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P04693 (TYRB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aromatic-amino-acid aminotransferase

Short name=ARAT
Short name=AROAT
EC=2.6.1.57
Alternative name(s):
Beta-methylphenylalanine transaminase
EC=2.6.1.107
Gene names
Name:tyrB
Ordered Locus Names:b4054, JW4014
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Broad-specificity enzyme that catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively. In vitro, is able to catalyze the conversion of beta-methyl phenylpyruvate to the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin produced by Streptomyces hygroscopicus NRRL3085. Ref.8

Catalytic activity

An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate. Ref.8

(2S,3S)-3-methylphenylalanine + 2-oxoglutarate = (3S)-2-oxo-3-phenylbutanoate + L-glutamate. Ref.8

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-phenylalanine from phenylpyruvate (ArAT route): step 1/1.

Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine from (4-hydroxyphenyl)pyruvate: step 1/1.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397Aromatic-amino-acid aminotransferase
PRO_0000123892

Sites

Binding site341Substrate; via amide nitrogen By similarity
Binding site661Substrate By similarity
Binding site1311Substrate By similarity
Binding site1841Substrate By similarity
Binding site2811Substrate By similarity
Binding site3751Substrate By similarity

Amino acid modifications

Modified residue2471N6-(pyridoxal phosphate)lysine

Secondary structure

................................................................... 397
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04693 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 46E69B4B8378BA6B

FASTA39743,538
        10         20         30         40         50         60 
MFQKVDAYAG DPILTLMERF KEDPRSDKVN LSIGLYYNED GIIPQLQAVA EAEARLNAQP 

        70         80         90        100        110        120 
HGASLYLPME GLNCYRHAIA PLLFGADHPV LKQQRVATIQ TLGGSGALKV GADFLKRYFP 

       130        140        150        160        170        180 
ESGVWVSDPT WENHVAIFAG AGFEVSTYPW YDEATNGVRF NDLLATLKTL PARSIVLLHP 

       190        200        210        220        230        240 
CCHNPTGADL TNDQWDAVIE ILKARELIPF LDIAYQGFGA GMEEDAYAIR AIASAGLPAL 

       250        260        270        280        290        300 
VSNSFSKIFS LYGERVGGLS VMCEDAEAAG RVLGQLKATV RRNYSSPPNF GAQVVAAVLN 

       310        320        330        340        350        360 
DEALKASWLA EVEEMRTRIL AMRQELVKVL STEMPERNFD YLLNQRGMFS YTGLSAAQVD 

       370        380        390 
RLREEFGVYL IASGRMCVAG LNTANVQRVA KAFAAVM 

« Hide

References

« Hide 'large scale' references
[1]"The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes."
Fotheringham I.G., Dacey S.A., Taylor P.P., Smith T.J., Hunter M.G., Finlay M.E., Primrose S.B., Parker D.M., Edwards R.M.
Biochem. J. 234:593-604(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene."
Kuramitsu S., Inoue K., Ogawa T., Ogawa H., Kagamiyama H.
Biochem. Biophys. Res. Commun. 133:134-139(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"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.
[6]"Molecular analysis of the regulatory region of the Escherichia coli K-12 tyrB gene."
Yang J., Pittard J.
J. Bacteriol. 169:4710-4715(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
Strain: K12.
[7]"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.
[8]"In vitro characterization of enzymes involved in the synthesis of nonproteinogenic residue (2S,3S)-beta-methylphenylalanine in glycopeptide antibiotic mannopeptimycin."
Huang Y.T., Lyu S.Y., Chuang P.H., Hsu N.S., Li Y.S., Chan H.C., Huang C.J., Liu Y.C., Wu C.J., Yang W.B., Li T.L.
ChemBioChem 10:2480-2487(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS BETA-METHYLPHENYLALANINE TRANSAMINASE, CATALYTIC ACTIVITY.
[9]"Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase."
Ko T.-P., Wu S.-P., Yang W.-Z., Tsai H., Yuan H.S.
Acta Crystallogr. D 55:1474-1477(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03628 Genomic DNA. Translation: CAA27278.1.
M12047 Genomic DNA. Translation: AAA24703.1.
U00006 Genomic DNA. Translation: AAC43148.1.
U00096 Genomic DNA. Translation: AAC77024.1.
AP009048 Genomic DNA. Translation: BAE78056.1.
M17809 Genomic DNA. Translation: AAA24704.1.
PIRXNECY. A30379.
RefSeqNP_418478.1. NC_000913.3.
YP_492197.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FSLX-ray2.35A/B/C/D/E/F1-397[»]
3TATX-ray3.50A/B/C/D/E/F1-397[»]
ProteinModelPortalP04693.
SMRP04693. Positions 1-397.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP04693. 2 interactions.
STRING511145.b4054.

Proteomic databases

PaxDbP04693.
PRIDEP04693.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77024; AAC77024; b4054.
BAE78056; BAE78056; BAE78056.
GeneID12933673.
948563.
KEGGecj:Y75_p3941.
eco:b4054.
PATRIC32123649. VBIEscCol129921_4173.

Organism-specific databases

EchoBASEEB1033.
EcoGeneEG11040. tyrB.

Phylogenomic databases

eggNOGCOG1448.
HOGENOMHOG000185899.
KOK00832.
OMACMAGLNH.
OrthoDBEOG6C2WBK.
PhylomeDBP04693.

Enzyme and pathway databases

BioCycEcoCyc:TYRB-MONOMER.
ECOL316407:JW4014-MONOMER.
MetaCyc:TYRB-MONOMER.
UniPathwayUPA00121; UER00347.
UPA00122; UER00350.

Gene expression databases

GenevestigatorP04693.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11879. PTHR11879. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00799. TRANSAMINASE.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04693.
PROP04693.

Entry information

Entry nameTYRB_ECOLI
AccessionPrimary (citable) accession number: P04693
Secondary accession number(s): Q2M6Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 14, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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