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Protein

Branched-chain-amino-acid aminotransferase

Gene

ilvE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts on leucine, isoleucine and valine.

Catalytic activityi

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.

Cofactori

Pathway:iL-isoleucine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathway:iL-leucine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 2-isopropylmalate synthase (leuA)
  2. 3-isopropylmalate dehydratase small subunit (leuD), 3-isopropylmalate dehydratase large subunit (leuC)
  3. 3-isopropylmalate dehydrogenase (leuB)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-leucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate, the pathway L-leucine biosynthesis and in Amino-acid biosynthesis.

Pathway:iL-valine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

  • aspartate biosynthetic process Source: EcoliWiki
  • isoleucine biosynthetic process Source: UniProtKB-UniPathway
  • leucine biosynthetic process Source: EcoCyc
  • valine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER.
ECOL316407:JW5606-MONOMER.
MetaCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER.
BRENDAi2.6.1.42. 2026.
UniPathwayiUPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.

Names & Taxonomyi

Protein namesi
Recommended name:
Branched-chain-amino-acid aminotransferase (EC:2.6.1.42)
Short name:
BCAT
Alternative name(s):
Transaminase B
Gene namesi
Name:ilvE
Ordered Locus Names:b3770, JW5606
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10497. ilvE.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 309308Branched-chain-amino-acid aminotransferasePRO_0000103262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei160 – 1601N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiP0AB80.
PRIDEiP0AB80.

2D gel databases

SWISS-2DPAGEP0AB80.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

DIPiDIP-10022N.
STRINGi511145.b3770.

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Beta strandi14 – 174Combined sources
Helixi18 – 203Combined sources
Helixi28 – 325Combined sources
Beta strandi35 – 373Combined sources
Beta strandi40 – 434Combined sources
Beta strandi48 – 525Combined sources
Helixi54 – 6815Combined sources
Helixi76 – 8914Combined sources
Beta strandi93 – 10311Combined sources
Beta strandi108 – 1114Combined sources
Beta strandi118 – 1258Combined sources
Helixi135 – 1384Combined sources
Beta strandi140 – 1445Combined sources
Turni152 – 1543Combined sources
Beta strandi157 – 1593Combined sources
Helixi162 – 1643Combined sources
Helixi165 – 17713Combined sources
Beta strandi181 – 1866Combined sources
Beta strandi190 – 1956Combined sources
Beta strandi198 – 2047Combined sources
Beta strandi207 – 2104Combined sources
Helixi213 – 2153Combined sources
Helixi221 – 23212Combined sources
Beta strandi237 – 2393Combined sources
Helixi246 – 2494Combined sources
Beta strandi251 – 2577Combined sources
Turni258 – 2603Combined sources
Beta strandi261 – 2688Combined sources
Helixi274 – 2763Combined sources
Helixi280 – 29011Combined sources
Turni291 – 2944Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi304 – 3063Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0AB80.
SMRiP0AB80. Positions 5-308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AB80.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0115.
HOGENOMiHOG000276706.
InParanoidiP0AB80.
KOiK00826.
OMAiAMISSWN.
OrthoDBiEOG67MF3R.
PhylomeDBiP0AB80.

Family and domain databases

InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005785. B_amino_transI.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR01122. ilvE_I. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AB80-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTKKADYIW FNGEMVRWED AKVHVMSHAL HYGTSVFEGI RCYDSHKGPV
60 70 80 90 100
VFRHREHMQR LHDSAKIYRF PVSQSIDELM EACRDVIRKN NLTSAYIRPL
110 120 130 140 150
IFVGDVGMGV NPPAGYSTDV IIAAFPWGAY LGAEALEQGI DAMVSSWNRA
160 170 180 190 200
APNTIPTAAK AGGNYLSSLL VGSEARRHGY QEGIALDVNG YISEGAGENL
210 220 230 240 250
FEVKDGVLFT PPFTSSALPG ITRDAIIKLA KELGIEVREQ VLSRESLYLA
260 270 280 290 300
DEVFMSGTAA EITPVRSVDG IQVGEGRCGP VTKRIQQAFF GLFTGETEDK

WGWLDQVNQ
Length:309
Mass (Da):34,094
Last modified:January 23, 2007 - v2
Checksum:iE8A2B953168CD09D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 1511A → R in AAA67573 (PubMed:1379743).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiE65180. XNECV.
RefSeqiWP_000208520.1. NZ_CP010445.1.
YP_026247.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48207; AAT48207; b3770.
BAE77527; BAE77527; BAE77527.
GeneIDi948278.
KEGGieco:b3770.
PATRICi32123035. VBIEscCol129921_3887.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiE65180. XNECV.
RefSeqiWP_000208520.1. NZ_CP010445.1.
YP_026247.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0AB80.
SMRiP0AB80. Positions 5-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10022N.
STRINGi511145.b3770.

2D gel databases

SWISS-2DPAGEP0AB80.

Proteomic databases

PaxDbiP0AB80.
PRIDEiP0AB80.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48207; AAT48207; b3770.
BAE77527; BAE77527; BAE77527.
GeneIDi948278.
KEGGieco:b3770.
PATRICi32123035. VBIEscCol129921_3887.

Organism-specific databases

EchoBASEiEB0492.
EcoGeneiEG10497. ilvE.

Phylogenomic databases

eggNOGiCOG0115.
HOGENOMiHOG000276706.
InParanoidiP0AB80.
KOiK00826.
OMAiAMISSWN.
OrthoDBiEOG67MF3R.
PhylomeDBiP0AB80.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.
BioCyciEcoCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER.
ECOL316407:JW5606-MONOMER.
MetaCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER.
BRENDAi2.6.1.42. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AB80.
PROiP0AB80.

Family and domain databases

InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005785. B_amino_transI.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR01122. ilvE_I. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. 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).

Entry informationi

Entry nameiILVE_ECOLI
AccessioniPrimary (citable) accession number: P0AB80
Secondary accession number(s): P00510, Q2M879, Q47299
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.