ID G2LQ72_BUCUM Unreviewed; 205 AA.
AC G2LQ72;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=anthranilate synthase {ECO:0000256|ARBA:ARBA00012266};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN Name=trpG {ECO:0000313|EMBL:AEO08373.1};
GN ORFNames=BUAMB_pTrp002 {ECO:0000313|EMBL:AEO08373.1};
OS Buchnera aphidicola str. Ua (Uroleucon ambrosiae).
OG Plasmid pTrp {ECO:0000313|EMBL:AEO08373.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=1005057 {ECO:0000313|EMBL:AEO08373.1, ECO:0000313|Proteomes:UP000006139};
RN [1] {ECO:0000313|EMBL:AEO08373.1, ECO:0000313|Proteomes:UP000006139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ua {ECO:0000313|Proteomes:UP000006139};
RC PLASMID=pTrp {ECO:0000313|EMBL:AEO08373.1,
RC ECO:0000313|Proteomes:UP000006139};
RX PubMed=21912528; DOI=10.1371/journal.pgen.1002252;
RA Degnan P.H., Ochman H., Moran N.A.;
RT "Sequence conservation and functional constraint on intergenic spacers in
RT reduced genomes of the obligate symbiont buchnera.";
RL PLoS Genet. 7:E1002252-E1002252(2011).
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DR EMBL; CP002650; AEO08373.1; -; Genomic_DNA.
DR RefSeq; WP_014500268.1; NC_017260.1.
DR AlphaFoldDB; G2LQ72; -.
DR MEROPS; C26.960; -.
DR KEGG; buh:BUAMB_pTrp002; -.
DR PATRIC; fig|1005057.4.peg.564; -.
DR HOGENOM; CLU_014340_1_0_6; -.
DR OrthoDB; 9806430at2; -.
DR Proteomes; UP000006139; Plasmid pTrp.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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 NCBIfam; TIGR00566; trpG_papA; 1.
DR PANTHER; PTHR43418:SF2; BIFUNCTIONAL PROTEIN TRPGD; 1.
DR PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Plasmid {ECO:0000313|EMBL:AEO08373.1}.
FT DOMAIN 5..187
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 85
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 205 AA; 22967 MW; F2C144847B8D8834 CRC64;
MANILLLDNI DSFTYNLVDQ LRKHKNNVVV YRNTVDIKII SHALIQLTNP ILMLSPGPGL
PRDAGCMSSL IKIVKSQKIP MIGICLGHQA IVEAYGGQIK YSGEIFHGKV SSISHDGLEM
FKNVPQYLPV ARYHSLICSN APKDFVINSY FNQIIMSVRH KTERVCGLQF HPESILTPAG
DQILKQIIHW ASLKNEIKGQ KISYS
//