ID   TRPG_BUCAI              Reviewed;         200 AA.
AC   Q44696; Q9K2G8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Anthranilate synthase component 2;
DE            EC=4.1.3.27;
DE   AltName: Full=Anthranilate synthase component II;
DE   AltName: Full=Glutamine amido-transferase;
GN   Name=trpG; OrderedLocusNames=BUpT02;
GN   and
GN   Name=trpG2; OrderedLocusNames=BUpT04;
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.
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: Contains 1 glutamine amidotransferase type-1 domain.
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DR   EMBL; L43555; AAD09347.1; -; Genomic_DNA.
DR   EMBL; AP001070; BAA95418.1; -; Genomic_DNA.
DR   EMBL; AP001070; BAA95419.1; -; Genomic_DNA.
DR   RefSeq; NP_057963.1; -.
DR   RefSeq; NP_057964.1; -.
DR   HSSP; P00905; 1I1Q.
DR   GeneID; 1109446; -.
DR   GeneID; 1109447; -.
DR   GenomeReviews; AP001070_GR; BUpT02.
DR   GenomeReviews; AP001070_GR; BUpT04.
DR   KEGG; buc:BUpT02; -.
DR   KEGG; buc:BUpT04; -.
DR   HOGENOM; Q44696; -.
DR   OMA; Q44696; VVIYRND.
DR   BioCyc; BSP107806:BUPT02-MON; -.
DR   BioCyc; BSP107806:BUPT04-MON; -.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006220; Anth_synthII.
DR   InterPro; IPR011702; GATASE.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR000991; GATase_class1_C.
DR   InterPro; IPR006221; TrpG_papA.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00096; GATASE.
DR   TIGRFAMs; TIGR00566; trpG_papA; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Glutamine amidotransferase; Lyase; Plasmid;
KW   Tryptophan biosynthesis.
FT   CHAIN         1    200       Anthranilate synthase component 2.
FT                                /FTId=PRO_0000056872.
FT   DOMAIN        3    196       Glutamine amidotransferase type-1.
FT   ACT_SITE     84     84       By similarity.
FT   ACT_SITE    170    170       By similarity.
FT   ACT_SITE    172    172       By similarity.
FT   CONFLICT     69     69       D -> N (in Ref. 1; AAD09347).
SQ   SEQUENCE   200 AA;  22569 MW;  FF16C661D5887B04 CRC64;
     MANILLLDNI DSFTYNLVEQ LRNQKNNVLV YRNTVSIDII FNSLKKLTHP ILMLSPGPSL
     PKHAGCMLDL IKKVKGDIPI VGICLGHQAI VEAYGGIIGY AGEIFHGKAS LIRHDGLEMF
     EGVPQPLPVA RYHSLICNKI PEKFVINSYF EKMIMSVRNN CDRVCGFQFH PESILTTHGD
     QILEKIIHWA SLKYITNKKQ
//