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UniProtKB/Swiss-Prot entry Q9ZP06


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

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Entry information
Entry name MDHM1_ARATH
Primary accession number Q9ZP06
Secondary accession numbers Q8LBB9 Q9MAH7
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 85)
Name and origin of the protein
Protein name Malate dehydrogenase 1, mitochondrial [Precursor]
Synonyms EC 1.1.1.37
mNAD-MDH 1
Gene name
OrderedLocusNames: At1g53240
ORFNames: F12M16.14
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].
STRAIN=cv. Columbia;
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=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 23-37, AND SUBCELLULAR LOCATION.
TISSUE=Leaf, and Stem;
DOI=10.1104/pp.127.4.1694; PubMed=11743114 [NCBI, ExPASy, EBI, Israel, Japan]
Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
"Proteomic approach to identify novel mitochondrial proteins in Arabidopsis.";
Plant Physiol. 127:1694-1710(2001).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1105/tpc.016055; PubMed=14671022 [NCBI, ExPASy, EBI, Israel, Japan]
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins.";
Plant Cell 16:241-256(2004).
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
AJ131205; CAA10320.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC008007; AAF69549.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF324670; AAG40021.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF339684; AAK00366.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY062580; AAL32658.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128783; AAM91183.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087304; AAM64855.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T51311; T51311.
RefSeq NP_564625.1; -.
UniGene At.23771
3D structure databases
HSSP P00346; 1MLD. [HSSP ENTRY / PDB]
ModBase Q9ZP06.
2D gel databases
SWISS-2DPAGE Q9ZP06; -.
Organism-specific databases
GeneFarm 2023; 159.
TAIR At1g53240; -.
Gene expression databases
ArrayExpress Q9ZP06; -.
GermOnline AT1G53240; Arabidopsis thaliana.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
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 Q9ZP06.
Proteomic databases
ProMEX Q9ZP06; -.
Genome annotation databases
GeneID 841757; -.
GenomeReviews CT485782_GR; AT1G53240.
KEGG ath:AT1G53240; -.
NMPDR fig|3702.1.peg.4820; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    22  22     Mitochondrion. 
CHAIN   23   341  319     Malate dehydrogenase 1, mitochondrial. PRO_0000018622
NP_BIND   36    42  7     NAD (By similarity). 
NP_BIND   145   147  3     NAD (By similarity). 
ACT_SITE   205   205        Proton acceptor (By similarity). 
BINDING   62    62        NAD (By similarity). 
BINDING   109   109        Substrate (By similarity). 
BINDING   115   115        Substrate (By similarity). 
BINDING   122   122        NAD (By similarity). 
BINDING   147   147        Substrate (By similarity). 
BINDING   181   181        Substrate (By similarity). 
BINDING   256   256        NAD (By similarity). 
CONFLICT   17    17        V -> A (in Ref. 4; AAM64855). 
Sequence information
Length: 341 AA [This is the length of the unprocessed precursor] Molecular weight: 35804 Da [This is the MW of the unprocessed precursor] CRC64: D035C4C38785BE57 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFRSMLVRSS ASAKQAVIRR SFSSGSVPER KVAILGAAGG IGQPLALLMK LNPLVSSLSL 

        70         80         90        100        110        120 
YDIANTPGVA ADVGHINTRS EVVGYMGDDN LAKALEGADL VIIPAGVPRK PGMTRDDLFN 

       130        140        150        160        170        180 
INAGIVKNLC TAIAKYCPHA LINMISNPVN STVPIAAEIF KKAGMYDEKK LFGVTTLDVV 

       190        200        210        220        230        240 
RARTFYAGKA NVPVAEVNVP VIGGHAGVTI LPLFSQATPQ ANLSSDILTA LTKRTQDGGT 

       250        260        270        280        290        300 
EVVEAKAGKG SATLSMAYAG ALFADACLKG LNGVPDVIEC SYVQSTITEL PFFASKVRLG 

       310        320        330        340 
KNGVEEVLDL GPLSDFEKEG LEALKPELKS SIEKGVKFAN Q 

Q9ZP06 in FASTA format

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