ID K6U458_9CLOT Unreviewed; 474 AA.
AC K6U458;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Beta-glucosidase/6-phospho-beta-glucosidase/beta-galactosidase {ECO:0000313|EMBL:EKQ55462.1};
GN ORFNames=A370_02678 {ECO:0000313|EMBL:EKQ55462.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ55462.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ55462.1, 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:EKQ55462.1}.
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DR EMBL; ALXI01000094; EKQ55462.1; -; Genomic_DNA.
DR AlphaFoldDB; K6U458; -.
DR STRING; 1196322.A370_02678; -.
DR PATRIC; fig|1196322.3.peg.2595; -.
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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001325}.
FT ACT_SITE 372
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 474 AA; 54623 MW; 692A3DB2EC955986 CRC64;
MSKYSFPEEF LWGGAIAANQ AEGAYREDGK GLSTVDVIPH GINRMKVKLG LEEDLTLKDN
EFYPSHEAID FYHHYKEDIA LMAEMGFKVF RTSIAWTRIF PNGDDSKPNA AGIKFYKDLF
LECKKYNIEP LVTLCHFDVP MELVNKYGSW KSREMIGFFE KYARCCFEEF DGLVKYWLTF
NEINILIHSP FSGAGIYFKE GENKDQVKYQ AAHHMLVASA LITKIAHEQN PENKVGCMLA
GGDFYPYSCD PKDVWMAHAK DRENLFFIDV QARGKYPSYS KRVFAEKEVS IAMEENDLDI
LKNTVDFISF SYYSSRCASK NMENQTEANV VKSIKNPYLE VSEWGWAIDP LGLRITMNTL
YDRYEKPLFI VENGLGAKDT IEEDGSINDD YRIDYLRQHI IEMKEAMEDG VELLGYTSWG
CIDLVSASTG EMSKRYGFVY VDKQDDGTGT LERKRKKSFY WYKKVIETNG ECLI
//
