ID   G1092_BACTN             Reviewed;         419 AA.
AC   Q89ZW9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Glycosyl hydrolase family 109 protein 2;
DE            EC=3.2.1.-;
GN   OrderedLocusNames=BT_4252;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO79357.1; -; Genomic_DNA.
DR   RefSeq; NP_813163.1; NC_004663.1.
DR   RefSeq; WP_008764451.1; NC_004663.1.
DR   AlphaFoldDB; Q89ZW9; -.
DR   SMR; Q89ZW9; -.
DR   STRING; 226186.BT_4252; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   PaxDb; Q89ZW9; -.
DR   PRIDE; Q89ZW9; -.
DR   EnsemblBacteria; AAO79357; AAO79357; BT_4252.
DR   GeneID; 60925427; -.
DR   KEGG; bth:BT_4252; -.
DR   PATRIC; fig|226186.12.peg.4323; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_10; -.
DR   InParanoid; Q89ZW9; -.
DR   OMA; ENCCYDP; -.
DR   Proteomes; UP000001414; 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; Reference proteome.
FT   CHAIN           1..419
FT                   /note="Glycosyl hydrolase family 109 protein 2"
FT                   /id="PRO_0000348552"
FT   BINDING         30..31
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         100..103
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         120..121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         195..199
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         212..215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   419 AA;  47308 MW;  D726E4E2F5217AFE CRC64;
     MEDSPTQSHV LQLAHPPIPI VRIGIIGLGN RGLLTLQRYL QIEGTEIKAL SEIREGNLNK
     AQLILKEAKH PEATGYTGPG GWRKMCECND LDLIFICTDW LTHTPMATYA MECGKHVAIE
     VPAAMNIAEC WQLVDTAEKT RRHCIMLENC CYDPFALTTL EMARQGVLGE IMHVEGAYIH
     DLRSMYFAEE SEGGYHNHWG KRYSIEHTGN PYPTHGLGPA CQILDIHRND RMEYLVSMST
     HQAGMSEYAR KRFGENSPEA RQKYKLGDVN TTLIHTAKGK TIMLQYNVST PRPYSRLQTV
     CGTLGFAQKY PVPCIALDSH GDTPLEGEAL ETVLTRYKHP FSATIGEEAH RKGLPNEMNY
     VMDYRLIYCL RNGLPLDMDV YDAAEWSCIT ELSEKSVLNG SIPVEIPDFT RGVWKKHKH