ID G7LXX2_9CLOT Unreviewed; 473 AA.
AC G7LXX2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:EHI97639.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:EHI97639.1};
GN ORFNames=CDLVIII_0931 {ECO:0000313|EMBL:EHI97639.1};
OS Clostridium sp. DL-VIII.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI97639.1, ECO:0000313|Proteomes:UP000005106};
RN [1] {ECO:0000313|EMBL:EHI97639.1, ECO:0000313|Proteomes:UP000005106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHI97639.1,
RC ECO:0000313|Proteomes:UP000005106};
RX PubMed=23929491;
RA Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL Genome Announc. 1:e00605-e00613(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; CM001240; EHI97639.1; -; Genomic_DNA.
DR RefSeq; WP_009168321.1; NZ_CM001240.1.
DR AlphaFoldDB; G7LXX2; -.
DR STRING; 641107.CDLVIII_0931; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_9; -.
DR Proteomes; UP000005106; Chromosome.
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: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, ECO:0000313|EMBL:EHI97639.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005106}.
FT ACT_SITE 366
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 473 AA; 54389 MW; B69AAB818181333D CRC64;
MSIKFPEGFL WGGATAANQF EGAYNEDGKG LSIQDILILP KGLRGTKTSE PTEDNMKLIG
IDFYHRYKED IKLFAEMGFK VFRLSIAWSR IFPNGDDKEP NEKGLQFYDN VFDELAKYGI
EPLITISHYE TPLALAKNYD GWVNRKLIGF FENYVRTIFT RYKDKVKYWI TFNEINSALH
SPYMSAGVWT PKEQLSKQDL YQAMHHELVA SALAVKIGHE INPEFKIGCM ILGVPNYPLT
PIPSDVLKTM EQDRQNLFFA DIHARGEYPK YMNRFFKENN IEIRIEQGDE EILKNTVDFI
SFSYYMSSCA TSDPERNKKG EGNIISGVPN PYLKASEWGW QIDPEGLRYI LNQLYDRYQK
PLFIVENGLG AVDELITDEN GNKSVNDYYR INYLNDHLVQ VAEAVEDGVE LMGYTTWGCI
DLVSASTAEL KKRYGFIYVD RNDDGSGTLE RYKKKSFNWY KEVIATNGAS LKK
//
