ID   G1092_PHOV8             Reviewed;         413 AA.
AC   A6KY05;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Glycosyl hydrolase family 109 protein 2;
DE            EC=3.2.1.-;
GN   OrderedLocusNames=BVU_0611;
OS   Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS   NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Phocaeicola.
OX   NCBI_TaxID=435590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC   11154;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000139; ABR38319.1; -; Genomic_DNA.
DR   RefSeq; WP_008667589.1; NC_009614.1.
DR   AlphaFoldDB; A6KY05; -.
DR   SMR; A6KY05; -.
DR   STRING; 435590.BVU_0611; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   EnsemblBacteria; ABR38319; ABR38319; BVU_0611.
DR   KEGG; bvu:BVU_0611; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_10; -.
DR   OMA; LENACYD; -.
DR   OrthoDB; 1465613at2; -.
DR   BioCyc; BVUL435590:G1G59-638-MON; -.
DR   Proteomes; UP000002861; 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..413
FT                   /note="Glycosyl hydrolase family 109 protein 2"
FT                   /id="PRO_0000348554"
FT   BINDING         26..27
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         96..99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..117
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         191..195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         208..211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  47369 MW;  CEFFE1AFC55F51E6 CRC64;
     MKRPNVLNLT CPAIPVVRIG FVGLGNRGIL ALERYMHLEG IEVKALCDLR KENIERAEHI
     LREFGRPEAE NYSEEGMWRK MCECKEIDLI YICTDWLTHT DIAVYALQQG RHVALEVPAA
     MSVADCWRLV DTAEETRRHC MMLENCCYDA FALTTLNMVQ QGVLGEITHA EGAYIHDLRK
     HYFADEKAGG YHNHWIKLYS QQHTGNPYPT HGLGPVCQWM NIHRGDRMEY LVSMSSRQAG
     LSAYAGQVFG ASSEEAAQSY EMGDVNTTLI HTAKGRTILL QYDVTTPRPY SRHQTVCGTK
     GFMQKYPVPC LLLDEYGKEP LSGEQFERMM EQYKHPFTAV IGEEARRKNM PNEMNYIMDY
     RLIHCLRNGL PLDQDVYDAA EWSCITELSE RSVRQGSVPV EIPDFTRGNW KER