ID   YDJC_LISMO              Reviewed;         245 AA.
AC   Q8YAE0;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, 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=lmo0191;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591973; CAC98406.1; -; Genomic_DNA.
DR   PIR; AH1098; AH1098.
DR   RefSeq; NP_463722.1; NC_003210.1.
DR   RefSeq; WP_003722720.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8YAE0; -.
DR   SMR; Q8YAE0; -.
DR   STRING; 169963.lmo0191; -.
DR   PaxDb; Q8YAE0; -.
DR   EnsemblBacteria; CAC98406; CAC98406; CAC98406.
DR   GeneID; 987017; -.
DR   KEGG; lmo:lmo0191; -.
DR   PATRIC; fig|169963.11.peg.196; -.
DR   eggNOG; COG3394; Bacteria.
DR   HOGENOM; CLU_064244_4_0_9; -.
DR   OMA; EPTHIDS; -.
DR   PhylomeDB; Q8YAE0; -.
DR   BioCyc; LMON169963:LMO0191-MON; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
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..245
FT                   /note="Carbohydrate deacetylase"
FT                   /id="PRO_0000051596"
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;  27301 MW;  02BE255584AF4626 CRC64;
     MKIIFNADDF GISPGAVYGI LESYKRGVVK STTLLANSPA FDLAVEVAKE NPGLDIGAHL
     TLTFGSPVLQ GLETLTDDDG RFRRNYTSLE NGLADVDMNE VERELTAQIE KILDAGITIS
     HFDTHHSIEP LIYPVQHKLA EKYGVSIRRH SDVSDFGAIK TPDLFATEFY ADGVSFETIK
     KLVQKHIGTN DVVEVMTHPA FIDETLREIS SYVEPRIKEV SILTSRELQA YLGQQEVEII
     SFRDL