MDHP_ARATH
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 03-AUG-2022, entry version 142.
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.AT3G47520.1; -.
DR PaxDb; Q9SN86; -.
DR PRIDE; Q9SN86; -.
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; locus:2079177; AT3G47520.
DR eggNOG; KOG1494; Eukaryota.
DR HOGENOM; CLU_047181_0_0_1; -.
DR InParanoid; Q9SN86; -.
DR OMA; CIVECAY; -.
DR OrthoDB; 976445at2759; -.
DR PhylomeDB; Q9SN86; -.
DR BioCyc; ARA:AT3G47520-MON; -.
DR BioCyc; MetaCyc:AT3G47520-MON; -.
DR BRENDA; 1.1.1.37; 399.
DR PRO; PR:Q9SN86; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SN86; baseline and differential.
DR Genevisible; Q9SN86; AT.
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:0005737; C:cytoplasm; IBA:GO_Central.
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; -; 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 Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 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 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
