ID A0A0X3UM34_9ACTN Unreviewed; 446 AA.
AC A0A0X3UM34;
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:KUL33605.1};
GN ORFNames=ADL22_32800 {ECO:0000313|EMBL:KUL33605.1};
OS Streptomyces sp. NRRL F-4489.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL33605.1, ECO:0000313|Proteomes:UP000053256};
RN [1] {ECO:0000313|EMBL:KUL33605.1, ECO:0000313|Proteomes:UP000053256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL33605.1,
RC ECO:0000313|Proteomes:UP000053256};
RA Gilbert D.G.;
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:KUL33605.1}.
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DR EMBL; LLZI01000292; KUL33605.1; -; Genomic_DNA.
DR RefSeq; WP_066988166.1; NZ_LLZI01000292.1.
DR AlphaFoldDB; A0A0X3UM34; -.
DR STRING; 1609095.ADL22_32800; -.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000053256; 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:UP000053256}.
FT DOMAIN 195..429
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 165
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 143
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 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 105
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 446 AA; 47882 MW; FDF92D9FC5968CAD CRC64;
MRLTILGGGG FRVPLVYRAL LDDPARSVSE LTLYDTDPAR VAVISGVLAR LAQGRPSPVP
VRVAESLDAA LTGADFVFSA IRVGGTEGRI RDERIPLAEG VLGQETVGAG GILYGLRTIP
VALHIAERVA ALAPGAWVIN FTNPAGMVTE AMAQVLGDRV IGICDSPVGL VRRAARAAGA
DPAALKDPAR SGYDYVGLNH LGWLRSLTVD GTDVLPALLA DESALGSFEE GRLFGAEWLR
VLGALPNEYL HYYYFRRETL HSIQDTAQTR GEFLDHQQGG FFERAAAAGS PDAVYELWER
TRLEREETYM AHSREATGGW QRDSHDLEGG GYDRVALALM HAIAGNSGRR LILNVRNGTT
VPQLAPDAIV ETVCEVTSQG ARPLPCTPLR EDQLGLMLQI KSVERATIDA ALYKDRDAAL
RALALHPLVD SATVASHILE RAAEGA
//
