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Reviewed, UniProtKB/Swiss-Prot P06557 (TRPE_CORGL)

Last modified February 9, 2010. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Anthranilate synthase component 1
    EC=4.1.3.27
Alternative name(s):
    Anthranilate synthase component I
Gene names
Name: trpE
Ordered Locus Names: Cgl3029, cg3359
OrganismCorynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.

Subunit structure

Tetramer of two components I and two components II By similarity.

Miscellaneous

Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity.

Sequence similarities

Belongs to the anthranilate synthase component I family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
Tryptophan biosynthesis
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtryptophan biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionanthranilate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 518518Anthranilate synthase component 1
PRO_0000154091

Experimental info

Sequence conflict161E → A in AAB59111. Ref.6
Sequence conflict1851A → T Ref.1
Sequence conflict1851A → T Ref.2
Sequence conflict1851A → T Ref.5
Sequence conflict1851A → T Ref.6
Sequence conflict357 – 3582EH → DD Ref.1
Sequence conflict357 – 3582EH → DD Ref.2

Sequences

Sequence LengthMass (Da)Tools
P06557-1 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: 0662D4A660C16FF5

FASTA51856,384
        10         20         30         40         50         60 
MSTNPHVFSL DVRYHEDASA LFAHLGGTTA DDAALLESAD ITTKNGISSL AVLKSSVRIT 

        70         80         90        100        110        120 
CTGNTVVTQP LTDSGRAVVA RLTQQLGQYN TAENTFSFPA SDAVDERERL TAPSTIEVLR 

       130        140        150        160        170        180 
KLQFESGYSD ASLPLLMGGF AFDFLETFET LPAVEESVNT YPDYQFVLAE IVLDINHQDQ 

       190        200        210        220        230        240 
TAKLAGVSNA PGELEAELNK LSLLIDAALP ATEHAYQTTP HDGDTLRVVA DIPDAQFRTQ 

       250        260        270        280        290        300 
INELKENIYN GDIYQVVPAR TFTAPCPDAF AAYLQLRATN PSPYMFYIRG LNEGRSYELF 

       310        320        330        340        350        360 
GASPESNLKF TAANRELQLY PIAGTRPRGL NPDGSINDEL DIRNELDMRT DAKEIAEHTM 

       370        380        390        400        410        420 
LVDLARNDLA RVSVPASRRV ADLLQVDRYS RVMHLVSRVT ATLDPELDAL DAYRACMNMG 

       430        440        450        460        470        480 
TLTGAPKLRA MELLRGVEKR RRGSYGGAVG YLRGNGDMDN CIVIRSAFVQ DGVAAVQAGA 

       490        500        510 
GVVRDSNPQS EADETLHKAY AVLNAIALAA GSTLEVIR 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide and deduced amino acid sequences of the Brevibacterium lactofermentum tryptophan operon."
Matsui K., Sano K., Ohtsubo E.
Nucleic Acids Res. 14:10113-10114(1986) [PubMed: 3808947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence of the Corynebacterium glutamicum trpE gene."
Heery D.M., Dunican L.K.
Nucleic Acids Res. 18:7138-7138(1990) [PubMed: 2263476] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[3]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[5]"Structure and function of the trp operon control regions of Brevibacterium lactofermentum, a glutamic-acid-producing bacterium."
Sano K., Matsui K.
Gene 53:191-200(1987) [PubMed: 3609747] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-275.
[6]"Two single-base-pair substitutions causing desensitization to tryptophan feedback inhibition of anthranilate synthase and enhanced expression of tryptophan genes of Brevibacterium lactofermentum."
Matsui K., Miwa K., Sano K.
J. Bacteriol. 169:5330-5332(1987) [PubMed: 3667535] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04960 Genomic DNA. Translation: CAA28623.1.
X55994 Genomic DNA. Translation: CAA39467.1.
BA000036 Genomic DNA. Translation: BAC00424.1.
BX927157 Genomic DNA. Translation: CAF18969.1.
M16663 Genomic DNA. Translation: AAA83989.1.
M17892 Genomic DNA. Translation: AAB59111.1.
PIRB24723.
RefSeqNP_602223.1.
YP_227280.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1020972.
3345521.
GenomeReviewsGene locus Cgl3029 in contig BA000036_GR.
KEGGcgb:cg3359.
cgl:NCgl2927.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG507440.
OMARIYEWEN.
PhylomeDBP06557.

Enzyme and pathway databases

BioCycCGLU196627:CG3359-MONOMER.
BRENDA4.1.3.27. 812.

Family and domain databases

InterProIPR005801. ADC_synthase.
IPR006805. Anth_synth_I_N.
IPR019999. Anthranilate_synth_I_C.
IPR015890. Chorismate-bd_C.
IPR005257. TrpE_synth.
[Graphical view]
Gene3DG3DSA:3.60.120.10. TRPE_1_chor_bd. 1 hit.
PANTHERPTHR11236. TRPE_1_chor_bd. 1 hit.
PfamPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PRINTSPR00095. ANTSNTHASEI.
TIGRFAMsTIGR00565. trpE_proteo. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRPE_CORGL
AccessionPrimary (citable) accession number: P06557
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 11, 2002
Last modified: February 9, 2010
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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