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Protein

Branched-chain-amino-acid aminotransferase

Gene

ilvE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Pathwayi: L-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. Putative acetolactate synthase isozyme 2 large subunit (ilvG), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 2 large subunit (ilvG), 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)
  2. Ketol-acid reductoisomerase (NADP(+)) (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.

Pathwayi: L-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.

Pathwayi: L-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. Putative acetolactate synthase isozyme 2 large subunit (ilvG), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 2 large subunit (ilvG), 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)
  2. Ketol-acid reductoisomerase (NADP(+)) (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

Keywordsi

Molecular functionAminotransferase, Transferase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:BRANCHED-CHAINAMINOTRANSFER-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10497 ilvE

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Pathology & Biotechi

Chemistry databases

DrugBankiDB04063 2-Methylleucine
DB03993 4-Methyl Valeric Acid
DB03553 Glutaric Acid
DB01813 Pyridoxyl-Glutamic Acid-5'-Monophosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001032622 – 309Branched-chain-amino-acid aminotransferaseAdd BLAST308

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei160N6-(pyridoxal phosphate)lysine1

Proteomic databases

EPDiP0AB80
PaxDbiP0AB80
PRIDEiP0AB80

2D gel databases

SWISS-2DPAGEiP0AB80

Interactioni

Subunit structurei

Homohexamer.

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261272, 73 interactors
DIPiDIP-10022N
STRINGi316385.ECDH10B_3959

Structurei

Secondary structure

1309
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Beta strandi14 – 17Combined sources4
Helixi18 – 20Combined sources3
Helixi28 – 32Combined sources5
Beta strandi35 – 37Combined sources3
Beta strandi40 – 43Combined sources4
Beta strandi48 – 52Combined sources5
Helixi54 – 68Combined sources15
Helixi76 – 89Combined sources14
Beta strandi93 – 103Combined sources11
Beta strandi108 – 111Combined sources4
Beta strandi118 – 125Combined sources8
Helixi135 – 138Combined sources4
Beta strandi140 – 144Combined sources5
Turni152 – 154Combined sources3
Beta strandi157 – 159Combined sources3
Helixi162 – 164Combined sources3
Helixi165 – 177Combined sources13
Beta strandi181 – 186Combined sources6
Beta strandi190 – 195Combined sources6
Beta strandi198 – 204Combined sources7
Beta strandi207 – 210Combined sources4
Helixi213 – 215Combined sources3
Helixi221 – 232Combined sources12
Beta strandi237 – 239Combined sources3
Helixi246 – 249Combined sources4
Beta strandi251 – 257Combined sources7
Turni258 – 260Combined sources3
Beta strandi261 – 268Combined sources8
Helixi274 – 276Combined sources3
Helixi280 – 290Combined sources11
Turni291 – 294Combined sources4
Beta strandi295 – 297Combined sources3
Beta strandi304 – 306Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AB80

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CM2 Bacteria
COG0115 LUCA
HOGENOMiHOG000276706
InParanoidiP0AB80
KOiK00826
OMAiNFFGITH
PhylomeDBiP0AB80

Family and domain databases

CDDicd01557 BCAT_beta_family, 1 hit
InterProiView protein in InterPro
IPR001544 Aminotrans_IV
IPR018300 Aminotrans_IV_CS
IPR036038 Aminotransferase-like
IPR005785 B_amino_transI
IPR033939 BCAT_family
PfamiView protein in Pfam
PF01063 Aminotran_4, 1 hit
SUPFAMiSSF56752 SSF56752, 1 hit
TIGRFAMsiTIGR01122 ilvE_I, 1 hit
PROSITEiView protein in PROSITE
PS00770 AA_TRANSFER_CLASS_4, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti151A → R in AAA67573 (PubMed:1379743).Curated1

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_LN832404.1
YP_026247.1, NC_000913.3

Genome annotation databases

EnsemblBacteriaiAAT48207; AAT48207; b3770
BAE77527; BAE77527; BAE77527
GeneIDi948278
KEGGiecj:JW5606
eco:b3770
PATRICifig|511145.12.peg.3887

Similar proteinsi

Entry informationi

Entry nameiILVE_ECOLI
AccessioniPrimary (citable) accession number: P0AB80
Secondary accession number(s): P00510, Q2M879, Q47299
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 110 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health