ID   G1091_PHOV8             Reviewed;         471 AA.
AC   A6KX96;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Glycosyl hydrolase family 109 protein 1;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=BVU_0340;
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP000139; ABR38060.1; -; Genomic_DNA.
DR   RefSeq; WP_011964715.1; NC_009614.1.
DR   AlphaFoldDB; A6KX96; -.
DR   SMR; A6KX96; -.
DR   STRING; 435590.BVU_0340; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   EnsemblBacteria; ABR38060; ABR38060; BVU_0340.
DR   GeneID; 66748448; -.
DR   KEGG; bvu:BVU_0340; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_10; -.
DR   OMA; MESGKHA; -.
DR   OrthoDB; 1465613at2; -.
DR   BioCyc; BVUL435590:G1G59-358-MON; -.
DR   Proteomes; UP000002861; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycosidase; Hydrolase; Lipoprotein; Membrane; NAD;
KW   Palmitate; Reference proteome; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           16..471
FT                   /note="Glycosyl hydrolase family 109 protein 1"
FT                   /id="PRO_0000348553"
FT   BINDING         70..71
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
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         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247..250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   471 AA;  53449 MW;  8F9B3FACDD334804 CRC64;
     MIKNLSTFFV GIALSCLAGC TPIPKETTAT KEYAPLEVPV PERPAGQQDV IELTTPKLDT
     VRVGFIGLGM RGPSAVERWT HIPGTKIVAL CDLLPENAEK AQKIVTNAGM EAPALYSGSE
     DAWKQLCERN DIDLVYIATD WKHHTEMGIY AMEHGKHAAI EVPAAMSLDE IWALINTSEK
     TRKHCMQLEN CVYDFFELTT LNMAQKGLFG EVLHVEGSYI HNLEEFWPYY WNNWRLDYNR
     EFRGDVYATH GLGPACQLLN IHRGDRMKTL VAMDTKAVTG PELVKQYQKE EAPDFQNGDH
     TMTFIRTENG KTIHIQHDVM NPRPYSRMYQ LTGTKGFANK YPIEQYCFRP DQIDSTSIPD
     HENLSMHSAV PEKVKEALMS QYKHPIHQEL EETAKKIGGH GGMDFIMDYR LVYCLRNGLP
     LDMDVYDLAE WCCMADLTRL SIENGNAPVA VPDFTRGNWN KVDGYHHAFA Q