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Database: UniProt
Entry: W4QL83_9BACI
LinkDB: W4QL83_9BACI
Original site: W4QL83_9BACI 
ID   W4QL83_9BACI            Unreviewed;       431 AA.
AC   W4QL83;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:GAE32846.1};
GN   ORFNames=JCM9152_4433 {ECO:0000313|EMBL:GAE32846.1};
OS   Halalkalibacter hemicellulosilyticusJCM 9152.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=1236971 {ECO:0000313|EMBL:GAE32846.1, ECO:0000313|Proteomes:UP000018895};
RN   [1] {ECO:0000313|EMBL:GAE32846.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9152 {ECO:0000313|EMBL:GAE32846.1};
RA   Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT   wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT   hemicellulosilyticus JCM 9152T.";
RL   Genome Announc. 2:e01258-13(2014).
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:GAE32846.1}.
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DR   EMBL; BAUU01000057; GAE32846.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4QL83; -.
DR   STRING; 1236971.JCM9152_4433; -.
DR   Proteomes; UP000018895; 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:UP000018895}.
FT   DOMAIN          193..407
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         167
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         197
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            108
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   431 AA;  48247 MW;  93D0FD084FD3AF95 CRC64;
     MKIAVIGGGS SYTPELIEGF INHYWELPVS EIYLVDIEQG KEKLEIVGNL ARRMVENANV
     PITINMTLDR RKAIEQADFV TTQIRVGLLE ARVRDEQIPL AFNLIGQETT GAGGFAKALR
     TIPVILDICK EIEELAPDAH LLNFTNPAGI VTEAVLKYSN VKTIGLCNLP IGTKMRIAQL
     YDVNPEHVEF EMIGINHLVW TTKIMVEGKN VTDDVLKKAS YTKGITVRNV PDFGWDPLFL
     KSLGALPCSY HKYYYMPNQM LQDQMKAMKG GEIRAKVVKK IEDELFELYQ ESNLKVKPKQ
     LELRGGAYYS EAAVNLMTSI YNNKKDIQVV NVQNKGILPC LPINCSIEIN CLIDKEGARP
     IQPSENLPTQ IRGLLQIVKA YEELTIEAAV RGDVDMALQA LSIHPLVGAD VAQPLLAKIL
     NENRRYLPQF N
//
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