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Database: UniProt
Entry: C4ILM9_CLOBU
LinkDB: C4ILM9_CLOBU
Original site: C4ILM9_CLOBU 
ID   C4ILM9_CLOBU            Unreviewed;       476 AA.
AC   C4ILM9;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=6-phospho-beta-glucosidase BglA {ECO:0000313|EMBL:EEP52733.1};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:EEP52733.1};
GN   ORFNames=CLP_0057 {ECO:0000313|EMBL:EEP52733.1};
OS   Clostridium butyricum E4 str. BoNT E BL5262.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP52733.1, ECO:0000313|Proteomes:UP000003081};
RN   [1] {ECO:0000313|EMBL:EEP52733.1, ECO:0000313|Proteomes:UP000003081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081};
RA   Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C.,
RA   Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.;
RL   Submitted (AUG-2009) 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:EEP52733.1}.
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DR   EMBL; ACOM01000007; EEP52733.1; -; Genomic_DNA.
DR   RefSeq; WP_003408091.1; NZ_ACOM01000007.1.
DR   AlphaFoldDB; C4ILM9; -.
DR   STRING; 1492.ATN24_15905; -.
DR   GeneID; 66380429; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_0_2_9; -.
DR   Proteomes; UP000003081; 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:SF85; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLA; 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:EEP52733.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003081}.
FT   ACT_SITE        374
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   476 AA;  54559 MW;  2A8FB31A08CC9FDD CRC64;
     MAFNEKFLWG GAVAAHQLEG GWNEGGKGPS TADVMTAGAH GVPREITDGV IEGLNYPNHE
     AIDFYHRYKE DIALFAEMGF KCFRTSIAWS RIFPNGDELE PNEEGLKFYD DMFDELLKYN
     IEPVITLSHF EIPYGICKKY GGWRNRKVID MFVRFATTVM ERYKDKVKYW MTFNEINNQA
     ETEYDLFAWT CSGVRFEDGE NRVEVTYQAV HHELVASALV VKKGHEINPH FKIGCMLAYV
     PVYPYSCNPE DMMLSVEAMH ERYLYGDVHC RGYYPSYALN KWKRDGINIK MEDGDAEILK
     EGCVDYIGFS YYMSASVKSD IGTDEGDGMS GYSRAVKNPY VEASDWGWQI DPVGLRYALN
     SLYERYQKPL FIVENGFGAV DVKEEDGTCN DDYRIDYLAK HIVQMKKAVE LDGVDLMGYT
     PWGCIDLVSF GTGEMKKRYG FIYVDKDNDG NGTLNRSKKK SFDWYKNVID TNGEEL
//
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