ID   YDJC_GEOSE              Reviewed;         245 AA.
AC   Q45401;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Carbohydrate deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE            EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01246};
GN   Name=celC;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=XL-65-6;
RX   PubMed=8407820; DOI=10.1128/jb.175.20.6441-6450.1993;
RA   Lai X., Ingram L.O.;
RT   "Cloning and sequencing of a cellobiose phosphotransferase system operon
RT   from Bacillus stearothermophilus XL-65-6 and functional expression in
RT   Escherichia coli.";
RL   J. Bacteriol. 175:6441-6450(1993).
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; U07818; AAA17391.1; -; Unassigned_DNA.
DR   PIR; D49898; D49898.
DR   AlphaFoldDB; Q45401; -.
DR   SMR; Q45401; -.
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..245
FT                   /note="Carbohydrate deacetylase"
FT                   /id="PRO_0000051588"
FT   BINDING         61
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
SQ   SEQUENCE   245 AA;  27430 MW;  554698A89142EF75 CRC64;
     MPRYCIVNAD DFGYSKGVNY GILEAFQNGV VTSATLMANM PAAEHAARLA KDHPELGVGI
     HFVLTCGRPL ADVPSLVNEN GEFPRRGEAL VGARRGDIER ELCAQLERFF SFGLTPTHID
     SHHHVHEHPN VFPVVEQLAE RYRLPIRPVR TARPHRLPTV DVFFPDFYGD GLTKDRFISL
     IDRIGDGQTA EVMCHPAYID VPLASGSSYC QQRVEELAVL TDPTLVAEMA ERGVQLITYR
     EFYKL