ID   EGLD_ASPKW              Reviewed;         408 AA.
AC   Q96WQ9; G7XU08;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-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 61A;
DE   AltName: Full=Cellulase D;
DE   Flags: Precursor;
GN   Name=eglD; Synonyms=cel61A; ORFNames=AKAW_08531;
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RX   PubMed=14519993; DOI=10.1271/bbb.67.2010;
RA   Hara Y., Hinoki Y., Shimoi H., Ito K.;
RT   "Cloning and sequence analysis of endoglucanase genes from an industrial
RT   fungus, Aspergillus kawachii.";
RL   Biosci. Biotechnol. Biochem. 67:2010-2013(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RX   PubMed=22045919; DOI=10.1128/ec.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB055432; BAB62318.1; -; Genomic_DNA.
DR   EMBL; DF126473; GAA90417.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96WQ9; -.
DR   SMR; Q96WQ9; -.
DR   STRING; 1033177.Q96WQ9; -.
DR   CAZy; AA9; Auxiliary Activities 9.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   VEuPathDB; FungiDB:AKAW_08531; -.
DR   eggNOG; ENOG502QRTW; Eukaryota.
DR   InParanoid; Q96WQ9; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
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; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..408
FT                   /note="Probable endo-beta-1,4-glucanase D"
FT                   /id="PRO_0000394064"
FT   DOMAIN          369..405
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          21..237
FT                   /note="Catalytic"
FT   REGION          238..254
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:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        377..394
FT                   /evidence="ECO:0000250"
FT   DISULFID        388..404
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   408 AA;  41650 MW;  B7CA86C9019F0089 CRC64;
     MKTTTYSLLA LAAASKLASA HTTVQAVWIN GEDQGLGNTD DGYIRSPPSN SPVTDVTSTD
     MTCNVNGDQA ASKTLSVKAG DVVTFEWHHS DRSDSDDIIA SSHKGPVQVY MAPTAKGSNG
     NNWVKIAEDG YHKSSDEWAT DILIANKGKH NITVPDVPAG NYLFRPEIIA LHEGNREGGA
     QFYMECVQFK VTSDGSNELP SGVSIPGVYT ATDPGILFDI YNSFDSYPIP GPDVWDGSSS
     GSSSSGSSSA AVSSAAAAAT TSAVAATTPA TQAAVEVSSS AAAATTEAAA PVVSSAAPVQ
     QATSAVTSQA QAAPTTFATS SKKSSKTACK NKTKSNSQVA AATSSVVAPA ATSSVVPVVS
     ASASASAGGV AKQYERCGGI NHTGPTTCES GSVCKKWNPY YYQCVASQ