TYRB_ECOLI
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 03-AUG-2022, entry version 182.
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; Proteobacteria; 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; P04693; -.
DR PRIDE; P04693; -.
DR EnsemblBacteria; AAC77024; AAC77024; b4054.
DR EnsemblBacteria; BAE78056; BAE78056; BAE78056.
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; WDQNKRQ; -.
DR PhylomeDB; P04693; -.
DR BioCyc; EcoCyc:TYRB-MON; -.
DR BioCyc; MetaCyc:TYRB-MON; -.
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:0030170; F:pyridoxal phosphate binding; IDA:EcoliWiki.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 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
