ID H2BPT0_NEOPA Unreviewed; 786 AA.
AC H2BPT0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
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};
OS Neocallimastix patriciarum (Rumen fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=4758 {ECO:0000313|EMBL:AEX92706.1};
RN [1] {ECO:0000313|EMBL:AEX92706.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W5 {ECO:0000313|EMBL:AEX92706.1};
RX PubMed=21849025; DOI=10.1186/1754-6834-4-24;
RA Wang T.Y., Chen H.L., Lu M.Y., Chen Y.C., Sung H.M., Mao C.T., Cho H.Y.,
RA Ke H.M., Hwa T.Y., Ruan S.K., Hung K.Y., Chen C.K., Li J.Y., Wu Y.C.,
RA Chen Y.H., Chou S.P., Tsai Y.W., Chu T.C., Shih C.C., Li W.H., Shih M.C.;
RT "Functional characterization of cellulases identified from the cow rumen
RT fungus Neocallimastix patriciarum W5 by transcriptomic and secretomic
RT analyses.";
RL Biotechnol. Biofuels 4:24-24(2011).
RN [2] {ECO:0000313|EMBL:AEX92706.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W5 {ECO:0000313|EMBL:AEX92706.1};
RA Wang T.-Y., Chen H.-L., Lu M.-Y.J., Chen Y.-C., Sung H.-M., Mao C.-T.,
RA Cho H.-Y., Ke H.-M., Hwa T.-Y., Ruan S.-K., Hung K.-Y., Chen C.-K.,
RA Li J.-Y., Wu Y.-C., Chen Y.-H., Chou S.-P., Tsai Y.-W., Chu T.-C.,
RA Shih A.C.-C., Li W.-H., Shih M.-C.;
RL Submitted (MAY-2011) 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}.
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DR EMBL; JF906703; AEX92706.1; -; mRNA.
DR AlphaFoldDB; H2BPT0; -.
DR SMR; H2BPT0; -.
DR UniPathway; UPA00696; -.
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.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361161};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
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|RuleBase:RU361161};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..786
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003560304"
FT DOMAIN 632..703
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 715..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..756
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 786 AA; 85817 MW; FCCFB5DD9355CA31 CRC64;
MNRSSQVSYQ LLLFFLSANT LAMTWEEADA KAREWCADLT NEEKISLVTG RENMTGVCVG
SIDPIERKGF KGLCLQDGPA GVRFAKGTAT SWQAGINNAA TFDRQLMRKV GEAQGNEFYQ
RGINFALGPA MNIQRAPAAG RIWESFGEDP FLAGQCGIEV VKGMQSSGVI ATSKHFVGND
QENNRGASSS NIPEQALWEV YIEPFYRVVK EAETNAIMSS YNAVNGTYLV QNKRLLTDVL
KGKLGFQGMV MSDWWSIYDV EKSFGAGMDM NMPGGKYWGP DYVGDSFWGE HIQECIDNGV
FPQERLDDAA LRIIRTLYKA GQMEDYPDVN LYVDTNNEEN TALNRKVAAD STVLLKNEAV
LPIKGVKKIA IIGKDAMPAN FCEDMKCADG TVALGWGSGT TDFKYVADPL SSITERAKKD
NIEIVSSGED DAEAGAEVAK DADLAIVFVQ ADSGEEYIVV EGNKGDRLNL DLWHNGNELV
DAVASVNENT IVVIHAPGPV NVPFLDKVKG IVFAGMPGQE SGNAIADVLF GDVNPSGHLP
YTWAPREDFP TDVNYDPSLP GGGEEKTQYD YNEGLFVGYR WFDKQGIDPT FAFGYGLSYT
TFEYSNLKAQ MEEDGLHVTL TVSNTGDVAG AAVPMIFLSF PDVVKDYPSR LFKGFDKVLL
EAGESKEVKI LVDNHDLSYY DVDAADFVKP AEGEYTVLAG SNARDLPLKV TVSADGTNAG
NAEEVTEECS SEEEEVTGVN GDDVTAEDSA EDDVQEIDAD AEVEEAEDSA NEADEAELRK
RAYKLY
//
