ID A0A0L8KT34_9ACTN Unreviewed; 439 AA.
AC A0A0L8KT34;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:KOG29106.1};
GN ORFNames=ADK37_37640 {ECO:0000313|EMBL:KOG29106.1}, AQJ84_37895
GN {ECO:0000313|EMBL:KUN91047.1};
OS Streptomyces resistomycificus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=67356 {ECO:0000313|EMBL:KOG29106.1, ECO:0000313|Proteomes:UP000037251};
RN [1] {ECO:0000313|EMBL:KOG29106.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 2290 {ECO:0000313|EMBL:KOG29106.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000037251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2290 {ECO:0000313|Proteomes:UP000037251};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KUN91047.1, ECO:0000313|Proteomes:UP000052992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40133 {ECO:0000313|EMBL:KUN91047.1,
RC ECO:0000313|Proteomes:UP000052992};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces resistomycificus DSM 40133, type
RT strain for the species Streptomyces resistomycificus.";
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:KOG29106.1}.
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DR EMBL; LGUS01000223; KOG29106.1; -; Genomic_DNA.
DR EMBL; LMWZ01000040; KUN91047.1; -; Genomic_DNA.
DR RefSeq; WP_030043797.1; NZ_LGUS01000223.1.
DR AlphaFoldDB; A0A0L8KT34; -.
DR STRING; 67356.AQJ84_37895; -.
DR PATRIC; fig|67356.5.peg.8054; -.
DR eggNOG; COG1486; Bacteria.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000037251; Unassembled WGS sequence.
DR Proteomes; UP000052992; 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; 2.
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:UP000037251}.
FT DOMAIN 190..314
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT DOMAIN 336..415
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT REGION 311..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 439 AA; 46830 MW; C0D1BFACE36BE00D CRC64;
MKLTVVGGGS TYTPELVDGF ARLRDTLPVE ELVLVDPAAD RLELVGGLAR RIFARHGHDG
RIVTTGDLDA GVEGADAVLL QLRVGGQAAR EQDETWPLEC GCVGQETTGA GGLAKALRTV
PVVLDIAERV RRTNPDAWII DFTNPVGIVT RALLEAGHKA VGLCNVAIGF QRKFARMLGV
APGEIHLDHV GLNHLTWETG VRLGGPEGED VLPGLLSEYG EAIAADLRLP RPLLDRLGVV
PSYYLRYYYA HDEVVRELRS KPSRAAEVAE MERQLLTMYA DPTLDEKPEL LARRGGAYYS
EAAVDLAAGL LGGTGSGPEE PSVDGGGGRR AGGSPYQVVN TRNGGTLPFL PDDAVIEVQA
AVGPKGAAPL AVPAVDPLYA GLMAQVTAYE ELALEAALRG GRDRVFRTLL AHPLVGQYAY
AETLTDQLIA HNREHLAWA
//
