ID A0A089I614_9BACL Unreviewed; 478 AA.
AC A0A089I614;
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:AIQ18510.1};
GN ORFNames=H70357_18745 {ECO:0000313|EMBL:AIQ18510.1};
OS Paenibacillus sp. FSL H7-0357.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536774 {ECO:0000313|EMBL:AIQ18510.1, ECO:0000313|Proteomes:UP000029508};
RN [1] {ECO:0000313|EMBL:AIQ18510.1, ECO:0000313|Proteomes:UP000029508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0357 {ECO:0000313|EMBL:AIQ18510.1,
RC ECO:0000313|Proteomes:UP000029508};
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; CP009241; AIQ18510.1; -; Genomic_DNA.
DR RefSeq; WP_038592332.1; NZ_CP009241.1.
DR AlphaFoldDB; A0A089I614; -.
DR STRING; 1536774.H70357_18745; -.
DR KEGG; paeh:H70357_18745; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_9; -.
DR Proteomes; UP000029508; 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; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLH; 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 370
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 478 AA; 54488 MW; 3E98C8D9F21080CB CRC64;
MKNLSQTGLS FPEGFLWGGA VAANQLEGAY NEGGKGLSTQ DVSPQGAMGA ITEEPTEDNM
KLIGIDFYHR YKEDIKLFAE MGFKVFRTSI AWSRIFPYGD ETEPNEEGLR FYDSLFDECL
KYGIEPLVTL SHYETPLHLS KQYDGWVNRK LVDFYAQYAS TVFKRYKGKV KYWLTFNEIN
SILEVPFMSG GIYTPKEKLS KQDLYQAIHH ELVASATAVK LCHEIDPKAQ IGCMVLSVPT
YPLTPHPDDI IAVMKYNHSN YFFGDVHVRG RYPGYMKRYF REQGINIHME PGDEEQLLHT
VDFVSFSYYM SVCQTADPEK NIHGEGNIMG GVANPYLPAS EWGWQIDPQG LRFTLNTFYE
RYQKPLFIVE NGLGAADELI VNEAGEKTVE DDYRIQYLND HLFQVAEAVA DGVEVMGYTS
WGCIDLVSAS SAQLKKRYGY IYVDRHDDGS GTLERYRKKS FHWYKDIIAS NGAKLSVK
//
