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Database: UniProt
Entry: A0A124HFB5_9ACTN
LinkDB: A0A124HFB5_9ACTN
Original site: A0A124HFB5_9ACTN 
ID   A0A124HFB5_9ACTN        Unreviewed;       445 AA.
AC   A0A124HFB5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:KUN03309.1};
GN   ORFNames=AQI95_22585 {ECO:0000313|EMBL:KUN03309.1};
OS   Streptomyces yokosukanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67386 {ECO:0000313|EMBL:KUN03309.1, ECO:0000313|Proteomes:UP000053127};
RN   [1] {ECO:0000313|EMBL:KUN03309.1, ECO:0000313|Proteomes:UP000053127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40224 {ECO:0000313|EMBL:KUN03309.1,
RC   ECO:0000313|Proteomes:UP000053127};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces yokosukanensis DSM 40224, type
RT   strain for the species Streptomyces yokosukanensis.";
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:KUN03309.1}.
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DR   EMBL; LMWN01000033; KUN03309.1; -; Genomic_DNA.
DR   RefSeq; WP_067126577.1; NZ_KQ948214.1.
DR   AlphaFoldDB; A0A124HFB5; -.
DR   STRING; 67386.AQI95_22585; -.
DR   OrthoDB; 9767022at2; -.
DR   Proteomes; UP000053127; 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:UP000053127}.
FT   DOMAIN          190..421
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        244
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         195
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   445 AA;  47859 MW;  050B41B2D9BB3836 CRC64;
     MKLTILGGGG FRVPLVYGAL LADRAEGRVT EVVLHDLDDR RLHAVGRVLD EQAAGVPDAP
     RVTATTDLDE ALAGADFVFS AIRVGGLAGR ADDERVALAE GVLGQETVGA GGIAYGLRTV
     PVAVDIARRV ARLAPDAWVI NFTNPAGLVT EAMSRHLGDR VIGICDSPVG LGRRVARALG
     ADPKQAFVDY VGLNHLGWVR ALRVAGRDEL PRLLADPALL GSFEEGRLFG VDWLQSLGAI
     PNEYLHYYYF NREAVRAYRQ AERTRGAFLR DQQARFYVEA QRTERSALHA WERTRAEREA
     TYMAENRENA GAGEREADDL SGGYEKVALA LMRAIARDER TTLILNVRNG STLAALDGDA
     VIEVPCLVDA GGAHPLAVAP LPAHATGLVC AVKAVEREVL AAAESGSRRT AVKAFALHPL
     VDSVNVARRL VDGYTEVHPG LAYLE
//
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