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
//