ID A0A3P1VU83_9FUSO Unreviewed; 476 AA.
AC A0A3P1VU83;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:RRD37824.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:RRD37824.1};
GN ORFNames=EII29_10970 {ECO:0000313|EMBL:RRD37824.1};
OS Leptotrichia sp. OH3620_COT-345.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=2491048 {ECO:0000313|EMBL:RRD37824.1, ECO:0000313|Proteomes:UP000280115};
RN [1] {ECO:0000313|EMBL:RRD37824.1, ECO:0000313|Proteomes:UP000280115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH3620_COT-345 {ECO:0000313|EMBL:RRD37824.1,
RC ECO:0000313|Proteomes:UP000280115};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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:RRD37824.1}.
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DR EMBL; RQYW01000031; RRD37824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1VU83; -.
DR OrthoDB; 108629at2; -.
DR Proteomes; UP000280115; Unassembled WGS sequence.
DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
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|RuleBase:RU004468, ECO:0000313|EMBL:RRD37824.1};
KW Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:RRD37824.1}.
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 476 AA; 54737 MW; E3BD5774FC862B8F CRC64;
MSEKGFKKDF LWGGATAANQ YEGGYNEGGR GAANVDLIPL GKDRGDIIKG KKEMLDFEEG
YYYPAKEGVD FYHRYKEDIA LLGEMGFKVF RLSIGWSRIF PKGDEESPNE AGLAFYENVF
RECRKYGIEP LITITHFDCP IHLIKEYGGW RNRKLIKFYK KLCETIFTRY KGLVKYWITF
NEINMILHAP FMGAGIVFKE GENEEQVKYE AAHNELVASA WATKIAHEID PENKVGCMLA
AGEYYPLTAK PEDVFKSMKQ NRENYCFIDV QARGYYPSYL LKEFKQKGIE INITEEDKKI
LKDNTVDFIS FSYYSSRCSS ADPKEKTEGN IFTTVKNPYL KVSEWGWQID PLGFRITMNN
LYDRYQKPLF VVENGLGAID VPDENGYVQD DYRIDYLRAH IKAMKDAVIL DGVELLGYTT
WGCIDLVSAG TGEMKKRYGF VHVDKDNDGN GTLKRNKKKS FNWYKKVIAS NGENLD
//
