ID C1G0U3_PARBD Unreviewed; 885 AA.
AC C1G0U3;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 24-JAN-2024, entry version 61.
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=PADG_00483 {ECO:0000313|EMBL:EEH44194.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH44194.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH44194.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH44194.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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}.
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DR EMBL; KN275957; EEH44194.2; -; Genomic_DNA.
DR RefSeq; XP_010755849.1; XM_010757547.1.
DR AlphaFoldDB; C1G0U3; -.
DR STRING; 502780.C1G0U3; -.
DR GeneID; 22580315; -.
DR KEGG; pbn:PADG_00483; -.
DR VEuPathDB; FungiDB:PADG_00483; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR InParanoid; C1G0U3; -.
DR OMA; YYPSPWA; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000001628; 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; 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 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 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 PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 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:UP000001628}.
FT DOMAIN 803..871
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 885 AA; 95406 MW; A8E93B9574992546 CRC64;
MKFAASEQTT FLPFAVTTLH IAMRAGWLQF GAILIAKFAI AEEFLAHSPP YYPSPWVSGQ
GDWADAVQKA RDFVSQLTLT EKVNLTTGVG WMQESCVGQS GSIPRLGFRS LCLQDGPLGI
RFADYVSAFP AGVNVASTFS KELAYERGRA IGEEHRDKGV DVVLGPAIGP LGRSPDGGRN
WEGFSPDPVN SGFLAAETIK GIQSAGVVAC AKHFIANEQE RFRQALEAQS YGFNISESSS
SNIDDITMHE LYLWPFADAV RAGVGSIMCS YNQINNSYGC ANSYTQNKLL KAELGFQGFI
MSDWQAQHSG VGSALAGLDM SMPGDTVFGT GRSFWGTNLT VAVANGTVPG WRVDDMAIRI
MAAYFRVGRH EEEVPVNFNS WTRNEYGYQH ALVGNGYGKV NERVNVRARH ADIIRRVGAA
SVVLLKNTGS LPLTGLEKTT AIIGEDAGPN IFGPNGCPDR GCASGTLAMG WGSGTADFPY
LVTPAEAIQN VILTKGEGIV APIFHNWALS QIKTVSSQAT VSLVFVNAGS GEGYISVDGN
EGDRKNLTLW KGGDELIKTV ASNCNNTVVV IHSSGPVLVS KWNEHPNVTA ILWAGLPGQE
SGNSIADILY GNINPGGKTP FTWGETADDY GTSILKEPNA GNGAPQIDFT EGIFIDYRAF
DKANKSPIYE FGFGLSYSTF SYSDLDISPV KSRPYIPTEG KTEPARSFEY SDRNLSFYLF
PMDVDRVPLY IYPWLNTSDA AKATMDPHYG LFTSEYVPPG ATDGSAQELL PAGGGPGGNP
GLYDILYQIT ATITNTGDIP GDEVPQLYVS LGGPNDAKVV LRNFDRLTIS PGEAKVWKAV
LSRRDISNWD PISQNWVISE HPKTVYVGSS SRNLPLSAPL PPINV
//
