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Database: UniProt
Entry: E3FSZ5_STIAD
LinkDB: E3FSZ5_STIAD
Original site: E3FSZ5_STIAD 
ID   E3FSZ5_STIAD            Unreviewed;       438 AA.
AC   E3FSZ5;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Beta-glucosidase A {ECO:0000313|EMBL:ADO74619.1};
DE            EC=3.2.1.21 {ECO:0000313|EMBL:ADO74619.1};
GN   Name=bglA {ECO:0000313|EMBL:ADO74619.1};
GN   OrderedLocusNames=STAUR_6863 {ECO:0000313|EMBL:ADO74619.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO74619.1, ECO:0000313|Proteomes:UP000001351};
RN   [1] {ECO:0000313|EMBL:ADO74619.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO74619.1,
RC   ECO:0000313|Proteomes:UP000001351};
RX   PubMed=21037205; DOI=10.1093/molbev/msq292;
RA   Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA   Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA   Sogaard-Andersen L.;
RT   "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL   Mol. Biol. Evol. 28:1083-1097(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CP002271; ADO74619.1; -; Genomic_DNA.
DR   RefSeq; WP_013377523.1; NZ_AAMD01000061.1.
DR   AlphaFoldDB; E3FSZ5; -.
DR   STRING; 378806.STAUR_6863; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; sur:STAUR_6863; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_1_3_7; -.
DR   OrthoDB; 9765195at2; -.
DR   Proteomes; UP000001351; Chromosome.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase 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; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:ADO74619.1};
KW   Hydrolase {ECO:0000313|EMBL:ADO74619.1}.
SQ   SEQUENCE   438 AA;  49896 MW;  5023B91F6E3F3918 CRC64;
     MSADEKTFPR DFTFGVATSA YQVEGGIEND WAEWERAGRL KEPHTRCGRA VDHWNRYEED
     YGLAVDVGAS AFRVSLEWAR IEPERGRFDG AALEAYRERL LRMKARGLRP VVTLHHFTHP
     TWFHRETPWH TPASVDAFRA YVRACAPLLK GLEALLISLN EPMVVLLGGY LQGLLPPGFA
     DGPKTMAALE NMVRAHVAAR EELQAVLGRV ELGISQNMLC FTPDRWWHPL DHAAVRLGAH
     AYNHAFHEAL VTGKLRVTMP GLASTRAEIP QARGSCEFIG VNYYSRAHLR FLPRYPFLAF
     QFRDRLGRGL TDIGWEDYPE GFGEILRETK RYGLPVWVTE NGIDDRGGQR RPHFLHRHLE
     QVLAARAQGV DVRGYLYWSL LDNFEWLEGW GPRFGLYHVD FDTLERRPTP ACAYFRAVAQ
     GRRLIAPEAL EAQPSAAR
//
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