ID A0A0G2HYF3_9EURO Unreviewed; 875 AA.
AC A0A0G2HYF3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=EMCG_02343 {ECO:0000313|EMBL:KKZ63342.1};
OS Emmonsia crescens UAMH 3008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ63342.1, ECO:0000313|Proteomes:UP000034164};
RN [1] {ECO:0000313|Proteomes:UP000034164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
CC -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose.
CC {ECO:0000256|ARBA:ARBA00024983}.
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:KKZ63342.1}.
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DR EMBL; LCZI01000988; KKZ63342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2HYF3; -.
DR VEuPathDB; FungiDB:EMCG_02343; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000034164; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..875
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002545259"
FT DOMAIN 785..859
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 875 AA; 94984 MW; B7A19DB31D9C2B8E CRC64;
MPFFKSFLIG VIGALGCSSA LAEPDTSKSP VLESRRDGLE GWTSPPYYPA PVGGWVPEWE
EAYGKAHAVV ANMTLAEKVN LTTGTGFSMG PCVGQTGSAP RFGIPRLCLQ DGPLGVRNTD
HITAFPAGIT VGATFDKQLM YDRGVAMGKE FRGKGVNVHL GPSVGPLGRK PRGGRNWEGF
GMDPSLQGIA SALTIKGVQS RGVIATVKHL VGNEQEMFRM VFPVQPFDFL QQPYSANIDD
RTMHELYLWP FAESVKAGVG AVMMAYNDVN SSSSSQNSQL INGILKDELG FQGFTMTDWF
AHIGGVSSAL AGLDMAMPGD GASPLSGHSY WAGELSRSVL NGTVPLERLN DMAARIVATW
FKLGQDKDFP LPNFSTHTNA QSGLLYPGAI FSPIGVVNQF VDVQENHNTI ARAVARDGIT
LLKNEDNVLP LSPDASIRVF GTDAGPDPLG LNPCADRGCN RGVLTMGWGS GSASVPYLVT
PQEGIEARAP KTKFHITNNF PRNLDVKPDD IAIVFINSDS GENYIMVEGN PGDRTLVGLY
AWHGGDQLVI DAAKKFSTVV VVVHTVGPII MEKWIDLPSV KAVLFAHLPG QEAGTIADIL
FGDHSPSGHL PYTIPKAEAD YPDSVNLIYN PIIQIQDTFT EGLYIDYRHF IKANITTRYP
FGHGLSYTTF KFSESKIAAV TPLSEYPPER PAKISPPTFS SDIPPAAEVA WPKGLNRIWR
YLYPYLDNPS SIKPGKVYPY PEGYSTTPQP APRAGGREGG NPALWDIAYK VYVKVTNTGK
VAGRSVAQLY VQPPPEQVAD TPKLQLRQFE KTRVLQPGES EVLCLEITRK DLSIWDVTMQ
DWQVPQLAKG AKLWVGESVE NLRVVCEIGG ECKDT
//
