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UniProtKB/Swiss-Prot entry Q9SN86


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MDHP_ARATH
Primary accession number Q9SN86
Secondary accession number O81844
Integrated into Swiss-Prot on February 21, 2006
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Malate dehydrogenase, chloroplastic [Precursor]
Synonyms EC 1.1.1.37
pNAD-MDH
Gene name
OrderedLocusNames: At3g47520
ORFNames: F1P2.70
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
TISSUE=Leaf;
DOI=10.1074/jbc.273.43.27927; PubMed=9774405 [NCBI, ExPASy, EBI, Israel, Japan]
Berkemeyer M., Scheibe R., Ocheretina O.;
"A novel, non-redox-regulated NAD-dependent malate dehydrogenase from chloroplasts of Arabidopsis thaliana L.";
J. Biol. Chem. 273:27927-27933(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1074/mcp.M300030-MCP200; PubMed=12766230 [NCBI, ExPASy, EBI, Israel, Japan]
Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.;
"Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana.";
Mol. Cell. Proteomics 2:325-345(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y13987; CAA74320.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL132955; CAB61978.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128281; AAM91090.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000621; AAN18188.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T45712; T45712.
T51862; T51862.
RefSeq NP_190336.1; -.
UniGene At.20474
3D structure databases
HSSP P00346; 1MLD. [HSSP ENTRY / PDB]
ModBase Q9SN86.
Organism-specific databases
TAIR At3g47520; -.
Gene expression databases
GermOnline AT3G47520; Arabidopsis thaliana.
Ontologies
GO
GO:0048046; Cellular component: apoplast (inferred from direct assay from TAIR).
GO:0009941; Cellular component: chloroplast envelope (inferred from direct assay from TAIR).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from TAIR).
GO:0010319; Cellular component: stromule (inferred from direct assay from TAIR).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0030060; Molecular function: L-malate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
GO:0006108; Biological process: malate metabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099; Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001557; L-lactate/malate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
IPR001252; Malate_DHase_AS.
IPR010097; Malate_DHase_NAD-dep_euk_g_bac.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.90.110.10; lact_mal_DH; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11540:SF1; MDH_euk_g_bac; 1.
Pfam PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000102; Lac_mal_DH; 1.
TIGRFAMs TIGR01772; MDH_euk_gproteo; 1.
PROSITE PS00068; MDH; 1.
ProtoNet Q9SN86.
Proteomic databases
ProMEX Q9SN86; -.
Genome annotation databases
GeneID 823906; -.
GenomeReviews BA000014_GR; AT3G47520.
KEGG ath:AT3G47520; -.
NMPDR fig|3702.1.peg.15975; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chloroplast; Complete proteome; NAD; Oxidoreductase; Plastid; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    80  80     Chloroplast (Potential). 
CHAIN   81   403  323     Malate dehydrogenase, chloroplastic. PRO_0000224149
NP_BIND   89    95  7     NAD (By similarity). 
NP_BIND   198   200  3     NAD (By similarity). 
ACT_SITE   258   258        Proton acceptor (By similarity). 
BINDING   115   115        NAD (By similarity). 
BINDING   162   162        Substrate (By similarity). 
BINDING   168   168        Substrate (By similarity). 
BINDING   175   175        NAD (By similarity). 
BINDING   200   200        Substrate (By similarity). 
BINDING   234   234        Substrate (By similarity). 
BINDING   309   309        NAD (By similarity). 
CONFLICT   57    57        A -> T (in Ref. 1; CAA74320). 
CONFLICT   66    66        K -> N (in Ref. 1; CAA74320). 
Sequence information
Length: 403 AA [This is the length of the unprocessed precursor] Molecular weight: 42406 Da [This is the MW of the unprocessed precursor] CRC64: 65B54DE66392D229 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATATSASLF STVSSSYSKA SSIPHSRLQS VKFNSVPSFT GLKSTSLISG SDSSSLAKTL 

        70         80         90        100        110        120 
RGSVTKAQTS DKKPYGFKIN ASYKVAVLGA AGGIGQPLSL LIKMSPLVST LHLYDIANVK 

       130        140        150        160        170        180 
GVAADLSHCN TPSQVRDFTG PSELADCLKD VNVVVIPAGV PRKPGMTRDD LFNINANIVK 

       190        200        210        220        230        240 
TLVEAVAENC PNAFIHIISN PVNSTVPIAA EVLKKKGVYD PKKLFGVTTL DVVRANTFVS 

       250        260        270        280        290        300 
QKKNLKLIDV DVPVIGGHAG ITILPLLSKT KPSVNFTDEE IQELTVRIQN AGTEVVDAKA 

       310        320        330        340        350        360 
GAGSATLSMA YAAARFVESS LRALDGDGDV YECSFVESTL TDLPFFASRV KIGKNGLEAV 

       370        380        390        400 
IESDLQGLTE YEQKALEALK VELKASIDKG VAFANKPAAA AAN 

Q9SN86 in FASTA format

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