CEL3A_MAGO7
ID CEL3A_MAGO7 Reviewed; 726 AA.
AC G4NI45;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 47.
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=cel3A {ECO:0000303|PubMed:21626020}; ORFNames=MGG_09353;
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, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
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. Has a broad
CC substrate specificity but preferentially hydrolyzes highly polymerized
CC 1,3- and 1,4-beta-glucans. {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=4.21 mM for cellobiose {ECO:0000269|PubMed:21626020};
CC KM=0.59 mM for cellohexaose {ECO:0000269|PubMed:21626020};
CC KM=1.95 mM for laminaribiose {ECO:0000269|PubMed:21626020};
CC KM=0.47 mM for laminarihexaose {ECO:0000269|PubMed:21626020};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:21626020};
CC Temperature dependence:
CC Optimum temperature is 50 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}.
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; CM001236; EHA47905.1; -; Genomic_DNA.
DR RefSeq; XP_003720272.1; XM_003720224.1.
DR AlphaFoldDB; G4NI45; -.
DR SMR; G4NI45; -.
DR STRING; 318829.MGG_09353T0; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR CLAE; BGL3A_MAGOR; -.
DR EnsemblFungi; MGG_09353T0; MGG_09353T0; MGG_09353.
DR GeneID; 2680435; -.
DR KEGG; mgr:MGG_09353; -.
DR VEuPathDB; FungiDB:MGG_09353; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_3_1; -.
DR InParanoid; G4NI45; -.
DR OMA; YFVAPYD; -.
DR OrthoDB; 321444at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000009058; Chromosome 6.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..726
FT /note="Beta-glucosidase cel3A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432719"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 726 AA; 77093 MW; D4C474B8B7D862C1 CRC64;
MASRLVAGLQ VLALAGTATA VLTWDEAYAK ANTALARITQ QDKVSLVSGI GWDKGPCVGN
TAPVSAINYP QLCLQDGPTG VRFGTGVTAF TPGIQAASTW DVELMRQRGQ FQAEEQKGCG
VHVMLTPVAG ALGKIPEGGR NWEGFGVDPY LAGIAMEVTI EGQQSVGVQA TAKHYLLNEQ
ELNRNTMSSN VDDRTLHELY LWPFADAVRA NVASVMCSYN KINGSWACEN EHAMQKLLKD
ELGFKGYVMS DWNAQHTTTG SANAGMDMTM PGSDFNGGNV LWGPQLNTAV NNNQVARTRL
DDMARRVLAA WYLTEQDKGY PPINIRANVQ GNHKENVRAV ARDGIVLLKN DAGALPFKAP
RRLAIVGSAS VANPRGINSC VDRGCNEGAL GMGWGSGTTN YPYFSAPADA IRARAQQDGA
TVTLSASDST ADVANTVRDA DAAIVFLTSN SGEGYLLVDG SYGDRLNLDP LHNGNQLVQA
VAQANKNTIV VVHSVGPLVL ESILSTPGVT AVVWAGLPGQ ESGNALVDVL YGSVSPSGKL
PYTIARATAD YGTAIVPGDD NFPEGLFVDY RHFDRANIQP RFEFGYGLSY TNFTYSNIKV
ASTVRSGPAT GPVVSGGRAD LWETVATVTA TVTNSGGVAG AEVAQLYVSY PKGGSVPETP
PRQLRGFNKL KLAPGASGTA TFNIRRRDLS YWHVGQQNWV VPAGAFGLEV GASSRDLRLK
ESITVV
