ID   GH109_STRNV             Reviewed;         494 AA.
AC   Q50HM6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Glycosyl hydrolase family 109 protein;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
OS   Streptomyces niveus (Streptomyces spheroides).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=193462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC   2449;
RX   PubMed=15870333; DOI=10.1128/aem.71.5.2452-2459.2005;
RA   Eustaquio A.S., Gust B., Galm U., Li S.M., Chater K.F., Heide L.;
RT   "Heterologous expression of novobiocin and clorobiocin biosynthetic gene
RT   clusters.";
RL   Appl. Environ. Microbiol. 71:2452-2459(2005).
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; AY227005; AAP48602.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q50HM6; -.
DR   SMR; Q50HM6; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   PRIDE; Q50HM6; -.
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..55
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           56..494
FT                   /note="Glycosyl hydrolase family 109 protein"
FT                   /id="PRO_0000348568"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         103..104
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         174..177
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         194..195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283..286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         365
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  54036 MW;  405D14B874FBB035 CRC64;
     MNDAAPQNPG QDEAKGTGEK DNGGSMSPRS ALRTTAGVAG AGLGLSALGT GTASASVPEA
     AQTAVPAAES DESAAPKRQG RTMAGVPFER RSTVRVGIIG LGNRGGSMID LFLAVPGVRV
     VALCDTVRDK AASAAAKVVK AGQPAPAVYT KDEHDYEQLC ARGDVDFVYV ATPWDFHFEM
     AKTAMLNGKH VGVECPVAMR LDELWKLVDL SERTRRHCMQ LENCAYGKNE MRVLRMAHAG
     LFGDLLHGAG AYNHDLRGLM FDPDYYEGPW RRLWHTRLRG DLYPNHGFGP VANYLDINRG
     DRAVSITSMG TPALGLAQYR EENMPPGDAS WKETYVSSDR TISLVQTAKG RVVRLEHDVS
     TPHPYSRINS LGGTRGVFED YPERIYIEPD HANDEWGDFA AYADWDHWLW KEHANPPGGH
     GGMDYIMVFR LMQCVRLGLV PDFDVYDAAT WTAPVPLSHA SIKANGKPQQ IPDFTRGEWK
     KSRPGTDSEK PSEP