TRPG_BUCAI
ID TRPG_BUCAI Reviewed; 200 AA.
AC Q44696; Q5GL25; Q9K2G8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Anthranilate synthase component 2;
DE Short=AS;
DE Short=ASII;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase, GATase component;
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
GN Name=trpG; OrderedLocusNames=BUpT02;
GN and
GN Name=trpG2; OrderedLocusNames=BUpT04;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OG Plasmid pTrp (pBAp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8642610; DOI=10.1007/bf02498635;
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 (Buchnera):
RT genetics and evolution of plasmid-associated anthranilate synthase (trpEG)
RT within the aphididae.";
RL J. Mol. Evol. 42:414-421(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=APS;
RA Plague G.R., Kaur S., Wilcox J.L., Bishop B., Moran N.A.;
RT "Genetic mechanisms for regulating nutrient provisioning by symbionts to
RT hosts: the pTrp plasmid in Buchnera.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX 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 Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC step biosynthesis of anthranilate, an intermediate in the biosynthesis
CC of L-tryptophan. In the first step, the glutamine-binding beta subunit
CC (TrpG) of anthranilate synthase (AS) provides the glutamine
CC amidotransferase activity which generates ammonia as a substrate that,
CC along with chorismate, is used in the second step, catalyzed by the
CC large alpha subunit of AS (TrpE) to produce anthranilate. In the
CC absence of TrpG, TrpE can synthesize anthranilate directly from
CC chorismate and high concentrations of ammonia (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE). {ECO:0000250}.
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DR EMBL; L43555; AAD09347.1; -; Genomic_DNA.
DR EMBL; AY444795; AAS02054.1; -; Genomic_DNA.
DR EMBL; AP001070; BAA95418.1; -; Genomic_DNA.
DR EMBL; AP001070; BAA95419.1; -; Genomic_DNA.
DR RefSeq; NP_057963.1; NC_002252.1.
DR RefSeq; NP_057964.1; NC_002252.1.
DR RefSeq; WP_010892290.1; NC_002252.1.
DR AlphaFoldDB; Q44696; -.
DR SMR; Q44696; -.
DR STRING; 107806.7707815; -.
DR MEROPS; C26.960; -.
DR PRIDE; Q44696; -.
DR EnsemblBacteria; BAA95418; BAA95418; BAA95418.
DR EnsemblBacteria; BAA95419; BAA95419; BAA95419.
DR KEGG; buc:BUpT02; -.
DR KEGG; buc:BUpT04; -.
DR PATRIC; fig|107806.10.peg.2; -.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_014340_1_0_6; -.
DR OMA; HQVVIYR; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000001806; Plasmid pTrp.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Glutamine amidotransferase; Lyase; Plasmid; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..200
FT /note="Anthranilate synthase component 2"
FT /id="PRO_0000056872"
FT DOMAIN 3..196
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 84
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 170
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 172
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 57..59
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 88
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 134..135
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT CONFLICT 69
FT /note="D -> N (in Ref. 1; AAD09347)"
FT /evidence="ECO:0000305"
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
