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UniProtKB/Swiss-Prot entry P59028

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

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Entry information
Entry name LEU3_CHLTE
Primary accession number P59028
Secondary accession numbers None
Integrated into Swiss-Prot on October 19, 2002
Sequence was last modified on October 19, 2002 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 43)
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: CT0615
From
Chlorobium tepidum [TaxID: 1097] [HAMAP proteome]
Taxonomy Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49652 / DSM 12025 / TLS;
DOI=10.1073/pnas.132181499; PubMed=12093901 [NCBI, ExPASy, EBI, Israel, Japan]
Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium.";
Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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
AE006470; AAM71857.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_661515.1; -.
3D structure databases
HSSP P30125; 1CM7. [HSSP ENTRY / PDB]
ModBase P59028.
Enzyme and pathway databases
BioCyc CTEP194439:CT_0615-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 P59028.
ProtoNet P59028.
Genome annotation databases
GeneID 1006259; -.
GenomeReviews AE006470_GR; CT0615.
KEGG cte:CT0615; -.
NMPDR fig|194439.1.peg.609; -.
TIGR CT0615; -.
Phylogenomic databases
HOGENOM P59028; -.
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   352  352     3-isopropylmalate dehydrogenase. PRO_0000083678
NP_BIND   76    89  14     NAD (By similarity). 
NP_BIND   277   289  13     NAD (By similarity). 
METAL   220   220        Magnesium or manganese (By similarity). 
METAL   244   244        Magnesium or manganese (By similarity). 
METAL   248   248        Magnesium or manganese (By similarity). 
BINDING   96    96        Substrate (By similarity). 
BINDING   106   106        Substrate (By similarity). 
BINDING   134   134        Substrate (By similarity). 
BINDING   220   220        Substrate (By similarity). 
SITE   141   141  1     Important for catalysis (By similarity). 
SITE   188   188  1     Important for catalysis (By similarity). 
Sequence information
Length: 352 AA [This is the length of the unprocessed precursor] Molecular weight: 38169 Da [This is the MW of the unprocessed precursor] CRC64: 28F202BC704BB3A0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MMYKIVSIPG DGIGPEVVAG ALDVLNAVAK KHGFEVSVEE HLFGGASYDV HGSMLTDETL 

        70         80         90        100        110        120 
EACKNCDAVL LGAVGGYKWE NLPHDKKPEA ALLKIRKELG LFANLRPARV YDALVASSTL 

       130        140        150        160        170        180 
KTEVVQGTDF MVFRELTGGI YFGQPRGYDE TRGWNTMVYE RYEVERIARL AFEYAQKRGN 

       190        200        210        220        230        240 
AKVTSIDKAN VLEVSQFWRN IVHEVHQDFP EIELVDMYVD NAAMQVVRNP KQFEVIVTSN 

       250        260        270        280        290        300 
LFGDILSDIS GMITGSLGML PSASIGSEHA LYEPIHGSAP DIAGQNKANP IATIASVAMM 

       310        320        330        340        350 
FENSFNRPEV AADIYAAIEG ALAAGFRTGD IAAAGEAISS TTEMTAAIVA RI
P59028 in FASTA format

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