CEL6A_MAGO7
ID CEL6A_MAGO7 Reviewed; 487 AA.
AC G4MM92;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=1,4-beta-D-glucan cellobiohydrolase CEL6A {ECO:0000305};
DE EC=3.2.1.91 {ECO:0000269|PubMed:20709852};
DE AltName: Full=Beta-glucancellobiohydrolase CEL6A {ECO:0000305};
DE AltName: Full=Exocellobiohydrolase CEL6A {ECO:0000305};
DE AltName: Full=Exoglucanase CEL6A {ECO:0000305};
DE Flags: Precursor;
GN Name=cel6A {ECO:0000303|PubMed:20709852}; ORFNames=MGG_05520;
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=20709852; DOI=10.1128/aem.00618-10;
RA Takahashi M., Takahashi H., Nakano Y., Konishi T., Terauchi R., Takeda T.;
RT "Characterization of a cellobiohydrolase (MoCel6A) produced by Magnaporthe
RT oryzae.";
RL Appl. Environ. Microbiol. 76:6583-6590(2010).
CC -!- FUNCTION: Exoglucanase that plays an important function in biomass
CC degradation by catalyzing the hydrolysis of the non-reducing end beta-
CC 1,4-glucosidic linkages in cellulose and cellotetraose to release
CC cellobiose. Shows higher hydrolytic activities on phosphoric acid-
CC swollen cellulose (PSC), beta-glucan, and cellooligosaccharide
CC derivatives than on cellulose, of which the best substrates were
CC cellooligosaccharides. {ECO:0000269|PubMed:20709852}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC and cellotetraose, releasing cellobiose from the non-reducing ends of
CC the chains.; EC=3.2.1.91; Evidence={ECO:0000269|PubMed:20709852};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24.3 mM for cellotetraose {ECO:0000269|PubMed:20709852};
CC Vmax=454.5 umol/min/mg enzyme toward cellotetraose
CC {ECO:0000269|PubMed:20709852};
CC pH dependence:
CC Optimum pH is 4.5-9.0. {ECO:0000269|PubMed:20709852};
CC Temperature dependence:
CC Optimum temperature is 30-50 degrees Celsius.
CC {ECO:0000269|PubMed:20709852};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- INDUCTION: Expression increases during infection of rice.
CC {ECO:0000269|PubMed:20709852}.
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 6 (cellulase B) family.
CC {ECO:0000305}.
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DR EMBL; CM001231; EHA57773.1; -; Genomic_DNA.
DR RefSeq; XP_003710385.1; XM_003710337.1.
DR AlphaFoldDB; G4MM92; -.
DR SMR; G4MM92; -.
DR STRING; 318829.MGG_05520T0; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR CLAE; CBH6A_MAGOR; -.
DR EnsemblFungi; MGG_05520T0; MGG_05520T0; MGG_05520.
DR GeneID; 2675858; -.
DR KEGG; mgr:MGG_05520; -.
DR VEuPathDB; FungiDB:MGG_05520; -.
DR eggNOG; ENOG502QWHE; Eukaryota.
DR HOGENOM; CLU_015488_0_0_1; -.
DR InParanoid; G4MM92; -.
DR OMA; NTPQAYW; -.
DR OrthoDB; 957754at2759; -.
DR Proteomes; UP000009058; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51989; SSF51989; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..487
FT /note="1,4-beta-D-glucan cellobiohydrolase CEL6A"
FT /evidence="ECO:0000255"
FT /id="PRO_5001345334"
FT DOMAIN 27..63
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 64..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT ACT_SITE 262
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT ACT_SITE 441
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9,
FT ECO:0000255|PROSITE-ProRule:PRU10056"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 435
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT DISULFID 35..52
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT DISULFID 46..62
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
SQ SEQUENCE 487 AA; 51225 MW; AFBD3DDD5FEDF4E0 CRC64;
MASKLFLAAA LLQGALSSPL AVEERQACAA QWGQCGGQDY TGPTCCQSGS TCVVSNQWYS
QCLPGSSNPT TTSRTSTSSS SSTSRTSSST SRPPSSVPTT PTSVPPTITT TPTTTPTGGS
GPGTTASFTG NPFAGVNLFP NKFYSSEVHT LAIPSLTGSL VAKASAVAQV PSFQWLDIAA
KVETLMPGAL ADVRAANAAG GNYAAQLVVY DLPDRDCAAA ASNGEFSIAD GGVVKYKAYI
DAIRKQLLAY SDVRTILVIE PDSLANMVTN MGVPKCAGAK DAYLECTIYA VKQLNLPHVA
MYLDGGHAGW LGWPANLQPA ADLFGKLYAD AGKPSQLRGM ATNVANYNAW DLTTAPSYTT
PNPNFDEKKY ISAFAPLLAA KGWSAHFIID QGRSGKQPTG QKEWGHWCNQ QGVGFGRRPS
ANTGSELADA FVWIKPGGEC DGVSDPTAPR FDHFCGTDYG AMSDAPQAGQ WFQKYFEMLL
TNANPPL
