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Database: UniProt
Entry: A0A0X3VU62_9ACTN
LinkDB: A0A0X3VU62_9ACTN
Original site: A0A0X3VU62_9ACTN 
ID   A0A0X3VU62_9ACTN        Unreviewed;       447 AA.
AC   A0A0X3VU62;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:KUL48057.1};
GN   ORFNames=ADL30_35660 {ECO:0000313|EMBL:KUL48057.1};
OS   Streptomyces sp. NRRL S-1521.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL48057.1, ECO:0000313|Proteomes:UP000053420};
RN   [1] {ECO:0000313|EMBL:KUL48057.1, ECO:0000313|Proteomes:UP000053420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL48057.1,
RC   ECO:0000313|Proteomes:UP000053420};
RA   Gilbert D.G.;
RL   Submitted (OCT-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:KUL48057.1}.
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DR   EMBL; LLZK01000272; KUL48057.1; -; Genomic_DNA.
DR   RefSeq; WP_062783333.1; NZ_LLZK01000272.1.
DR   AlphaFoldDB; A0A0X3VU62; -.
DR   Proteomes; UP000053420; 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:UP000053420}.
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   447 AA;  47220 MW;  372528B78052B272 CRC64;
     MQLTILGGGG FRVPLVYGAL LGDRAEGRVT DVVLHDLDAG RLDAVARVLA EQAAGVPGAP
     AVTATTDLDE ALRGADFVFS AIRVGGLEGR AADERVALAE GVLGQETVGA GGIAYGLRTV
     PVAVDIARRV ARLAPDAWVI NFTNPAGLVT EAMSRHLGNR VIGICDSPVG LGRRVARVLG
     GDPDEAFIDY VGLNHLGWLR GLRIAGRDEL PRLLADPELL GSFEEGRLFG VDWLRSLGAI
     PNEYLHYYYF NREAVAAYQA AEQTRGAFLR DQQARFYEAL GHPGAPALKT WDATRAEREA
     TYMAENREAA GAGERAEEDL GSGGYEKVAL ALMRAIARDE RATLILNVRN GATLAALDAD
     AVIEVPCSVD ANGAHPMAVG PLPGHATGLV CSVKAVEREV LAAADSGSRA TAVKAFALHP
     LVDSVAVARR LVEGYREAHP GLAYLRG
//
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