CHBG_ESCF3
ID CHBG_ESCF3 Reviewed; 252 AA.
AC B7LQ59;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=EFER_1334;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ88856.1; -; Genomic_DNA.
DR RefSeq; WP_000440485.1; NC_011740.1.
DR AlphaFoldDB; B7LQ59; -.
DR SMR; B7LQ59; -.
DR EnsemblBacteria; CAQ88856; CAQ88856; EFER_1334.
DR KEGG; efe:EFER_1334; -.
DR HOGENOM; CLU_064244_4_1_6; -.
DR OMA; EPTHIDS; -.
DR OrthoDB; 1204930at2; -.
DR BioCyc; EFER585054:EFER_RS06740-MON; -.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000000745; 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..252
FT /note="Chitooligosaccharide deacetylase"
FT /id="PRO_1000139827"
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; 27890 MW; A1E4AD644A3607A7 CRC64;
MERLLIVNAD DFGLSKGQNY GIIEACRNGV VTSTTALVNG EAIDHAAQLS RGAPGLAVGM
HFVLTMGKPL TEMPGLTREG MLGKWIWQMA EEGALPLEEI SLELASQYQR FIELFGRKPT
HIDSHHHVHM FPQIFPIVAS FAAEQGIALR IDRQAVFNDS DLPGELRSSQ GFSSAFYGEE
ISNALFLKVL DDSSHRGERS LEVMCHPAFI DNTIRQSAYC FPRLTELDVL TSASLKYAIA
ERGYRLGSYL DV
