ID   G1093_PHOV8             Reviewed;         548 AA.
AC   A6KYY1;
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 3;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=BVU_0950;
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; ABR38645.1; -; Genomic_DNA.
DR   RefSeq; WP_011964970.1; NC_009614.1.
DR   AlphaFoldDB; A6KYY1; -.
DR   SMR; A6KYY1; -.
DR   STRING; 435590.BVU_0950; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   EnsemblBacteria; ABR38645; ABR38645; BVU_0950.
DR   KEGG; bvu:BVU_0950; -.
DR   PATRIC; fig|435590.9.peg.982; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_10; -.
DR   OrthoDB; 1465613at2; -.
DR   BioCyc; BVUL435590:G1G59-995-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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..548
FT                   /note="Glycosyl hydrolase family 109 protein 3"
FT                   /id="PRO_0000348555"
FT   BINDING         71..72
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         141..144
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..162
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         240..244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         257..260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         335
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   548 AA;  62114 MW;  3618525A90D880A3 CRC64;
     MKLKKLLLSV LMLLSISGLQ AQSLSPSTQI HWDKGTLVIE TPERPTDQQH VLGLTAPKME
     TVRVAFVGLG MRGPWAVWRF CNIPGVEVVA LCDYEEDRAE ASQKYLRDAS LIPADIYSGE
     KGYETLCQRP DIDLVYIATD WNHHFPVAKY AMKHGKHVAI EVPSAMNLEQ CWSLIDLSEQ
     TRLHCFILEN CCYDYYEMNA LAMAKDGVFG EIIRAEGAYI HELSAFWKSY WQDPNDNDTD
     NLHWRMKYNM ENRGDVYATH GLGPVAQCMD IHRGDRFTTL VAMDTESFVG KQYVENLTGK
     EPKEFRNGDH TTTLMRTARG KVVEIQHNVM TPQPYNRLFK LTGTKGYATK YPTPEYALSG
     DVMKDTAPNM DDINAHSFLN DAQKEALEKK YYHPILTKFG EKGRAMGHGG MDYIMDARLV
     YCLQNGLPLD MDVYDLAEWC CLSELGALSM DNNCAAVTFP DFTRGHWDEM KGYKHAYASA
     EEEEATEAKA EAYTIAQKEV AAAANLWTLY DNVKNAADEK AQDKALKIYQ RAKAKAHQQL
     AKKLKVKK