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Protein

Aromatic-amino-acid aminotransferase

Gene

tyrB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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: L-phenylalanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-phenylalanine from phenylpyruvate (ArAT route).
Proteins known to be involved in this subpathway in this organism are:
  1. Aromatic-amino-acid aminotransferase (tyrB)
This subpathway is part of the pathway L-phenylalanine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-phenylalanine from phenylpyruvate (ArAT route), the pathway L-phenylalanine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-tyrosine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-tyrosine from (4-hydroxyphenyl)pyruvate.
Proteins known to be involved in this subpathway in this organism are:
  1. Aromatic-amino-acid aminotransferase (tyrB)
This subpathway is part of the pathway L-tyrosine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tyrosine from (4-hydroxyphenyl)pyruvate, the pathway L-tyrosine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei34Substrate; via amide nitrogenBy similarity1
Binding sitei66SubstrateBy similarity1
Binding sitei131SubstrateBy similarity1
Binding sitei184SubstrateBy similarity1
Binding sitei281SubstrateBy similarity1
Binding sitei375SubstrateBy similarity1

GO - Molecular functioni

  • aromatic-amino-acid:2-oxoglutarate aminotransferase activity Source: EcoCyc
  • identical protein binding Source: GO_Central
  • L-leucine:2-oxoglutarate aminotransferase activity Source: EcoCyc
  • L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
  • L-tyrosine:2-oxoglutarate aminotransferase activity Source: EcoCyc
  • pyridoxal phosphate binding Source: EcoliWiki

GO - Biological processi

  • aspartate biosynthetic process Source: EcoliWiki
  • leucine biosynthetic process Source: EcoCyc
  • L-phenylalanine biosynthetic process from chorismate via phenylpyruvate Source: EcoCyc
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11040. tyrB.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001238921 – 397Aromatic-amino-acid aminotransferaseAdd BLAST397

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei247N6-(pyridoxal phosphate)lysine1

Proteomic databases

EPDiP04693.
PaxDbiP04693.
PRIDEiP04693.

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4262667. 7 interactors.
IntActiP04693. 2 interactors.
STRINGi511145.b4054.

Structurei

Secondary structure

1397
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 21Combined sources10
Helixi47 – 58Combined sources12
Beta strandi62 – 64Combined sources3
Helixi73 – 84Combined sources12
Helixi89 – 92Combined sources4
Beta strandi96 – 102Combined sources7
Helixi103 – 118Combined sources16
Beta strandi124 – 129Combined sources6
Helixi132 – 140Combined sources9
Beta strandi145 – 148Combined sources4
Turni153 – 156Combined sources4
Helixi160 – 167Combined sources8
Beta strandi175 – 178Combined sources4
Beta strandi180 – 182Combined sources3
Turni184 – 186Combined sources3
Helixi192 – 204Combined sources13
Beta strandi208 – 214Combined sources7
Beta strandi218 – 220Combined sources3
Helixi224 – 226Combined sources3
Helixi227 – 234Combined sources8
Beta strandi239 – 244Combined sources6
Turni246 – 250Combined sources5
Helixi252 – 254Combined sources3
Beta strandi257 – 262Combined sources6
Helixi266 – 281Combined sources16
Turni282 – 284Combined sources3
Helixi290 – 299Combined sources10
Helixi302 – 333Combined sources32
Helixi341 – 344Combined sources4
Beta strandi347 – 351Combined sources5
Helixi356 – 364Combined sources9
Beta strandi372 – 374Combined sources3
Beta strandi375 – 377Combined sources3
Helixi378 – 380Combined sources3
Turni383 – 385Combined sources3
Helixi386 – 396Combined sources11

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP04693.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CGF. Bacteria.
COG1448. LUCA.
HOGENOMiHOG000185899.
InParanoidiP04693.
KOiK00832.
OMAiMETFKQD.
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.
WP_000486985.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77024; AAC77024; b4054.
BAE78056; BAE78056; BAE78056.
GeneIDi948563.
KEGGiecj:JW4014.
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.
PIRiA30379. XNECY.
RefSeqiNP_418478.1. NC_000913.3.
WP_000486985.1. NZ_LN832404.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi4262667. 7 interactors.
IntActiP04693. 2 interactors.
STRINGi511145.b4054.

Proteomic databases

EPDiP04693.
PaxDbiP04693.
PRIDEiP04693.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77024; AAC77024; b4054.
BAE78056; BAE78056; BAE78056.
GeneIDi948563.
KEGGiecj:JW4014.
eco:b4054.
PATRICi32123649. VBIEscCol129921_4173.

Organism-specific databases

EchoBASEiEB1033.
EcoGeneiEG11040. tyrB.

Phylogenomic databases

eggNOGiENOG4105CGF. Bacteria.
COG1448. LUCA.
HOGENOMiHOG000185899.
InParanoidiP04693.
KOiK00832.
OMAiMETFKQD.
PhylomeDBiP04693.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP04693.
PROiP04693.

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]
ProtoNetiSearch...

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 2, 2016
This is version 149 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.