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UniProtKB/Swiss-Prot entry O14429


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

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Entry information
Entry name LEU3_CANGA
Primary accession number O14429
Secondary accession number Q6FS35
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on August 16, 2004 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 55)
Name and origin of the protein
Protein name 3-isopropylmalate dehydrogenase
Synonyms 3-IPM-DH
IMDH
EC 1.1.1.85
Beta-IPM dehydrogenase
Gene name
Name: LEU2
OrderedLocusNames: CAGL0H03795g
From
Candida glabrata (Yeast) (Torulopsis glabrata) [TaxID: 5478] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65;
Kitada K.;
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(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
U90626; AAB62089.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR380954; CAG59892.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_446959.1; -.
3D structure databases
HSSP P12010; 2AYQ. [HSSP ENTRY / PDB]
ModBase O14429.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
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).
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.
Genome annotation databases
GeneID 2888798; -.
KEGG cgr:CAGL0H03795g; -.
Phylogenomic databases
HOGENOM O14429; -.
Other
ProtoNet O14429.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   365  365     3-isopropylmalate dehydrogenase. PRO_0000083603
NP_BIND   80    91  12     NAD (By similarity). 
NP_BIND   290   301  12     NAD (By similarity). 
METAL   226   226        Magnesium or manganese (By similarity). 
METAL   251   251        Magnesium or manganese (By similarity). 
METAL   255   255        Magnesium or manganese (By similarity). 
BINDING   98    98        Substrate (By similarity). 
BINDING   108   108        Substrate (By similarity). 
BINDING   137   137        Substrate (By similarity). 
BINDING   226   226        Substrate (By similarity). 
SITE   144   144  1     Important for catalysis (By similarity). 
SITE   193   193  1     Important for catalysis (By similarity). 
CONFLICT   10    10        L -> P (in Ref. 1; AAB62089). 
CONFLICT   24    24        I -> N (in Ref. 1; AAB62089). 
CONFLICT   51    51        A -> P (in Ref. 1; AAB62089). 
Sequence information
Length: 365 AA [This is the length of the unprocessed precursor] Molecular weight: 39305 Da [This is the MW of the unprocessed precursor] CRC64: 05D59E0986360B82 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVTKTIVVL PGDHVGQEIT EEAIKVLNAI QECRPDKVNF KFDHHLIGGA AIDATGVPLP 

        70         80         90        100        110        120 
DEALEASKKA DAVLLGAVGG PKWGTGAVRP EQGLLKIRKE LQLYANLRPC NFASDSLLDL 

       130        140        150        160        170        180 
SPLKPEIARG TDFVVVRELV GGIYFGERKE DEGDGVAWDS EKYSVPEVQR ITRMAAFMAL 

       190        200        210        220        230        240 
QHNPPLPIWS LDKANVLASS RLWRKTVEET IKNEFPQLTV QHQLIDSAAM ILVKNPTHLN 

       250        260        270        280        290        300 
GIIITNNMFG DIISDEASVI PGSLGLLPSA SLASLPDKNT AFGLYEPCHG SAPDLPKGKV 

       310        320        330        340        350        360 
NPVATILSAA MMLKLSLDLF EEGEIIEQAV KKVLDSGIRT ADLKGTNSTT EVGDAVAKAV 


RELLA 

O14429 in FASTA format

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