ID B7JFN8_BACC0 Unreviewed; 441 AA.
AC B7JFN8;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ACK90542.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:ACK90542.1};
GN Name=celF {ECO:0000313|EMBL:ACK90542.1};
GN OrderedLocusNames=BCAH820_5297 {ECO:0000313|EMBL:ACK90542.1};
OS Bacillus cereus (strain AH820).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405535 {ECO:0000313|EMBL:ACK90542.1, ECO:0000313|Proteomes:UP000001363};
RN [1] {ECO:0000313|EMBL:ACK90542.1, ECO:0000313|Proteomes:UP000001363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH820 {ECO:0000313|EMBL:ACK90542.1,
RC ECO:0000313|Proteomes:UP000001363};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH820.";
RL Submitted (OCT-2008) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001283; ACK90542.1; -; Genomic_DNA.
DR RefSeq; WP_000145771.1; NC_011773.1.
DR AlphaFoldDB; B7JFN8; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR KEGG; bcu:BCAH820_5297; -.
DR HOGENOM; CLU_045951_0_1_9; -.
DR Proteomes; UP000001363; Chromosome.
DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
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}.
FT DOMAIN 196..411
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 111
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 441 AA; 49244 MW; 8F21EA42C501AD18 CRC64;
MTGIKIATIG GGSSYTPELI EGFIKRYDEL PVREIWLVDI EAGKEKLEVV GNLAKRMVKK
SGLPIEVHLT LDRREALKDA DFVTTQLRVG LLEARAKDEA IPLKYDVIGQ ETNGPGGLFK
ALRTIPVILD ICKDMEELCP NAWLINFANP AGMVTEAVLR YTNIQRVVGL CNVPIGIRMG
LAKLLEVDAS RVHVDFAGLN HMVYGLDVYL DGVSVMDRVL ELVTDPEKQI TMENIAALNW
EPDFIRGLRA IPCPYHRYYY KTREMLEEEK EASVEKGTRA EVVKQLEDDL FELYKDPNLD
IKPPQLEKRG GAYYSDAACS LITSIYNNKG DIQPVNTRNN GTIASLPHDS AVEVNCIITK
EGPKPIAVGD LPVPVRGLVQ QIKSFERTTI EAAVTGDYHK ALLAMTINPL VPSDKVAKQI
LDEMLEAHKE YLPQFFKKVE K
//
