ID   EGLB_ASPKW              Reviewed;         332 AA.
AC   Q96WQ8; G7XEC0;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Probable endo-beta-1,4-glucanase B;
DE            Short=Endoglucanase B;
DE            EC=3.2.1.4;
DE   AltName: Full=Carboxymethylcellulase B;
DE   AltName: Full=Cellulase 5B;
DE   AltName: Full=Cellulase B;
DE   Flags: Precursor;
GN   Name=eglB; Synonyms=cel5B; ORFNames=AKAW_03613;
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AB055433; BAB62319.1; -; Genomic_DNA.
DR   EMBL; DF126453; GAA85499.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96WQ8; -.
DR   SMR; Q96WQ8; -.
DR   STRING; 40384.Q96WQ8; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   VEuPathDB; FungiDB:AKAW_03613; -.
DR   eggNOG; ENOG502QXN4; Eukaryota.
DR   InParanoid; Q96WQ8; -.
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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..332
FT                   /note="Probable endo-beta-1,4-glucanase B"
FT                   /id="PRO_0000394056"
FT   ACT_SITE        160
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        267
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   332 AA;  36733 MW;  A709672F5DEB1830 CRC64;
     MKFQSTLLLA AAAGSALAVP HGPGHKKRAS VFEWFGSNES GAEFGTNIPG VWGTDYIFPD
     PSAISTLIDK GMNFFRVQFM MERLLPDSMT GSYDEEYLAN LTTVIKAVTD GGAHALVDPH
     NYGRYNGEII SSTSDFQTFW ENLAGQYKDN DLVMFDTNNE YHDMDQDLVL NLNQAAINGI
     RAAGATSQYI FVEGNSWTGA WTWVDVNDNM KNLTDPEDKI VYEMHQYLDS DGSGTSETCV
     SETIGKERVT EATQWLKDNK KVGFIGEYAG GSNDVCRSAV SGMLEYMANN TDVWKGASWW
     AAGPWWGDYI FSMEPPDGTA YTGMLDILEA YL