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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//