CE12B_MAGO7
ID CE12B_MAGO7 Reviewed; 264 AA.
AC G4N5V2;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Endoglucanase cel12B {ECO:0000303|PubMed:20680265};
DE EC=3.2.1.4 {ECO:0000269|PubMed:20680265};
DE AltName: Full=Cellulase cel12B {ECO:0000305};
DE AltName: Full=Endo-1,4-beta-glucanase cel12B {ECO:0000305};
DE Flags: Precursor;
GN Name=cel12B {ECO:0000303|PubMed:20680265}; ORFNames=MGG_08537;
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=20680265; DOI=10.1007/s00253-010-2781-2;
RA Takeda T., Takahashi M., Nakanishi-Masuno T., Nakano Y., Saitoh H.,
RA Hirabuchi A., Fujisawa S., Terauchi R.;
RT "Characterization of endo-1,3-1,4-beta-glucanases in GH family 12 from
RT Magnaporthe oryzae.";
RL Appl. Microbiol. Biotechnol. 88:1113-1123(2010).
CC -!- FUNCTION: Endoglucanase that functions in part to hydrolyze 1,3-1,4-
CC beta-glucan during infection and spore formation. Shows preferential
CC hydrolysis of barley beta-glucan and lichenan, but also hydrolyzes
CC carboxymethylcellulose (CMC) to a slight extent.
CC {ECO:0000269|PubMed:20680265}.
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:20680265};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.18 mg/ml for barley beta-glucan (when expressed in M.oryzae)
CC {ECO:0000269|PubMed:20680265};
CC pH dependence:
CC Optimum pH is 6.0-7.5. {ECO:0000269|PubMed:20680265};
CC Temperature dependence:
CC Optimum temperature is 30-40 degrees Celsius.
CC {ECO:0000269|PubMed:20680265};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- INDUCTION: Expression invreases increased 4-5 days after inoculation,
CC but is not detected during spore formation.
CC {ECO:0000269|PubMed:20680265}.
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 12 (cellulase H) family.
CC {ECO:0000305}.
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DR EMBL; CM001234; EHA49727.1; -; Genomic_DNA.
DR EMBL; CM001234; EHA49728.1; -; Genomic_DNA.
DR RefSeq; XP_003716046.1; XM_003715998.1.
DR RefSeq; XP_003716047.1; XM_003715999.1.
DR AlphaFoldDB; G4N5V2; -.
DR SMR; G4N5V2; -.
DR CAZy; GH12; Glycoside Hydrolase Family 12.
DR CLAE; EGL12B_MAGOR; -.
DR EnsemblFungi; MGG_08537T0; MGG_08537T0; MGG_08537.
DR EnsemblFungi; MGG_08537T1; MGG_08537T1; MGG_08537.
DR GeneID; 2678841; -.
DR KEGG; mgr:MGG_08537; -.
DR VEuPathDB; FungiDB:MGG_08537; -.
DR eggNOG; ENOG502SH4Y; Eukaryota.
DR HOGENOM; CLU_051064_0_1_1; -.
DR InParanoid; G4N5V2; -.
DR OMA; VWPISES; -.
DR OrthoDB; 1122671at2759; -.
DR PHI-base; PHI:2978; -.
DR Proteomes; UP000009058; Chromosome 4.
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 Gene3D; 2.60.120.180; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR002594; GH12.
DR PANTHER; PTHR34002; PTHR34002; 1.
DR Pfam; PF01670; Glyco_hydro_12; 1.
DR SUPFAM; SSF49899; SSF49899; 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..264
FT /note="Endoglucanase cel12B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432717"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 264 AA; 29173 MW; CCB214C72006C597 CRC64;
MLPRLATVLL SALGASASVL PTTTTRDLAS RAAPVASLCT QYAYLKTNGY EILNNLWGID
TATGGGSQCT YYNGAVGPAV AFSSDWTWRG NDNTVKSYVY ANRVFERRLV GDIKSLPTSV
QWSYNTTNVR ANVAYDIFTH TDVNHPNSSG DFELMIWLQR YGGIWPITES STGSPVERVT
IAGYTWELFT GWNGAMRVYS FLPPSGTSYN SFSADVKLFF DYLGQKYAFP ASEQYMLIYN
FGTEAFTGGP AHFDVSRFQA EVQV
