YDJC_ENTFA
ID YDJC_ENTFA Reviewed; 262 AA.
AC P59745;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Carbohydrate deacetylase {ECO:0000255|HAMAP-Rule:MF_01246};
DE EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_01246};
GN OrderedLocusNames=EF_3048;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SUBUNIT.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of hypothetical protein (ef3048) from Enterococcus
RT faecalis V583 at 1.70 a resolution.";
RL Submitted (JUL-2011) to the PDB data bank.
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:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the YdjC deacetylase family. {ECO:0000255|HAMAP-
CC Rule:MF_01246}.
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DR EMBL; AE016830; AAO82730.1; -; Genomic_DNA.
DR RefSeq; NP_816660.1; NC_004668.1.
DR RefSeq; WP_010706778.1; NZ_KE136524.1.
DR PDB; 2I5I; X-ray; 1.70 A; A/B=1-262.
DR PDBsum; 2I5I; -.
DR AlphaFoldDB; P59745; -.
DR SMR; P59745; -.
DR STRING; 226185.EF_3048; -.
DR PRIDE; P59745; -.
DR EnsemblBacteria; AAO82730; AAO82730; EF_3048.
DR KEGG; efa:EF3048; -.
DR PATRIC; fig|226185.45.peg.522; -.
DR eggNOG; COG3394; Bacteria.
DR HOGENOM; CLU_064244_4_0_9; -.
DR OMA; EPTHIDS; -.
DR EvolutionaryTrace; P59745; -.
DR Proteomes; UP000001415; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..262
FT /note="Carbohydrate deacetylase"
FT /id="PRO_0000051592"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01246"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:2I5I"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2I5I"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:2I5I"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2I5I"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:2I5I"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2I5I"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:2I5I"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:2I5I"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:2I5I"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:2I5I"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2I5I"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:2I5I"
SQ SEQUENCE 262 AA; 29733 MW; EBA2944867B917B0 CRC64;
MSNKKLIINA DDFGYTPAVT QGIIEAHKRG VVTSTTALPT SPYFLEAMES ARISAPTLAI
GVHLTLTLNQ AKPILPREMV PSLVDEAGYF WHQSIFEEKV NLEEVYNEWD AQIISFMKSG
RRPDHIDSHH NVHGKNKKLL GVALALARKY QLPLRNASRS IETKDYLELY QDVRTPDEML
YQFYDKAIST ETILQLLDMV VCSEGEVFEI NCHPAFIDTI LQNQSGYCMP RIREVEILTS
QEVKEAIEER GILLANYESL AM
