ID K6TH15_9CLOT Unreviewed; 480 AA.
AC K6TH15;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Beta-glucosidase/6-phospho-beta-glucosidase/beta-galactosidase {ECO:0000313|EMBL:EKQ50385.1};
GN ORFNames=A370_05636 {ECO:0000313|EMBL:EKQ50385.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ50385.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ50385.1, ECO:0000313|Proteomes:UP000001325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX PubMed=23405323;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA Midgley D.J., Hendry P.;
RT "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT Seam Gas Formation Water.";
RL Genome Announc. 1:E00081-12(2013).
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:EKQ50385.1}.
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DR EMBL; ALXI01000175; EKQ50385.1; -; Genomic_DNA.
DR AlphaFoldDB; K6TH15; -.
DR STRING; 1196322.A370_05636; -.
DR PATRIC; fig|1196322.3.peg.5507; -.
DR eggNOG; COG2723; Bacteria.
DR Proteomes; UP000001325; Unassembled WGS sequence.
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:SF136; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLC; 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:UP000001325}.
FT ACT_SITE 380
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 480 AA; 55311 MW; 0E75DBDDAD1FF157 CRC64;
MYFKEKHGFP DNFLWGSASA AYQVEGAAEE DGKGRSNWDE FVRIPGKTFK GTNGDVAVDH
YHRYKEDIAL MAEMGLKTYR FSISWPRIYP KGKGEINEKG LQFYDNVIDE CLKYGIEPMV
TIYHWDLPLA LQEEYNGWES RKIIDDFENY AVTLFKRYKD KVKYWITLNE QNIFTSMGWI
LATHPPGKKN DSKTFYQVNH HANLAHAKAI LAFREIVPNG KIGASFAFGP SYAIDCNPIN
NIAKADYDDL QTFWWMDVYA FGRYPKPALK YLQSQGVAPT FEEGDEELMK AAAQVDFMGV
NYYQTAVVEY NPIDGVGMAE MNTTGKKGTS QVSGTPGLYK NPLNPFLKTT DWDWTIDPMG
IRMCCRIISS RYDLPIVISE NGLGAFDKKT EDNKIHDDYR IAYLKAHVEE LKEAINEGCE
VLAYCTWSIT DLLSWLNGYQ KRYGFIYVDR EEEEGASMNR YKKDSYYWYQ NVIKTNGEEL
//
