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Database: UniProt
Entry: A0A1D7VJ35_9ACTN
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ID   A0A1D7VJ35_9ACTN        Unreviewed;       232 AA.
AC   A0A1D7VJ35;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Gamma-glutamyl-gamma-aminobutyrate hydrolase {ECO:0000313|EMBL:AOP46775.1};
GN   ORFNames=SL103_11430 {ECO:0000313|EMBL:AOP46775.1};
OS   Streptomyces lydicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=47763 {ECO:0000313|EMBL:AOP46775.1, ECO:0000313|Proteomes:UP000094094};
RN   [1] {ECO:0000313|EMBL:AOP46775.1, ECO:0000313|Proteomes:UP000094094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=103 {ECO:0000313|EMBL:AOP46775.1,
RC   ECO:0000313|Proteomes:UP000094094};
RA   Jia N., Ding M.-Z., Gao F., Yuan Y.-J.;
RT   "Complete genome sequencing of Streptomyces lydicus 103 and metabolic
RT   pathways analysis of antibiotic biosynthesis.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP017157; AOP46775.1; -; Genomic_DNA.
DR   RefSeq; WP_069568755.1; NZ_CP017157.1.
DR   AlphaFoldDB; A0A1D7VJ35; -.
DR   KEGG; slc:SL103_11430; -.
DR   OrthoDB; 9813383at2; -.
DR   Proteomes; UP000094094; Chromosome.
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:AOP46775.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094094}.
FT   ACT_SITE        113
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        208
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   232 AA;  23639 MW;  2E84EC9043C42CDD CRC64;
     MSQPLIGIST YQQEASWGVW TMPAALVPAG YPRLVQRAGG LAALLPPGDP ATAAGAVARL
     DGLVIAGGAD VAPARYGAEP DPRTGPPSLD RDAWELALIE AALAGGVPLL GICRGMQLLN
     VALGGTLVQH LDGHAGPPGV FERHTVEPVP GTLLGRTLPE PVSVPTYHHQ AVDRLGSGLL
     PSAHAADGTI EALELPAGRG FTLAVQWHPE AGDDTRVMAA LVAAARGTSP GE
//
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