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P03963 (TRPE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BSU22680
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length515 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.

Sequence caution

The sequence described in Ref.1 differs from that shown. Reason: Frameshift at positions 343 and 402.

The sequence described in Ref.2 differs from that shown. Reason: Frameshift at positions 343 and 402.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 515515Anthranilate synthase component 1
PRO_0000154079

Experimental info

Sequence conflict801A → P Ref.1
Sequence conflict801A → P Ref.2
Sequence conflict1201A → S Ref.1
Sequence conflict1201A → S Ref.2

Sequences

Sequence LengthMass (Da)Tools
P03963 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: 33B88D9D80BCD991

FASTA51558,116
        10         20         30         40         50         60 
MNFQSNISAF LEDSLSHHTI PIVETFTVDT LTPIQMIEKL DREITYLLES KDDTSTWSRY 

        70         80         90        100        110        120 
SFIGLNPFLT IKEEQGRFSA ADQDSKSLYT GNELKEVLNW MNTTYKIKTP ELGIPFVGGA 

       130        140        150        160        170        180 
VGYLSYDMIP LIEPSVPSHT KETDMEKCML FVCRTLIAYD HETKNVHFIQ YARLTGEETK 

       190        200        210        220        230        240 
NEKMDVFHQN HLELQNLIEK MMDQKNIKEL FLSADSYKTP SFETVSSNYE KSAFMADVEK 

       250        260        270        280        290        300 
IKSYIKAGDI FQGVLSQKFE VPIKADAFEL YRVLRIVNPS PYMYYMKLLD REIVGSSPER 

       310        320        330        340        350        360 
LIHVQDGHLE IHPIAGTRKR GADKAEDERL KVELMKDEKE KAEHYMLVDL ARNDIGRVAE 

       370        380        390        400        410        420 
YGSVSVPEFT KIVSFSHVMH IISVVTGRLK KGVHPVDALM SAFPAGTLTG APKIRAMQLL 

       430        440        450        460        470        480 
QELEPTPRET YGGCIAYIGF DGNIDSCITI RTMSVKNGVA SIQAGAGIVA DSVPEAEYEE 

       490        500        510 
SCNKAGALLK TIHIAEDMFH SKEDKADEQI STIVR

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Bacillus subtilis tryptophan operon."
Henner D.J., Band L., Shimotsu H.
Gene 34:169-177(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence of the Bacillus subtilis trpE and trpD genes."
Band L., Shimotsu H., Henner D.J.
Gene 27:55-65(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Sequence of Bacillus subtilis dbpA, mtr(A,B), gerC(1-3), ndk, cheR, aro(B,E,F,H), trp(A-F), hisH, and tyrA genes."
Henner D.J.
Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[5]"Characterization of the Bacillus subtilis tryptophan promoter region."
Shimotsu H., Henner D.J.
Proc. Natl. Acad. Sci. U.S.A. 81:6315-6319(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
[6]"Novel form of transcription attenuation regulates expression the Bacillus subtilis tryptophan operon."
Shimotsu H., Kuroda M.I., Yanofsky C., Henner D.J.
J. Bacteriol. 166:461-471(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		K01391 Genomic DNA. Translation: AAA22865.1. Frameshift.
M80245 Genomic DNA. Translation: AAA20862.1.
AL009126 Genomic DNA. Translation: CAB14184.1.
M27566 Genomic DNA. Translation: AAA22875.1.
PIRNNBS1. A01119.
RefSeqNP_390149.1. NC_000964.3.

3D structure databases

ProteinModelPortalP03963.
SMRP03963. Positions 25-494.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU22680.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14184; CAB14184; BSU22680.
GeneID939008.
KEGGbsu:BSU22680.
PATRIC18976345. VBIBacSub10457_2363.

Organism-specific databases

GenoListBSU22680. [Micado]

Phylogenomic databases

HOGENOMHOG000025142.
KOK01657.
OMAIGRVAEY.
ProtClustDBPRK13569.

Enzyme and pathway databases

BioCycBSUB:BSU22680-MONOMER.
UniPathwayUPA00035; UER00040.

Family and domain databases

Gene3D3.60.120.10. 1 hit.
InterProIPR005801. ADC_synthase.
IPR019999. Anth_synth_I.
IPR006805. Anth_synth_I_N.
IPR005256. Anth_synth_I_PabB.
IPR015890. Chorismate-bd_C.
[Graphical view]
PfamPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PRINTSPR00095. ANTSNTHASEI.
SUPFAMSSF56322. TRPE_1_chor_bd. 1 hit.
TIGRFAMsTIGR00564. trpE_most. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRPE_BACSU
AccessionPrimary (citable) accession number: P03963
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: July 1, 1993
Last modified: May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents