CEL3B_MAGO7
ID CEL3B_MAGO7 Reviewed; 765 AA.
AC G4N7Z0;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Beta-glucosidase cel3A {ECO:0000303|PubMed:21626020};
DE EC=3.2.1.21 {ECO:0000269|PubMed:21626020};
DE AltName: Full=Beta-D-glucoside glucohydrolase cel3A {ECO:0000305};
DE AltName: Full=Cellobiase cel3A {ECO:0000305};
DE AltName: Full=Gentiobiase cel3A {ECO:0000305};
DE Flags: Precursor;
GN Name=cel3B {ECO:0000303|PubMed:21626020}; ORFNames=MGG_0350;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21626020; DOI=10.1007/s00253-011-3340-1;
RA Takahashi M., Konishi T., Takeda T.;
RT "Biochemical characterization of Magnaporthe oryzae beta-glucosidases for
RT efficient beta-glucan hydrolysis.";
RL Appl. Microbiol. Biotechnol. 91:1073-1082(2011).
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. Shows higher
CC activities on cellobiose and cellotriose but lower activities on
CC laminarioligosaccharides and polymers. {ECO:0000269|PubMed:21626020}.
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:0000269|PubMed:21626020};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27.93 mM for cellobiose {ECO:0000269|PubMed:21626020};
CC KM=13.01 mM for cellohexaose {ECO:0000269|PubMed:21626020};
CC KM=23.39 mM for laminaribiose {ECO:0000269|PubMed:21626020};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:21626020};
CC Temperature dependence:
CC Optimum temperature is 40-60 degrees Celsius.
CC {ECO:0000269|PubMed:21626020};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000269|PubMed:21626020}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- INDUCTION: The transcript levels are constant during infection.
CC {ECO:0000269|PubMed:21626020}.
CC -!- MISCELLANEOUS: The biological conversion of cellulose to glucose
CC generally requires three types of hydrolytic enzymes: (1)
CC Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2)
CC Exocellobiohydrolases that cut the disaccharide cellobiose from the
CC non-reducing end of the cellulose polymer chain; (3) Beta-1,4-
CC glucosidases which hydrolyze the cellobiose and other short cello-
CC oligosaccharides to glucose. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; CM001234; EHA50092.1; -; Genomic_DNA.
DR RefSeq; XP_003716411.1; XM_003716363.1.
DR AlphaFoldDB; G4N7Z0; -.
DR SMR; G4N7Z0; -.
DR STRING; 318829.MGG_03508T0; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR CLAE; BGL3B_MAGOR; -.
DR EnsemblFungi; MGG_03508T0; MGG_03508T0; MGG_03508.
DR GeneID; 2676605; -.
DR KEGG; mgr:MGG_03508; -.
DR VEuPathDB; FungiDB:MGG_03508; -.
DR eggNOG; ENOG502SMNU; Eukaryota.
DR HOGENOM; CLU_004542_2_1_1; -.
DR InParanoid; G4N7Z0; -.
DR OMA; LDWNAQH; -.
DR OrthoDB; 201102at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000009058; Chromosome 4.
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; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 1.
DR InterPro; IPR026891; Fn3-like.
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 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; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..765
FT /note="Beta-glucosidase cel3A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432720"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 765 AA; 82814 MW; 3A4CDA5663D201E6 CRC64;
MRWSSPTSSS LSLVALLLVA HVDAAERATS PPVHPSPPMK GAGVWSAAYA SAKELVSQMT
LEEMVNITGG FATTENVCAG NTGTVPRLGW PGLCLHDAGN GVRATDLVSA YPSGLHVGAS
WDKNLTYERG LYMGKEFKAK GVNVLLGPNA GALGRVPVAG RNWEGFTIDP YLSGILNAES
IVGHQEAGVI ATTKHFIGNE QELYRRPYFG VEAVSSNIDD KTVHELYMWP FMDSVKAGAA
SAMCSYQRVN NTYACMNSKL MNGLLKGELE FEGFIMLDWN AVHTVDSAEA GLDMVMPRGN
WGTNLTAAIN NGTTSKERLV DMATRIVAAW YFVGQDGDKF PKPGVGMYNL TQPHTPVEAR
VSESKPIIME GAVAGHVLLK NEKNALPLKK PKMLSVYGYD ATVPRTKNTD VLFTLGYYSS
AEMAQAVLGT EQHFDQAAKG GTIISGGRAG ANGPPYISDP LSAIQHRAAD DDTWVNWDLD
SGNPDVNSGS DACLVFINAI ATEGWDRDGL HDDFSDGLVL NVASKCENTI VVIHNAGVRL
VDQWVDHPNV TALVMAHLPG QDSGAALVKL LYGEEYFSGK LPYTIPHNES DYGHVYRSCA
HDRAQDDKDP QCDFTEGVYI DYRDFDARNV TPRFEFGFGL GYTTFEFSEL SIETSENLTA
GVGSGSIWDH VAIVHATIKN NGSADGAEVA QLYLGIPNSP PKQLRGFEKV ALSPGVSAPV
RFELTRRDFS IWDVVAQKWV VQEGSYSVHV GASSRDIRLS DDIKI
