ID U4K1D5_9VIBR Unreviewed; 239 AA.
AC U4K1D5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Carbohydrate deacetylase {ECO:0000256|HAMAP-Rule:MF_01246};
DE EC=3.5.1.- {ECO:0000256|HAMAP-Rule:MF_01246};
GN ORFNames=VIBNI_A3049 {ECO:0000313|EMBL:CCO59070.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO59070.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO59070.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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}.
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DR EMBL; FO203526; CCO59070.1; -; Genomic_DNA.
DR RefSeq; WP_022551640.1; NC_022528.1.
DR AlphaFoldDB; U4K1D5; -.
DR STRING; 28173.VIBNI_A3049; -.
DR KEGG; vni:VIBNI_A3049; -.
DR PATRIC; fig|1260221.3.peg.2897; -.
DR eggNOG; COG3394; Bacteria.
DR OrthoDB; 9774177at2; -.
DR Proteomes; UP000016895; Chromosome 1.
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:0016740; F:transferase activity; 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}; Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW Transferase {ECO:0000313|EMBL:CCO59070.1}.
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01246"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01246"
SQ SEQUENCE 239 AA; 26870 MW; 481612BE11860CC0 CRC64;
MKVIFNADDF GLTHGVNQGI KEAHTQGVVN STTLMVGMDA DKEAVEMAKQ LPDLKVGIHL
RFTAGKPLTG SPNLQGDDGL FPKQPDFWPR RDFDAEAIEK EVRAQLEYFD QLGLDLSHID
SHHHAHGHPQ ILPIVENIAK ERGVPLRAQT VENCRYQFTE KFFDKTVELD ALLTLVSSYQ
DRCDVLEVMC HPAHVDEHLK QISSYALQRE KELSVLTDPR LKASLKDMGI EVSDYSAVL
//
