ID G7M4V8_9CLOT Unreviewed; 471 AA.
AC G7M4V8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:EHI99178.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:EHI99178.1};
GN ORFNames=CDLVIII_2563 {ECO:0000313|EMBL:EHI99178.1};
OS Clostridium sp. DL-VIII.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI99178.1, ECO:0000313|Proteomes:UP000005106};
RN [1] {ECO:0000313|EMBL:EHI99178.1, ECO:0000313|Proteomes:UP000005106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHI99178.1,
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; EHI99178.1; -; Genomic_DNA.
DR RefSeq; WP_009169850.1; NZ_CM001240.1.
DR AlphaFoldDB; G7M4V8; -.
DR STRING; 641107.CDLVIII_2563; -.
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: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, ECO:0000313|EMBL:EHI99178.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005106}.
FT ACT_SITE 368
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 471 AA; 54393 MW; F4FE658041ED2F8C CRC64;
MKNNIFKKDF LWGGAISANQ SEGAYDANGK GLSILDVMEV GSKLTPRRRT ETIEAGVRYP
SHDGIDFYHN YKDDIKLFKE LGIKCFRTSI NWTRIYPNGI EKEPSEEGLK FYDDLFDELL
TNGITPLVTI QHSDTPLHLA LEYGGWKNRV LVDMFEKYAE TVFKRYKDKI KYWITINEIN
AINFVSWFGA ASEDLSDKEK EQAAYHLLLA SAKAVEIGKK INPDFMIGGM VTDCYSYPYT
CNPKDVMLSF EDKRYNIYFA DVMCRGYYPR YKLKELERKN IMLDTREEDI ETLKNGKIDF
LSFSYYASHV SSIVKNEILQ GNLLQNIIGK TNPYLKSSDW GWQIDPLGLR ISLNEFYDRY
QIPLFIVENG LGAHDDTSDN ENIQDDYRID YLKKHIEAIR DAVNIDGIEL LGYLVWGFID
IVSGTTGEMG KRYGLIYVDK DNQGIGSGKR CKKKSFYWYK KVIETNGENL D
//
