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Database: UniProt
Entry: A0A150WR62_BDEBC
LinkDB: A0A150WR62_BDEBC
Original site: A0A150WR62_BDEBC 
ID   A0A150WR62_BDEBC        Unreviewed;       272 AA.
AC   A0A150WR62;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Anthranilate synthase {ECO:0000313|EMBL:KYG66910.1};
GN   ORFNames=AZI86_07735 {ECO:0000313|EMBL:KYG66910.1};
OS   Bdellovibrio bacteriovorus.
OC   Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC   Pseudobdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=959 {ECO:0000313|EMBL:KYG66910.1, ECO:0000313|Proteomes:UP000075320};
RN   [1] {ECO:0000313|EMBL:KYG66910.1, ECO:0000313|Proteomes:UP000075320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R0 {ECO:0000313|EMBL:KYG66910.1,
RC   ECO:0000313|Proteomes:UP000075320};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYG66910.1}.
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DR   EMBL; LUKE01000001; KYG66910.1; -; Genomic_DNA.
DR   RefSeq; WP_061834488.1; NZ_LUKE01000001.1.
DR   AlphaFoldDB; A0A150WR62; -.
DR   Proteomes; UP000075320; Unassembled WGS sequence.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01745; GATase1_2; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR011697; Peptidase_C26.
DR   InterPro; IPR044668; PuuD-like.
DR   PANTHER; PTHR43235; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR   PANTHER; PTHR43235:SF1; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR   Pfam; PF07722; Peptidase_C26; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000075320}.
FT   ACT_SITE        129
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   272 AA;  30766 MW;  94AB6512D5C6BDD9 CRC64;
     MDSERPLLIG ISARILYDPP EGFEIKKKTV QYLEDSLAHL VTKRGGLIFM VPSLEMHSRL
     EKKDLDVHQY ADVLDGLVLQ GGVDISPTTY GEEPIEVMKD HRTDPIRDRY ELKLLKAFVQ
     KKKPVLGICR GFQLMNVFKG GTLFQDLPTQ HEHGVAHRSD SYDAFTHAVK VVNGGMMDKM
     YERKFGEIVS IHHQGVNKLG TGLQIEAVSD DGLVEAFSST EEDFYFGVQW HPEFHADEEE
     RFLSAEPLMK AFLKACKKAK EATPIQEPPL NP
//
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