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Database: UniProt
Entry: A0A0J5L7J8_PLUGE
LinkDB: A0A0J5L7J8_PLUGE
Original site: A0A0J5L7J8_PLUGE 
ID   A0A0J5L7J8_PLUGE        Unreviewed;       252 AA.
AC   A0A0J5L7J8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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};
GN   ORFNames=ABW06_03565 {ECO:0000313|EMBL:KMK15696.1};
OS   Pluralibacter gergoviae (Enterobacter gergoviae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Pluralibacter.
OX   NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK15696.1, ECO:0000313|Proteomes:UP000036196};
RN   [1] {ECO:0000313|EMBL:KMK15696.1, ECO:0000313|Proteomes:UP000036196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS81F13 {ECO:0000313|EMBL:KMK15696.1,
RC   ECO:0000313|Proteomes:UP000036196};
RA   Greninger A.L., Miller S.;
RT   "Genome sequences of Pluralibacter gergoviae.";
RL   Submitted (MAY-2015) 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:KMK15696.1}.
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DR   EMBL; LDZF01000003; KMK15696.1; -; Genomic_DNA.
DR   RefSeq; WP_048278207.1; NZ_LDZF01000003.1.
DR   AlphaFoldDB; A0A0J5L7J8; -.
DR   STRING; 61647.LG71_18365; -.
DR   PATRIC; fig|61647.15.peg.3037; -.
DR   eggNOG; COG3394; Bacteria.
DR   UniPathway; UPA00349; -.
DR   Proteomes; UP000036196; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000036196}.
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;  27401 MW;  A6B3147EDD2314C0 CRC64;
     MERILIVNAD DFGLSRGQNY GIVEACRNGL VTSTTALVNG EAIVHAAGLS RTLPELAVGM
     HFALTLGKPL TAMPGLTRDG RLGKWIWEMA EAGALPLDEI RRELIAQYQR FIDLFGAAPT
     HIDSHHHVHM IPPVFAIVAA FAKEMGVPVR IDRALQQRDG LDAAGLRSSD GFSSVFYGNG
     VSEALFLEVL ETSIAAGERS LEVMCHPAFV DNTIMGSAYC YPRLAELEIL TSASLQQEVA
     MKGYRLGSYR DV
//
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