GUN3_NEUCR
ID GUN3_NEUCR Reviewed; 390 AA.
AC Q7SDR1;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Endoglucanase gh5-1 {ECO:0000303|PubMed:20826217};
DE EC=3.2.1.4 {ECO:0000269|PubMed:20826217};
DE AltName: Full=Cellulase gh5-1 {ECO:0000305};
DE AltName: Full=Endo-1,4-beta-glucanase gh5-1 {ECO:0000305};
DE Flags: Precursor;
GN Name=gh5-1 {ECO:0000303|PubMed:20826217}; ORFNames=NCU00762;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=20826217; DOI=10.1016/j.pep.2010.08.016;
RA Sun J., Phillips C.M., Anderson C.T., Beeson W.T., Marletta M.A.,
RA Glass N.L.;
RT "Expression and characterization of the Neurospora crassa endoglucanase
RT GH5-1.";
RL Protein Expr. Purif. 75:147-154(2011).
CC -!- FUNCTION: Endoglucanase that plays an important role in biomass
CC degradation. Binds onto plant cell walls to participate in the
CC hydrolysis of cellulose. {ECO:0000269|PubMed:20826217}.
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:20826217};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20826217}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20826217}.
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 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; CM002236; EAA34923.1; -; Genomic_DNA.
DR RefSeq; XP_964159.1; XM_959066.2.
DR AlphaFoldDB; Q7SDR1; -.
DR SMR; Q7SDR1; -.
DR STRING; 5141.EFNCRP00000000813; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR CLAE; EGL5C_NEUCR; -.
DR EnsemblFungi; EAA34923; EAA34923; NCU00762.
DR GeneID; 3880299; -.
DR KEGG; ncr:NCU00762; -.
DR VEuPathDB; FungiDB:NCU00762; -.
DR HOGENOM; CLU_029718_0_1_1; -.
DR InParanoid; Q7SDR1; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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:0009251; P:glucan catabolic process; IBA:GO_Central.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; SSF51445; 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 Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..390
FT /note="Endoglucanase gh5-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432747"
FT DOMAIN 17..52
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 390 AA; 41907 MW; 99207A84F51CB97B CRC64;
MKATILASTF AAGALAQSGA WGQCGGNGWS GATSCISGYA CNYVNDWYSQ CQPGTAAPTT
TAAATTLVTS TKTAPPASTT TATASGKFKW FGVNEAGGEF GDGIFPGRWG TEFTFPDTNT
IQTLRSQGYN IFRVGFAMER LVPNTLTSSF DNGYLTNLTQ VVNSVTNSGA YIVLDPHNYG
RYYGKIITDT DAFKTFWQNV AAKFASNSKV IFDTNNEYNT MDQTLVLNLN QAAIDGIRAA
GATSQYIFVE GNQWTGAWSW NVTNTNLAAL TDPENKIVYE MHQYLDSDSS GTSTACVSSE
IGVQRIVGAT AWLRANGKKG VLGEFAGGAN SVCKAAVTGL LEHLKANTDV WEGALWWAAG
PWWGDYMYSF EPPSGTGYTY YNSLLKTYTP
