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P0AB80 (ILVE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Branched-chain-amino-acid aminotransferase

Short name=BCAT
EC=2.6.1.42
Alternative name(s):
Transaminase B
Gene names
Name:ilvE
Ordered Locus Names:b3770, JW5606
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts on leucine, isoleucine and valine.

Catalytic activity

L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.

L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate.

L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate.

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4.

Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4.

Subunit structure

Homohexamer.

Sequence similarities

Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 309308Branched-chain-amino-acid aminotransferase
PRO_0000103262

Amino acid modifications

Modified residue1601N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict1511A → R in AAA67573. Ref.3

Secondary structure

............................................................... 309
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AB80 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E8A2B953168CD09D

FASTA30934,094
        10         20         30         40         50         60 
MTTKKADYIW FNGEMVRWED AKVHVMSHAL HYGTSVFEGI RCYDSHKGPV VFRHREHMQR 

        70         80         90        100        110        120 
LHDSAKIYRF PVSQSIDELM EACRDVIRKN NLTSAYIRPL IFVGDVGMGV NPPAGYSTDV 

       130        140        150        160        170        180 
IIAAFPWGAY LGAEALEQGI DAMVSSWNRA APNTIPTAAK AGGNYLSSLL VGSEARRHGY 

       190        200        210        220        230        240 
QEGIALDVNG YISEGAGENL FEVKDGVLFT PPFTSSALPG ITRDAIIKLA KELGIEVREQ 

       250        260        270        280        290        300 
VLSRESLYLA DEVFMSGTAA EITPVRSVDG IQVGEGRCGP VTKRIQQAFF GLFTGETEDK 


WGWLDQVNQ 

« Hide

References

« Hide 'large scale' references
[1]"Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence."
Kuramitsu S., Ogawa T., Ogawa H., Kagamiyama H.
J. Biochem. 97:993-999(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"The complete nucleotide sequence of the ilvGMEDA operon of Escherichia coli K-12."
Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E., Hatfield G.W.
Nucleic Acids Res. 15:2137-2155(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005."
Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L.
Nucleic Acids Res. 34:1-9(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 151.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"The nucleotide sequence preceding and including the beginning of the ilvE gene of the ilvGEDA operon of Escherichia coli K12."
Lawther R.P., Nichols B.P., Zurawski G., Hatfield G.W.
Nucleic Acids Res. 7:2289-2301(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
Strain: K12.
[8]"DNA topology-mediated regulation of transcription initiation from the tandem promoters of the ilvGMEDA operon of Escherichia coli."
Pagel J.M., Winkelman J.W., Adams C.W., Hatfield G.W.
J. Mol. Biol. 224:919-935(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[9]"Branched-chain amino acid aminotransferase of Escherichia coli: overproduction and properties."
Inoue K., Kuramitsu S., Aki K., Watanabe Y., Takagi T., Nishigai M., Ikaiu A., Kagamiyama H.
J. Biochem. 104:777-784(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PYRIDOXAL PHOSPHATE AT LYS-160.
[10]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[11]"Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5-A resolution."
Okada K., Hirotsu K., Sato M., Hyashi H., Kagamiyama H.
J. Biochem. 121:637-641(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02413 Genomic DNA. Translation: CAA26262.1.
M32253 Genomic DNA. Translation: AAA24022.1.
M10313 Genomic DNA. Translation: AAB59052.1.
X04890 Genomic DNA. Translation: CAA28575.1.
M87049 Genomic DNA. Translation: AAA67573.1.
U00096 Genomic DNA. Translation: AAT48207.1.
AP009048 Genomic DNA. Translation: BAE77527.1.
V00290 Genomic DNA. Translation: CAA23559.1.
PIRXNECV. E65180.
RefSeqYP_026247.1. NC_000913.3.
YP_491668.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A3GX-ray2.50A/B/C2-309[»]
1I1KX-ray2.10A/B/C1-309[»]
1I1LX-ray2.40A/B/C1-309[»]
1I1MX-ray2.40A/B/C1-309[»]
1IYDX-ray2.15A/B/C1-309[»]
1IYEX-ray1.82A/B/C1-309[»]
ProteinModelPortalP0AB80.
SMRP0AB80. Positions 5-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10022N.
STRING511145.b3770.

2D gel databases

SWISS-2DPAGEP0AB80.

Proteomic databases

PaxDbP0AB80.
PRIDEP0AB80.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT48207; AAT48207; b3770.
BAE77527; BAE77527; BAE77527.
GeneID12932278.
948278.
KEGGecj:Y75_p3405.
eco:b3770.
PATRIC32123035. VBIEscCol129921_3887.

Organism-specific databases

EchoBASEEB0492.
EcoGeneEG10497. ilvE.

Phylogenomic databases

eggNOGCOG0115.
HOGENOMHOG000276706.
KOK00826.
OMAFPWGSYL.
OrthoDBEOG67MF3R.
PhylomeDBP0AB80.

Enzyme and pathway databases

BioCycEcoCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER.
ECOL316407:JW5606-MONOMER.
MetaCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER.
UniPathwayUPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.

Gene expression databases

GenevestigatorP0AB80.

Family and domain databases

InterProIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005785. B_amino_transI.
[Graphical view]
PANTHERPTHR11825. PTHR11825. 1 hit.
PfamPF01063. Aminotran_4. 1 hit.
[Graphical view]
SUPFAMSSF56752. SSF56752. 1 hit.
TIGRFAMsTIGR01122. ilvE_I. 1 hit.
PROSITEPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AB80.
PROP0AB80.

Entry information

Entry nameILVE_ECOLI
AccessionPrimary (citable) accession number: P0AB80
Secondary accession number(s): P00510, Q2M879, Q47299
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene