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UniProtKB/Swiss-Prot entry P59515

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

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Entry information
Entry name LEU3_BUCBP
Primary accession number P59515
Secondary accession numbers None
Integrated into Swiss-Prot on April 11, 2003
Sequence was last modified on April 11, 2003 (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: bbp_496
From
Buchnera aphidicola subsp. Baizongia pistaciae [TaxID: 135842] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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
AE016826; AAO27201.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_778096.1; -.
3D structure databases
HSSP P37412; 1CNZ. [HSSP ENTRY / PDB]
ModBase P59515.
Enzyme and pathway databases
BioCyc BAPH224915:BBP_496-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 P59515.
ProtoNet P59515.
Genome annotation databases
GeneID 1058649; -.
GenomeReviews AE016826_GR; bbp_496.
KEGG bab:bbp496; -.
Phylogenomic databases
HOGENOM P59515; -.
Genome annotation databases
CMR P59515; bbp_496.
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   366  366     3-isopropylmalate dehydrogenase. PRO_0000083656
NP_BIND   78    91  14     NAD (By similarity). 
NP_BIND   285   297  13     NAD (By similarity). 
METAL   227   227        Magnesium or manganese (By similarity). 
METAL   251   251        Magnesium or manganese (By similarity). 
METAL   255   255        Magnesium or manganese (By similarity). 
BINDING   99    99        Substrate (By similarity). 
BINDING   109   109        Substrate (By similarity). 
BINDING   138   138        Substrate (By similarity). 
BINDING   227   227        Substrate (By similarity). 
SITE   145   145  1     Important for catalysis (By similarity). 
SITE   195   195  1     Important for catalysis (By similarity). 
Sequence information
Length: 366 AA [This is the length of the unprocessed precursor] Molecular weight: 40731 Da [This is the MW of the unprocessed precursor] CRC64: 9405C5075BFEEA66 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKRNYKIAVL PGDGIGPEIM REGYKILRIL KSKLSLNIMT QEFDVGGVAI DKYGVALPKK 

        70         80         90        100        110        120 
TLQGCRDSHA ILFGSIGGPK WEDLPSHLQP ERGALLPLRK YFNLFSNLRL ARIYSGLEKL 

       130        140        150        160        170        180 
SPLKSRISNL GCDILCVREL TGGIYFGDPK GSKVSKSLNC AFDTEVYYQF EIERIAHMAF 

       190        200        210        220        230        240 
DLALTRRCKV TSIDKANVLE SSMFWRKIVN RISTQYSQVK LSHLYVDNAA MQIIKNPSQF 

       250        260        270        280        290        300 
DVLLCSNLFG DILSDECAAI TGSIGLLPSA SLNDKNFGLY EPAGGSAPDI KGKNIANPIA 

       310        320        330        340        350        360 
LILSIGMMMR YSFKLYDVAD LIDWAVNKTL KLGYRTQDIS ENNKFINTSS MGDIIAEILA 


NRIHKI
P59515 in FASTA format

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