ID A0A364L561_9EURO Unreviewed; 1097 AA.
AC A0A364L561;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=BHQ10_006948 {ECO:0000313|EMBL:RAO70936.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO70936.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO70936.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO70936.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
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:RAO70936.1}.
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; MIKG01000013; RAO70936.1; -; Genomic_DNA.
DR STRING; 1196081.A0A364L561; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000249363; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
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; 1.10.489.10; Chloroperoxidase-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; IPR000028; Chloroperoxidase.
DR InterPro; IPR036851; Chloroperoxidase-like_sf.
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 PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF12; BETA-GLUCOSIDASE A-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF01328; Peroxidase_2; 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.
DR SUPFAM; SSF47571; Cloroperoxidase; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR PROSITE; PS51405; HEME_HALOPEROXIDASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361161};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
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:UP000249363};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1097
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016637685"
FT DOMAIN 24..245
FT /note="Heme haloperoxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS51405"
SQ SEQUENCE 1097 AA; 119030 MW; 0627C48285EC648D CRC64;
MKLTLFLEVY VFSVAAHGWQ LPPKGHEWHP PVTGDSRSPC PGLNVMANHG FLPRSGKNID
LAAVRDGVSQ AYNFAPTTFD SAFEQAIDLG VSTTGNASTF HLEDLKKHDA VEFDGSLSRN
DAYFGDDNSF NHAIWWTTAL RLGLYDYGLF GNNTHVNVET AARARAARVR DAKAVNPKFN
ASANELTGSP GTTALYLATL WDDAADAAPK AWIRAFFENE RIPYLEGYQP PTVARDGSTI
GELFARVTAV NDNEPYSPPY YPSPWGDGEG EWADAYEKAR EFVSQLTLPE KVNLTTGTGW
MQGSCVGETG SIPRLGFRGL CLQDGPMGIR FSDYNSAFPA GVNVAATWDR SLAYLRGLAM
GKEFNSKGVD IQLGPVSGPL GRTPEGGRNW EGFSPDPVNT GVMMAETIKG IQEAGVIACA
KHYILNEQEH FRLVGEAKGY GYNITASASS NVDDRTMHEL YLWPFADAVR AGVGSIMCSY
NQVNNSYACA NSYTLNRLLK GELDFQGFVM SDWGAHTSGV SSTLAGLDMS MPGDTSFDSG
DSYWGANLTI SVVNGTVPTY RIDDMAVRIM AAYYKVGRDK FQVPINFNSW TRDEYGPIYA
AAGPEYGVGK VNERVDVRGN HASLIRKIGA ASVVLLKNTD SVLPLSGKEK FTAIFGSDAR
ADPVGINGCA DHGCDNGTLA IGWGSGTSNF PYIVTPEDAI KQEILSKGVG IVDSVADDWA
YDKIQVLASQ ADVALVFVNS DSGENFIVVD GNEGDRNNLT LWRDGDKLIE TVASQNNNTV
VVIHSGGPVL VGDWYNNSNV TAILWAGMPG QESGNSIADV LYGYVNPGGK SPFTWGTARE
DYSTDVLYTP NNGVNAPQID FTEGLFIDYR GFDRANVTPI YEFGFGLSYT TFEYQNIRIR
PLQNAAPYTP TTGFTAPAPV ASNFSTDWSD YLFPRFIRRV PLFLYPWLNT TDPAASSGDP
DYGLQANEYL PENATSASPQ PLLAAGGAPG GNPGLYEEVA IVTADITNTG SVAGDEVPQL
YISHGGPDDP PVVLRGFDRI SLRPQETKEF SVVLTRRDIS NWDVVLQDWV VTRYPKTVYV
GSSSRELLLE AGXPDLF
//
