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Database: UniProt
Entry: A0A1Q4VBV8_9ACTN
LinkDB: A0A1Q4VBV8_9ACTN
Original site: A0A1Q4VBV8_9ACTN 
ID   A0A1Q4VBV8_9ACTN        Unreviewed;       455 AA.
AC   A0A1Q4VBV8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:OKH95341.1};
GN   ORFNames=AB852_00145 {ECO:0000313|EMBL:OKH95341.1};
OS   Streptomyces uncialis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1048205 {ECO:0000313|EMBL:OKH95341.1, ECO:0000313|Proteomes:UP000186455};
RN   [1] {ECO:0000313|EMBL:OKH95341.1, ECO:0000313|Proteomes:UP000186455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCA2648 {ECO:0000313|EMBL:OKH95341.1,
RC   ECO:0000313|Proteomes:UP000186455};
RA   Yan X., Huang T., Ge H., Shen B.;
RT   "Cloning and characterization of the uncialamcin biosynthetic gene
RT   cluster.";
RL   Submitted (JUN-2015) 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:OKH95341.1}.
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DR   EMBL; LFBV01000001; OKH95341.1; -; Genomic_DNA.
DR   RefSeq; WP_073782335.1; NZ_LFBV01000001.1.
DR   AlphaFoldDB; A0A1Q4VBV8; -.
DR   STRING; 1048205.AB852_00145; -.
DR   Proteomes; UP000186455; 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:UP000186455}.
FT   DOMAIN          198..431
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   ACT_SITE        173
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   ACT_SITE        252
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
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         172
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   455 AA;  48387 MW;  A2154EC762F3B23C CRC64;
     MRLAILGGGG FRVPLVHSAL LADRAEGRVT EVALHDTDPH RAAAIARVLA EQAQRAAEAD
     PTAPPAPRLT VTGDLDTALR GAHFVFSAIR VGGLAGRAAD ERVALAEGVL GQETVGAGGI
     AYGLRTLPVT DRIARRVAEI APDAWFINFT NPAGLVTEAM SRHLGDRVIG ICDSPVGLGR
     RVARALGATG RSDVEVDYVG LNHLGWLRGL RIDGEDELPR LFASTELLES FEEGRLFGAD
     WLRALGAVPN EYLHYYYFNR EAVRAYQAAP LTRGAFLDEQ QSRFYARVAD PGVPALRAWD
     EVRAEREATY MSESREAAGA GERDEASLTE SGGYEKVALA LMRAIARDER ATLVLNVRNR
     GALPGLDADA VVETPCRVDA HGAHPLPGGP LPAHAAGLVT SVKAVEREVM AAADSGSRAT
     AVKAFALHPL VDSVSVARRL VDGYVAAHPG LGYLT
//
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