ID CHBG_ECO57 Reviewed; 252 AA.
AC Q8XE10;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 105.
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};
GN OrderedLocusNames=Z2763, ECs2439;
OS Escherichia coli O157:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG56719.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35862.1; -; Genomic_DNA.
DR PIR; C85782; C85782.
DR PIR; G90933; G90933.
DR RefSeq; NP_310466.1; NC_002695.1.
DR RefSeq; WP_000440480.1; NZ_VOAI01000007.1.
DR AlphaFoldDB; Q8XE10; -.
DR SMR; Q8XE10; -.
DR STRING; 155864.Z2763; -.
DR GeneID; 914120; -.
DR KEGG; ece:Z2763; -.
DR KEGG; ecs:ECs_2439; -.
DR PATRIC; fig|386585.9.peg.2553; -.
DR eggNOG; COG3394; Bacteria.
DR HOGENOM; CLU_064244_4_1_6; -.
DR OMA; DHIDSHH; -.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 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; Chitin degradation; Cytoplasm; Hydrolase;
KW Magnesium; Metal-binding; Polysaccharide degradation; Reference proteome.
FT CHAIN 1..252
FT /note="Chitooligosaccharide deacetylase"
FT /id="PRO_0000051591"
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; 28017 MW; 49183FE1A7B785FB CRC64;
MERLLIVNAD DFGLSKGQNY GIIEACRNGI VTSTTALVNG QAIDHAVQLS RDEPSLAIGM
NFVLTMGKPL TAMPGLTRDG VLGKWIWQLA EEDALPLEEI TQELASQYLR FIELFGRKPT
HLDSHHHVHM FPQIFPIVAR FAAEEGIALR IDRQPLSNAG DLPANLRSSH GFSSAFYGEE
ISEALFLQVL DDSSHRGERS LEVMCHPAFV DNTIRQSAYC FPRLTELEVL TSASLKYAIA
ERGYRLGSYL DV
//
