EGLD_ASPNC
ID EGLD_ASPNC Reviewed; 412 AA.
AC A2R5N0;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Probable endo-beta-1,4-glucanase D;
DE Short=Endoglucanase D;
DE EC=3.2.1.4;
DE AltName: Full=Carboxymethylcellulase D;
DE AltName: Full=Cellulase D;
DE Flags: Precursor;
GN Name=eglD; ORFNames=An15g04900;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Has endoglucanase activity on substrates containing beta-1,4
CC glycosidic bonds, like in carboxymethylcellulose (CMC),
CC hydroxyethylcellulose (HEC) and beta-glucan. Involved in the
CC degradation of complex natural cellulosic substrates (By similarity).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DOMAIN: Has a modular structure: an endo-beta-1,4-glucanase catalytic
CC module at the N-terminus, a linker rich in serines and threonines, and
CC a C-terminal carbohydrate-binding module (CBM). The genes for catalytic
CC modules and CBMs seem to have evolved separately and have been linked
CC by gene fusion.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family. {ECO:0000305}.
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DR EMBL; AM270345; CAK42466.1; -; Genomic_DNA.
DR AlphaFoldDB; A2R5N0; -.
DR SMR; A2R5N0; -.
DR CAZy; AA9; Auxiliary Activities 9.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR PaxDb; A2R5N0; -.
DR EnsemblFungi; CAK42466; CAK42466; An15g04900.
DR VEuPathDB; FungiDB:An15g04900; -.
DR HOGENOM; CLU_031730_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 3R.
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 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 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..412
FT /note="Probable endo-beta-1,4-glucanase D"
FT /id="PRO_5000221057"
FT DOMAIN 373..409
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 21..237
FT /note="Catalytic"
FT REGION 238..370
FT /note="Ser/Thr-rich linker"
FT ACT_SITE 167
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 213
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 381..398
FT /evidence="ECO:0000250"
FT DISULFID 392..408
FT /evidence="ECO:0000250"
SQ SEQUENCE 412 AA; 41981 MW; B90018CCC26771C3 CRC64;
MKTTTYSLLA LAAASKLASA HTTVQAVWIN GEDQGLGNSA DGYIRSPPSN SPVTDVTSTD
MTCNVNGDQA ASKTLSVKAG DVVTFEWHHS DRSDSDDIIA SSHKGPVQVY MAPTAKGSNG
NNWVKIAEDG YHKSSDEWAT DILIANKGKH NITVPDVPAG NYLFRPEIIA LHEGNREGGA
QFYMECVQFK VTSDGSSELP SGVSIPGVYT ATDPGILFDI YNSFDSYPIP GPDVWDGSSS
GSSSGSSSAA AAATTSAAVA ATTPATQAAV EVSSSAAAVV ESTSSAAAAT TEAAAPVVSS
AAPVQQATSA VTSQAQAPTT FATSSKSSKT ACKNKTKSKS KVAASSTEAV VAPAPTSSVV
PAVSASASAS AGGVAKMYER CGGINHTGPT TCESGSVCKK WNPYYYQCVA SQ
