YDJC_VIBC1
ID YDJC_VIBC1 Reviewed; 251 AA.
AC A7MTM7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Carbohydrate deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01246};
GN OrderedLocusNames=VIBHAR_03621;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) 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: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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000789; ABU72536.1; -; Genomic_DNA.
DR RefSeq; WP_012128955.1; NC_022269.1.
DR AlphaFoldDB; A7MTM7; -.
DR SMR; A7MTM7; -.
DR EnsemblBacteria; ABU72536; ABU72536; VIBHAR_03621.
DR KEGG; vha:VIBHAR_03621; -.
DR PATRIC; fig|338187.25.peg.2611; -.
DR OMA; EPTHIDS; -.
DR OrthoDB; 1204930at2; -.
DR Proteomes; UP000008152; Chromosome I.
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..251
FT /note="Carbohydrate deacetylase"
FT /id="PRO_1000067090"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
SQ SEQUENCE 251 AA; 28080 MW; 01ED92AB5BE7B169 CRC64;
MKVIFNADDF GLTQGVNNGI IKAHQQGVVL STTMMMGMDA EQHAVELANQ NPNLKIGVHL
RFTAGNPLTG HPNLTGGGEQ FVRFNELWKK RDFQEEAVYQ EAVAQVERFL SLGLPLSHID
SHHHAHTHPQ LLPVIRRVAE QYRVPLRGSG LCHIDCDTTY HFTDEFYDQG VSLDGVMAHL
KSLKSQYDVV EVMCHPADVD QHLLSISGYA LLRELELQVL TSPILKQELA EHGMSITDYS
TLISTRKFAS V