ID J8YPS9_ENTFC Unreviewed; 447 AA.
AC J8YPS9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative 6-phospho-beta-glucosidase {ECO:0000313|EMBL:EJV43414.1};
GN ORFNames=HMPREF1345_02465 {ECO:0000313|EMBL:EJV43414.1};
OS Enterococcus faecium TX1337RF.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1134802 {ECO:0000313|EMBL:EJV43414.1, ECO:0000313|Proteomes:UP000003117};
RN [1] {ECO:0000313|EMBL:EJV43414.1, ECO:0000313|Proteomes:UP000003117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX1337RF {ECO:0000313|EMBL:EJV43414.1,
RC ECO:0000313|Proteomes:UP000003117};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2012) 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:EJV43414.1}.
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DR EMBL; AMAA01000099; EJV43414.1; -; Genomic_DNA.
DR AlphaFoldDB; J8YPS9; -.
DR PATRIC; fig|1134802.3.peg.2309; -.
DR HOGENOM; CLU_045951_0_1_9; -.
DR Proteomes; UP000003117; 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}.
FT DOMAIN 177..391
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 182
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 92
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 447 AA; 50969 MW; 162A75121AC978BC CRC64;
MEGFIKRYEE LPIREIWLVD VEEGKEKLEI VSQMSQRMWD ASPYEVKIYA TLDREEALKD
ADFVTTQFRV GQLDARIKDE RIPSYYGMIG QETNGAGGIF KAFRTVPVVL AIVEDMKRLC
PNAWLINFAN PSGMVTEAVI RYGKWDKVIG LCNVPVMAMM TEPTMLGKKK EELIYKFAGL
NHFHWHKVAD NKGNDRTAEL IDHLYDEDNG LPKNIFDIPF FKEQLKQMNM IPCGYHRYYY
REEEMLEHAL EEYQTIGTRA QQVKETEAEL FELYKDPELD HKPEQLQKRG GAYYSDAACE
TIASIYGNKE TQIVVSTKND GAVPDLPADC VVEVTAYVGA QGARNVAFGS LPAAERGWLQ
VMKNMELLTI EAAVTGDYGT ALQAFTINPL IRSGKTAKRI MDELFIAHQQ YLPQFKETIS
RLKAEGIEVQ DELARELSSN THVMEEV
//
