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Branched-chain-amino-acid aminotransferase (BCAT) (EC 2.6.1.42) (Transaminase B)

 ILVE_ECOLI              Reviewed;         309 AA.
P0AB80; P00510; Q2M879; Q47299;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 107.
RecName: Full=Branched-chain-amino-acid aminotransferase;
Short=BCAT;
EC=2.6.1.42;
AltName: Full=Transaminase B;
Name=ilvE; OrderedLocusNames=b3770, JW5606;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=3897211; DOI=10.1093/oxfordjournals.jbchem.a135176;
Kuramitsu S., Ogawa T., Ogawa H., Kagamiyama H.;
"Branched-chain amino acid aminotransferase of Escherichia coli:
nucleotide sequence of the ilvE gene and the deduced amino acid
sequence.";
J. Biochem. 97:993-999(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=3550695; DOI=10.1093/nar/15.5.2137;
Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E.,
Hatfield G.W.;
"The complete nucleotide sequence of the ilvGMEDA operon of
Escherichia coli K-12.";
Nucleic Acids Res. 15:2137-2155(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=1379743; DOI=10.1126/science.1379743;
Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
"Analysis of the Escherichia coli genome: DNA sequence of the region
from 84.5 to 86.5 minutes.";
Science 257:771-778(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
SEQUENCE REVISION TO 151.
PubMed=16397293; DOI=10.1093/nar/gkj405;
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.;
"Escherichia coli K-12: a cooperatively developed annotation snapshot
-- 2005.";
Nucleic Acids Res. 34:1-9(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[7]
PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
STRAIN=K12;
PubMed=392469; DOI=10.1093/nar/7.8.2289;
Lawther R.P., Nichols B.P., Zurawski G., Hatfield G.W.;
"The nucleotide sequence preceding and including the beginning of the
ilvE gene of the ilvGEDA operon of Escherichia coli K12.";
Nucleic Acids Res. 7:2289-2301(1979).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
PubMed=1569580; DOI=10.1016/0022-2836(92)90460-2;
Pagel J.M., Winkelman J.W., Adams C.W., Hatfield G.W.;
"DNA topology-mediated regulation of transcription initiation from the
tandem promoters of the ilvGMEDA operon of Escherichia coli.";
J. Mol. Biol. 224:919-935(1992).
[9]
PYRIDOXAL PHOSPHATE AT LYS-160.
PubMed=3069843;
Inoue K., Kuramitsu S., Aki K., Watanabe Y., Takagi T., Nishigai M.,
Ikaiu A., Kagamiyama H.;
"Branched-chain amino acid aminotransferase of Escherichia coli:
overproduction and properties.";
J. Biochem. 104:777-784(1988).
[10]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=9163511; DOI=10.1093/oxfordjournals.jbchem.a021633;
Okada K., Hirotsu K., Sato M., Hyashi H., Kagamiyama H.;
"Three-dimensional structure of Escherichia coli branched-chain amino
acid aminotransferase at 2.5-A resolution.";
J. Biochem. 121:637-641(1997).
-!- FUNCTION: Acts on leucine, isoleucine and valine.
-!- CATALYTIC ACTIVITY: L-leucine + 2-oxoglutarate = 4-methyl-2-
oxopentanoate + L-glutamate.
-!- CATALYTIC ACTIVITY: L-isoleucine + 2-oxoglutarate = (S)-3-methyl-
2-oxopentanoate + L-glutamate.
-!- CATALYTIC ACTIVITY: L-valine + 2-oxoglutarate = 3-methyl-2-
oxobutanoate + L-glutamate.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
isoleucine from 2-oxobutanoate: step 4/4.
-!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
leucine from 3-methyl-2-oxobutanoate: step 4/4.
-!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
from pyruvate: step 4/4.
-!- SUBUNIT: Homohexamer.
-!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X02413; CAA26262.1; -; Genomic_DNA.
EMBL; M32253; AAA24022.1; -; Genomic_DNA.
EMBL; M10313; AAB59052.1; -; Genomic_DNA.
EMBL; X04890; CAA28575.1; -; Genomic_DNA.
EMBL; M87049; AAA67573.1; -; Genomic_DNA.
EMBL; U00096; AAT48207.1; -; Genomic_DNA.
EMBL; AP009048; BAE77527.1; -; Genomic_DNA.
EMBL; V00290; CAA23559.1; -; Genomic_DNA.
PIR; E65180; XNECV.
RefSeq; WP_000208520.1; NZ_LN832404.1.
RefSeq; YP_026247.1; NC_000913.3.
PDB; 1A3G; X-ray; 2.50 A; A/B/C=2-309.
PDB; 1I1K; X-ray; 2.10 A; A/B/C=1-309.
PDB; 1I1L; X-ray; 2.40 A; A/B/C=1-309.
PDB; 1I1M; X-ray; 2.40 A; A/B/C=1-309.
PDB; 1IYD; X-ray; 2.15 A; A/B/C=1-309.
PDB; 1IYE; X-ray; 1.82 A; A/B/C=1-309.
PDBsum; 1A3G; -.
PDBsum; 1I1K; -.
PDBsum; 1I1L; -.
PDBsum; 1I1M; -.
PDBsum; 1IYD; -.
PDBsum; 1IYE; -.
ProteinModelPortal; P0AB80; -.
SMR; P0AB80; -.
BioGrid; 4261272; 66.
DIP; DIP-10022N; -.
STRING; 316385.ECDH10B_3959; -.
DrugBank; DB04063; 2-Methylleucine.
DrugBank; DB03993; 4-Methyl Valeric Acid.
DrugBank; DB03553; Glutaric Acid.
DrugBank; DB01813; Pyridoxyl-Glutamic Acid-5'-Monophosphate.
SWISS-2DPAGE; P0AB80; -.
PaxDb; P0AB80; -.
PRIDE; P0AB80; -.
EnsemblBacteria; AAT48207; AAT48207; b3770.
EnsemblBacteria; BAE77527; BAE77527; BAE77527.
GeneID; 948278; -.
KEGG; ecj:JW5606; -.
KEGG; eco:b3770; -.
PATRIC; fig|511145.12.peg.3887; -.
EchoBASE; EB0492; -.
EcoGene; EG10497; ilvE.
eggNOG; ENOG4105CM2; Bacteria.
eggNOG; COG0115; LUCA.
HOGENOM; HOG000276706; -.
InParanoid; P0AB80; -.
KO; K00826; -.
PhylomeDB; P0AB80; -.
BioCyc; EcoCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER; -.
BioCyc; MetaCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER; -.
BRENDA; 2.6.1.42; 2026.
UniPathway; UPA00047; UER00058.
UniPathway; UPA00048; UER00073.
UniPathway; UPA00049; UER00062.
EvolutionaryTrace; P0AB80; -.
PRO; PR:P0AB80; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
GO; GO:0006532; P:aspartate biosynthetic process; IGI:EcoliWiki.
GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009098; P:leucine biosynthetic process; IDA:EcoCyc.
GO; GO:0009099; P:valine biosynthetic process; IDA:EcoCyc.
CDD; cd01557; BCAT_beta_family; 1.
InterPro; IPR001544; Aminotrans_IV.
InterPro; IPR018300; Aminotrans_IV_CS.
InterPro; IPR036038; Aminotransferase-like.
InterPro; IPR005785; B_amino_transI.
InterPro; IPR033939; BCAT_family.
Pfam; PF01063; Aminotran_4; 1.
SUPFAM; SSF56752; SSF56752; 1.
TIGRFAMs; TIGR01122; ilvE_I; 1.
PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis; Aminotransferase;
Branched-chain amino acid biosynthesis; Complete proteome;
Pyridoxal phosphate; Reference proteome; Transferase.
INIT_MET 1 1 Removed.
CHAIN 2 309 Branched-chain-amino-acid
aminotransferase.
/FTId=PRO_0000103262.
MOD_RES 160 160 N6-(pyridoxal phosphate)lysine.
CONFLICT 151 151 A -> R (in Ref. 3; AAA67573).
{ECO:0000305}.
STRAND 7 11 {ECO:0000244|PDB:1IYE}.
STRAND 14 17 {ECO:0000244|PDB:1IYE}.
HELIX 18 20 {ECO:0000244|PDB:1IYE}.
HELIX 28 32 {ECO:0000244|PDB:1IYE}.
STRAND 35 37 {ECO:0000244|PDB:1IYE}.
STRAND 40 43 {ECO:0000244|PDB:1IYE}.
STRAND 48 52 {ECO:0000244|PDB:1IYE}.
HELIX 54 68 {ECO:0000244|PDB:1IYE}.
HELIX 76 89 {ECO:0000244|PDB:1IYE}.
STRAND 93 103 {ECO:0000244|PDB:1IYE}.
STRAND 108 111 {ECO:0000244|PDB:1IYE}.
STRAND 118 125 {ECO:0000244|PDB:1IYE}.
HELIX 135 138 {ECO:0000244|PDB:1IYE}.
STRAND 140 144 {ECO:0000244|PDB:1IYE}.
TURN 152 154 {ECO:0000244|PDB:1IYE}.
STRAND 157 159 {ECO:0000244|PDB:1I1L}.
HELIX 162 164 {ECO:0000244|PDB:1IYE}.
HELIX 165 177 {ECO:0000244|PDB:1IYE}.
STRAND 181 186 {ECO:0000244|PDB:1IYE}.
STRAND 190 195 {ECO:0000244|PDB:1IYE}.
STRAND 198 204 {ECO:0000244|PDB:1IYE}.
STRAND 207 210 {ECO:0000244|PDB:1IYE}.
HELIX 213 215 {ECO:0000244|PDB:1IYE}.
HELIX 221 232 {ECO:0000244|PDB:1IYE}.
STRAND 237 239 {ECO:0000244|PDB:1IYE}.
HELIX 246 249 {ECO:0000244|PDB:1IYE}.
STRAND 251 257 {ECO:0000244|PDB:1IYE}.
TURN 258 260 {ECO:0000244|PDB:1IYE}.
STRAND 261 268 {ECO:0000244|PDB:1IYE}.
HELIX 274 276 {ECO:0000244|PDB:1I1K}.
HELIX 280 290 {ECO:0000244|PDB:1IYE}.
TURN 291 294 {ECO:0000244|PDB:1IYE}.
STRAND 295 297 {ECO:0000244|PDB:1IYE}.
STRAND 304 306 {ECO:0000244|PDB:1IYE}.
SEQUENCE 309 AA; 34094 MW; E8A2B953168CD09D CRC64;
MTTKKADYIW FNGEMVRWED AKVHVMSHAL HYGTSVFEGI RCYDSHKGPV VFRHREHMQR
LHDSAKIYRF PVSQSIDELM EACRDVIRKN NLTSAYIRPL IFVGDVGMGV NPPAGYSTDV
IIAAFPWGAY LGAEALEQGI DAMVSSWNRA APNTIPTAAK AGGNYLSSLL VGSEARRHGY
QEGIALDVNG YISEGAGENL FEVKDGVLFT PPFTSSALPG ITRDAIIKLA KELGIEVREQ
VLSRESLYLA DEVFMSGTAA EITPVRSVDG IQVGEGRCGP VTKRIQQAFF GLFTGETEDK
WGWLDQVNQ


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