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P04693

- TYRB_ECOLI

UniProt

P04693 - TYRB_ECOLI

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 2110Combined sources
Helixi47 – 5812Combined sources
Beta strandi62 – 643Combined sources
Helixi73 – 8412Combined sources
Helixi89 – 924Combined sources
Beta strandi96 – 1027Combined sources
Helixi103 – 11816Combined sources
Beta strandi124 – 1296Combined sources
Helixi132 – 1409Combined sources
Beta strandi145 – 1484Combined sources
Turni153 – 1564Combined sources
Helixi160 – 1678Combined sources
Beta strandi175 – 1784Combined sources
Beta strandi180 – 1823Combined sources
Turni184 – 1863Combined sources
Helixi192 – 20413Combined sources
Beta strandi208 – 2147Combined sources
Beta strandi218 – 2203Combined sources
Helixi224 – 2263Combined sources
Helixi227 – 2348Combined sources
Beta strandi239 – 2446Combined sources
Turni246 – 2505Combined sources
Helixi252 – 2543Combined sources
Beta strandi257 – 2626Combined sources
Helixi266 – 28116Combined sources
Turni282 – 2843Combined sources
Helixi290 – 29910Combined sources
Helixi302 – 33332Combined sources
Helixi341 – 3444Combined sources
Beta strandi347 – 3515Combined sources
Helixi356 – 3649Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi375 – 3773Combined sources
Helixi378 – 3803Combined sources
Turni383 – 3853Combined sources
Helixi386 – 39611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP04693.
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

        10         20         30         40         50
MFQKVDAYAG DPILTLMERF KEDPRSDKVN LSIGLYYNED GIIPQLQAVA
60 70 80 90 100
EAEARLNAQP HGASLYLPME GLNCYRHAIA PLLFGADHPV LKQQRVATIQ
110 120 130 140 150
TLGGSGALKV GADFLKRYFP ESGVWVSDPT WENHVAIFAG AGFEVSTYPW
160 170 180 190 200
YDEATNGVRF NDLLATLKTL PARSIVLLHP CCHNPTGADL TNDQWDAVIE
210 220 230 240 250
ILKARELIPF LDIAYQGFGA GMEEDAYAIR AIASAGLPAL VSNSFSKIFS
260 270 280 290 300
LYGERVGGLS VMCEDAEAAG RVLGQLKATV RRNYSSPPNF GAQVVAAVLN
310 320 330 340 350
DEALKASWLA EVEEMRTRIL AMRQELVKVL STEMPERNFD YLLNQRGMFS
360 370 380 390
YTGLSAAQVD RLREEFGVYL IASGRMCVAG LNTANVQRVA KAFAAVM
Length:397
Mass (Da):43,538
Last modified:August 13, 1987 - v1
Checksum:i46E69B4B8378BA6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P04693.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 138 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