ID   GH109_STRGG             Reviewed;         494 AA.
AC   B1W5J7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Glycosyl hydrolase family 109 protein;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=SGR_6325;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG23154.1; -; Genomic_DNA.
DR   RefSeq; WP_012381859.1; NC_010572.1.
DR   AlphaFoldDB; B1W5J7; -.
DR   SMR; B1W5J7; -.
DR   STRING; 455632.SGR_6325; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   EnsemblBacteria; BAG23154; BAG23154; SGR_6325.
DR   GeneID; 6210621; -.
DR   KEGG; sgr:SGR_6325; -.
DR   PATRIC; fig|455632.4.peg.6483; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_11; -.
DR   OMA; MESGKHA; -.
DR   OrthoDB; 1465613at2; -.
DR   Proteomes; UP000001685; 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   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; NAD; Signal.
FT   SIGNAL          1..58
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           59..494
FT                   /note="Glycosyl hydrolase family 109 protein"
FT                   /id="PRO_0000348567"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         104..105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         175..178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         195..196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         284..287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  54437 MW;  1DA3431A2D940FD3 CRC64;
     MNDDARPAPE PQDMPPHSGA ADEPARQDPS RRSVLWTTAG VAGAGIGLGA LGTGNASAAE
     STAPQALSAA EAAAAAPARQ GRTMAGVRFE GRSTIRVGIV GLGNRGGSMI DLFLAVPGVQ
     VKAVCDPVRD KAERAAAKVT AAGQPAPTVY AKGEDDYENL CKRGDLDFVY VATPWELHFP
     MAKTAMLNGK HVGVECPIAM RLDELWQLVD LSERTRRHCM QLENCCYGRN EMRVLRMAHA
     GLFGDLLHGA GAYNHDLREL MFDPDYYEGP WRRLWHTRLR GDLYPNHGFG PVANYMDVNR
     GDRASSISSI GTPALSLAEY RKERMPAGDP SWKESYIGAD RTISLVQTAK GRVIRLEHDV
     SSPHPYSRIN SLGGTRGVFE DYPERIYLEP TNTNHQWDDF KKYAEWDHWL WKEHANPPGG
     HGGMDYMMVF RLMQCMRLGL VPDFDVYDAA TWTAPVPLSH LSIKAKGAPL PIPDFTRGEW
     KKTRSGVDSE KPAE