YDJC2_LISIN
ID YDJC2_LISIN Reviewed; 248 AA.
AC Q928S6;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Carbohydrate deacetylase 2 {ECO:0000255|HAMAP-Rule:MF_01246};
DE EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01246};
GN OrderedLocusNames=lin2456;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
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; AL596172; CAC97683.1; -; Genomic_DNA.
DR PIR; AC1739; AC1739.
DR RefSeq; WP_010991202.1; NC_003212.1.
DR AlphaFoldDB; Q928S6; -.
DR SMR; Q928S6; -.
DR STRING; 272626.lin2456; -.
DR DNASU; 1131244; -.
DR EnsemblBacteria; CAC97683; CAC97683; CAC97683.
DR KEGG; lin:lin2456; -.
DR eggNOG; COG3394; Bacteria.
DR HOGENOM; CLU_064244_4_0_9; -.
DR OMA; IGRDYGM; -.
DR OrthoDB; 1204930at2; -.
DR Proteomes; UP000002513; 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..248
FT /note="Carbohydrate deacetylase 2"
FT /id="PRO_0000051594"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
SQ SEQUENCE 248 AA; 28461 MW; 570B44FAA4EF8739 CRC64;
MKLIINADDF GFTRAINYGI IDAHNLGVLT STTLMVTMPA FEHAVDLSKK TPTLGIGLHL
NLTLGKPLTN GATLVNEDGE LIKPKFTTPE YPYNEEEVYQ EFKAQYHRFT EFMKKKPSHL
DSHLFSTDIY PVVTSAAKRL AEEIGIPLRN HDTKGFEHVE FMWEKPLEIP YGEYDNLDYI
YDNAASILCY DYVEIMTHPG YLDTFILENS TFSTPRANEL ESLISPRMRQ FLNENNVELI
SYHDIPKK
