ID W1F7L5_ECOLX Unreviewed; 252 AA.
AC W1F7L5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|HAMAP-Rule:MF_01246};
DE Short=COD {ECO:0000256|HAMAP-Rule:MF_01246};
DE EC=3.5.1.105 {ECO:0000256|HAMAP-Rule:MF_01246};
DE AltName: Full=Chitin disaccharide deacetylase {ECO:0000256|HAMAP-Rule:MF_01246};
DE AltName: Full=Chitobiose deacetylase {ECO:0000256|HAMAP-Rule:MF_01246};
DE AltName: Full=Chitobiose-6P deacetylase {ECO:0000256|HAMAP-Rule:MF_01246};
DE AltName: Full=Chitotriose deacetylase {ECO:0000256|HAMAP-Rule:MF_01246};
DE AltName: Full=Chitotriose-6P deacetylase {ECO:0000256|HAMAP-Rule:MF_01246};
GN Name=chbG {ECO:0000256|HAMAP-Rule:MF_01246};
OS Escherichia coli ISC7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=1432555 {ECO:0000313|EMBL:CDL30364.1, ECO:0000313|Proteomes:UP000019199};
RN [1] {ECO:0000313|EMBL:CDL30364.1, ECO:0000313|Proteomes:UP000019199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISC7 {ECO:0000313|EMBL:CDL30364.1,
RC ECO:0000313|Proteomes:UP000019199};
RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT "Antibiotic resistance diversity of beta-lactamase producers in the General
RT Hospital Vienna.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01246};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01246};
CC -!- PATHWAY: Glycan degradation; chitin degradation. {ECO:0000256|HAMAP-
CC Rule:MF_01246}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01246}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01246}.
CC -!- SIMILARITY: Belongs to the YdjC deacetylase family. ChbG subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01246}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDL30364.1}.
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DR EMBL; CBWN010000191; CDL30364.1; -; Genomic_DNA.
DR AlphaFoldDB; W1F7L5; -.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000019199; Unassembled WGS sequence.
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:0016740; F:transferase activity; 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 Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 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:SF1; CARBOHYDRATE DEACETYLASE; 1.
DR PANTHER; PTHR31609; YDJC DEACETYLASE FAMILY MEMBER; 1.
DR Pfam; PF04794; YdjC; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01246};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024, ECO:0000256|HAMAP-
KW Rule:MF_01246}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01246};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01246};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01246};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01246};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|HAMAP-Rule:MF_01246};
KW Transferase {ECO:0000313|EMBL:CDL30364.1}.
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01246"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01246"
SQ SEQUENCE 252 AA; 28058 MW; 9BBB1FC26B6636CB CRC64;
MERLLIVNAD DFGLSKGQNY GIIEACRNGI VTSTTALVNG QAIDHAVQLS RDEPSLAIGM
HFVLTMGKPL TAMPGLTRDG VLGKWIWQLA EEDALPLEEI TQELASQYLR FIELFGRKPT
HLDSHHHVHM FPQIFPIVAR FAAEEGIALR IDRQPLSNAG DLPANLRSSQ GFSSAFYGEE
ISEALFLQVL DDASHRGDRS LEVMCHPAFI DNTIRQSAYC FPRLTELEVL TSASLKYAIA
ERGYRLGSYR DV
//
