ID S0KY46_9ENTE Unreviewed; 464 AA.
AC S0KY46;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:EOT87404.1};
GN ORFNames=I573_00460 {ECO:0000313|EMBL:EOT87404.1};
OS Enterococcus sulfureus ATCC 49903.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1140003 {ECO:0000313|EMBL:EOT87404.1, ECO:0000313|Proteomes:UP000015961};
RN [1] {ECO:0000313|EMBL:EOT87404.1, ECO:0000313|Proteomes:UP000015961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49903 {ECO:0000313|EMBL:EOT87404.1,
RC ECO:0000313|Proteomes:UP000015961};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sulfureus ATCC_49903 (PacBio/Illumina
RT hybrid assembly).";
RL Submitted (MAR-2013) 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:EOT87404.1}.
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DR EMBL; ASWO01000001; EOT87404.1; -; Genomic_DNA.
DR RefSeq; WP_016184956.1; NZ_KE136393.1.
DR AlphaFoldDB; S0KY46; -.
DR STRING; 1140003.OMY_00465; -.
DR PATRIC; fig|1140003.3.peg.460; -.
DR eggNOG; COG1486; Bacteria.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000015961; 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; 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.
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:UP000015961}.
FT DOMAIN 198..415
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 113
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 464 AA; 52061 MW; AD0FA0F046125566 CRC64;
MTRGALKIAT IGGGSSYTPE LIEGYIKRKD ELPIKEIWLV DIEEGKEKLE IVGEMAKRMV
QAAGLDWEVH LTLDRRAALK DADFVSTQFR VGLLDARIKD ERIPLSHGVL GQETNGAGGM
FKAFRTIPVI LSIIEDMKEL CPDAWLVNFT NPAGMVTEAA IKHGGWKKTA GLCNVPIGHR
KQAAEKLGLP EEDLFFKFAG INHFHWHRVW DKEGNERTME LIDLIYGPQE DSESHLKNIH
NAPFHYEQIK DLGMLPCGYH RYYYIEDEML KHSIEEFERG ETRAQVVKDT EARLFELYKD
PNLDYKPKEL EQRGGTHYSD AACELIASIY NDKRTDMVVS TANNGTITDL PYDCVVEVSG
PVTAHGHEPY NWGAFPPAAR GIIQVMKGME ETVIRAAIDG DYGAALHAFT INPLVPGGMM
AKTLLDELLI AHKDHLPNFS EAIAKIETEQ PDTVAYVTEL MKSN
//
