CHBG_SHIF8
ID CHBG_SHIF8 Reviewed; 252 AA.
AC Q0T4U2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=SFV_1487;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(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; CP000266; ABF03673.1; -; Genomic_DNA.
DR RefSeq; WP_000440442.1; NC_008258.1.
DR AlphaFoldDB; Q0T4U2; -.
DR SMR; Q0T4U2; -.
DR EnsemblBacteria; ABF03673; ABF03673; SFV_1487.
DR GeneID; 58389719; -.
DR KEGG; sfv:SFV_1487; -.
DR HOGENOM; CLU_064244_4_1_6; -.
DR OMA; EPTHIDS; -.
DR BioCyc; SFLE373384:SFV_RS08330-MON; -.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000000659; 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; 2.
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..252
FT /note="Chitooligosaccharide deacetylase"
FT /id="PRO_1000067088"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
SQ SEQUENCE 252 AA; 27956 MW; 39B90CE26B65BB7D CRC64;
MERLLIVNAD DFGLSKGQNY GIIEACRNGI VTSTTALVNG QAIDHAVQLS RDEPSLAIGM
HFVLTMGKPL TAMPGLTRDG VLGKWIWQLA EEDALPLEEI TQELASQYLR FIELFGRKPT
HLDSHHHVHM FPQIFPIVAR FAAEEGIALR IDRQPLSNAG DLPANLRSSQ GFSSAFYGEE
ISEALFLQVL DDASHRGDPS LEVMCHPAFI DNTIRQSAYC FPRLTELEVL TSASLKYAIA
ERGYRLGSYL DV
