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Database: UniProt
Entry: A0A0R1HWA6_9LACO
LinkDB: A0A0R1HWA6_9LACO
Original site: A0A0R1HWA6_9LACO 
ID   A0A0R1HWA6_9LACO        Unreviewed;       250 AA.
AC   A0A0R1HWA6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Gamma-glutamyl-gamma-aminobutyrate hydrolase {ECO:0000313|EMBL:KRK47793.1};
GN   ORFNames=FC96_GL002281 {ECO:0000313|EMBL:KRK47793.1};
OS   Secundilactobacillus kimchicus JCM 15530.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1302272 {ECO:0000313|EMBL:KRK47793.1, ECO:0000313|Proteomes:UP000050911};
RN   [1] {ECO:0000313|EMBL:KRK47793.1, ECO:0000313|Proteomes:UP000050911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15530 {ECO:0000313|EMBL:KRK47793.1,
RC   ECO:0000313|Proteomes:UP000050911};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRK47793.1}.
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DR   EMBL; AZCX01000006; KRK47793.1; -; Genomic_DNA.
DR   RefSeq; WP_054661182.1; NZ_BBFK01000008.1.
DR   AlphaFoldDB; A0A0R1HWA6; -.
DR   STRING; 1302272.FC96_GL002281; -.
DR   PATRIC; fig|1302272.5.peg.2328; -.
DR   OrthoDB; 9813383at2; -.
DR   Proteomes; UP000050911; 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   Hydrolase {ECO:0000313|EMBL:KRK47793.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050911}.
FT   ACT_SITE        113
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        215
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        217
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   250 AA;  27312 MW;  8746A00BC7242B0D CRC64;
     MRPRIALPAD TLAEATNIIN ERNAAFAPRP AIEAVVKAGG VPVIFPSVDP VDVPDYMDLF
     DGVAFLGGSD VDPTFYGEEP YEKLGVTYRK RDLFEIELLK QAVASGKAIL GICRGMQLIN
     VGLGGTLYQD LSQDPHATLK HDQLAPGNMP SHHISVADDS KIISIVGERP YVNSRHHEAV
     KDVAPNLRVV ARADDQVVEA VESIGSDQII GVQWHPENMY KHHADSKAIF ADFIERSARV
     AESSRSVRQP
//
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