YDJC_THET8
ID YDJC_THET8 Reviewed; 264 AA.
AC Q53WD3;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Carbohydrate deacetylase {ECO:0000303|PubMed:18177738};
DE EC=3.5.1.- {ECO:0000305|PubMed:18177738};
GN OrderedLocusNames=TTHB029;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, FUNCTION,
RP COFACTOR, ACTIVE SITE, AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=18177738; DOI=10.1016/j.bbrc.2007.12.144;
RA Imagawa T., Iino H., Kanagawa M., Ebihara A., Kuramitsu S., Tsuge H.;
RT "Crystal structure of the YdjC-family protein TTHB029 from Thermus
RT thermophilus HB8: structural relationship with peptidoglycan N-
RT acetylglucosamine deacetylase.";
RL Biochem. Biophys. Res. Commun. 367:535-541(2008).
CC -!- FUNCTION: Probably catalyzes the deacetylation of acetylated
CC carbohydrates an important step in the degradation of oligosaccharides.
CC {ECO:0000305|PubMed:18177738}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18177738};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18177738}.
CC -!- SIMILARITY: Belongs to the YdjC deacetylase family. {ECO:0000305}.
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DR EMBL; AP008227; BAD71825.1; -; Genomic_DNA.
DR RefSeq; WP_011229247.1; NC_006462.1.
DR RefSeq; YP_145268.1; NC_006462.1.
DR PDB; 2E67; X-ray; 2.90 A; A/B/C/D/E/F=1-264.
DR PDBsum; 2E67; -.
DR AlphaFoldDB; Q53WD3; -.
DR SMR; Q53WD3; -.
DR EnsemblBacteria; BAD71825; BAD71825; BAD71825.
DR GeneID; 3169536; -.
DR KEGG; ttj:TTHB029; -.
DR PATRIC; fig|300852.9.peg.1973; -.
DR HOGENOM; CLU_064244_0_0_0; -.
DR OMA; DFHCLAD; -.
DR EvolutionaryTrace; Q53WD3; -.
DR Proteomes; UP000000532; Plasmid pTT27.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR006879; YdjC-like.
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 Plasmid; Reference proteome.
FT CHAIN 1..264
FT /note="Carbohydrate deacetylase"
FT /id="PRO_0000432126"
FT ACT_SITE 20
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:18177738"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:18177738"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18177738"
FT BINDING 60
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18177738"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18177738"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:2E67"
FT STRAND 12..22
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:2E67"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:2E67"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2E67"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2E67"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 101..116
FT /evidence="ECO:0007829|PDB:2E67"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:2E67"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:2E67"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 242..249
FT /evidence="ECO:0007829|PDB:2E67"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:2E67"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:2E67"
SQ SEQUENCE 264 AA; 29599 MW; 7A7CD632DF2424E9 CRC64;
MDLLERLGLG GRRVLILHHD DLGLTHAQNG AYQALGLPTG SVMVPGAWAS GVKGEDLGVH
LVLTSEWPAP RMRPLTEGES LRDEAGYFPE SLEALWRKAR AEEVERELKA QIQAAAKLFS
PTHLDAHQGA VLRPDLAEVY LRLAEAYRLV PLVPESLEGL GVPPPFLPEL ERLLYETPFP
QVRFLDPYGL PPEERLGFYL DLAHLPPGLY YLVHHSALPT PEGRALPDWP TREADYFALS
HPEVRRVLAE FHPLTWRAVR EALF
