ID J2JX73_9ACTN Unreviewed; 446 AA.
AC J2JX73;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:QTZ91873.1};
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:EJJ05008.1};
GN ORFNames=SU9_010595 {ECO:0000313|EMBL:QTZ91873.1}, SU9_20873
GN {ECO:0000313|EMBL:EJJ05008.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ05008.1};
RN [1] {ECO:0000313|EMBL:EJJ05008.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ05008.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ91873.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ91873.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) 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; AJGV01000127; EJJ05008.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ91873.1; -; Genomic_DNA.
DR RefSeq; WP_006605695.1; NZ_CP072931.1.
DR AlphaFoldDB; J2JX73; -.
DR STRING; 1160718.SU9_20873; -.
DR KEGG; sauh:SU9_010595; -.
DR PATRIC; fig|1160718.3.peg.4227; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_0_1_11; -.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000009036; 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 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:UP000009036}.
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; 47508 MW; 5A353602F398F867 CRC64;
MRLTILGGGG FRVPLVYRAL LDDPAPAVSE VVLHDTDPQR VAVIAEVLAR LAQGHPAPVP
VRVAKGLDEA LAGAGFVFSA IRVGGTAGRI RDERIPLSEG VLGQETVGAG GVLYGLRTVP
VALHIAERVA ALAPGAWVIN FTNPAGTVTE AMSQVLGDRV IGICDSPVGL VRRAARAAGA
DPAALADPAR AGYDYVGLNH LGWLRSLTVD GTELLPGLLA DDAALESFEE GRLFGGDWLR
ALGALPNEYL HYYYFRRETL DSVRHTRETR GEFLDQQQGG FFARAAAAGG PDEAYRLWER
TRLEREETYM AHSREATGGW QRDSHDLEGG GYDRVALALM HAIIGDSGTR LILNVRNGTT
VPQLPPDAIV ETVCEVTAKG ARPLPTAPLR ADQLGLMLQL KAVERATVEA ATFKDRGAAL
RALALHPLVD SAAVAARILE RAATEA
//
