ID   G1091_BACTN             Reviewed;         467 AA.
AC   Q89ZX8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Glycosyl hydrolase family 109 protein 1;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=BT_4243;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO79348.1; -; Genomic_DNA.
DR   RefSeq; NP_813154.1; NC_004663.1.
DR   RefSeq; WP_008759920.1; NZ_UYXG01000012.1.
DR   AlphaFoldDB; Q89ZX8; -.
DR   SMR; Q89ZX8; -.
DR   STRING; 226186.BT_4243; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   PaxDb; Q89ZX8; -.
DR   PRIDE; Q89ZX8; -.
DR   EnsemblBacteria; AAO79348; AAO79348; BT_4243.
DR   GeneID; 60925418; -.
DR   KEGG; bth:BT_4243; -.
DR   PATRIC; fig|226186.12.peg.4314; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_10; -.
DR   InParanoid; Q89ZX8; -.
DR   OMA; MESGKHA; -.
DR   Proteomes; UP000001414; 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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..467
FT                   /note="Glycosyl hydrolase family 109 protein 1"
FT                   /id="PRO_0000348551"
FT   BINDING         66..67
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         137..140
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..158
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         243..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  52832 MW;  E0CE1286819FC2FB CRC64;
     MKKLLLNTLI GLALLTCQTS FAQKTKAKFS PIKVETPARP ANQQDVIQLV TPKLETVRVG
     FIGLGMRGPG AVERWTHIPG TQIVALCDLL PERVENAQKI LEKAGLPKAA SYAGDEKAWK
     KLCERDDIDV VYIATDWKHH ADMGVYAMEH GKHVAIEVPA AMTLDEIWKL INTSEKTRKH
     CMQLENCVYD FFELTSLNMA QQGVFGEVLH VEGAYIHNLE DFWPYYWNNW RMDYNQKHRG
     DVYATHGMGP ACQVLNIHRG DRMKTLVAMD TKAVNGPAYI KKSTGKEVKD FQNGDQTTTL
     IRTENGKTML IQHNVMTPRP YSRMYQVVGA DGYASKYPIE EYCLRPTQVD SNDVPNHEKL
     NAHGSVSEDV KKALMAKYKD PIHKELEETA KKVGGHGGMD YIMDYRLVYC LRNGLPLDMD
     VYDLAEWCCM AELTRLSIEN GSAPVEVPDF TRGGWNKVQG YRHAFAE