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P04693

- TYRB_ECOLI

UniProt

P04693 - TYRB_ECOLI

Protein

Aromatic-amino-acid aminotransferase

Gene

tyrB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    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 NRRL3085.1 Publication

    Catalytic activityi

    An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate.1 Publication
    (2S,3S)-3-methylphenylalanine + 2-oxoglutarate = (3S)-2-oxo-3-phenylbutanoate + L-glutamate.1 Publication

    Cofactori

    Pyridoxal phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei34 – 341Substrate; via amide nitrogenBy similarity
    Binding sitei66 – 661SubstrateBy similarity
    Binding sitei131 – 1311SubstrateBy similarity
    Binding sitei184 – 1841SubstrateBy similarity
    Binding sitei281 – 2811SubstrateBy similarity
    Binding sitei375 – 3751SubstrateBy similarity

    GO - Molecular functioni

    1. aromatic-amino-acid:2-oxoglutarate aminotransferase activity Source: EcoCyc
    2. L-leucine:2-oxoglutarate aminotransferase activity Source: EcoCyc
    3. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
    4. L-tyrosine:2-oxoglutarate aminotransferase activity Source: EcoCyc
    5. pyridoxal phosphate binding Source: EcoliWiki

    GO - Biological processi

    1. aspartate biosynthetic process Source: EcoliWiki
    2. leucine biosynthetic process Source: EcoCyc
    3. L-phenylalanine biosynthetic process from chorismate via phenylpyruvate Source: EcoCyc
    4. tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate Source: EcoCyc

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:TYRB-MONOMER.
    ECOL316407:JW4014-MONOMER.
    MetaCyc:TYRB-MONOMER.
    UniPathwayiUPA00121; UER00347.
    UPA00122; UER00350.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aromatic-amino-acid aminotransferase (EC:2.6.1.57)
    Short name:
    ARAT
    Short name:
    AROAT
    Alternative name(s):
    Beta-methylphenylalanine transaminase (EC:2.6.1.107)
    Gene namesi
    Name:tyrB
    Ordered Locus Names:b4054, JW4014
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11040. tyrB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 397397Aromatic-amino-acid aminotransferasePRO_0000123892Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei247 – 2471N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiP04693.
    PRIDEiP04693.

    Expressioni

    Gene expression databases

    GenevestigatoriP04693.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    IntActiP04693. 2 interactions.
    STRINGi511145.b4054.

    Structurei

    Secondary structure

    1
    397
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 2110
    Helixi47 – 5812
    Beta strandi62 – 643
    Helixi73 – 8412
    Helixi89 – 924
    Beta strandi96 – 1027
    Helixi103 – 11816
    Beta strandi124 – 1296
    Helixi132 – 1409
    Beta strandi145 – 1484
    Turni153 – 1564
    Helixi160 – 1678
    Beta strandi175 – 1784
    Beta strandi180 – 1823
    Turni184 – 1863
    Helixi192 – 20413
    Beta strandi208 – 2147
    Beta strandi218 – 2203
    Helixi224 – 2263
    Helixi227 – 2348
    Beta strandi239 – 2446
    Turni246 – 2505
    Helixi252 – 2543
    Beta strandi257 – 2626
    Helixi266 – 28116
    Turni282 – 2843
    Helixi290 – 29910
    Helixi302 – 33332
    Helixi341 – 3444
    Beta strandi347 – 3515
    Helixi356 – 3649
    Beta strandi372 – 3743
    Beta strandi375 – 3773
    Helixi378 – 3803
    Turni383 – 3853
    Helixi386 – 39611

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FSLX-ray2.35A/B/C/D/E/F1-397[»]
    3TATX-ray3.50A/B/C/D/E/F1-397[»]
    ProteinModelPortaliP04693.
    SMRiP04693. Positions 1-397.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04693.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1448.
    HOGENOMiHOG000185899.
    KOiK00832.
    OMAiCMAGLNH.
    OrthoDBiEOG6C2WBK.
    PhylomeDBiP04693.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR000796. Asp_trans.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view]
    PANTHERiPTHR11879. PTHR11879. 1 hit.
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    PRINTSiPR00799. TRANSAMINASE.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P04693-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFQKVDAYAG DPILTLMERF KEDPRSDKVN LSIGLYYNED GIIPQLQAVA    50
    EAEARLNAQP HGASLYLPME GLNCYRHAIA PLLFGADHPV LKQQRVATIQ 100
    TLGGSGALKV GADFLKRYFP ESGVWVSDPT WENHVAIFAG AGFEVSTYPW 150
    YDEATNGVRF NDLLATLKTL PARSIVLLHP CCHNPTGADL TNDQWDAVIE 200
    ILKARELIPF LDIAYQGFGA GMEEDAYAIR AIASAGLPAL VSNSFSKIFS 250
    LYGERVGGLS VMCEDAEAAG RVLGQLKATV RRNYSSPPNF GAQVVAAVLN 300
    DEALKASWLA EVEEMRTRIL AMRQELVKVL STEMPERNFD YLLNQRGMFS 350
    YTGLSAAQVD RLREEFGVYL IASGRMCVAG LNTANVQRVA KAFAAVM 397
    Length:397
    Mass (Da):43,538
    Last modified:August 13, 1987 - v1
    Checksum:i46E69B4B8378BA6B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA30379. XNECY.
    RefSeqiNP_418478.1. NC_000913.3.
    YP_492197.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77024; AAC77024; b4054.
    BAE78056; BAE78056; BAE78056.
    GeneIDi12933673.
    948563.
    KEGGiecj:Y75_p3941.
    eco:b4054.
    PATRICi32123649. VBIEscCol129921_4173.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi A30379. XNECY.
    RefSeqi NP_418478.1. NC_000913.3.
    YP_492197.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FSL X-ray 2.35 A/B/C/D/E/F 1-397 [» ]
    3TAT X-ray 3.50 A/B/C/D/E/F 1-397 [» ]
    ProteinModelPortali P04693.
    SMRi P04693. Positions 1-397.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P04693. 2 interactions.
    STRINGi 511145.b4054.

    Proteomic databases

    PaxDbi P04693.
    PRIDEi P04693.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77024 ; AAC77024 ; b4054 .
    BAE78056 ; BAE78056 ; BAE78056 .
    GeneIDi 12933673.
    948563.
    KEGGi ecj:Y75_p3941.
    eco:b4054.
    PATRICi 32123649. VBIEscCol129921_4173.

    Organism-specific databases

    EchoBASEi EB1033.
    EcoGenei EG11040. tyrB.

    Phylogenomic databases

    eggNOGi COG1448.
    HOGENOMi HOG000185899.
    KOi K00832.
    OMAi CMAGLNH.
    OrthoDBi EOG6C2WBK.
    PhylomeDBi P04693.

    Enzyme and pathway databases

    UniPathwayi UPA00121 ; UER00347 .
    UPA00122 ; UER00350 .
    BioCyci EcoCyc:TYRB-MONOMER.
    ECOL316407:JW4014-MONOMER.
    MetaCyc:TYRB-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P04693.
    PROi P04693.

    Gene expression databases

    Genevestigatori P04693.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    InterProi IPR004839. Aminotransferase_I/II.
    IPR000796. Asp_trans.
    IPR004838. NHTrfase_class1_PyrdxlP-BS.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view ]
    PANTHERi PTHR11879. PTHR11879. 1 hit.
    Pfami PF00155. Aminotran_1_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00799. TRANSAMINASE.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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).

    Entry informationi

    Entry nameiTYRB_ECOLI
    AccessioniPrimary (citable) accession number: P04693
    Secondary accession number(s): Q2M6Q0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3