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Database: UniProt
Entry: Q67LY5_SYMTH
LinkDB: Q67LY5_SYMTH
Original site: Q67LY5_SYMTH 
ID   Q67LY5_SYMTH            Unreviewed;       265 AA.
AC   Q67LY5;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Putative glutamine amidotransferase {ECO:0000313|EMBL:BAD41311.1};
GN   OrderedLocusNames=STH2326 {ECO:0000313|EMBL:BAD41311.1};
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD41311.1, ECO:0000313|Proteomes:UP000000417};
RN   [1] {ECO:0000313|EMBL:BAD41311.1, ECO:0000313|Proteomes:UP000000417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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DR   EMBL; AP006840; BAD41311.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q67LY5; -.
DR   STRING; 292459.STH2326; -.
DR   KEGG; sth:STH2326; -.
DR   eggNOG; COG2071; Bacteria.
DR   HOGENOM; CLU_030756_2_0_9; -.
DR   OrthoDB; 9813383at2; -.
DR   Proteomes; UP000000417; Chromosome.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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   ECO:0000313|EMBL:BAD41311.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000417};
KW   Transferase {ECO:0000313|EMBL:BAD41311.1}.
FT   ACT_SITE        130
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   265 AA;  29200 MW;  A7DA945222C6F107 CRC64;
     MTASLRAAGP ADRRPARKPI IGITPSFDRE CDRPLISGRP LLYVTQENVR AIRAAGGHAV
     ILPTCLDDED DLLDQLDGLL VTGTETPLPR RLRQREQLPG LREQNPERYD SDSRWLRGAL
     ARRMPVLAIC HGMQMLNDIL GGSLWPRIFP KNESERHAQT APPDQPWHPL HVLPGSLLAA
     SLGVTETMVN SFHVQAVRRP GDGVQVTGFS ADGVVEAIEC PGYPFVIGVQ FHPERLVRSN
     PHMLNLFRAF VSAAAAYAGE RCAVF
//
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