CEL7A_MYCTT
ID CEL7A_MYCTT Reviewed; 464 AA.
AC G2QCS4;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Endoglucanase 7a {ECO:0000303|PubMed:23615741};
DE EC=3.2.1.4 {ECO:0000269|PubMed:23615741};
DE AltName: Full=Cellulase 7a {ECO:0000305};
DE AltName: Full=Endo-1,4-beta-glucanase 7a {ECO:0000305};
DE Flags: Precursor;
GN Name=eg7A {ECO:0000303|PubMed:23615741}; ORFNames=MYCTH_111372;
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, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23615741; DOI=10.1007/s00253-013-4895-9;
RA Karnaouri A.C., Topakas E., Christakopoulos P.;
RT "Cloning, expression, and characterization of a thermostable GH7
RT endoglucanase from Myceliophthora thermophila capable of high-consistency
RT enzymatic liquefaction.";
RL Appl. Microbiol. Biotechnol. 98:231-242(2014).
CC -!- FUNCTION: Endoglucanase that is involved in the biological conversion
CC of cellulose to glucose. Hydrolyzes internal beta-1,4-glucosidic bonds.
CC Shows relatively high activity toward barley beta-glucan and
CC carboxymethyl cellulose (CMC), and lower activity toward lichenan,
CC wheat arabinoxylan and other xylans. {ECO:0000269|PubMed:23615741}.
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:23615741};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24 mg/ml for carboxymethyl cellulose
CC {ECO:0000269|PubMed:23615741};
CC Vmax=622 umol/min/mg enzyme toward glucose released by carboxymethyl
CC cellulose hydrolysis {ECO:0000269|PubMed:23615741};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:23615741};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:23615741};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P56680}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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}.
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DR EMBL; CP003004; AEO58196.1; -; Genomic_DNA.
DR RefSeq; XP_003663441.1; XM_003663393.1.
DR AlphaFoldDB; G2QCS4; -.
DR SMR; G2QCS4; -.
DR STRING; 78579.XP_003663441.1; -.
DR CLAE; EGL7A_MYCTH; -.
DR EnsemblFungi; AEO58196; AEO58196; MYCTH_111372.
DR GeneID; 11509397; -.
DR KEGG; mtm:MYCTH_111372; -.
DR VEuPathDB; FungiDB:MYCTH_111372; -.
DR eggNOG; ENOG502RWSR; Eukaryota.
DR HOGENOM; CLU_020817_3_2_1; -.
DR InParanoid; G2QCS4; -.
DR OrthoDB; 875234at2759; -.
DR Proteomes; UP000007322; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase 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 CDD; cd07999; GH7_CBH_EG; 1.
DR Gene3D; 2.70.100.10; -; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR Pfam; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF49899; SSF49899; 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 Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..464
FT /note="Endoglucanase 7a"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432748"
FT DOMAIN 428..464
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 394..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT ACT_SITE 224
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 41..47
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 83..89
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 162..363
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 194..217
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 198..216
FT /evidence="ECO:0000250|UniProtKB:P56680"
FT DISULFID 237..242
FT /evidence="ECO:0000250|UniProtKB:P56680"
SQ SEQUENCE 464 AA; 48667 MW; 3F10982FBAC0379F CRC64;
MGQKTLQGLV AAAALAASVA NAQQPGTFTP EVHPTLPTWK CTTSGGCVQQ DTSVVLDWNY
RWFHTEDGSK SCITSSGVDR TLCPDEATCA KNCFVEGVNY TSSGVETSGS SLTLRQFFKG
SDGAINSVSP RVYLLGGDGN YVVLKLLGQE LSFDVDVSSL PCGENAALYL SEMDATGGRN
EYNTGGAEYG SGYCDAQCPV QNWNNGTLNT GRVGSCCNEM DILEANSKAE AFTPHPCIGN
SCDKSGCGFN AYARGYHNYW APGGTLDTSR PFTMITRFVT DDGTTSGKLA RIERVYVQDG
KKVPSAAPGG DVITADGCTS AQPYGGLSGM GDALGRGMVL ALSIWNDASG YMNWLDAGSN
GPCSDTEGNP SNILANHPDA HVVLSNIRWG DIGSTVDTGD GDNNGGGPNP SSTTTATATT
TSSGPAEPTQ THYGQCGGKG WTGPTRCETP YTCKYQNDWY SQCL
