ID B6BEQ4_9RHOB Unreviewed; 193 AA.
AC B6BEQ4;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Anthranilate synthase component II {ECO:0000313|EMBL:EDZ48257.1};
DE EC=4.1.3.27 {ECO:0000313|EMBL:EDZ48257.1};
GN Name=trpG {ECO:0000313|EMBL:EDZ48257.1};
GN ORFNames=RBY4I_3477 {ECO:0000313|EMBL:EDZ48257.1};
OS Rhodobacterales bacterium Y4I.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX NCBI_TaxID=439496 {ECO:0000313|EMBL:EDZ48257.1, ECO:0000313|Proteomes:UP000005133};
RN [1] {ECO:0000313|EMBL:EDZ48257.1, ECO:0000313|Proteomes:UP000005133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y4I {ECO:0000313|EMBL:EDZ48257.1,
RC ECO:0000313|Proteomes:UP000005133};
RA Moran M.A., Buchan A., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS995281; EDZ48257.1; -; Genomic_DNA.
DR AlphaFoldDB; B6BEQ4; -.
DR STRING; 439496.RBY4I_3477; -.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_014340_1_2_5; -.
DR OrthoDB; 9786812at2; -.
DR Proteomes; UP000005133; Unassembled WGS sequence.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
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 Lyase {ECO:0000313|EMBL:EDZ48257.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005133}.
FT DOMAIN 3..186
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 193 AA; 20896 MW; 1F1194148EF89C5E CRC64;
MLLLIDNYDS FTYNLVHYLG ELGAEMEVHR NDAINVQEAM AMKPAGILLS PGPCDPDQAG
ICLALTEAAA ETGTPLLGVC LGHQTIGQAF GGKVVRCHEI VHGKMGKMHH NNTGVFKGLP
SPFEATRYHS LVVERDSLPD CLEITAELDD GTIMGLQHKD LPIHGVQFHP ESIASEHGHA
LLKNFLDVMK VPA
//