ID G5KFQ9_9STRE Unreviewed; 479 AA.
AC G5KFQ9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:EHJ56792.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:EHJ56792.1};
GN ORFNames=STRUR_1067 {ECO:0000313|EMBL:EHJ56792.1};
OS Streptococcus urinalis 2285-97.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=764291 {ECO:0000313|EMBL:EHJ56792.1, ECO:0000313|Proteomes:UP000005388};
RN [1] {ECO:0000313|EMBL:EHJ56792.1, ECO:0000313|Proteomes:UP000005388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2285-97 {ECO:0000313|EMBL:EHJ56792.1};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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:EHJ56792.1}.
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DR EMBL; AEUZ02000001; EHJ56792.1; -; Genomic_DNA.
DR RefSeq; WP_006739535.1; NZ_AEUZ02000001.1.
DR AlphaFoldDB; G5KFQ9; -.
DR STRING; 764291.STRUR_1067; -.
DR eggNOG; COG2723; Bacteria.
DR Proteomes; UP000005388; Unassembled WGS sequence.
DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:EHJ56792.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005388}.
FT ACT_SITE 376
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 479 AA; 55318 MW; 86C379E8A5E561D0 CRC64;
MSENKAFPKG FLWGGATAAN QVEGAYDADG RGLANVDVVP IGKDRFPIIS GQKKMFDFEE
GYFYPAKESI DFYHHYKEDI ALFAEMGFKT YRMSIGWTRI FPKGDELEPN EAGLQFYENV
FKECRKYGIE PLVTITHFDF PMHLIEEYGG WRNRKVIKFY ERLCQVIFNR YKGLVKYWLT
FNEINMILHA PFMGAGLYFE EGENQEEVKY QAAHHELVAS AIATKIAHEV DPENKVGCML
AAGQYYPNTC HPDDYWAAMK EDRENYFFID VQARGQYPNY AKKKFEREHL NIKMTEEDLT
LLKENTVDFI SFSYYSSRVA SGDPKVNEQT EGNIFASIKN PYLPASEWGW QIDPLGLRIT
LNTIWDRYQK PMFIVENGLG AVDTPDENSY VEDDYRIDYL RAHVKAMNEA INEDGVELLG
YTTWGPIDLV SAGTGEMKKR YGFIYVDRDN DGNGSLKRSK KKSFDWYKKV IASNGTDID
//
