CEL61_MYCTT
ID CEL61_MYCTT Reviewed; 342 AA.
AC G2Q9T3;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Polysaccharide monooxygenase Cel61a;
DE AltName: Full=Cellulase-61a;
DE Short=Cel61a;
DE AltName: Full=Endoglucanase-61a;
DE AltName: Full=Glycoside hydrolase-61;
DE Short=GH-61;
DE EC=1.13.-.-;
DE Flags: Precursor;
GN Name=Cel61a; ORFNames=MYCTH_46583;
OS Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS (Sporotrichum thermophile).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX NCBI_TaxID=573729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799;
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOTECHNOLOGY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND ACTIVITY REGULATION.
RX PubMed=22342036; DOI=10.1016/j.biortech.2012.01.116;
RA Dimarogona M., Topakas E., Olsson L., Christakopoulos P.;
RT "Lignin boosts the cellulase performance of a GH-61 enzyme from
RT Sporotrichum thermophile.";
RL Bioresour. Technol. 110:480-487(2012).
CC -!- FUNCTION: Enzyme involved in the degradation of lignocellulosic
CC biomass. Hydrolyzes weakly barley beta-glucan, carboxymethyl cellulose,
CC lichenan, wheat arabinoxylan and birchwood xylan. Stimulates the
CC hydrolysis of lignocellulosic substrates (such as hydrothermal
CC pretreated wheat straw or steam-pretreated spruce), when combined with
CC other cellulolytic enzymes. Lignin is a significant source of reductant
CC residues that probably stimulate GH-61 activity by acting as electron
CC donors. {ECO:0000269|PubMed:22342036}.
CC -!- ACTIVITY REGULATION: The presence of lignin presents a significant
CC source of antioxidants, which probably increase the activity by
CC trapping liberated oxidized fragments. {ECO:0000269|PubMed:22342036}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:22342036};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.
CC {ECO:0000269|PubMed:22342036};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- BIOTECHNOLOGY: The use of glycoside hydrolase-61-boosting enzymes in
CC cellulase mixtures enhanced their hydrolytic activity almost 1.5-fold
CC and could further improve the technoeconomic analysis for producing
CC fermentable sugars towards second generation biofuels.
CC {ECO:0000269|PubMed:22342036}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family. {ECO:0000305}.
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DR EMBL; CP003003; AEO56542.1; -; Genomic_DNA.
DR RefSeq; XP_003661787.1; XM_003661739.1.
DR AlphaFoldDB; G2Q9T3; -.
DR SMR; G2Q9T3; -.
DR STRING; 573729.G2Q9T3; -.
DR CAZy; AA9; Auxiliary Activities 9.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR EnsemblFungi; AEO56542; AEO56542; MYCTH_46583.
DR GeneID; 11510592; -.
DR KEGG; mtm:MYCTH_46583; -.
DR VEuPathDB; FungiDB:MYCTH_46583; -.
DR eggNOG; ENOG502RY3D; Eukaryota.
DR HOGENOM; CLU_031730_1_0_1; -.
DR InParanoid; G2Q9T3; -.
DR OrthoDB; 1157687at2759; -.
DR Proteomes; UP000007322; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR005103; AA9.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR Pfam; PF03443; AA9; 1.
DR Pfam; PF00734; CBM_1; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycosidase; Hydrolase; Oxidoreductase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..342
FT /note="Polysaccharide monooxygenase Cel61a"
FT /id="PRO_0000419258"
FT DOMAIN 306..342
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 20..253
FT /note="Catalytic"
FT /evidence="ECO:0000255"
FT REGION 254..306
FT /note="Linker"
FT /evidence="ECO:0000255"
FT REGION 263..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 314..331
FT /evidence="ECO:0000250"
FT DISULFID 325..341
FT /evidence="ECO:0000250"
SQ SEQUENCE 342 AA; 34936 MW; ABE32A8B3AF90ADE CRC64;
MSKASALLAG LTGAALVAAH GHVSHIVVNG VYYRNYDPTT DWYQPNPPTV IGWTAADQDN
GFVEPNSFGT PDIICHKSAT PGGGHATVAA GDKINIVWTP EWPESHIGPV IDYLAACNGD
CETVDKSSLR WFKIDGAGYD KAAGRWAADA LRANGNSWLV QIPSDLKAGN YVLRHEIIAL
HGAQSPNGAQ AYPQCINLRV TGGGSNLPSG VAGTSLYKAT DPGILFNPYV SSPDYTVPGP
ALIAGAASSI AQSTSVATAT GTATVPGGGG ANPTATTTAA TSAAPSTTLR TTTTSAAQTT
APPSGDVQTK YGQCGGNGWT GPTVCAPGSS CSVLNEWYSQ CL
