ID   TRPE_BUCAI              Reviewed;         521 AA.
AC   Q44695; Q9KGQ2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 3.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=Anthranilate synthase component 1;
DE            EC=4.1.3.27;
DE   AltName: Full=Anthranilate synthase component I;
GN   Name=trpE; OrderedLocusNames=BUpT01;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum
OS   symbiotic bacterium).
OG   Plasmid pTrp (pBAp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=118099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96215866; PubMed=8642610;
RA   Rouhbakhsh D., Lai C.-Y., von Dohlen C.D., Clark M.A., Baumann L.,
RA   Baumann P., Moran N.A., Voegtlin D.J.;
RT   "The tryptophan biosynthetic pathway of aphid endosymbionts
RT   (Buchnera): genetics and evolution of plasmid-associated anthranilate
RT   synthase (trpEG) within the aphididae.";
RL   J. Mol. Evol. 42:414-421(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tokyo 1998;
RX   MEDLINE=20445173; PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids
RT   Buchnera sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate +
CC       pyruvate + L-glutamate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- SUBUNIT: Tetramer of two components I and two components II (By
CC       similarity).
CC   -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC       using ammonia rather than glutamine, whereas component II provides
CC       glutamine amidotransferase activity.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I
CC       family.
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DR   EMBL; L43555; AAD09346.1; -; Genomic_DNA.
DR   EMBL; AP001070; BAA95417.1; -; Genomic_DNA.
DR   RefSeq; NP_057962.1; -.
DR   HSSP; P00898; 1I1Q.
DR   GeneID; 1109444; -.
DR   GenomeReviews; AP001070_GR; BUpT01.
DR   KEGG; buc:BUpT01; -.
DR   HOGENOM; Q44695; -.
DR   OMA; Q44695; HKELAEH.
DR   BioCyc; BSP107806:BUPT01-MON; -.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:EC.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR019999; Anthranilate_synth_I_C.
DR   InterPro; IPR015890; Chorismate-bd_C.
DR   InterPro; IPR005257; TrpE_synth.
DR   Gene3D; G3DSA:3.60.120.10; TRPE_1_chor_bd; 1.
DR   PANTHER; PTHR11236; TRPE_1_chor_bd; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   ProDom; PD000779; Anth_synth_chor; 1.
DR   TIGRFAMs; TIGR00565; trpE_proteo; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Plasmid; Tryptophan biosynthesis.
FT   CHAIN         1    521       Anthranilate synthase component 1.
FT                                /FTId=PRO_0000154080.
FT   CONFLICT      1     10       MFLIEKRRKL -> MQKSPYEIEI (in Ref. 1).
FT   CONFLICT    276    276       D -> N (in Ref. 1; AAD09346).
SQ   SEQUENCE   521 AA;  58793 MW;  1F09602A47F0E7C5 CRC64;
     MFLIEKRRKL IQKKANYHSD PTTVFNHLCG SRPATLLLET AEVNKKNNLE SIMIVDSAIR
     VSAVKNSVKI TALSENGAEI LSILKENPHK KIKFFEKNKS INLIFPSLDN NLDEDKKIFS
     LSVFDSFRFI MKSVNNTKRT SKAMFFGGLF SYDLISNFES LPNVKKKQKC PDFCFYLAET
     LLVVDHQKKT CLIQSSLFGR NVDEKNRIKK RTEEIEKKLE EKLTSIPKNK TTVPVQLTSN
     ISDFQYSSTI KKLQKLIQKG EIFQVVPSRK FFLPCDNSLS AYQELKKSNP SPYMFFMQDE
     DFILFGASPE SSLKYDEKNR QIELYPIAGT RPRGRKKDGT LDLDLDSRIE LEMRTNHKEL
     AEHLMLVDLA RNDLARICEP GSRYVSDLVK VDKYSHVMHL VSKVVGQLKY GLDALHAYSS
     CMNMGTLTGA PKVRAMQLIA EYEGEGRGSY GGAIGYFTDL GNLDTCITIR SAYVESGVAT
     IQAGAGVVFN SIPEDEVKES LNKAQAVINA IKKAHFTMGS S
//