ID   GH109_PARD8             Reviewed;         466 AA.
AC   A6LB54;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Glycosyl hydrolase family 109 protein;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=BDI_1155;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
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   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP000140; ABR42918.1; -; Genomic_DNA.
DR   RefSeq; WP_005856826.1; NZ_LR215978.1.
DR   AlphaFoldDB; A6LB54; -.
DR   SMR; A6LB54; -.
DR   STRING; 435591.BDI_1155; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   EnsemblBacteria; ABR42918; ABR42918; BDI_1155.
DR   KEGG; pdi:BDI_1155; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_10; -.
DR   OMA; HPLWKKY; -.
DR   OrthoDB; 1465613at2; -.
DR   BioCyc; PDIS435591:G1G5A-1190-MON; -.
DR   Proteomes; UP000000566; 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   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; NAD; Reference proteome; Signal.
FT   SIGNAL          1..30
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           31..466
FT                   /note="Glycosyl hydrolase family 109 protein"
FT                   /id="PRO_0000348558"
FT   BINDING         59..60
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..133
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..152
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         241..245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         258..261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         340
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   466 AA;  51271 MW;  F1AB689EBAF06009 CRC64;
     MENTRRSFLK KVSAAGIGAA GLAMAGNAGA TTTAAEPQKK KTAGKDDGKL RFGFIGTGSR
     CHEHINNVLA IPGNKIVAIC DIQQGPIDST LKHIAKFNVP APKVYKGGER EFENMLNNEE
     FDCVIIASPW EWHVPMSVAA MKAGVPYVGV EVSAANTLEE CWDLVNVSEA TGSHLNIMEN
     VCYRRDCMAA LNMVRQGLFG EILHGGCGYE HDLREVKFND GTHYNYVPGS GDLRMGPTAF
     AEAQWRTNHS VHRNGDIYPT HGIGPIAHCM DINRGNRFLS LSAMATQSRG LHKFIVDNGG
     ENHPLAKVNF NLGDIVTSMI KCSNGQTIIV THDTNSPRPY SLGFRVQGTE GLWMNDGDHV
     YVQGKSKPHR WDDSDEWFKK YDHKLWASLE SQAAEAGHGG MDYIMMYDLI DAIRNKKPAP
     MDCYDAAAWS AISGLSEMSI ARGGALVDFP DFTRGQWIHR QPQFAL