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Database: UniProt
Entry: Q5M6P3_CAMJU
LinkDB: Q5M6P3_CAMJU
Original site: Q5M6P3_CAMJU 
ID   Q5M6P3_CAMJU            Unreviewed;       200 AA.
AC   Q5M6P3;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 92.
DE   SubName: Full=Gamma-glutamyl-gamma-aminobutyrate hydrolase family protein {ECO:0000313|EMBL:EAK8194104.1};
GN   ORFNames=E7N58_08120 {ECO:0000313|EMBL:EAK8194104.1}, HS23.03
GN   {ECO:0000313|EMBL:CAI38892.1};
OS   Campylobacter jejuni.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=197 {ECO:0000313|EMBL:CAI38892.1};
RN   [1] {ECO:0000313|EMBL:CAI38892.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=G1 {ECO:0000313|EMBL:CAI38892.1};
RX   PubMed=15612919; DOI=10.1111/j.1365-2958.2004.04374.x;
RA   Karlyshev A.V., Champion O.L., Churcher C., Brisson J.R., Jarrell H.C.,
RA   Gilbert M., Brochu D., St Michael F., Li J., Wakarchuk W.W., Goodhead I.,
RA   Sanders M., Stevens K., White B., Parkhill J., Wren B.W., Szymanski C.M.;
RT   "Analysis of Campylobacter jejuni capsular loci reveals multiple mechanisms
RT   for the generation of structural diversity and the ability to form complex
RT   heptoses.";
RL   Mol. Microbiol. 55:90-103(2005).
RN   [2] {ECO:0000313|EMBL:EAK8194104.1, ECO:0000313|Proteomes:UP000358933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OXC2299 {ECO:0000313|EMBL:EAK8194104.1,
RC   ECO:0000313|Proteomes:UP000358933};
RA   Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BX545859; CAI38892.1; -; Genomic_DNA.
DR   EMBL; AACJKW010000012; EAK8194104.1; -; Genomic_DNA.
DR   RefSeq; WP_002860377.1; NZ_VACV01000018.1.
DR   AlphaFoldDB; Q5M6P3; -.
DR   PATRIC; fig|197.5165.peg.1389; -.
DR   Proteomes; UP000358933; 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   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
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; PF00117; GATase; 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:EAK8194104.1}.
FT   DOMAIN          56..195
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        101
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   200 AA;  23548 MW;  92DED997F47450FA CRC64;
     MFIGITQRLI CNDSYHEERE CLALDWGKLF NKDLFKNFTP LPLSYEIDFS YYKHLIKAVI
     LSGGNDLSFY SPNVLSKKRD LYEKQVIEIC LEEKIPLLGI CRGAQMIAHY FNSHMSPCEN
     HIGKHEVFFS KEKFISNSFH NFAIEKLGED LVELCLAEDN TIEAFKHKYE NIFGIMWHIE
     RENGLNNIQI LREWFSLIKE
//
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