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Database: UniProt/TrEMBL
Entry: E3EA12_PAEPS
LinkDB: E3EA12_PAEPS
Original site: E3EA12_PAEPS 
ID   E3EA12_PAEPS            Unreviewed;       485 AA.
AC   E3EA12;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ADO58145.1};
GN   Name=bglH5 {ECO:0000313|EMBL:ADO58145.1};
GN   ORFNames=PPSC2_19620 {ECO:0000313|EMBL:ADO58145.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO58145.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO58145.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO58145.1,
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; ADO58145.1; -; Genomic_DNA.
DR   RefSeq; WP_013372717.1; NC_014622.2.
DR   AlphaFoldDB; E3EA12; -.
DR   STRING; 1406.LK13_06840; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; ppm:PPSC2_19620; -.
DR   PATRIC; fig|886882.15.peg.4184; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_0_1_9; -.
DR   OMA; ICTINEP; -.
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:SF122; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT   ACT_SITE        384
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   485 AA;  55274 MW;  68E515376757362E CRC64;
     MTKTLKGFPQ NFLWGGATAA NQLEGAFDVD GKGLSSADMI AYVPKAERKN DHAIEISSER
     LEDILAGKVN ARFPKREGVD FYHRYKEDIA LFAEMGFKVF RMSIHWSRIF PNGYDAEPNE
     AGLQFYDNVF DELRKYGIEP LVTLSHYETP LGLTQKYNGW LGREVVDHYV KYAETVFTRY
     KDKVKYWLTF NEINVMTMSP FTGGGVVIDR VENKQQAIYQ ALHHQFVASA LATKRGHEII
     PGAQIGCMLA RIESYPHTCN PEDILKAQHE NQMNLFFTDV HARGEYPNYM NRYFEENNIV
     IQTEPGDAEI LKNNTVDFIS FSYYMTLTVS AGPEGEKAAG NLIGGVKNPY LQSSDWGWQI
     DPIGLRVTLN TFYDRYQKPL FIVENGLGAY DKVEEDGSVH DTYRIDYLRQ HIAQMKEAIA
     DGVDLIGYTS WGPIDLVSMS TSEMSKRYGF IYVDLDDDGN GTLQRSKKDS FNWYKNVIAT
     NGEEL
//
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