ID   EGLD_ASPOR              Reviewed;         367 AA.
AC   Q2US83;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=AO090005000531;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007151; BAE55582.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2US83; -.
DR   SMR; Q2US83; -.
DR   CAZy; AA9; Auxiliary Activities 9.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   EnsemblFungi; BAE55582; BAE55582; AO090005000531.
DR   VEuPathDB; FungiDB:AO090005000531; -.
DR   HOGENOM; CLU_031730_0_0_1; -.
DR   OMA; YIDSPPN; -.
DR   Proteomes; UP000006564; Chromosome 1.
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..367
FT                   /note="Probable endo-beta-1,4-glucanase D"
FT                   /id="PRO_0000394065"
FT   DOMAIN          329..365
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          21..235
FT                   /note="Catalytic"
FT   REGION          37..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..325
FT                   /note="Ser/Thr-rich linker"
FT   ACT_SITE        164
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        210
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        337..354
FT                   /evidence="ECO:0000250"
FT   DISULFID        348..364
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   367 AA;  38033 MW;  0C038474B7C681F3 CRC64;
     MKSSTFGMLA LAAAAKLVSA HATVHAVWIN DVDQGEGNSE SGYIRSPPSN SPITDVTSKD
     MTCNVNNKAT AKTLEVKAGD KITFEWHHDS RSDSDDIIAS SHKGPIMVYM APTEKGTAGN
     GWVKIAEDGY TDGTWAVDTL IKNRGKHSVT VPDVAAGEYL FRPEIIALHE GNRQGGAQFY
     MECVQVKVTS SGSKTLPEGV SIPGAYTATD KGILFDIYNS FDSYPFPGPA VWDGASGSSS
     SPSASASASA PAATSAAPAP SSFTTIAKQP ATSSTEAPST ENTSTTSTIV STTAAASATA
     PATPSSTSAI ASSAASTNSV PQPSSNAGGA VKEWYQCGGL NYKGSTQCEE GLTCKKWNPY
     YYQCISA