ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q89X19

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name LEU32_BRAJA
Primary accession number Q89X19
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 2003
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 37)
Name and origin of the protein
Protein name 3-isopropylmalate dehydrogenase 2
Synonyms EC 1.1.1.85
Beta-IPM dehydrogenase 2
IMDH 2
3-IPM-DH 2
Gene name
Name: leuB2
OrderedLocusNames: bll0504
From
Bradyrhizobium japonicum [TaxID: 375] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Bradyrhizobium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(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
BA000040; BAC45768.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_767143.1; -.
3D structure databases
HSSP Q56268; 1A05. [HSSP ENTRY / PDB]
ModBase Q89X19.
Enzyme and pathway databases
BioCyc BJAP224911:BLL0504-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:0009098; Biological process: leucine biosynthetic process (inferred from electronic annotation from HAMAP).
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 Q89X19.
Genome annotation databases
GeneID 1049819; -.
GenomeReviews BA000040_GR; bll0504.
KEGG bja:bll0504; -.
NMPDR fig|224911.1.peg.503; -.
Phylogenomic databases
HOGENOM Q89X19; -.
Genome annotation databases
CMR Q89X19; bll0504.
Other
ProtoNet Q89X19.
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   370  370     3-isopropylmalate dehydrogenase 2. PRO_0000083652
NP_BIND   77    90  14     NAD (By similarity). 
NP_BIND   290   302  13     NAD (By similarity). 
METAL   226   226        Magnesium or manganese (By similarity). 
METAL   250   250        Magnesium or manganese (By similarity). 
METAL   254   254        Magnesium or manganese (By similarity). 
BINDING   97    97        Substrate (By similarity). 
BINDING   107   107        Substrate (By similarity). 
BINDING   135   135        Substrate (By similarity). 
BINDING   226   226        Substrate (By similarity). 
SITE   142   142  1     Important for catalysis (By similarity). 
SITE   193   193  1     Important for catalysis (By similarity). 
Sequence information
Length: 370 AA [This is the length of the unprocessed precursor] Molecular weight: 39707 Da [This is the MW of the unprocessed precursor] CRC64: 54FB249F9F1578AD [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MATHKLLLLP GDGIGPEVMG EVKRLIDWLN SAGIAKFETD TGLVGGSAYD AHKVSISEGD 

        70         80         90        100        110        120 
MAKALAADAI IFGAVGGPKW DAVPYEVRPE AGLLRLRKDL GLFANLRPAV CYPALADASS 

       130        140        150        160        170        180 
LKREAVEGLD IMIVRELTGG VYFGEPKTIT DLGNGQKRAI DTQVYDTYEI ERIARVAFDL 

       190        200        210        220        230        240 
AKKRKNKVTS MEKRNVMKSG VLWNEVVTQV HKREYPDVTL EHQLADSGGM MLVKWPKQFD 

       250        260        270        280        290        300 
VIVTDNLFGD MLSDIAAMLT GSLGMLPSAS LGEVDVKSKK RKALYEPVHG SAPDIAGKGL 

       310        320        330        340        350        360 
ANPIAMISSF GMALRYSFDM GALADKVDAA IAAVLASGLR TADIKSEGTT AASTTQMGEA 

       370 
ILKELQKLHA
Q89X19 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!