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Database: UniProt
Entry: A0A101URR6_9ACTN
LinkDB: A0A101URR6_9ACTN
Original site: A0A101URR6_9ACTN 
ID   A0A101URR6_9ACTN        Unreviewed;       446 AA.
AC   A0A101URR6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:KUO15670.1};
GN   ORFNames=AQJ91_40065 {ECO:0000313|EMBL:KUO15670.1};
OS   Streptomyces dysideae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO15670.1, ECO:0000313|Proteomes:UP000053260};
RN   [1] {ECO:0000313|EMBL:KUO15670.1, ECO:0000313|Proteomes:UP000053260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RV15 {ECO:0000313|EMBL:KUO15670.1,
RC   ECO:0000313|Proteomes:UP000053260};
RA   Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA   Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT   sponge.";
RL   Submitted (OCT-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:KUO15670.1}.
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DR   EMBL; LMXB01000108; KUO15670.1; -; Genomic_DNA.
DR   RefSeq; WP_067032384.1; NZ_KQ949113.1.
DR   AlphaFoldDB; A0A101URR6; -.
DR   STRING; 909626.AQJ91_40065; -.
DR   OrthoDB; 9767022at2; -.
DR   Proteomes; UP000053260; 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:UP000053260}.
FT   DOMAIN          191..422
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   ACT_SITE        166
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   ACT_SITE        245
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         165
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         196
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            106
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   446 AA;  48030 MW;  B77B5CB59D69461B CRC64;
     MKLTILGGGG FRVPLVYGAL LGDRAEGRVT HVVLHDLDAG RLSAVTRVLV EQAGDVPDAP
     KVTATTDLDE ALRGADFIFS AIRVGGLEGR ANDERVALAE GVLGQETVGA GGIAYGLRTV
     PVAVDIAQRV ARLAPDAWLI NFTNPAGLVT EAMSRHLGDR VIGICDSPVG LGRRIARVLG
     AKNPGEAWID YVGLNHLGWV RGLRIAGRDE LPRLLADPDL LGSFEEGKLF GVDWLQSLGA
     IPNEYLHYYY FNREAVRSYQ EAEKTRGAFL ADQQARFYEE MKRPDAAALT AWDRTRAERE
     ATYMSENRET AGAGEREADD LSGGYEKVAL ALMRAIARDE RTTLILNVRN QGTLSVLDTD
     AVIEVPCLVD ANGAHPVAVA PLPDHATGLV CAVKAVEREV LAAAESGSRR TAVKAFALHP
     LVDSVNVARR LVEGYTDVHP GLAYLK
//
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