G1092_BACFR
ID G1092_BACFR Reviewed; 425 AA.
AC Q64XS1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Glycosyl hydrolase family 109 protein 2;
DE EC=3.2.1.-;
GN OrderedLocusNames=BF0955;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
CC -!- FUNCTION: Glycosidase. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC Note=Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
CC {ECO:0000250};
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC subfamily. {ECO:0000305}.
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DR EMBL; AP006841; BAD47705.1; -; Genomic_DNA.
DR RefSeq; WP_011202216.1; NC_006347.1.
DR RefSeq; YP_098239.1; NC_006347.1.
DR AlphaFoldDB; Q64XS1; -.
DR SMR; Q64XS1; -.
DR CAZy; GH109; Glycoside Hydrolase Family 109.
DR EnsemblBacteria; BAD47705; BAD47705; BF0955.
DR KEGG; bfr:BF0955; -.
DR PATRIC; fig|295405.11.peg.956; -.
DR HOGENOM; CLU_046965_0_0_10; -.
DR OMA; ENCCYDP; -.
DR Proteomes; UP000002197; Chromosome.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; NAD.
FT CHAIN 1..425
FT /note="Glycosyl hydrolase family 109 protein 2"
FT /id="PRO_0000348550"
FT BINDING 29..30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 99..102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 119..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 194..198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 211..214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 425 AA; 47924 MW; 3724765F807705F2 CRC64;
MKTPSQTHVL GLAHPPLPMV RLAFIGLGNR GVLTLQRYLQ IEGVEIKALC EIREGNLVKA
QKILREAGYP QPDGYTGPDG WKRMCERDDI DLVFICTDWL THTPMAVYSM EHGKHVAIEV
PAAMTVEECW KLVDTAEKTR QHCMMLENCC YDPFALTTLN MAQQGAFGEI THVEGAYIHD
LRSIYFADES KGGFHNHWGK KYSIEHTGNP YPTHGLGPVC QILNIHRGDR MNYLVSLSSL
QAGMTEYARK NFGADSPEAR QKYLLGDMNT TLIQTVKGKS IMIQYNVVTP RPYSRLHTVC
GTKGFAQKYP VPSIALEPDA GSPLEGKALE EIMERYKHPF TATFGTEAHR RNLPNEMNYV
MDCRLIYCLR NGLPLDMDVY DAAEWSCITE LSEQSVLNGS IPVEIPDFTR GAWKKCHISR
TSDLY
