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Database: UniProt
Entry: A0A2J9DXD1_9GAMM
LinkDB: A0A2J9DXD1_9GAMM
Original site: A0A2J9DXD1_9GAMM 
ID   A0A2J9DXD1_9GAMM        Unreviewed;       247 AA.
AC   A0A2J9DXD1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Gamma-glutamyl-gamma-aminobutyrate hydrolase {ECO:0000313|EMBL:PNK60182.1};
GN   ORFNames=A6J60_004385 {ECO:0000313|EMBL:PNK60182.1};
OS   Psychrobacter sp. FDAARGOS_221.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=1975705 {ECO:0000313|EMBL:PNK60182.1, ECO:0000313|Proteomes:UP000217719};
RN   [1] {ECO:0000313|Proteomes:UP000217719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_221 {ECO:0000313|Proteomes:UP000217719};
RA   Hoffmann M., Allard M., Evans P., Brown E., Tallon L., Sadzewicz L.,
RA   Sengamalay N., Ott S., Godinez A., Nagaraj S., Vavikolanu K.,
RA   Aluvathingal J., Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (DEC-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:PNK60182.1}.
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DR   EMBL; NWFK02000001; PNK60182.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J9DXD1; -.
DR   OrthoDB; 9813383at2; -.
DR   Proteomes; UP000217719; 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:PNK60182.1}.
FT   ACT_SITE        112
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        218
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   247 AA;  27624 MW;  C0754B189309039C CRC64;
     MTISKPIIGI VCCQKTVDKQ PTQAVYDKYV QAIQHHGGAP VLLPHALVED DSFHTVLSMV
     DGILLTGSYS NVAPERYGAT HEELKKDLTR DALTFKLLEY AETNQVPLLA ICRGLQEMNV
     YFGGTLHPDW REVEGFYEQH LEDGNAPMEV QYQPVHDVII QSGGHLSAFN TQWKVNSLHK
     QCINQVGEGL LVEATAPDTL IEAISLPTHP YLLGVQWHPE ADYNNDEMSK YLFSGFINHA
     KQAKGRD
//
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