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UniProtKB/Swiss-Prot entry Q6HLF2


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

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Entry information
Entry name LEU3_BACHK
Primary accession number Q6HLF2
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 34)
Name and origin of the protein
Protein name 3-isopropylmalate dehydrogenase
Synonyms EC 1.1.1.85
Beta-IPM dehydrogenase
IMDH
3-IPM-DH
Gene name
Name: leuB
OrderedLocusNames: BT9727_1285
From
Bacillus thuringiensis subsp. konkukian [TaxID: 180856] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=97-27;
DOI=10.1128/JB.188.9.3382-3390.2006; PubMed=16621833 [NCBI, ExPASy, EBI, Israel, Japan]
Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis.";
J. Bacteriol. 188:3382-3390(2006).
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
AE017355; AAT59415.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_035619.1; -.
3D structure databases
ModBase Q6HLF2.
Enzyme and pathway databases
BioCyc BTHU281309:BT9727_1285-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003862; Molecular function: 3-isopropylmalate dehydrogenase activity (inferred from electronic annotation from HAMAP).
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 HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01033; -; 1.
PBIL [Tree]
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.
BLOCKS Q6HLF2.
ProtoNet Q6HLF2.
Genome annotation databases
GeneID 2855825; -.
GenomeReviews AE017355_GR; BT9727_1285.
KEGG btk:BT9727_1285; -.
NMPDR fig|281309.1.peg.1259; -.
Phylogenomic databases
HOGENOM Q6HLF2; -.
Genome annotation databases
CMR Q6HLF2; BT9727_1285.
Other
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   354  354     3-isopropylmalate dehydrogenase. PRO_0000083643
NP_BIND   76    87  12     NAD (By similarity). 
NP_BIND   273   285  13     NAD (By similarity). 
METAL   215   215        Magnesium or manganese (By similarity). 
METAL   239   239        Magnesium or manganese (By similarity). 
METAL   243   243        Magnesium or manganese (By similarity). 
BINDING   94    94        Substrate (By similarity). 
BINDING   104   104        Substrate (By similarity). 
BINDING   130   130        Substrate (By similarity). 
BINDING   215   215        Substrate (By similarity). 
SITE   137   137  1     Important for catalysis (By similarity). 
SITE   183   183  1     Important for catalysis (By similarity). 
Sequence information
Length: 354 AA [This is the length of the unprocessed precursor] Molecular weight: 38274 Da [This is the MW of the unprocessed precursor] CRC64: D7F4738258A3641F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEKRIVCLAG DGVGPEVMES AKGVLHMVER LYGHHFHLQD EHFGGVAIDL TGQPLPQRTL 

        70         80         90        100        110        120 
AACLASDAVL LGAVGGPRWD GAKERPEKGL LALRKGLGVF ANVRPVTVES ATAHLSPLKK 

       130        140        150        160        170        180 
ADEIDFVVVR ELTGGIYFSY PKKRTDEVAT DTLTYHRHEI ERIVSYAFQL ASKRKKKVTS 

       190        200        210        220        230        240 
IDKANVLESS KLWRTVTEEV ALRYPDVELE HILVDAAAME LIRNPGRFDV IVTENLFGDI 

       250        260        270        280        290        300 
LSDEASVLAG SLGMLPSASH AEKGPSLYEP IHGSAPDIAG KNKANPIAMM RSVAMMLGQS 

       310        320        330        340        350 
FGLTREGCAI EEAISAVLKS GKCTADIGGA ETTTSFTKAV MQEMEEQALV GRGR 

Q6HLF2 in FASTA format

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