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Database: UniProt
Entry: B1SYW7_9BURK
LinkDB: B1SYW7_9BURK
Original site: B1SYW7_9BURK 
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
//
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