ID E3EET0_PAEPS Unreviewed; 469 AA.
AC E3EET0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ADO55767.1};
GN Name=bglH1 {ECO:0000313|EMBL:ADO55767.1};
GN ORFNames=PPSC2_08490 {ECO:0000313|EMBL:ADO55767.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO55767.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO55767.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO55767.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(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; CP002213; ADO55767.1; -; Genomic_DNA.
DR RefSeq; WP_013370386.1; NC_014622.2.
DR AlphaFoldDB; E3EET0; -.
DR STRING; 1406.LK13_21095; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; ppm:PPSC2_08490; -.
DR PATRIC; fig|886882.15.peg.1784; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_1_9; -.
DR OrthoDB; 108629at2; -.
DR Proteomes; UP000006868; 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:SF136; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLC; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT ACT_SITE 369
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 469 AA; 53586 MW; 84B0B9E17379FF25 CRC64;
MKHNQLKAFP ENFFWGGSTS AYQVEGAWDE DGKGPSVIDM ANHVEGVTDF KVTSDHYHMF
KEDVALMAEM GFKAYRFSIA WTRIYPQGAG EVNPKGIAFY SSLIDELIKY GIEPIVTMYH
FDLPYALEQQ GGWSKRETID AFEQYAKTLF ENFGDRVKYW LTINEQNMLI LHPGSIGTLD
TSLENPQKVL YQQNHHMLVA QAKAMVLCHE MLPDAKIGPA PNIGVIYPAS SKPEDTLAAD
NYAAIRNWLY LDMAVFGRYN HIAWSYLVEK GYEPVIEEGD MDILAKGNPD FIAFNYYTSQ
TVGESLDDGN DFSHTGDQHE IVGEPGAYRG SVNPNLQTTE FGWEIDPVGF RTTLRQIYSR
YRLPLIVTEN GLGAFDKLEE GDVVNDPYRI DFFKKHIEQI QLAITDGVEV FGFCPWSAID
LVSTHQGSSK RYGFIYVDRE EFDLKDLRRI RKQSFYWYQK LIATNGEIR
//
