ID K6U489_9CLOT Unreviewed; 476 AA.
AC K6U489;
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:EKQ55522.1};
GN ORFNames=A370_02738 {ECO:0000313|EMBL:EKQ55522.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ55522.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ55522.1, 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:EKQ55522.1}.
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DR EMBL; ALXI01000094; EKQ55522.1; -; Genomic_DNA.
DR AlphaFoldDB; K6U489; -.
DR STRING; 1196322.A370_02738; -.
DR PATRIC; fig|1196322.3.peg.2653; -.
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 374
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 476 AA; 54747 MW; A6F3F024B2344DDC CRC64;
MSKGFPEGFL WGGATAANQC EGGYLEGNKG LSTVDVIPAG KDRFPVMLGK MKMFKCDEEH
YYPSHEAIDF YHNYKEDIGL FAEMGFKTFR LSLSWARIFP NGDDEVPNEE GLKFYDNVFD
ECLKYGIEPL VTITHFDVPM HLVETIGSWR SRKMVGYYER LCEVIFKRYK DKVKYWLTFN
EINMLLHLPF IGAGLVFEEG ENEEAIKYQA AHHQLVASAK ATEIAHKINP EFKIGCMLAA
GNTYANTCAP EDVWKAMEKD RENYFFIDVQ SRGEYPNYAK KMFERMNISL EIEDGDEELL
RNNTVDFISF SYYASRLTSA DPEVNAQTEG NVFATLKNPY LKASEWGWQI DPLGLRITLN
SLYDRYQKPL FIVENGLGAV DTPDENGYVE DDYRIEYLRE HIKTMRDAVN IDGVELMGYT
PWGCIDLVSA STGEMKKRYG FIYVDKDNEG NGTLKRSKKK SFEWYNNVIA RNGEIL
//
