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UniProtKB/Swiss-Prot entry Q01987

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

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Entry information
Entry name LEU3_CANBO
Primary accession number Q01987
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on April 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 53)
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
From
Candida boidinii (Yeast) [TaxID: 5477] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1522074 [NCBI, ExPASy, EBI, Israel, Japan]
Sakai Y., Tani Y.;
"Directed mutagenesis in an asporogenous methylotrophic yeast: cloning, sequencing, and one-step gene disruption of the 3-isopropylmalate dehydrogenase gene (LEU2) of Candida boidinii to derive doubly auxotrophic marker strains.";
J. Bacteriol. 174:5988-5993(1992).
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
M98832; AAA34349.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A43324; A43324.
3D structure databases
HSSP P12010; 2AYQ. [HSSP ENTRY / PDB]
ModBase Q01987.
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.
ProtoNet Q01987.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; 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_0000083602
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). 
Sequence information
Length: 365 AA [This is the length of the unprocessed precursor] Molecular weight: 39124 Da [This is the MW of the unprocessed precursor] CRC64: D3B0B89858653BCF [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSIIEKKIVL LPGDHVGVEV VEEAVKILKS ISEVKPEIQF KFENHLIGGA AIDATGVPLP 

        70         80         90        100        110        120 
DEALEAAKKS DAVLLGAVGG PKWGTGEVRP EQGLLKIRKE LNLYANLRPC NFASDKLLDL 

       130        140        150        160        170        180 
SPLKSDIVKG TDFTVVRELV GGIYFGDRVE DDGSGFASDS ESYSVPEVER ITRMAAFLSL 

       190        200        210        220        230        240 
QNDPPLPIWS LDKANVLASS RLWRKTVDRV IKEEFPKLTV QHQLIDSAAM ILVKSPTKLN 

       250        260        270        280        290        300 
GIVITNNMFG DIISDEASVI PGSLGLLPSA SLASLPDTNQ AFGLYEPCHG SAPDLPKNKV 

       310        320        330        340        350        360 
NPIATILSAA MMLKLSLNLV KEGNAVEEAV RKVLDQGIMT GDLGGNNSTT EVGDAIAKEV 


KLLLA
Q01987 in FASTA format

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