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Database: UniProt
Entry: A0A101QV13_9ACTN
LinkDB: A0A101QV13_9ACTN
Original site: A0A101QV13_9ACTN 
ID   A0A101QV13_9ACTN        Unreviewed;       421 AA.
AC   A0A101QV13;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:KUN36458.1};
GN   ORFNames=AQJ30_21420 {ECO:0000313|EMBL:KUN36458.1};
OS   Streptomyces longwoodensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68231 {ECO:0000313|EMBL:KUN36458.1, ECO:0000313|Proteomes:UP000053271};
RN   [1] {ECO:0000313|EMBL:KUN36458.1, ECO:0000313|Proteomes:UP000053271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41677 {ECO:0000313|EMBL:KUN36458.1,
RC   ECO:0000313|Proteomes:UP000053271};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces longwoodensis DSM 41677, type strain
RT   for the species Streptomyces longwoodensis.";
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:KUN36458.1}.
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DR   EMBL; LMWS01000024; KUN36458.1; -; Genomic_DNA.
DR   RefSeq; WP_067236465.1; NZ_KQ948555.1.
DR   AlphaFoldDB; A0A101QV13; -.
DR   STRING; 68231.AQJ30_21420; -.
DR   Proteomes; UP000053271; 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:UP000053271}.
FT   DOMAIN          190..397
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
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         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         194
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   SITE            106
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   421 AA;  44948 MW;  A3B082D56F2E373E CRC64;
     MKLTVVGGGS TYTPELVDGF ARLRDTLPVE ELVLVDPAAD RLELVGGLAR RIFAKQGHAG
     RIVTTTDLDA GVDGADAVLL QLRVGGQAAR EQDETWPLEC GCVGQETTGA GGLAKALRTV
     PVVLDIAERV RRTNPRAWII DFTNPVGIVT RALLKAGHRS VGLCNVAIGF QRKFAALLGV
     APAQVHLDHV GLNHLTWETG VRLGGPEGED VLPKLLAGHA GAIAADLRLP RSLLDRLGVV
     PSYYLRYFYA HDEVVEEQRT KPPRAAEVAA MERELLEMYG DPALDEKPEL LARRGGAFYS
     EAAVDLAAAL LGGGGSPYQV VNTYNHGTLP FLPADAVVEV QAAVGAQGAS PLPVPRVDPL
     YAGLMAHVTA YEDLALEAAL RGGRDRVVRA LLAHPLIGQH AYADRLADEL IAHNREHLAW
     A
//
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