ID D2QAA0_BIFDB Unreviewed; 259 AA.
AC D2QAA0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Peptidase C26 {ECO:0000313|EMBL:ADB09736.1};
DE EC=6.3.5.2 {ECO:0000313|EMBL:ADB09736.1};
GN OrderedLocusNames=BDP_1100 {ECO:0000313|EMBL:ADB09736.1};
OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB09736.1, ECO:0000313|Proteomes:UP000008693};
RN [1] {ECO:0000313|EMBL:ADB09736.1, ECO:0000313|Proteomes:UP000008693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC {ECO:0000313|Proteomes:UP000008693};
RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT adaptation to the human oral cavity.";
RL PLoS Genet. 5:E1000785-E1000785(2009).
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DR EMBL; CP001750; ADB09736.1; -; Genomic_DNA.
DR RefSeq; WP_003840230.1; NC_013714.1.
DR AlphaFoldDB; D2QAA0; -.
DR STRING; 401473.BDP_1100; -.
DR GeneID; 69536720; -.
DR KEGG; bde:BDP_1100; -.
DR eggNOG; COG2071; Bacteria.
DR HOGENOM; CLU_030756_2_0_11; -.
DR Proteomes; UP000008693; Chromosome.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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 Ligase {ECO:0000313|EMBL:ADB09736.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008693}.
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 235
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 259 AA; 29056 MW; 4862EE55D3B7F5CA CRC64;
MKSRPIIGIT PLFDYERDSL WLLPGYMDGI EEAGGLPIML PLTSDDHEIR QLADMCDGIL
FTGGQDVNPT LYGEKVTPEY QATKPELSAE RDAMEPPLLD TMIRLDKPVL GICRGIQLIN
ACLGGTLWRD LPSEHPSDVK HHMMKPPYDA FGHDVTVEPG TPLDDMLNGM PQSQVDESTM
KRNDDGNWSI AVNSYHHQAV RTVAPTLKVM ATATDGITEA VYRPESRFLW AVQWHPEFLH
NVDARSRTIF SEFVNAARR
//
