ID Q97L23_CLOAB Unreviewed; 471 AA.
AC Q97L23;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:AAK78719.1};
GN OrderedLocusNames=CA_C0743 {ECO:0000313|EMBL:AAK78719.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK78719.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK78719.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; AE001437; AAK78719.1; -; Genomic_DNA.
DR PIR; D96991; D96991.
DR RefSeq; NP_347379.1; NC_003030.1.
DR RefSeq; WP_010964061.1; NC_003030.1.
DR AlphaFoldDB; Q97L23; -.
DR STRING; 272562.CA_C0743; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR GeneID; 44997254; -.
DR KEGG; cac:CA_C0743; -.
DR PATRIC; fig|272562.8.peg.949; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_9; -.
DR OrthoDB; 2339329at2; -.
DR Proteomes; UP000000814; 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: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:UP000000814}.
FT ACT_SITE 364
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 471 AA; 53967 MW; 6C7E16B3324AA5A9 CRC64;
MGVKFPEGFL WGGATAANQF EGAYNQDGKG LSIQDIMPKG IRGPITDKPT EDNMKLIGID
FYNRYKEDIK LFAEMGFKTF RLSIAWSRIF PNGDDKQPNE KGLQFYDNVF DELAKYNIEP
LVTISHYETP LALAKNYDGW TNRKLIGFFE NYVRTIFNRY KNKVKYWLTF NEINSALHAP
YMSAGIWTPK EKLSKQDLYQ AMHHELLASA LAVKIGHEIN PEFKIGCMIL GVPNYPLTSK
PSDVLKAMNQ DRENLFFADV HARGRYPKYM NRLFKENNVH IKMEPGDEEI LKNTVDFISF
SYYMSSCATS DTKKSKGGAG NIISGVPNPY LKASEWGWQI DPEGLRYILN LLYDRYQKPL
FIVENGLGAV DELITDERGN KTVNDDYRIN YLNDHLVQVG EAIEDGVELM GYTTWGCIDL
VSASTAELKK RYGFIYVDRH DDGSGTLERY KKKSFYWYKE VIATNGASLK K
//
