ID B1SYW7_9BURK Unreviewed; 317 AA.
AC B1SYW7;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Peptidase C26 {ECO:0000313|EMBL:EDT43459.1};
GN ORFNames=BamMEX5DRAFT_0733 {ECO:0000313|EMBL:EDT43459.1};
OS Burkholderia ambifaria MEX-5.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT43459.1, ECO:0000313|Proteomes:UP000004814};
RN [1] {ECO:0000313|EMBL:EDT43459.1, ECO:0000313|Proteomes:UP000004814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEX-5 {ECO:0000313|EMBL:EDT43459.1,
RC ECO:0000313|Proteomes:UP000004814};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria MEX-
RT 5.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDT43459.1}.
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DR EMBL; ABLK01000014; EDT43459.1; -; Genomic_DNA.
DR AlphaFoldDB; B1SYW7; -.
DR PATRIC; fig|396597.7.peg.7643; -.
DR Proteomes; UP000004814; 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 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}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 287
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 289
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 317 AA; 35215 MW; CE8666B40A428E6F CRC64;
MPPGFGAQPD FDTPRPPPAS AQNAPPAYLK NSDTPWSVFG RIVAARARRL FDRAGQRITQ
RTLRIGVSAR IFHPEPGAKG LRGKTLQYLE ESIAHWVMSR DVLVFMIPTV GHQGMLHPSN
IRLRDYAKHL DGLLLQGGAD VSPQTYAASD ARPEWPGDRV RDMYELELFH EFVESGKPVL
GVCRGCQLIN VAFGGSLYQD IATDVPTAHP HVSEHYDQHR HSIRFPDSST LASMFPGRSE
AIVNSIHHQA IRDLGRDLNI EAVSAGDGII EGIRYRRAPF VVGVQWHPEF HRAGGSELLD
CTPLLDAFLR AARETRL
//