ID   YDJC_VIBC3              Reviewed;         252 AA.
AC   A5F1P8; C3M046;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Carbohydrate deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE            EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01246};
GN   OrderedLocusNames=VC0395_A0904, VC395_1404;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
CC   -!- FUNCTION: Probably catalyzes the deacetylation of acetylated
CC       carbohydrates an important step in the degradation of oligosaccharides.
CC       {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   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01246}.
CC   -!- SIMILARITY: Belongs to the YdjC deacetylase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01246}.
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DR   EMBL; CP000627; ABQ20068.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP09412.1; -; Genomic_DNA.
DR   RefSeq; WP_000864268.1; NZ_JAACZH010000002.1.
DR   AlphaFoldDB; A5F1P8; -.
DR   SMR; A5F1P8; -.
DR   STRING; 345073.VC395_1404; -.
DR   PRIDE; A5F1P8; -.
DR   EnsemblBacteria; ABQ20068; ABQ20068; VC0395_A0904.
DR   KEGG; vco:VC0395_A0904; -.
DR   KEGG; vcr:VC395_1404; -.
DR   PATRIC; fig|345073.21.peg.1363; -.
DR   eggNOG; COG3394; Bacteria.
DR   HOGENOM; CLU_064244_4_0_6; -.
DR   OMA; EPTHIDS; -.
DR   Proteomes; UP000000249; Chromosome 2.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
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; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..252
FT                   /note="Carbohydrate deacetylase"
FT                   /id="PRO_1000073175"
FT   BINDING         59
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
SQ   SEQUENCE   252 AA;  28696 MW;  C17F0C9342B76AC5 CRC64;
     MKVIFNADDF GLTQGVNQGI VKAHLDGVVK STTLMVGMPA EQHAVQLAKQ LPELKIGLHL
     RFTAGRPLTG ERNLTDEHGV FTAYRDFWQR RDYQPEAIYH EAIAQVEHFL KLGLTLSHLD
     SHHHAHTHPQ LAPIIYEVAK KYHVPLRDIG MAGEEAFGCR YHFTDFFYDQ RLGIDPLMKH
     LLELKERFDL VEVMCHPAFV DPLLEKCSGY AKQREEELRI LTSAQLIQLL VAHDIEITDY
     SALISAPLHS CV