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Database: UniProt
Entry: A0A140DX84_9FIRM
LinkDB: A0A140DX84_9FIRM
Original site: A0A140DX84_9FIRM 
ID   A0A140DX84_9FIRM        Unreviewed;       494 AA.
AC   A0A140DX84;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=6-phospho-beta-glucosidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AALO17_21270 {ECO:0000313|EMBL:AMK55261.1};
OS   Faecalibaculum rodentium.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Faecalibaculum.
OX   NCBI_TaxID=1702221 {ECO:0000313|EMBL:AMK55261.1, ECO:0000313|Proteomes:UP000069771};
RN   [1] {ECO:0000313|EMBL:AMK55261.1, ECO:0000313|Proteomes:UP000069771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alo17 {ECO:0000313|EMBL:AMK55261.1,
RC   ECO:0000313|Proteomes:UP000069771};
RX   PubMed=26877770; DOI=10.1186/s13099-016-0087-3;
RA   Lim S., Chang D.H., Ahn S., Kim B.C.;
RT   "Whole genome sequencing of "Faecalibaculum rodentium" ALO17, isolated from
RT   C57BL/6J laboratory mouse feces.";
RL   Gut Pathog. 8:3-3(2016).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CP011391; AMK55261.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A140DX84; -.
DR   STRING; 1702221.AALO17_21270; -.
DR   KEGG; fro:AALO17_21270; -.
DR   PATRIC; fig|1702221.3.peg.2066; -.
DR   Proteomes; UP000069771; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000069771}.
FT   ACT_SITE        389
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   494 AA;  56747 MW;  9A97AA85A68EC528 CRC64;
     MTGLRMQKRV ADKESEETMS LPKDFLWGGA TAANQYEGGW NECGRGLANV DVTPWGPDRR
     KVMSGTAGVH SLDDSHFYPG LEAVDFYHHY KEDIALFAEM GFKVFRMSIA WSRIFPKGDE
     EEPNEEGLRF YEDVFRELKK HNIEPLVTIT HFDCPMYLIT EYGGWKNPKL IEFYKRLCQV
     LFTRFRPYVK WWLTFNEINM ILHLPFMGAG LEFEEGEDRE KAKYLAAHNE LLASAWAVKI
     GHEVNPENMI GCMVAAGEFY PYSPMPEDVF LAQQKERENL MFIDVQARGE YPAYAKKLFE
     RMGLDLGMTP EQEALLKDNP VDFISFSYYT SRCVSTRPDA GEQVGNAFKG VKNPYLKASD
     WGWAIDPLGL RTTMNSLYDR YQKPLFIVEN GLGAKDVPDA DGRVQDDYRI EYLQRHLQAM
     KDAVELDGIP LLGYTAWGCI DLVSASTGEM SKRYGFIYVD RDDQGHGTLK RLKKKSFDWY
     KKVIATNGED LTNE
//
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