ID F5X6T3_STRPX Unreviewed; 477 AA.
AC F5X6T3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:BAK30123.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:BAK30123.1};
GN Name=bglA.3 {ECO:0000313|EMBL:BAK30123.1};
GN OrderedLocusNames=SGPB_1058 {ECO:0000313|EMBL:BAK30123.1};
OS Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC 1723-81).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=981540 {ECO:0000313|EMBL:BAK30123.1, ECO:0000313|Proteomes:UP000007946};
RN [1] {ECO:0000313|EMBL:BAK30123.1, ECO:0000313|Proteomes:UP000007946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81
RC {ECO:0000313|Proteomes:UP000007946};
RX PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA Chang C.-H., Hsu M.-T.;
RT "Sequencing and comparative genome analysis of two pathogenic Streptococcus
RT gallolyticus subspecies: genome plasticity, adaptation and virulence.";
RL PLoS ONE 6:E20519-E20519(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; AP012054; BAK30123.1; -; Genomic_DNA.
DR RefSeq; WP_013851888.1; NC_015600.1.
DR AlphaFoldDB; F5X6T3; -.
DR STRING; 981540.SGPB_1058; -.
DR GeneID; 76468025; -.
DR KEGG; stb:SGPB_1058; -.
DR HOGENOM; CLU_001859_0_2_9; -.
DR Proteomes; UP000007946; Chromosome.
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:SF85; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLA; 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:BAK30123.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007946}.
FT ACT_SITE 375
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 477 AA; 54559 MW; 3D116234F3169AE2 CRC64;
MTFPKNFLWG GALAAHQFEG GVLETSKGLS VADVMTAGAH GIPRVITNGV IEGNYYPNHI
GIDFYHCYKE DIALFAAMGF KCFRTSIAWS RIFPTGFETE PEEEGLQFYD EVFDELLKYG
IEPVITLSHF EMPYELAKTN GGFMNRETVN HFVKFAEVCF KRYKSKVKYW MTFNEINNQM
NYANDIFGWT NSGVHFGDYK NPEEAMYICA HHTLVASALA VKIGKEINPD FQIGNMIAMV
PTYPYSSRPE DVLLAHQAMH DKWFFCDVQV RGHYPAYVLK MFERKGFNIP ITEEDKRILA
EGTVNYIGFS YYMTNTVDST ANRDISNAVE ASNSHTVTNP YIKESDWGWA IDPVGLRYAL
NIFYERYEKP LFIVENGFGA IDVKEKDGSV HDQYRIDYLS SHIKEMEKAI DEDGVELIGY
TPWGCIDCVS FTTGEMKKRY GFIYVDRNND GSGTLKRSKK DSFDWYKKVI SSNGKVL
//
