(data stored in ACNUC10821 zone)

SWISSPROT: YDJC_LISMF

ID   YDJC_LISMF              Reviewed;         245 AA.
AC   Q724M2;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=Carbohydrate deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE            EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01246};
GN   OrderedLocusNames=LMOf2365_0202;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
CC   -!- FUNCTION: Probably catalyzes the deacetylation of acetylated
CC       carbohydrates an important step in the degradation of
CC       oligosaccharides. {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.
CC       {ECO:0000255|HAMAP-Rule:MF_01246}.
DR   EMBL; AE017262; AAT02989.1; -; Genomic_DNA.
DR   RefSeq; WP_003722720.1; NC_002973.6.
DR   SMR; Q724M2; -.
DR   EnsemblBacteria; AAT02989; AAT02989; LMOf2365_0202.
DR   KEGG; lmf:LMOf2365_0202; -.
DR   HOGENOM; HOG000225034; -.
DR   KO; K03478; -.
DR   OMA; EPTHIDS; -.
DR   BioCyc; LMON265669:G1G0V-201-MONOMER; -.
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; 1.
DR   Pfam; PF04794; YdjC; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q724M2.
DR   SWISS-2DPAGE; Q724M2.
KW   Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN         1    245       Carbohydrate deacetylase.
FT                                /FTId=PRO_0000051595.
FT   METAL        59     59       Magnesium; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01246}.
FT   METAL       125    125       Magnesium; via pros nitrogen.
FT                                {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
//

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