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Database: UniProt
Entry: A0A1U7NQB0_9FIRM
LinkDB: A0A1U7NQB0_9FIRM
Original site: A0A1U7NQB0_9FIRM 
ID   A0A1U7NQB0_9FIRM        Unreviewed;       466 AA.
AC   A0A1U7NQB0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:OLU47800.1};
GN   ORFNames=BO225_01280 {ECO:0000313|EMBL:OLU47800.1};
OS   Dubosiella newyorkensis.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Dubosiella.
OX   NCBI_TaxID=1862672 {ECO:0000313|EMBL:OLU47800.1, ECO:0000313|Proteomes:UP000186705};
RN   [1] {ECO:0000313|EMBL:OLU47800.1, ECO:0000313|Proteomes:UP000186705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NYU-BL-A4 {ECO:0000313|EMBL:OLU47800.1,
RC   ECO:0000313|Proteomes:UP000186705};
RA   Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA   Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT   "Description of two novel members of the family Erysipelotrichaceae:
RT   Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT   gen. nov., sp. nov.";
RL   Submitted (NOV-2016) 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:OLU47800.1}.
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DR   EMBL; MPKA01000039; OLU47800.1; -; Genomic_DNA.
DR   RefSeq; WP_076340483.1; NZ_MPKA01000039.1.
DR   AlphaFoldDB; A0A1U7NQB0; -.
DR   STRING; 1862672.BO225_01280; -.
DR   GeneID; 78274581; -.
DR   OrthoDB; 9808275at2; -.
DR   Proteomes; UP000186705; 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:UP000186705}.
FT   DOMAIN          198..414
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   466 AA;  52429 MW;  425ADD3CB386CCE3 CRC64;
     MAKDGVKIAT IGGGSSYTPE LMEGFIKRYD ELPIKEIWLV DIEEGREKME IVGAMAQRMW
     DATPYDVRVH LTLDRKEALK DADFVTTQFR VGLLNARIKD ERIPLSYGIM GQETNGPGGI
     FKALRTIPVI LDIVEDMKEL CPNAWLINFT NPSGMVTEAV MKYGHWDKVI GLCNVPIGAM
     MKEPETIDKT LDELIYKFAG LNHFHWHRVW DNEGNEVTKG LIEAMYDPKK DSGIPANIFD
     MPFMKEQLLE MNMIPCGYHR YYYRQEEMLN HMLEEYASEE GVRAQQVKAT EAALFELYKD
     PNLNYKPEEL AKRGGAHYSD AACDTIASIY ANKNAHIVVT TRNNGAIPDL PEDVAVEVSS
     FIGATGAKPI AFGKLPTAER GWLQIMKAME QVTEEAAVTG DYAKLLTAFY LNPQIPSGAT
     AKRVMDELLV AHEKYLPQFA EDIARLKAEG VTIKDDVARE LYEKGL
//
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