ID I1ZNU7_STRPA Unreviewed; 479 AA.
AC I1ZNU7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:AFJ26721.1};
GN Name=bglA {ECO:0000313|EMBL:AFJ26721.1};
GN ORFNames=Spaf_1772 {ECO:0000313|EMBL:AFJ26721.1};
OS Streptococcus parasanguinis FW213.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1114965 {ECO:0000313|EMBL:AFJ26721.1, ECO:0000313|Proteomes:UP000002865};
RN [1] {ECO:0000313|EMBL:AFJ26721.1, ECO:0000313|Proteomes:UP000002865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW213 {ECO:0000313|EMBL:AFJ26721.1,
RC ECO:0000313|Proteomes:UP000002865};
RX PubMed=22529932; DOI=10.1371/journal.pone.0034769;
RA Geng J., Chiu C.H., Tang P., Chen Y., Shieh H.R., Hu S., Chen Y.Y.;
RT "Complete Genome and Transcriptomes of Streptococcus parasanguinis FW213:
RT Phylogenic Relations and Potential Virulence Mechanisms.";
RL PLoS ONE 7:E34769-E34769(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; CP003122; AFJ26721.1; -; Genomic_DNA.
DR RefSeq; WP_014713868.1; NC_017905.1.
DR AlphaFoldDB; I1ZNU7; -.
DR STRING; 1114965.Spaf_1772; -.
DR PaxDb; 1114965-Spaf_1772; -.
DR KEGG; scf:Spaf_1772; -.
DR PATRIC; fig|1114965.3.peg.1691; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_9; -.
DR Proteomes; UP000002865; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353:SF348; 6-PHOSPHO-BETA-GLUCOSIDASE ASCB-RELATED; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004468};
KW Hydrolase {ECO:0000256|RuleBase:RU004468}.
FT ACT_SITE 376
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 479 AA; 54864 MW; D1D34594E8B66DF5 CRC64;
MTDKLQFPDG FLWGGATAAN QCEGAYNEDG RGLANVDVVP IGPDRHAIIT GKRKMFDFEE
GYFYPAKDGI DMYHRYKEDI ALFGEMGFKT YRLSIAWSRI FPKGDELEPN EAGLQFYEDL
FKECHKYGIE PLVTITHFDC PMHLITEYGG WRSRKMLECY ERLCRTLFTR YKGLVNYWLT
FNEINMILHA PFMGAGLCFE EGENEEQVKY QAAHHELVAS AIATKLAHEI DPNNKVGCML
AAGQNYPHTC APRDVWAGLE EDRKNYFFID VQARGEYPNY AKKEWERQGI TVEMTEQDLQ
LLKDHTVDFI SFSYYASRVA SGDPAEREKT AGNIFASLKN PYLESSEWGW QIDPLGLRIT
LNTIWDRYQK PMFIVENGLG AVDTPNEAGE IEDDYRIDYL AAHVKAMREA INEDGVVLWG
YTTWGCIDLV SAGTGEMKKR YGFIYVDRDN EGKGSLARSR KKSFYWYKEV IATNGASVN
//
