA:TAIR. DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IMP:TAIR. DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR. DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR. DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0045037; P:protein import into chloroplast stroma; IMP:TAIR. DR GO; GO:0009409; P:response to cold; IEP:TAIR. 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; 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:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 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; Q9SN86; AT. PE 1: Evidence at protein level; KW Chloroplast; NAD; Oxidoreductase; Plastid; Reference proteome; KW Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1..80 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 81..403 FT /note="Malate dehydrogenase, chloroplastic" FT /id="PRO_0000224149" FT ACT_SITE 258 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P11708" FT BINDING 89..95 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 115 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 162 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11708" FT BINDING 168 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11708" FT BINDING 175 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 198..200 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT BINDING 200 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11708" FT BINDING 234 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P11708" FT BINDING 309 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P40926" FT CONFLICT 57 FT /note="A -> T (in Ref. 1; CAA74320)" FT /evidence="ECO:0000305" FT CONFLICT 66 FT /note="K -> N (in Ref. 1; CAA74320)" FT /evidence="ECO:0000305" SQ SEQUENCE 403 AA; 42406 MW; 65B54DE66392D229 CRC64; MATATSASLF STVSSSYSKA SSIPHSRLQS VKFNSVPSFT GLKSTSLISG SDSSSLAKTL RGSVTKAQTS DKKPYGFKIN ASYKVAVLGA AGGIGQPLSL LIKMSPLVST LHLYDIANVK GVAADLSHCN TPSQVRDFTG PSELADCLKD VNVVVIPAGV PRKPGMTRDD LFNINANIVK TLVEAVAENC PNAFIHIISN PVNSTVPIAA EVLKKKGVYD PKKLFGVTTL DVVRANTFVS QKKNLKLIDV DVPVIGGHAG ITILPLLSKT KPSVNFTDEE IQELTVRIQN AGTEVVDAKA GAGSATLSMA YAAARFVESS LRALDGDGDV YECSFVESTL TDLPFFASRV KIGKNGLEAV IESDLQGLTE YEQKALEALK VELKASIDKG VAFANKPAAA AAN //