ID A0A1Z2L711_9ACTN Unreviewed; 427 AA.
AC A0A1Z2L711;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ARZ70075.1};
GN ORFNames=SMD11_4474 {ECO:0000313|EMBL:ARZ70075.1};
OS Streptomyces albireticuli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1940 {ECO:0000313|EMBL:ARZ70075.1, ECO:0000313|Proteomes:UP000195755};
RN [1] {ECO:0000313|EMBL:ARZ70075.1, ECO:0000313|Proteomes:UP000195755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK11 {ECO:0000313|EMBL:ARZ70075.1,
RC ECO:0000313|Proteomes:UP000195755};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Yao L., Wang C.;
RT "Streptomyces albireticuli Genome sequencing and assembly.";
RL Submitted (JUN-2017) 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; CP021744; ARZ70075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z2L711; -.
DR KEGG; salj:SMD11_4474; -.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000195755; Chromosome.
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; 1.
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}.
FT DOMAIN 190..403
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
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 261
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 427 AA; 46148 MW; AF09E507594BA5DD CRC64;
MKLTVVGGGS TYTPELVDGF ARLRGTLPVT ELVLVDPAAD RLELVGGLAR RIFARQGHPG
RITWTADLDA AVDGADAVLL QLRVGGQAAR QQDETWPLTC GCVGQETTGA GGLAKALRTV
PVVLDIAERV RRRNPAAWIV DFTNPVGIVT RALLTAGHRA VGLCNVAIGF QRKFARLLGV
EPEAVALEHV GLNHLTWERA VTVGGRDVLP ELLAEHGAAV AEDLRMPRAL LDRLGVVPSY
YLRYFYQHDE VVRELRTKPS RAAEVAEMER RLLEMYGDPA LDEKPELLGK RGGAFYSEAA
VALTASLLRP EGARGAVPDA RPDVQVVNAF NNGTLPFLPD DAVIEVPAEV DARGARPLPV
RPLEPLFAGL VANVTAYERL ALEAALLGGR ERVFAALLAH PLIGQTERAD RLTDELLAHN
REHLAWA
//
