ID A0A093ZUE1_9PEZI Unreviewed; 895 AA.
AC A0A093ZUE1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN ORFNames=V491_03296 {ECO:0000313|EMBL:KFY20941.1};
OS Pseudogymnoascus sp. VKM F-3775.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY20941.1, ECO:0000313|Proteomes:UP000029338};
RN [1] {ECO:0000313|EMBL:KFY20941.1, ECO:0000313|Proteomes:UP000029338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY20941.1,
RC ECO:0000313|Proteomes:UP000029338};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 ECO:0000256|RuleBase:RU361161};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:KFY20941.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPJT01001899; KFY20941.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093ZUE1; -.
DR HOGENOM; CLU_004542_4_0_1; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000029338; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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; IPR019800; Glyco_hydro_3_AS.
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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF27; BETA-GLUCOSIDASE; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361161};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000029338}.
FT DOMAIN 459..619
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 18..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 98010 MW; 2B1811478E4BAB66 CRC64;
MTETAELPAP VVEVATDLTS DSIATTARGS EVHSPSSNRT TSTPASELSS IEALKGFKST
NLGVSKENAR VKAATLSLIE QVSLLRAADH WRTVAIPNKG IPNIKTSDGP NGARGAVFKA
GTRAALFPCG VSLAATWDTK LLYEVGQHLA EETKARSAHV LLAPTVCLHR GPLGGRNFES
FSEDPLLTGK LAASYINGLQ QKGIAATIKH FVANEQETER LTMDSELSER ALRELYLRPF
EIAVRESNPW AVMSSYNLIN GVHADMNTHT LKEILRGEWK YDGLVMSDWT GVNSVSESIE
AGCDLEMPYS DKWRGEKAVQ AVKDGKLSQD AVEKAAANVL YLIDRVRGQD TSPEEPEREE
DTPETRELIR RAGSQGLTLL KNRTNLLPLD PEKTKIAVIG PNANRAIAGG GGSASLNPYY
NTLPLWSIQR ASSKDVTYAL GCDIYKWVPL ATPFCKSLTG EEGVTIEFYT GDKFEGEPTV
VQTRTSTDLM LWDSAPTEVG NVWSAYVKAK LTPKTTGKHK FSFFSVGPGR LYIDGQLLAD
LWDWTEQGET MFDGSEDVVV EVELEAGRTY DLMSELTNEI RPLSKQITIG RTHGPGGVRI
GYKEEDKVDH LQQAVDAATE ADVAVVIVGL DAEWESEGYD RANMDLPKDG SQDRLVEAVL
KANPNTIVVV QAGSPVTMPW ADKVPSILQA WYQGQEAGNA LADVLFGHVN PSGKLPTTFP
VRLQDNPTYH TWPGENKKVI YGEGIFMGYR HYERLAIKPL FAFGHGLSYT TFTYGDITLS
NTTLSANDKL TVTIPITNSG KVDGAEVVQG YVHDVKSRLV RPEKELAVFD KVFLKAGETK
DVVLTLDKLS VGYYDTRLKA WIAEEGEFKI LVGSSSADIR QEATFDVAES FTWIF
//
