ID A0A0R1MT81_9LACO Unreviewed; 455 AA.
AC A0A0R1MT81;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:KRL11084.1};
GN ORFNames=FD09_GL000811 {ECO:0000313|EMBL:KRL11084.1};
OS Schleiferilactobacillus perolens DSM 12744.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Schleiferilactobacillus.
OX NCBI_TaxID=1423792 {ECO:0000313|EMBL:KRL11084.1, ECO:0000313|Proteomes:UP000051330};
RN [1] {ECO:0000313|EMBL:KRL11084.1, ECO:0000313|Proteomes:UP000051330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12744 {ECO:0000313|EMBL:KRL11084.1,
RC ECO:0000313|Proteomes:UP000051330};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRL11084.1}.
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DR EMBL; AZEC01000013; KRL11084.1; -; Genomic_DNA.
DR RefSeq; WP_057821782.1; NZ_AZEC01000013.1.
DR AlphaFoldDB; A0A0R1MT81; -.
DR STRING; 1423792.FD09_GL000811; -.
DR PATRIC; fig|1423792.3.peg.825; -.
DR Proteomes; UP000051330; 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:SF136; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLC; 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 348
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 455 AA; 51201 MW; A07E5B100C96D118 CRC64;
MALADFPKDF LWGASTSAYQ YEGAYNTDGK GLSVQDVATP PAGTADFKIT SDGYHHYPED
ISLYGEMGFK SYRFSIAWTR IYPNGAGEVN QAGLDYYQDV LDQLKAQHIE PVATLFHFDL
PAALQKQGGW ANRATIDAFV QYAKTVLNHF SPQITYYQTI NEQNMLFAGM LAAALKGKMT
LQEVAQANHN MFVAAAKVMI YAHEHHPEIK IGPAPNLVAV YPLTPRPEDA LAANVYDSVR
NLLFGDVTIL GHYNHVAWHL FEQFHATPEI AADDMATIAA AHPDLLYFNY YNTETIRAAE
PGSTLPFKKV INPFLDQTEF GWDLDPAGFR LTLRQLYDRY NLPMIITENG LGAHDTLTAD
GKVHDPYRIK YLNDHIYQMR LAIGEGIPVI GYHVWSAIDL VSTHEGFTKR YGFIYVDRGE
TNDSGTLKRY KKDSFDWYKD VIAHNGDDVT KQVED
//