tyrB:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

TyrB

Synonyms

tyrosine aminotransferase, tyrosine-repressible, PLP-dependent[1], B4054[2][1], TyrB[2][1] , ECK4046, JW4014, b4054

Product description

TyrB[2][3];

Component of TYRB-DIMER[2]; tyrosine aminotransferase[3]

Tyrosine aminotransferase; aromatic amino acid aminotransferase; phenylalanine aminotransferase; dicarboxylic amino acid aminotransferase; homodimeric[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005737

cytoplasm

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0086

C

Seeded from EcoCyc (v14.0)

complete

GO:0008793

aromatic-amino-acid:2-oxoglutarate aminotransferase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:2.6.1.57

F

Seeded from EcoCyc (v14.0)

complete

GO:0030170

pyridoxal phosphate binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004838

F

Seeded from EcoCyc (v14.0)

complete

GO:0030170

pyridoxal phosphate binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004839

F

Seeded from EcoCyc (v14.0)

complete

GO:0004838

L-tyrosine:2-oxoglutarate aminotransferase activity

PMID:15983[5]

IMP: Inferred from Mutant Phenotype

F

Table 4

complete

GO:0030170

pyridoxal phosphate binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015421

F

Seeded from EcoCyc (v14.0)

complete

GO:0006532

aspartate biosynthetic process

PMID:15983[5]

IGI: Inferred from Genetic Interaction

EcoliWiki:aspC|EcoliWiki:ilvE

P

Table 5.

complete

GO:0042803

protein homodimerization activity

PMID:352693[6]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0030170

pyridoxal phosphate binding

PMID:352693[6]

IDA: Inferred from Direct Assay

F

complete

GO:0005515

protein binding

PMID:352693[6]

IDA: Inferred from Direct Assay

F

complete

GO:0005737

cytoplasm

PMID:352693[6]

IDA: Inferred from Direct Assay

C

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

TyrB is a dimer.

[6]

Protein

groL

PMID:16606699[7]

Experiment(s):EBI-1147350
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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes
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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MFQKVDAYAG DPILTLMERF KEDPRSDKVN LSIGLYYNED GIIPQLQAVA EAEARLNAQP
HGASLYLPME GLNCYRHAIA PLLFGADHPV LKQQRVATIQ TLGGSGALKV GADFLKRYFP
ESGVWVSDPT WENHVAIFAG AGFEVSTYPW YDEATNGVRF NDLLATLKTL PARSIVLLHP
CCHNPTGADL TNDQWDAVIE ILKARELIPF LDIAYQGFGA GMEEDAYAIR AIASAGLPAL
VSNSFSKIFS LYGERVGGLS VMCEDAEAAG RVLGQLKATV RRNYSSPPNF GAQVVAAVLN
DEALKASWLA EVEEMRTRIL AMRQELVKVL STEMPERNFD YLLNQRGMFS YTGLSAAQVD
RLREEFGVYL IASGRMCVAG LNTANVQRVA KAFAAVM
Length

397

Mol. Wt

43.538 kDa

pI

5.3 (calculated)

Extinction coefficient

49,850 - 50,475 (calc based on 15 Y, 5 W, and 5 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

26..393

PF00155 Aminotransferase class I and II

PMID:19920124[8]

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Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=tyrB taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16131880

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:948563

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0013278

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P04693

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG11040

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG11040

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:948563

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120001029

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB1033

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 Gelfand, DH & Steinberg, RA (1977) Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. J. Bacteriol. 130 429-40 PubMed
  6. ↑ 6.0 6.1 6.2 6.3 6.4 Powell, JT & Morrison, JF (1978) The purification and properties of the aspartate aminotransferase and aromatic-amino-acid aminotransferase from Escherichia coli. Eur. J. Biochem. 87 391-400 PubMed
  7. ↑ Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  8. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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