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Database: UniProt
Entry: A0A0W7WUS5_9ACTN
LinkDB: A0A0W7WUS5_9ACTN
Original site: A0A0W7WUS5_9ACTN 
ID   A0A0W7WUS5_9ACTN        Unreviewed;       446 AA.
AC   A0A0W7WUS5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:KUF14346.1};
GN   ORFNames=AT728_35825 {ECO:0000313|EMBL:KUF14346.1};
OS   Streptomyces silvensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1765722 {ECO:0000313|EMBL:KUF14346.1, ECO:0000313|Proteomes:UP000054804};
RN   [1] {ECO:0000313|EMBL:KUF14346.1, ECO:0000313|Proteomes:UP000054804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53525 {ECO:0000313|EMBL:KUF14346.1,
RC   ECO:0000313|Proteomes:UP000054804};
RA   Johnston C.W., Li Y., Magarvey N.A.;
RT   "Draft genome sequence of Streptomyces silvensis ATCC 53525, a producer of
RT   novel hormone antagonists.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|RuleBase:RU361152};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC       {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUF14346.1}.
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DR   EMBL; LOCL01000061; KUF14346.1; -; Genomic_DNA.
DR   RefSeq; WP_058851393.1; NZ_LOCL01000061.1.
DR   AlphaFoldDB; A0A0W7WUS5; -.
DR   STRING; 1765722.AT728_35825; -.
DR   OrthoDB; 9767022at2; -.
DR   Proteomes; UP000054804; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05296; GH4_P_beta_glucosidase; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR019802; GlycHydrolase_4_CS.
DR   InterPro; IPR001088; Glyco_hydro_4.
DR   InterPro; IPR022616; Glyco_hydro_4_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR32092:SF5; 6-PHOSPHO-BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW   Iron {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Manganese {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601088-3};
KW   NAD {ECO:0000256|RuleBase:RU361152};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054804}.
FT   DOMAIN          190..422
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   ACT_SITE        166
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   ACT_SITE        244
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         165
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         195
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            106
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   446 AA;  47883 MW;  3EEDAB8005356B92 CRC64;
     MRLVILGGGG FRVPLVYRAL LGDRAEGRIT EVVLHDVDAD RAGAIARVLA EQAAGVPDAP
     GVRVTADLDE ALRGADFVFS AIRVGGLRGR AADERVALDE GVLGQETVGA GGIAYGLRTV
     PVAVDIARRV ARLAPDAWVI NFTNPAGLVT EAMSRHIGDR VIGICDSPVG LGRRVARLLG
     AEPGRARLDY VGLNHLGWLS GLQVDGEDLL PRLLKDRDLL ESFEEGKLFG ADWLQSLGAI
     PNEYLHYYYF NREAVRAYQQ AERTRGAFLH DQQARFYTRM RNPETAAFAT WDATRAEREA
     TYMAHSRDAA GAGERAAEDM ESGGYEQVAL ALMRAIARDE RALLILNVRN RATLPQLDTD
     AVIEVPCTVD ASGAHPAAVS PLPGHATGLV CAVKAVEREV LAAVESGSRA TAVKAFALHP
     LVDSVSVARR LMDGYGQAHP GLAYLT
//
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