ID   YDJC_LISW6              Reviewed;         245 AA.
AC   A0AEZ6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Carbohydrate deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE            EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01246};
GN   OrderedLocusNames=lwe0160;
OS   Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS   NCTC 11857 / SLCC 5334 / V8).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=386043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX   PubMed=16936040; DOI=10.1128/jb.00758-06;
RA   Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA   Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA   Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA   Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT   "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT   genome reduction with Listeria innocua as compared to Listeria
RT   monocytogenes.";
RL   J. Bacteriol. 188:7405-7415(2006).
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; AM263198; CAK19578.1; -; Genomic_DNA.
DR   RefSeq; WP_011701028.1; NC_008555.1.
DR   AlphaFoldDB; A0AEZ6; -.
DR   SMR; A0AEZ6; -.
DR   STRING; 386043.lwe0160; -.
DR   EnsemblBacteria; CAK19578; CAK19578; lwe0160.
DR   GeneID; 61188040; -.
DR   KEGG; lwe:lwe0160; -.
DR   eggNOG; COG3394; Bacteria.
DR   HOGENOM; CLU_064244_4_0_9; -.
DR   OMA; EPTHIDS; -.
DR   OrthoDB; 1204930at2; -.
DR   Proteomes; UP000000779; Chromosome.
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..245
FT                   /note="Carbohydrate deacetylase"
FT                   /id="PRO_1000067085"
FT   BINDING         59
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
FT   BINDING         125
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
SQ   SEQUENCE   245 AA;  27054 MW;  779C235D7F6D98A7 CRC64;
     MKIIFNADDF GISPGAVYGI LESYKKGVVK STTLLANSPA FDLAVEVAKE NPGLDIGAHL
     TLTFGSPLLQ GLETLTDDDG RFRKNYTALE NGLADVDMGE VERELTAQIK KILGAGLTIS
     HFDTHHSIEP LIYPIQHKLA EKYGVSIRRH ADVSDFGAIK TPDLFETAFY ADGVSFETIK
     KIVQAHIGTN DVVEVMTHPA FIDETLREIS SYVEPRIKEV SILTSRELQA YLGQQEVEVI
     SFRDL