Branched-chain-amino-acid aminotransferase - Escherichia coli (strain K12)

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P0AB80 (ILVE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aspartate biosynthetic process Inferred from genetic interaction PubMed 15983. Source: EcoliWiki isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway leucine biosynthetic process Inferred from direct assay PubMed 378964. Source: EcoCyc valine biosynthetic process Inferred from direct assay PubMed 378964. Source: EcoCyc
Molecular_function	L-isoleucine transaminase activity Inferred from electronic annotation. Source: EC L-leucine transaminase activity Inferred from electronic annotation. Source: EC L-valine transaminase activity Inferred from electronic annotation. Source: EC branched-chain-amino-acid transaminase activity Inferred from direct assay PubMed 378964. Source: EcoCyc identical protein binding Inferred from direct assay PubMed 378964. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 309

308

Branched-chain-amino-acid aminotransferase

PRO_0000103262

Amino acid modifications

Modified residue

160

N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict

151

A → R in AAA67573. Ref.3

Secondary structure

309

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AB80 [UniParc].

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

FASTA

309

34,094

        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' referencesShow '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 277:1453-1474(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.

PIR

XNECV. E65180.

RefSeq

YP_026247.1. NC_000913.2.
YP_491668.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A3G	X-ray	2.50	A/B/C	2-309	[»]
1I1K	X-ray	2.10	A/B/C	1-309	[»]
1I1L	X-ray	2.40	A/B/C	1-309	[»]
1I1M	X-ray	2.40	A/B/C	1-309	[»]
1IYD	X-ray	2.15	A/B/C	1-309	[»]
1IYE	X-ray	1.82	A/B/C	1-309	[»]

ProteinModelPortal

P0AB80.

SMR

P0AB80. Positions 5-308.

ModBase

Search...

Protein-protein interaction databases

STRING

511145.b3770.

2D gel databases

SWISS-2DPAGE

P0AB80.

Proteomic databases

PaxDb

P0AB80.

PRIDE

P0AB80.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAT48207; AAT48207; b3770.
BAE77527; BAE77527; BAE77527.

GeneID

12932278.
948278.

KEGG

ecj:Y75_p3405.
eco:b3770.

PATRIC

32123035. VBIEscCol129921_3887.

Organism-specific databases

EchoBASE

EB0492.

EcoGene

EG10497. ilvE.

Phylogenomic databases

eggNOG

COG0115.

HOGENOM

HOG000276706.

K00826.

OMA

RCYNSHK.

ProtClustDB

PRK06606.

Enzyme and pathway databases

BioCyc

EcoCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER.
ECOL316407:JW5606-MONOMER.
MetaCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER.

UniPathway

UPA00047; UER00058.
UPA00048; UER00073.
UPA00049; UER00062.

Gene expression databases

Genevestigator

P0AB80.

Family and domain databases

InterPro

IPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005785. B_amino_transI.
[Graphical view]

PANTHER

PTHR11825. PTHR11825. 1 hit.

Pfam

PF01063. Aminotran_4. 1 hit.
[Graphical view]

SUPFAM

SSF56752. Aminotrans_IV. 1 hit.

TIGRFAMs

TIGR01122. ilvE_I. 1 hit.

PROSITE

PS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AB80.

Entry information

Entry name

ILVE_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents