CEL7B_MAGO7
ID CEL7B_MAGO7 Reviewed; 424 AA.
AC G4NK46;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Endoglucanase 1 {ECO:0000303|PubMed:18247030};
DE EC=3.2.1.4 {ECO:0000269|PubMed:18247030};
DE AltName: Full=Cellulase 1 {ECO:0000305};
DE AltName: Full=Endo-1,4-beta-glucanase 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=egl1 {ECO:0000303|PubMed:18247030}; ORFNames=MGG_02532;
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, INDUCTION, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18247030; DOI=10.1007/s00294-008-0179-9;
RA Zhou J., Zheng X.Z., Lan L., Lin C.Z., Wu Y.B., Lin X.J., Ebbole D.,
RA Lu G.D., Wang Z.H.;
RT "Biochemical and molecular characterization of a putative endoglucanase in
RT Magnaporthe grisea.";
RL Curr. Genet. 53:217-224(2008).
CC -!- FUNCTION: Endoglucanase that is involved in the biological conversion
CC of cellulose to glucose. Hydrolyses internal beta-1,4-glucosidic bonds.
CC {ECO:0000269|PubMed:18247030}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000269|PubMed:18247030};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P56680}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18247030}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages, however, the highest
CC level appears in mycelia, followed by germinating spores, and the
CC lowest in spores. {ECO:0000269|PubMed:18247030}.
CC -!- INDUCTION: Expression is increased at 72 h of infection, and then the
CC expression level drops back to the lower level for the remainder of the
CC time course. {ECO:0000269|PubMed:18247030}.
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 7 (cellulase C) family.
CC {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; CM001237; EHA46531.1; -; Genomic_DNA.
DR RefSeq; XP_003721274.1; XM_003721226.1.
DR AlphaFoldDB; G4NK46; -.
DR SMR; G4NK46; -.
DR STRING; 318829.MGG_02532T0; -.
DR CLAE; EGL7A_MAGGR; -.
DR EnsemblFungi; MGG_02532T0; MGG_02532T0; MGG_02532.
DR GeneID; 2682835; -.
DR KEGG; mgr:MGG_02532; -.
DR VEuPathDB; FungiDB:MGG_02532; -.
DR eggNOG; ENOG502SJT6; Eukaryota.
DR HOGENOM; CLU_020817_0_1_1; -.
DR InParanoid; G4NK46; -.
DR OMA; VCCNEMD; -.
DR OrthoDB; 875234at2759; -.
DR Proteomes; UP000009058; Chromosome 7.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd07999; GH7_CBH_EG; 1.
DR Gene3D; 2.70.100.10; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001722; Glyco_hydro_7.
DR InterPro; IPR037019; Glyco_hydro_7_sf.
DR PANTHER; PTHR33753; PTHR33753; 1.
DR Pfam; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..424
FT /note="Endoglucanase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432715"
FT ACT_SITE 213
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT ACT_SITE 218
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 35..41
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 68..90
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 80..86
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 156..384
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 188..211
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 192..210
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 231..250
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 239..244
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 255..331
FT /evidence="ECO:0000250|UniProtKB:P56680"
SQ SEQUENCE 424 AA; 45062 MW; 35AD1C4C2B6490C1 CRC64;
MAKFSALCSL ALLGLATAQK PVGTETHEKL TTFRCTVAGG CVEKTNYIVL DSITGHRIYQ
PAAETLDCGA RGAAPNVTAC PTKEACAENC AMEGRTDYGS QGVSTDGASL RLQILHDGKK
VAPRVYLLDE TEAKYEMLRL TGNEFAFEVT MDKLPCGMNS ALYLSEMEED GGKSELNPGG
APWGTGYCDA QCYVTPFING EGNIKGNGAC CAEMDIWEAN SRATHIAPHP CSKPGLYLCE
GDECGSTGVC DKSGCAWNPN RIAQPHYYGN NDTFKVDTLK PMTVVTQFPT DASGKLAAIR
RLYVQGGVVI KAETVHKAGL PEVDALTDPF CEAFGSQRYM ALGATGGMGD ALARGMVLVM
SIWWDETGGN MQWLDGIASG SGPCNATEGA PANIPLVEPN PEVTFSNLKW GEIGSTFQGG
ARRL
