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UniProtKB/Swiss-Prot entry Q9ABN3

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

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Entry information
Entry name LEU3_CAUCR
Primary accession number Q9ABN3
Secondary accession numbers None
Integrated into Swiss-Prot on October 19, 2002
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 53)
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: CC_0193
From
Caulobacter crescentus (Caulobacter vibrioides) [TaxID: 155892] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; Caulobacteraceae; Caulobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 19089 / CB15;
DOI=10.1073/pnas.061029298; PubMed=11259647 [NCBI, ExPASy, EBI, Israel, Japan]
Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R., Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
"Complete genome sequence of Caulobacter crescentus.";
Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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
AE005673; AAK22180.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H87272; H87272.
RefSeq NP_419012.1; -.
3D structure databases
HSSP Q56268; 1A05. [HSSP ENTRY / PDB]
ModBase Q9ABN3.
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.
ProtoNet Q9ABN3.
Genome annotation databases
GeneID 944254; -.
GenomeReviews AE005673_GR; CC_0193.
KEGG ccr:CC_0193; -.
NMPDR fig|190650.1.peg.192; -.
TIGR CC_0193; -.
Phylogenomic databases
HOGENOM Q9ABN3; -.
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   350  350     3-isopropylmalate dehydrogenase. PRO_0000083677
NP_BIND   71    84  14     NAD (By similarity). 
NP_BIND   279   291  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   91    91        Substrate (By similarity). 
BINDING   101   101        Substrate (By similarity). 
BINDING   129   129        Substrate (By similarity). 
BINDING   220   220        Substrate (By similarity). 
SITE   136   136  1     Important for catalysis (By similarity). 
SITE   187   187  1     Important for catalysis (By similarity). 
Sequence information
Length: 350 AA [This is the length of the unprocessed precursor] Molecular weight: 37012 Da [This is the MW of the unprocessed precursor] CRC64: 0C5748110F9DE506 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MATLLLLPGD GIGPEVCAQV RRVAAALTPD LKVDEALYGG ASYDTHGTPL TDEVREQALA 

        70         80         90        100        110        120 
SDAVLMGAVG GPKWADAPRH LRPEAGLLNL RKAMDVFANL RPAYCFEALA GASSLKPELV 

       130        140        150        160        170        180 
SGLDIMFVRE LVGGVYFGQP RGIEDLADGQ KKGFDTQVYT TSEIERVGRV AFELARGRTN 

       190        200        210        220        230        240 
KVHSAEKSNV MESGLLWKQV ITELHAREYP DVQLEHILAD NCAMQLVRAP KQFDVIVTDN 

       250        260        270        280        290        300 
LFGDILSDAA AMLTGSLGML PSAALGAPGK PGLYEPIHGS APDIAGKGLA NPLAAILSFE 

       310        320        330        340        350 
MALRWSLKQT EAADALLAAV KAALDNGART RDLGGSLTTT QMGDAVLAAL
Q9ABN3 in FASTA format

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