ID A0A089KMM4_9BACL Unreviewed; 487 AA.
AC A0A089KMM4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:AIQ49070.1};
GN ORFNames=R70723_26570 {ECO:0000313|EMBL:AIQ49070.1};
OS Paenibacillus sp. FSL R7-0273.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536772 {ECO:0000313|EMBL:AIQ49070.1, ECO:0000313|Proteomes:UP000029520};
RN [1] {ECO:0000313|EMBL:AIQ49070.1, ECO:0000313|Proteomes:UP000029520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-0273 {ECO:0000313|EMBL:AIQ49070.1,
RC ECO:0000313|Proteomes:UP000029520};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; CP009283; AIQ49070.1; -; Genomic_DNA.
DR RefSeq; WP_039876656.1; NZ_MRTY01000013.1.
DR AlphaFoldDB; A0A089KMM4; -.
DR STRING; 1536772.R70723_26570; -.
DR KEGG; paea:R70723_26570; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_9; -.
DR OrthoDB; 108629at2; -.
DR Proteomes; UP000029520; 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:SF348; 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}.
FT ACT_SITE 383
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 487 AA; 55433 MW; 5DD401E50F6841F1 CRC64;
MPSPFPKEFL WGGAVAANQV EGAYNEGGKG LSTADVVKYC PPGERKSLEQ LLSMSRAELY
EAIADNGEGN YPKRRGIGFY HRYKEDIALF AEMGFKVFRL SISWPRIFPT GEETEPNEEG
LRFYDEVFDE LRKYNIEPLV TISHYEMPVH LVTKYNGWAS RELVELFLRY ADTLFNRYKD
KVKYWLTFNE INCTLKAPFL GAGIIMDGVE NEKQVAFQAL HHQFVASSLA VKRGREINPG
FSIGCMLARK LLYPYSCRPE DVLQAQAENQ MAQFCSDVQV RGYYPSYIQR HLKKHGVRIE
MLPGDLEILQ ENLVDFLSFS YYMSSAVSTD NSITATTAGN LSTGLANPYL QTSDWGWQID
PVGLRVVLKE MHDRYQLPLF VVENGLGAAD ELAEDGSIRD DYRIDYLAQH IAQMAEAIED
GVELMGYTSW GCIDLISAST SEMRKRYGYI YVDQDDEGNG TLARLRKKSF YWYKQVIASN
GAELHHS
//
