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Entry: A0A1I5QB20_9ACTN
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ID   A0A1I5QB20_9ACTN        Unreviewed;       423 AA.
AC   A0A1I5QB20;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:SFP43211.1};
GN   ORFNames=SAMN04489713_11458 {ECO:0000313|EMBL:SFP43211.1};
OS   Actinomadura madurae.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=1993 {ECO:0000313|EMBL:SFP43211.1, ECO:0000313|Proteomes:UP000183413};
RN   [1] {ECO:0000313|EMBL:SFP43211.1, ECO:0000313|Proteomes:UP000183413}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43067 {ECO:0000313|EMBL:SFP43211.1,
RC   ECO:0000313|Proteomes:UP000183413};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOVH01000014; SFP43211.1; -; Genomic_DNA.
DR   RefSeq; WP_075023351.1; NZ_FOVH01000014.1.
DR   AlphaFoldDB; A0A1I5QB20; -.
DR   STRING; 1993.SAMN04489713_11458; -.
DR   eggNOG; COG1486; Bacteria.
DR   InParanoid; A0A1I5QB20; -.
DR   Proteomes; UP000183413; 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   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:UP000183413}.
FT   DOMAIN          188..398
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   ACT_SITE        163
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         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         162
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         192
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   423 AA;  45137 MW;  93E26B43329075CD CRC64;
     MKIAIIGAGS GYMPGVIRGL LHRADDLAGA ELAFHDVDTA HLDVMTRLAR GMFSARGAAF
     TVESHTGLKP ALDGASYVFT TFRPGGLAAR HLDESIPLKH GVVGQETAGP GGFLMALRSV
     PVLLEIASAA DPGAWIVNYT NPTNIVTDAV ARATGARIIG LCDQFIGDTE MWADLLGLPS
     EGLEADWIGL NHATWARRLR LDGRELDVPL LLDGLEVPGG GATPWRDPSR MAELAKALGF
     LPNSYSKYYF FHDEVVGELR AKGRTRAQDV LAMLPGYYEQ VAAESRKADP DPSRERGGGE
     HGEFAVDVIC AMHRDEGRRM IVNTRNGGAV SSLDADAIVE VPSLVGRSGP VPLTMGALPG
     PVRGLTQAIH AYERLASDAA VTGDRRTALQ ALMAHPFVRS KHTAERILAE GLAAHRAHLP
     QFG
//
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