Aromatic-amino-acid aminotransferase - Escherichia coli (strain K12)

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P04693 (TYRB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aromatic-amino-acid aminotransferase
Short name=ARAT
Short name=AROAT
EC=2.6.1.57

Gene names

Name:	tyrB
Ordered Locus Names:	b4054, JW4014

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate.
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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate Inferred from direct assay PubMed 236311. Source: EcoCyc aspartate biosynthetic process Inferred from genetic interaction PubMed 15983. Source: EcoliWiki leucine biosynthetic process Inferred from mutant phenotype PubMed 361681. Source: EcoCyc tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate Inferred from direct assay PubMed 236311. Source: EcoCyc
Cellular_component	cytoplasm Inferred from direct assay PubMed 352693. Source: EcoliWiki
Molecular_function	L-leucine:2-oxoglutarate aminotransferase activity Inferred from mutant phenotype PubMed 361681. Source: EcoCyc L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC L-tyrosine:2-oxoglutarate aminotransferase activity Inferred from direct assay PubMed 236311. Source: EcoCyc aromatic-amino-acid:2-oxoglutarate aminotransferase activity Inferred from direct assay PubMed 236311. Source: EcoCyc pyridoxal phosphate binding Inferred from direct assay PubMed 352693. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 397

397

Aromatic-amino-acid aminotransferase

PRO_0000123892

Sites

Binding site

Substrate; via amide nitrogen By similarity

Binding site

Substrate By similarity

Binding site

131

Substrate By similarity

Binding site

184

Substrate By similarity

Binding site

281

Substrate By similarity

Binding site

375

Substrate By similarity

Amino acid modifications

Modified residue

247

N6-(pyridoxal phosphate)lysine

Secondary structure

397

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P04693 [UniParc].

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

397

43,538

        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' referencesShow '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 277:1453-1474(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]	"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.

PIR

XNECY. A30379.

RefSeq

NP_418478.1. NC_000913.2.
YP_492197.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P04693.

SMR

P04693. Positions 1-397.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04693. 2 interactions.

STRING

511145.b4054.

Proteomic databases

PaxDb

P04693.

PRIDE

P04693.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77024; AAC77024; b4054.
BAE78056; BAE78056; BAE78056.

GeneID

12933673.
948563.

KEGG

ecj:Y75_p3941.
eco:b4054.

PATRIC

32123649. VBIEscCol129921_4173.

Organism-specific databases

EchoBASE

EB1033.

EcoGene

EG11040. tyrB.

Phylogenomic databases

eggNOG

COG1448.

HOGENOM

HOG000185899.

K00832.

OMA

DFTGAIE.

ProtClustDB

PRK09257.

Enzyme and pathway databases

BioCyc

EcoCyc:TYRB-MONOMER.
ECOL316407:JW4014-MONOMER.
MetaCyc:TYRB-MONOMER.

UniPathway

UPA00121; UER00347.
UPA00122; UER00350.

Gene expression databases

Genevestigator

P04693.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.

InterPro

IPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]

PANTHER

PTHR11879. PTHR11879. 1 hit.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

PRINTS

PR00799. TRANSAMINASE.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P04693.

Entry information

Entry name

TYRB_ECOLI

Accession

Primary (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 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents