YDJC_BACCR
ID YDJC_BACCR Reviewed; 235 AA.
AC Q9L4R7;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Carbohydrate deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01246};
GN OrderedLocusNames=BC_5208;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hegna I.K., Borge S., Kolstoe A.-B.;
RT "Analysis of a possible efflux gene in Bacillus cereus.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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 -!- SIMILARITY: Belongs to the YdjC deacetylase family. {ECO:0000255|HAMAP-
CC Rule:MF_01246}.
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DR EMBL; AJ007952; CAB66320.1; -; Genomic_DNA.
DR EMBL; AE016877; AAP12073.1; -; Genomic_DNA.
DR RefSeq; NP_834872.1; NC_004722.1.
DR AlphaFoldDB; Q9L4R7; -.
DR SMR; Q9L4R7; -.
DR STRING; 226900.BC_5208; -.
DR EnsemblBacteria; AAP12073; AAP12073; BC_5208.
DR KEGG; bce:BC5208; -.
DR PATRIC; fig|226900.8.peg.5371; -.
DR HOGENOM; CLU_064244_4_0_9; -.
DR OMA; EPTHIDS; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1..235
FT /note="Carbohydrate deacetylase"
FT /id="PRO_0000051586"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
SQ SEQUENCE 235 AA; 26610 MW; 34D792FDB466D8F4 CRC64;
MMIKLIVNAD DFGLTEGTNY GIIDGHINGL VNSTTMMMNM PGTEHAVRLA KEYNLLGVGV
HLVLTAGEPL LKDVPSLVGE NGSFHKQSVV REGNINPEEV EREWTAQIEK FLSYGLTPTH
LDSHHHVHGL PILHDVLERL AAKYNVPIRR CEEDRAVHPF SDVFYSDFYA DGVTEDYFVK
LKERVQGEQT VEIMVHPAYI DPELVKRSSY VMDRVKELRI LTESELPEGI ELVKF
