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Database: UniProt
Entry: W9G7R0_9MICO
LinkDB: W9G7R0_9MICO
Original site: W9G7R0_9MICO 
ID   W9G7R0_9MICO            Unreviewed;       458 AA.
AC   W9G7R0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:EWT01317.1};
GN   ORFNames=N865_10915 {ECO:0000313|EMBL:EWT01317.1};
OS   Intrasporangium oryzae NRRL B-24470.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=1386089 {ECO:0000313|EMBL:EWT01317.1, ECO:0000313|Proteomes:UP000019489};
RN   [1] {ECO:0000313|EMBL:EWT01317.1, ECO:0000313|Proteomes:UP000019489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24470 {ECO:0000313|EMBL:EWT01317.1,
RC   ECO:0000313|Proteomes:UP000019489};
RA   Liu H., Wang G.;
RT   "Intrasporangium oryzae NRRL B-24470.";
RL   Submitted (AUG-2013) 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:EWT01317.1}.
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DR   EMBL; AWSA01000024; EWT01317.1; -; Genomic_DNA.
DR   RefSeq; WP_034806233.1; NZ_AWSA01000024.1.
DR   AlphaFoldDB; W9G7R0; -.
DR   STRING; 1386089.N865_10915; -.
DR   PATRIC; fig|1386089.3.peg.2459; -.
DR   eggNOG; COG1486; Bacteria.
DR   OrthoDB; 9767022at2; -.
DR   Proteomes; UP000019489; 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:UP000019489}.
FT   DOMAIN          200..431
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   ACT_SITE        176
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   ACT_SITE        254
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         175
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         205
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            116
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   458 AA;  48961 MW;  2AAB32EB7001F2C8 CRC64;
     MRLAILGGGG FRVPLVHGAL LTDASERRVD EVVLYDTDQG RLAAIARVVA QQAERAEQTG
     TGRARGLPAP RVTTTTDLDV AVEGADFVFS AVRVGGLEGR TADERVALDL GLLGQETTGP
     GGLAYGLRTV PVAVAVAERV RALAPDAWVI NFTNPAGMVT QAMQSVLGER VVGICDSPLG
     LAKRAASALG HSLDEVEIDY AGLNHLGWLQ GLRADGRDLL PELLADPVRL GAIEEGHLFG
     VEWLQTLGAL PNEYLYYFYF TRDAIASITD SRQTRGEFLL GQQTDFYAAV RDSPDRAFDE
     WDRVRRERNA TYMQETREQE GQERDEADVE GGGYEGVALA LMAAIARDEP ARLILNVRNG
     DTVPGLPDDA VVEVPCTVTA AGPRPSAVTR LPGHALGLAQ QVKAVDELVI TAAAERSVQR
     AVEAFALHPL VDSVTVARQL VAGYRAAIPA LDAVFARG
//
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