ID A0A0K9GNW8_9BACI Unreviewed; 485 AA.
AC A0A0K9GNW8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:KMY48281.1};
GN ORFNames=AC625_00980 {ECO:0000313|EMBL:KMY48281.1};
OS Peribacillus loiseleuriae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1679170 {ECO:0000313|EMBL:KMY48281.1, ECO:0000313|Proteomes:UP000037146};
RN [1] {ECO:0000313|Proteomes:UP000037146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27997 {ECO:0000313|Proteomes:UP000037146};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMY48281.1}.
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DR EMBL; LFZW01000001; KMY48281.1; -; Genomic_DNA.
DR RefSeq; WP_049679601.1; NZ_LFZW01000001.1.
DR AlphaFoldDB; A0A0K9GNW8; -.
DR STRING; 1679170.AC625_00980; -.
DR PATRIC; fig|1679170.3.peg.179; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000037146; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037146}.
FT ACT_SITE 384
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 485 AA; 55754 MW; 6A3B19E3DD8E2830 CRC64;
MTITNKEFPK GFLWGGATAA NQLEGAFDQD GKGLSSADLV AYIPKDQRKK DNAIEITSDE
IEKILSGEKV ARYPKREGID FYHRYKEDIA LFAEMGFKVF RLSLNWARIF PNGDDQEPNE
AGLKFYDDVF DELHKYGIEP LVTLSHYETP YGLTEKYNGW LGREVIGCFE RYAKTVFTRY
KDKVKYWLTF NEINMITLSP FTGGGIVSDR TEHPLQAQYQ GLHHQFVASA LVTKACHAII
PGAKIGCMLA RMETYPNTPN PLDVRKAQLE NQMNLFFTDV HARGEYPNYM NRFFKENQIS
IKKEDGDDEI LKEYTVDYVS FSYYMSLTAS ASPEGERAQG NLFGGVKNPY LESSDWGWQI
DPIGLRIMLN DMYDRYQKPL FLVENGLGAY DRVEEDGSIH DDYRIDYLRK HIEQMREAIE
DGVDLMGYTS WGPIDLVSMS TSEMTKRYGF IYVDLDDDGN GTLKRSKKDS FDWYKKVIES
NGVEL
//