ID   YDJC_VIBPA              Reviewed;         251 AA.
AC   Q87LH9;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Carbohydrate deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE            EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01246};
GN   OrderedLocusNames=VP2633;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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}.
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DR   EMBL; BA000031; BAC60896.1; -; Genomic_DNA.
DR   RefSeq; NP_799012.1; NC_004603.1.
DR   RefSeq; WP_005461089.1; NC_004603.1.
DR   AlphaFoldDB; Q87LH9; -.
DR   SMR; Q87LH9; -.
DR   STRING; 223926.28807643; -.
DR   EnsemblBacteria; BAC60896; BAC60896; BAC60896.
DR   GeneID; 1190177; -.
DR   KEGG; vpa:VP2633; -.
DR   PATRIC; fig|223926.6.peg.2529; -.
DR   eggNOG; COG3394; Bacteria.
DR   HOGENOM; CLU_064244_4_0_6; -.
DR   OMA; EPTHIDS; -.
DR   BRENDA; 3.5.1.105; 15981.
DR   Proteomes; UP000002493; Chromosome 1.
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..251
FT                   /note="Carbohydrate deacetylase"
FT                   /id="PRO_0000051604"
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   251 AA;  28031 MW;  23E07D5A670365FD CRC64;
     MKVIFNADDF GLTQGVNNGI VKSHQDGVVK STTMMVGMDA EQNAIELAHQ NPDLKIGVHL
     RFTAGAPLTE HPNLTNGRTH FVKYSELWNK QDFEAQAVYD EAKAQIDHFL SLGLTLSHLD
     SHHHAHTHPQ ILPIVQKLAK EHRVPLRGSG ICHQPMTTSY FFTDEFYDQK VSLDGLMQHL
     LSLKENYDVV EVMCHPAYAD QPLIMKSGYA LQRELELQVL TSPILKEQLA QHGIAVTDYS
     ALVSTSQVVG V