ID   YDJC_VIBVY              Reviewed;         252 AA.
AC   Q7MHH4;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Carbohydrate deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE            EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01246};
GN   OrderedLocusNames=VV2897;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC95661.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000037; BAC95661.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043877327.1; NC_005139.1.
DR   AlphaFoldDB; Q7MHH4; -.
DR   SMR; Q7MHH4; -.
DR   STRING; 672.VV93_v1c26030; -.
DR   EnsemblBacteria; BAC95661; BAC95661; BAC95661.
DR   KEGG; vvy:VV2897; -.
DR   PATRIC; fig|196600.6.peg.2880; -.
DR   eggNOG; COG3394; Bacteria.
DR   HOGENOM; CLU_064244_4_0_6; -.
DR   OMA; EPTHIDS; -.
DR   Proteomes; UP000002675; Chromosome I.
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;
KW   Reference proteome.
FT   CHAIN           1..252
FT                   /note="Carbohydrate deacetylase"
FT                   /id="PRO_0000051606"
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;  28480 MW;  DA6FCB6C28D74657 CRC64;
     MKVIFNADDF GLTRGVNDGI VHAHLDGVVR STTMMVGMPA EAHAVELANH LPELKVGLHL
     RFTAGRPLTE GQNLVGRDGD FTPYGQFWHR RDYDPIAIHN EAVAQVEYFL ALGLNLSHID
     SHHHAHTHPQ FEPVIYDIAR TYQVPLRSTG LAGEEEFGCR YHFTDHFYDK RVGHDSLIQH
     LLTLKEHYDV VEVMCHPAIL DTALEACSGY AKQRELELAI LTSDELKLSL RKHDIEVTDY
     SELIFAPLHS CV