ID   YDJC_OCEIH              Reviewed;         230 AA.
AC   Q8EP46;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Carbohydrate deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE            EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01246};
GN   OrderedLocusNames=OB2271;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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   -!- SUBUNIT: Homodimer. {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; BA000028; BAC14227.1; -; Genomic_DNA.
DR   RefSeq; WP_011066663.1; NC_004193.1.
DR   AlphaFoldDB; Q8EP46; -.
DR   SMR; Q8EP46; -.
DR   STRING; 221109.22777956; -.
DR   PRIDE; Q8EP46; -.
DR   EnsemblBacteria; BAC14227; BAC14227; BAC14227.
DR   KEGG; oih:OB2271; -.
DR   eggNOG; COG3394; Bacteria.
DR   HOGENOM; CLU_064244_4_0_9; -.
DR   OMA; EPTHIDS; -.
DR   OrthoDB; 1204930at2; -.
DR   PhylomeDB; Q8EP46; -.
DR   Proteomes; UP000000822; 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;
KW   Reference proteome.
FT   CHAIN           1..230
FT                   /note="Carbohydrate deacetylase"
FT                   /id="PRO_0000051597"
FT   BINDING         59
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   230 AA;  26373 MW;  65A0A08B84798C16 CRC64;
     MRVEINADDY GLTKGVTDGI IKAHRGGCVT STTLMMNGLS VEYAVEQAKS NPALKVGIHL
     VLTWGRPISN DVASLVQSNG KFRYTSSYRE MDPPSLADVE KEWRAQIEEF KKTGLTLNHI
     DSHHHIHAWS PLTDVIIKLA KEFEVPVRYA DTLKDYPEIC WTEKIWVQFY QDGVNDNLFE
     QLKEEKVRSL EIMTHPGFVD EDLKENSSYL FTREKEVDVL CSIQIPEWVE