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Database: UniProt
Entry: A0A1V3S2C9_9BURK
LinkDB: A0A1V3S2C9_9BURK
Original site: A0A1V3S2C9_9BURK 
ID   A0A1V3S2C9_9BURK        Unreviewed;       270 AA.
AC   A0A1V3S2C9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Gamma-glutamyl-gamma-aminobutyrate hydrolase {ECO:0000313|EMBL:OOG83248.1};
GN   ORFNames=B0E41_13245 {ECO:0000313|EMBL:OOG83248.1};
OS   Hydrogenophaga sp. A37.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1945864 {ECO:0000313|EMBL:OOG83248.1, ECO:0000313|Proteomes:UP000189189};
RN   [1] {ECO:0000313|EMBL:OOG83248.1, ECO:0000313|Proteomes:UP000189189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A37 {ECO:0000313|EMBL:OOG83248.1,
RC   ECO:0000313|Proteomes:UP000189189};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) 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:OOG83248.1}.
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DR   EMBL; MUNZ01000107; OOG83248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3S2C9; -.
DR   STRING; 1945864.B0E41_13245; -.
DR   OrthoDB; 9813383at2; -.
DR   Proteomes; UP000189189; 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:OOG83248.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189189}.
FT   ACT_SITE        118
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   270 AA;  29385 MW;  54F31FD22C38987F CRC64;
     MNKPPPCMVW LPADHRLMGD HGHQMPFLLL GDKYARAVKV GAQAQPVMFP LADAEQIPDL
     LPMVDGVMLT GSPSNVHPSH FDEDVADPSL PLDPVRDSLT LALVKACVHE GVPLLGVCRG
     FQEINVALGG TLHQRVHEVP GLTDHREPKT APFDEQYAPR HAIRLAPGSV FETWAGGPET
     MVNSLHGQGI NRLAAGLEAM AHAPDGVVEA FAVKGARTFA YAMQFHPEWR CWETPFYAAI
     FEAFGHACRQ RMSQRLQAAD LARSRAGIGA
//
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