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CHBG_YERE8
ID   CHBG_YERE8              Reviewed;         253 AA.
AC   A1JKF8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE            Short=COD {ECO:0000255|HAMAP-Rule:MF_01246};
DE            EC=3.5.1.105 {ECO:0000255|HAMAP-Rule:MF_01246};
DE   AltName: Full=Chitin disaccharide deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE   AltName: Full=Chitobiose deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE   AltName: Full=Chitobiose-6P deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE   AltName: Full=Chitotriose deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE   AltName: Full=Chitotriose-6P deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
GN   Name=chbG {ECO:0000255|HAMAP-Rule:MF_01246}; OrderedLocusNames=YE0972;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Involved in the degradation of chitin. ChbG is essential for
CC       growth on the acetylated chitooligosaccharides chitobiose and
CC       chitotriose but is dispensable for growth on cellobiose and chitosan
CC       dimer, the deacetylated form of chitobiose. Deacetylation of
CC       chitobiose-6-P and chitotriose-6-P is necessary for both the activation
CC       of the chb promoter by the regulatory protein ChbR and the hydrolysis
CC       of phosphorylated beta-glucosides by the phospho-beta-glucosidase ChbF.
CC       Catalyzes the removal of only one acetyl group from chitobiose-6-P to
CC       yield monoacetylchitobiose-6-P, the inducer of ChbR and the substrate
CC       of ChbF. {ECO:0000255|HAMAP-Rule:MF_01246}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N,N'-diacetylchitobiose = acetate + N-acetyl-beta-D-
CC         glucosaminyl-(1->4)-D-glucosamine; Xref=Rhea:RHEA:27469,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:28681, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:59910; EC=3.5.1.105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01246};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diacetylchitobiose-6'-phosphate + H2O = acetate + N'-
CC         monoacetylchitobiose-6'-phosphate; Xref=Rhea:RHEA:35083,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:64883,
CC         ChEBI:CHEBI:71315; Evidence={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   -!- PATHWAY: Glycan degradation; chitin degradation. {ECO:0000255|HAMAP-
CC       Rule:MF_01246}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01246}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01246}.
CC   -!- SIMILARITY: Belongs to the YdjC deacetylase family. ChbG subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01246}.
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DR   EMBL; AM286415; CAL11070.1; -; Genomic_DNA.
DR   RefSeq; WP_011815723.1; NC_008800.1.
DR   RefSeq; YP_001005306.1; NC_008800.1.
DR   AlphaFoldDB; A1JKF8; -.
DR   SMR; A1JKF8; -.
DR   STRING; 393305.YE0972; -.
DR   EnsemblBacteria; CAL11070; CAL11070; YE0972.
DR   KEGG; yen:YE0972; -.
DR   PATRIC; fig|393305.7.peg.1073; -.
DR   eggNOG; COG3394; Bacteria.
DR   HOGENOM; CLU_064244_4_1_6; -.
DR   OMA; EPTHIDS; -.
DR   UniPathway; UPA00349; -.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0036311; F:chitin disaccharide deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0052777; P:diacetylchitobiose catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-UniRule.
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; 1.
DR   Pfam; PF04794; YdjC; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Chitin degradation; Cytoplasm; Hydrolase;
KW   Magnesium; Metal-binding; Polysaccharide degradation.
FT   CHAIN           1..253
FT                   /note="Chitooligosaccharide deacetylase"
FT                   /id="PRO_1000067091"
FT   BINDING         61
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
FT   BINDING         126
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
SQ   SEQUENCE   253 AA;  28383 MW;  5052CB15037CB65C CRC64;
     MEKLLIVNAD DFGLCKGQNY GIIEAFRHGI VSSTTAMMNC AEIYHAAELS KQNPALPVGM
     HFVLTYGRPL TAMQSLVDAK GELGKWLWAR AEAGELNLDE IAQELTAQFN KFVAVFGRPP
     THVDSHHHVH MLPQIYPLIE SFAHEKSLPL RIDRHEAQQQ GMVLNSPRST EWFDAGFYGE
     NLTEQSFLQL LAKADQNGIN TIEVMCHPAF IDKILMTSGY CYPRLTELEI LTSPALKQSI
     EQLGYRLGSY SDC
 
 
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