ID   YDJC_BACC1              Reviewed;         234 AA.
AC   Q9XBH4;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Carbohydrate deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE            EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01246};
GN   OrderedLocusNames=BCE_5317;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10217496; DOI=10.1099/13500872-145-3-621;
RA   Oekstad O.A., Hegna I.K., Lindbaeck T., Rishovd A.-L., Kolstoe A.-B.;
RT   "Genome organization is not conserved between Bacillus cereus and Bacillus
RT   subtilis.";
RL   Microbiology 145:621-631(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
CC   -!- FUNCTION: Probably catalyzes the deacetylation of acetylated
CC       carbohydrates an important step in the degradation of oligosaccharides.
CC       {ECO:0000255|HAMAP-Rule:MF_01246}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01246};
CC   -!- SIMILARITY: Belongs to the YdjC deacetylase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01246}.
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DR   EMBL; AJ000394; CAB40624.1; -; Genomic_DNA.
DR   EMBL; AE017194; AAS44217.1; -; Genomic_DNA.
DR   RefSeq; WP_000593461.1; NC_003909.8.
DR   AlphaFoldDB; Q9XBH4; -.
DR   SMR; Q9XBH4; -.
DR   EnsemblBacteria; AAS44217; AAS44217; BCE_5317.
DR   GeneID; 59156696; -.
DR   KEGG; bca:BCE_5317; -.
DR   HOGENOM; CLU_064244_4_0_9; -.
DR   OMA; EPTHIDS; -.
DR   Proteomes; UP000002527; Chromosome.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   CDD; cd10803; YdjC_EF3048_like; 1.
DR   HAMAP; MF_01246; COD; 1.
DR   InterPro; IPR022948; COD_ChbG_bac.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR006879; YdjC-like.
DR   PANTHER; PTHR31609; PTHR31609; 2.
DR   Pfam; PF04794; YdjC; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..234
FT                   /note="Carbohydrate deacetylase"
FT                   /id="PRO_0000051585"
FT   BINDING         60
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
SQ   SEQUENCE   234 AA;  26406 MW;  D5DE81438BB1E086 CRC64;
     MIKLIVNADD FGLTEGTNYG IIDGHINGLV NSTTMMMNMP GTEHAVRLAK EHNTLGVGVH
     LVLTAGKPLL GDVPSLVSSD GLFHKQSVVW EGKINPEEVE REWTAQIEKF LSYGLTPTHL
     DSHHHVHGLP ILHDVLEKLA ATYNVPIRRC EEERAVRPFS DVFYSDFYAD GVTEDYFVKL
     KERVQGEQTV EIMVHPAYID PELVKRSSYV MDRVKELRIL TESELPEGIE LVKF