ID W7DGJ0_9LIST Unreviewed; 245 AA.
AC W7DGJ0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Carbohydrate deacetylase {ECO:0000256|HAMAP-Rule:MF_01246};
DE EC=3.5.1.- {ECO:0000256|HAMAP-Rule:MF_01246};
GN ORFNames=MCOL2_16642 {ECO:0000313|EMBL:EUJ48864.1};
OS Listeria fleischmannii FSL S10-1203.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265822 {ECO:0000313|EMBL:EUJ48864.1, ECO:0000313|Proteomes:UP000019241};
RN [1] {ECO:0000313|EMBL:EUJ48864.1, ECO:0000313|Proteomes:UP000019241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL S10-1203 {ECO:0000313|EMBL:EUJ48864.1,
RC ECO:0000313|Proteomes:UP000019241};
RA den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Novel taxa of Listeriaceae from agricultural environments in the United
RT States.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably catalyzes the deacetylation of acetylated
CC carbohydrates an important step in the degradation of oligosaccharides.
CC {ECO:0000256|HAMAP-Rule:MF_01246}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01246};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01246}.
CC -!- SIMILARITY: Belongs to the YdjC deacetylase family. {ECO:0000256|HAMAP-
CC Rule:MF_01246}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EUJ48864.1}.
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DR EMBL; AODM01000057; EUJ48864.1; -; Genomic_DNA.
DR RefSeq; WP_036064596.1; NZ_AODM01000057.1.
DR AlphaFoldDB; W7DGJ0; -.
DR PATRIC; fig|1265822.4.peg.3378; -.
DR Proteomes; UP000019241; Unassembled WGS sequence.
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 Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 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:SF1; CARBOHYDRATE DEACETYLASE; 1.
DR PANTHER; PTHR31609; YDJC DEACETYLASE FAMILY MEMBER; 1.
DR Pfam; PF04794; YdjC; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01246};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01246};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01246};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01246}.
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01246"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01246"
SQ SEQUENCE 245 AA; 27772 MW; DBA9C5298629DB26 CRC64;
MKLIFNADDF GMTKGAVYGT LDAYKNGVVR STTMLANGYA FDLGVQIAKE NPGLDIGVHL
ALTFGKPVLK DLKTLVDYEG KFYRNINELL QNAPDFSLEE VEREFTAQIE KIKAAGIAFT
HFDVHHMLEP HIYEVEHRLA EKYGVSVRRA LPEIGYERVT TTDLFMNDFY AEGVTMATIR
KIVEQYKGTD KVIEIMTHPA FLDEKLLAIS SYADIRMKEV TLLTSKELQN YLAQENVTLA
SFRDL
//
