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

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Reviewed, UniProtKB/Swiss-Prot P04693 (TYRB_ECOLI)

Last modified November 24, 2009. Version 98. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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

Gene names

Name:	tyrB
Ordered Locus Names:	b4054, JW4014

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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 prephenate: step 2/2.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

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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
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aromatic-amino-acid:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
groL	P0A6F5	1	EBI-1114498,EBI-543750

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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 By similarity

Binding site

281

Substrate By similarity

Amino acid modifications

Modified residue

247

N6-(pyridoxal phosphate)lysine

Secondary structure

397

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P04693-1 [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

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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: 3521591] [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: 3907634] [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: 8265357] [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: 9278503] [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: 16738553] [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: 3308851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39. Strain: K12.
[7]	"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: 10417420] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).

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Cross-references

Sequence databases

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

AP_004555.1.
NP_418478.1.

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P04693. 2 interactions.

STRING

P04693.

2-D gel databases

ECO2DBASE

E036.0. 6TH EDITION.

Genome annotation databases

GeneID

948563.

GenomeReviews

Gene locus JW4014 in contig AP009048_GR.
Gene locus b4054 in contig U00096_GR.

KEGG

ecj:JW4014.
eco:b4054.

Organism-specific databases

EchoBASE

EB1033.

EcoGene

EG11040. tyrB.

CMR

Search...

Phylogenomic databases

HOGENOM

P04693.

OMA

CVAGLNS

Enzyme and pathway databases

BioCyc

EcoCyc:TYRB-MON.
ECOL168927:B4054-MON.
MetaCyc:TYRB-MON.

Gene expression databases

Genevestigator

P04693.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.

PANTHER

PTHR11879. Asp_trans. 1 hit.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

PRINTS

PR00799. TRANSAMINASE.

PROSITE

PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

ProtoNet

Search...

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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:	November 24, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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 and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents