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UniProtKB/Swiss-Prot entry Q9FMT1


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

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Entry information
Entry name LEU33_ARATH
Primary accession number Q9FMT1
Secondary accession number Q8VXU4
Integrated into Swiss-Prot on July 11, 2002
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 54)
Name and origin of the protein
Protein name 3-isopropylmalate dehydrogenase 3, chloroplastic [Precursor]
Synonyms 3-IPM-DH 3
IMDH 3
EC 1.1.1.85
Beta-IPM dehydrogenase 3
Gene name
Name: IMDH3
OrderedLocusNames: At5g14200
ORFNames: MUA22.20
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 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/4.6.401; PubMed=9501997 [NCBI, ExPASy, EBI, Israel, Japan]
Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones.";
DNA Res. 4:401-414(1997).
[2]
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).
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
AB007650; BAB08299.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY074587; AAL67125.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_196924.1; -.
UniGene At.6515
3D structure databases
HSSP Q56268; 1A05. [HSSP ENTRY / PDB]
ModBase Q9FMT1.
Organism-specific databases
TAIR At5g14200; -.
Ontologies
GO
GO:0009570; Cellular component: chloroplast stroma (inferred from direct assay from TAIR).
GO:0003862; Molecular function: 3-isopropylmalate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009098; Biological process: leucine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009651; Biological process: response to salt stress (inferred from expression pattern from TAIR).
QuickGo view.
Family and domain databases
InterPro IPR004429; 3-isopropylmalate_DHase.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
PTHR11835:SF13; IPMDH; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00169; leuB; 1.
PROSITE PS00470; IDH_IMDH; 1.
Proteomics databases
PRIDE Q9FMT1; -.
Genome annotation databases
GeneID 831270; -.
GenomeReviews BA000015_GR; AT5G14200.
NMPDR fig|3702.1.peg.23549; -.
Other
ProtoNet Q9FMT1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Chloroplast; Complete proteome; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase; Plastid; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    37  37     Chloroplast (Potential). 
CHAIN   38   409  372     3-isopropylmalate dehydrogenase 3, chloroplastic. PRO_0000014455
NP_BIND   120   133  14     NAD (By similarity). 
NP_BIND   326   338  13     NAD (By similarity). 
METAL   268   268        Magnesium or manganese (By similarity). 
METAL   292   292        Magnesium or manganese (By similarity). 
METAL   296   296        Magnesium or manganese (By similarity). 
BINDING   140   140        Substrate (By similarity). 
BINDING   150   150        Substrate (By similarity). 
BINDING   178   178        Substrate (By similarity). 
BINDING   268   268        Substrate (By similarity). 
SITE   185   185  1     Important for catalysis (By similarity). 
SITE   236   236  1     Important for catalysis (By similarity). 
CONFLICT   251   251        T -> A (in Ref. 2; AAL67125). 
Sequence information
Length: 409 AA [This is the length of the unprocessed precursor] Molecular weight: 44162 Da [This is the MW of the unprocessed precursor] CRC64: 471293D4C3FB55DD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAFLQTNIS LNAIKIVPGK YSSLTDHQFR APYRIRCAAA SPGKKRYNIA LLPGDGIGPE 

        70         80         90        100        110        120 
VISVAKNVLQ KAGSLEGLEF DFKEMPVGGA ALDLVGVPLP EETFTAAKLS DAILLGAIGG 

       130        140        150        160        170        180 
YKWDKNEKHL RPEMALFYLR RDLKVFANLR PATVLPQLVD ASTLKKEVAE GVDMMIVREL 

       190        200        210        220        230        240 
TGGIYFGEPR GITINENGEE VGVSTEIYAA HEIDRIARVA FETARKRRGK LCSVDKANVL 

       250        260        270        280        290        300 
DASILWRKRV TALASEYPDV ELSHMYVDNA AMQLIRDPKQ FDTIVTNNIF GDILSDEASM 

       310        320        330        340        350        360 
ITGSIGMLPS ASLGESGPGL FEPIHGSAPD IAGQDKANPL ATILSAAMLL KYGLGEEKAA 

       370        380        390        400 
KRIEDAVVDA LNKGFRTGDI YSPGNKLVGC KEMGEEVLKS VESKVPATV 

Q9FMT1 in FASTA format

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