ID   EGLB_ASPOR              Reviewed;         333 AA.
AC   Q2UPQ4; Q5TKT6;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-MAY-2023, entry version 84.
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 B;
DE   Flags: Precursor;
GN   Name=eglB; Synonyms=celE; ORFNames=AO090005001553;
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 [GENOMIC DNA].
RC   STRAIN=KBN616;
RA   Yasuda-Yoshino S., Kitamoto N.;
RT   "Cloning and overexpression of a novel cellulase gene, celE, from
RT   Aspergillus oryzae KBN616.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AB195229; BAD72778.1; -; Genomic_DNA.
DR   EMBL; AP007151; BAE56461.1; -; Genomic_DNA.
DR   RefSeq; XP_001818463.1; XM_001818411.1.
DR   AlphaFoldDB; Q2UPQ4; -.
DR   SMR; Q2UPQ4; -.
DR   STRING; 510516.Q2UPQ4; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   GlyCosmos; Q2UPQ4; 2 sites, No reported glycans.
DR   EnsemblFungi; BAE56461; BAE56461; AO090005001553.
DR   GeneID; 5990408; -.
DR   KEGG; aor:AO090005001553; -.
DR   VEuPathDB; FungiDB:AO090005001553; -.
DR   HOGENOM; CLU_029718_0_2_1; -.
DR   OMA; FRMERLI; -.
DR   OrthoDB; 1638835at2759; -.
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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR   PANTHER; PTHR34142:SF6; ENDO-BETA-1,4-GLUCANASE B; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..333
FT                   /note="Probable endo-beta-1,4-glucanase B"
FT                   /id="PRO_0000394057"
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        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        145
FT                   /note="G -> E (in Ref. 1; BAD72778)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   333 AA;  36958 MW;  EA1271CB19A55C7A CRC64;
     MKFRNLFFAA VAGSAVAAPL AKEQKKRDSV FQWIGANESG AEFGENNLPG VWGTDYIFPD
     VSAITTLIDK GMNIFRIQFK MERLVPDSMT GAYDEAYLQN LTTVVNAVTD AGVHAILDPH
     NYGRFNGEIM STPSDFQTFW KNLAGQFQSN SLVIFDTNNE YHDMDQELVL NLNQAAIDGI
     REAGATEQYI FVEGNSYTGA WTWTDVNDNM KNLEDPQDKI VYQMHQYLDS DGSGTSETCV
     SGTIGQERVT SATQWLKDNK KVGIIGEFAG GNNDQCKTAV KGMLDYLAEN TDVWKGALWW
     AAGPWWGDYM YSLEPPNGVA FTGMLDVLQA YLG
//