ID   TYRB_ECOLI              Reviewed;         397 AA.
AC   P04693; Q2M6Q0;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   24-JAN-2024, entry version 189.
DE   RecName: Full=Aromatic-amino-acid aminotransferase;
DE            Short=ARAT;
DE            Short=AROAT;
DE            EC=2.6.1.57;
DE   AltName: Full=Beta-methylphenylalanine transaminase;
DE            EC=2.6.1.107;
GN   Name=tyrB; OrderedLocusNames=b4054, JW4014;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3521591; DOI=10.1042/bj2340593;
RA   Fotheringham I.G., Dacey S.A., Taylor P.P., Smith T.J., Hunter M.G.,
RA   Finlay M.E., Primrose S.B., Parker D.M., Edwards R.M.;
RT   "The cloning and sequence analysis of the aspC and tyrB genes from
RT   Escherichia coli K12. Comparison of the primary structures of the aspartate
RT   aminotransferase and aromatic aminotransferase of E. coli with those of the
RT   pig aspartate aminotransferase isoenzymes.";
RL   Biochem. J. 234:593-604(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3907634; DOI=10.1016/0006-291x(85)91851-0;
RA   Kuramitsu S., Inoue K., Ogawa T., Ogawa H., Kagamiyama H.;
RT   "Aromatic amino acid aminotransferase of Escherichia coli: nucleotide
RT   sequence of the tyrB gene.";
RL   Biochem. Biophys. Res. Commun. 133:134-139(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA   Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT   from 89.2 to 92.8 minutes.";
RL   Nucleic Acids Res. 21:5408-5417(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RC   STRAIN=K12;
RX   PubMed=3308851; DOI=10.1128/jb.169.10.4710-4715.1987;
RA   Yang J., Pittard J.;
RT   "Molecular analysis of the regulatory region of the Escherichia coli K-12
RT   tyrB gene.";
RL   J. Bacteriol. 169:4710-4715(1987).
RN   [7]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [8]
RP   FUNCTION AS BETA-METHYLPHENYLALANINE TRANSAMINASE, AND CATALYTIC ACTIVITY.
RX   PubMed=19731276; DOI=10.1002/cbic.200900351;
RA   Huang Y.T., Lyu S.Y., Chuang P.H., Hsu N.S., Li Y.S., Chan H.C.,
RA   Huang C.J., Liu Y.C., Wu C.J., Yang W.B., Li T.L.;
RT   "In vitro characterization of enzymes involved in the synthesis of
RT   nonproteinogenic residue (2S,3S)-beta-methylphenylalanine in glycopeptide
RT   antibiotic mannopeptimycin.";
RL   ChemBioChem 10:2480-2487(2009).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX   PubMed=10417420; DOI=10.1107/s0907444999006630;
RA   Ko T.-P., Wu S.-P., Yang W.-Z., Tsai H., Yuan H.S.;
RT   "Crystallization and preliminary crystallographic analysis of the
RT   Escherichia coli tyrosine aminotransferase.";
RL   Acta Crystallogr. D 55:1474-1477(1999).
CC   -!- FUNCTION: Broad-specificity enzyme that catalyzes the transamination of
CC       2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield
CC       leucine, tyrosine, and phenylalanine, respectively. In vitro, is able
CC       to catalyze the conversion of beta-methyl phenylpyruvate to the
CC       nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a
CC       building block of the antibiotic mannopeptimycin produced by
CC       Streptomyces hygroscopicus NRRL3085. {ECO:0000269|PubMed:19731276}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic
CC         oxo-acid + L-glutamate; Xref=Rhea:RHEA:17533, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:73309, ChEBI:CHEBI:84824; EC=2.6.1.57;
CC         Evidence={ECO:0000269|PubMed:19731276};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3S)-3-methylphenylalanine + 2-oxoglutarate = (3S)-2-oxo-3-
CC         phenylbutanoate + L-glutamate; Xref=Rhea:RHEA:39911,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:74119,
CC         ChEBI:CHEBI:76864; EC=2.6.1.107;
CC         Evidence={ECO:0000269|PubMed:19731276};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC       phenylalanine from phenylpyruvate (ArAT route): step 1/1.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine
CC       from (4-hydroxyphenyl)pyruvate: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; X03628; CAA27278.1; -; Genomic_DNA.
DR   EMBL; M12047; AAA24703.1; -; Genomic_DNA.
DR   EMBL; U00006; AAC43148.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77024.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78056.1; -; Genomic_DNA.
DR   EMBL; M17809; AAA24704.1; -; Genomic_DNA.
DR   PIR; A30379; XNECY.
DR   RefSeq; NP_418478.1; NC_000913.3.
DR   RefSeq; WP_000486985.1; NZ_SSZK01000016.1.
DR   PDB; 3FSL; X-ray; 2.35 A; A/B/C/D/E/F=1-397.
DR   PDB; 3TAT; X-ray; 3.50 A; A/B/C/D/E/F=1-397.
DR   PDBsum; 3FSL; -.
DR   PDBsum; 3TAT; -.
DR   AlphaFoldDB; P04693; -.
DR   SMR; P04693; -.
DR   BioGRID; 4262667; 9.
DR   IntAct; P04693; 2.
DR   STRING; 511145.b4054; -.
DR   jPOST; P04693; -.
DR   PaxDb; 511145-b4054; -.
DR   EnsemblBacteria; AAC77024; AAC77024; b4054.
DR   GeneID; 948563; -.
DR   KEGG; ecj:JW4014; -.
DR   KEGG; eco:b4054; -.
DR   PATRIC; fig|511145.12.peg.4173; -.
DR   EchoBASE; EB1033; -.
DR   eggNOG; COG1448; Bacteria.
DR   HOGENOM; CLU_032440_1_2_6; -.
DR   InParanoid; P04693; -.
DR   OMA; SWAIRYF; -.
DR   OrthoDB; 9766445at2; -.
DR   PhylomeDB; P04693; -.
DR   BioCyc; EcoCyc:TYRB-MONOMER; -.
DR   BioCyc; MetaCyc:TYRB-MONOMER; -.
DR   BRENDA; 2.6.1.57; 2026.
DR   UniPathway; UPA00121; UER00347.
DR   UniPathway; UPA00122; UER00350.
DR   EvolutionaryTrace; P04693; -.
DR   PRO; PR:P04693; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IMP:EcoCyc.
DR   GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IDA:EcoCyc.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoliWiki.
DR   GO; GO:0006532; P:aspartate biosynthetic process; IGI:EcoliWiki.
DR   GO; GO:0033585; P:L-phenylalanine biosynthetic process from chorismate via phenylpyruvate; IDA:EcoCyc.
DR   GO; GO:0009098; P:leucine biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0019292; P:tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate; IDA:EcoCyc.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR000796; Asp_trans.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11879:SF37; AROMATIC-AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aminotransferase;
KW   Aromatic amino acid biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..397
FT                   /note="Aromatic-amino-acid aminotransferase"
FT                   /id="PRO_0000123892"
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         247
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   HELIX           12..21
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           47..58
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:3TAT"
FT   HELIX           73..84
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           89..92
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   STRAND          96..102
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           103..118
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   STRAND          124..129
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           132..140
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   STRAND          145..148
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   TURN            153..156
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           160..167
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   STRAND          175..178
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   TURN            184..186
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           192..204
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   STRAND          208..214
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   STRAND          218..220
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           224..226
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           227..234
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   STRAND          239..244
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   TURN            246..250
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           252..254
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   STRAND          257..262
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           266..281
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   TURN            282..284
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           290..299
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           302..333
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           341..344
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   STRAND          347..351
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           356..364
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   STRAND          372..374
FT                   /evidence="ECO:0007829|PDB:3TAT"
FT   STRAND          375..377
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           378..380
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   TURN            383..385
FT                   /evidence="ECO:0007829|PDB:3FSL"
FT   HELIX           386..396
FT                   /evidence="ECO:0007829|PDB:3FSL"
SQ   SEQUENCE   397 AA;  43538 MW;  46E69B4B8378BA6B CRC64;
     MFQKVDAYAG DPILTLMERF KEDPRSDKVN LSIGLYYNED GIIPQLQAVA EAEARLNAQP
     HGASLYLPME GLNCYRHAIA PLLFGADHPV LKQQRVATIQ TLGGSGALKV GADFLKRYFP
     ESGVWVSDPT WENHVAIFAG AGFEVSTYPW YDEATNGVRF NDLLATLKTL PARSIVLLHP
     CCHNPTGADL TNDQWDAVIE ILKARELIPF LDIAYQGFGA GMEEDAYAIR AIASAGLPAL
     VSNSFSKIFS LYGERVGGLS VMCEDAEAAG RVLGQLKATV RRNYSSPPNF GAQVVAAVLN
     DEALKASWLA EVEEMRTRIL AMRQELVKVL STEMPERNFD YLLNQRGMFS YTGLSAAQVD
     RLREEFGVYL IASGRMCVAG LNTANVQRVA KAFAAVM
//