ID A0A1X2I6U9_9FUNG Unreviewed; 729 AA.
AC A0A1X2I6U9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=BCR42DRAFT_395791 {ECO:0000313|EMBL:ORZ10559.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ10559.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ10559.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ10559.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:ORZ10559.1}.
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DR EMBL; MCGE01000024; ORZ10559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2I6U9; -.
DR STRING; 90262.A0A1X2I6U9; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000193560; 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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ORZ10559.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000193560};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..729
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013027355"
FT DOMAIN 647..718
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 729 AA; 79355 MW; EE24841054D4505A CRC64;
MLVSSISKAS SLLLLALLGA SSVTTNADVK LRSWDEAQDL AKELVGQMSL EQKVNITTGM
GFNITPCVGN TYAITNPDFP SLCLQDGPLG VRSSYNVSAG VAGINAAASF DRKAILQRGE
MMGQEFRGKG AHIQLGPAMN FMRTAESGRG WESFGEDPFL QGVAAAETIT GVQSQGVIST
AKHFINNEQE TNRHEESSNV DDRTLHEIYL WPFARSVEAG VGSVMCSYNK VNGTSACEND
MMNRILKDEL DFKGFIQTDW WAAMSTVQSA VNGLDMVMPG NMNTTDDHSP SYYGANLVNA
VKNGKVDESR VNDMALRIVA AYYKMGQDND FPKTTIDSFH VDPKGSVDVE GDHKTLVREM
GAASVVLLTN QDNILPLKET DKSISVIGSD AFNDPLLFDP ENCSNFMCDP ATLIQGWGSG
VVSHPSYIVP PIEGIKSRVG NDVKIQSTND NYDMEKVKQI AEASDIAIVF ANSDSGEGST
PVNGTKGDRS TLTLWNNGDK LVQSVADANK NTIVVVHSVG AILMPWANHE NIKAIVWPGL
PGAESGNSLA DVLFGDVNPS GRLPYTIAKE LGDYVTTPSA DLEIDYTEKL NIGYRWFDSK
KIDPLFAFGH GLSYTKFDYG ELKVKARKDQ VNAEIQVQNT GDVDGAEVVQ LYLSFPESAE
EPPKVLRGFE KVFIKAGGHH KESVKFELTK TELSIWDVTT QSWVIPSGQF EIHVGASSRD
IRQFATFTL
//
