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Database: UniProt
Entry: A0A3D8YSP3_9BACL
LinkDB: A0A3D8YSP3_9BACL
Original site: A0A3D8YSP3_9BACL 
ID   A0A3D8YSP3_9BACL        Unreviewed;       438 AA.
AC   A0A3D8YSP3;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:REB05500.1};
GN   ORFNames=DVB69_14585 {ECO:0000313|EMBL:REB05500.1};
OS   Sporosarcina sp. BI001-red.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=2282866 {ECO:0000313|EMBL:REB05500.1, ECO:0000313|Proteomes:UP000256461};
RN   [1] {ECO:0000313|EMBL:REB05500.1, ECO:0000313|Proteomes:UP000256461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BI001-red {ECO:0000313|EMBL:REB05500.1,
RC   ECO:0000313|Proteomes:UP000256461};
RA   Rajandas H., Sivachandran P., Mai C.W., Cheong K.W., Teh C.S.J.,
RA   Lim E.S.H., Yap I.K.S., Convey P., Chong C.W.;
RT   "Draft Genome of Sporosarcina subantarcticus.";
RL   Submitted (JUL-2018) 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:REB05500.1}.
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DR   EMBL; QQAK01000015; REB05500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8YSP3; -.
DR   OrthoDB; 9808275at2; -.
DR   Proteomes; UP000256461; 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:UP000256461}.
FT   DOMAIN          195..409
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         170
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         200
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            110
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   438 AA;  48836 MW;  109B9C3EB270EED5 CRC64;
     MSLKIVIIGG GSSYTPEIIE GIIRRHDSFP VTDMVLVDIE EGKEKLRIVG ELSKRMILKS
     GKCINISWTL DRKEALVGAN FVSTQIRVGG LEARAKDERI PLSHGFIGQE TNGAGGIFKA
     FRTIPVMMEM AQDIHEICPD AWMINFTNPA GMITEALLKY SAHKKVIGVC NIPFNMRHST
     AEILDASPSD VDIEFIGMNH FVFGRKVTVN GVDRTEDVLS KLKSGLDYSP ANIVNLGWSQ
     TFIDSMKLLP NPYHQYYFQM KDVLKKDIQA FNEHGTRAEK VQELEKSLFE LYKSPELEDK
     PKELEERGGA FYSEVACSLM DSIYNNRKDI QTVNTFNNGA IPDLPNDAVI EVNSVITGNG
     PEPISVGPLP LTIKGIVCEM KAFEELVIQA GLSGNYHDAY VAMLMNPLMR DEKGSKMVLD
     ELLAAHKEYL PQFKGELE
//
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