ID   G1095_PHOV8             Reviewed;         520 AA.
AC   A6L1Z2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Glycosyl hydrolase family 109 protein 5;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=BVU_2041;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000139; ABR39706.1; -; Genomic_DNA.
DR   RefSeq; WP_011965420.1; NC_009614.1.
DR   AlphaFoldDB; A6L1Z2; -.
DR   SMR; A6L1Z2; -.
DR   STRING; 435590.BVU_2041; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   EnsemblBacteria; ABR39706; ABR39706; BVU_2041.
DR   KEGG; bvu:BVU_2041; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_10; -.
DR   OMA; ENCCYDP; -.
DR   OrthoDB; 1465613at2; -.
DR   BioCyc; BVUL435590:G1G59-2133-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; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..520
FT                   /note="Glycosyl hydrolase family 109 protein 5"
FT                   /id="PRO_0000348557"
FT   BINDING         77..78
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         147..150
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..168
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         260..263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   520 AA;  58126 MW;  FF93DBD4DF77ACC8 CRC64;
     MRTFKSLMIS LCMGTTLCMC LPQTTTAQTV SSGDSWTWDK GTIVIDTPER PTGQKSVLGL
     TTPKMEVVRV GFVGLGMRGP GAVERFTYIP GTQIVALCDY EASRAEKCQD ILKKASMPKA
     AIYSGEKGYE ELCKRTDIDL VYIAADWLHH FPVAKCALEN GKNVAIEVPS AMNLQECWDL
     INLSEKTRKH CMILENCCYD WFEMNTLNMA QQGVFGEVIR AQGAYIHNLS PFWDHYWKNG
     KEDKLGWRLD YNMKHRGDVY ATHGLGPVAQ ALDIHRGDRI TTLVAMDTKS VVGKDLVEKR
     TGEECKEFRN GDHTTTLLRT ANGKVIEIQH NVMTPQPYNR LYQLTGSKGF ANKYPVEGYA
     LDAAQLTASG VQPKVDDLNS HGFLPQAEME ALVEKYQHPI LKKYGEMAKE VGGHGGMDFI
     MDSRLVYCLQ NGLPLDMDVY DLAEWCCLAE LGAISMDNGC AAVAFPDFTR GEWNVTKGYK
     HAYASPEDEN ANMEKAKAFT AKLKEQGAKE WAKEAKKKKK