ID   EGLB_ASPFN              Reviewed;         333 AA.
AC   B8MW97;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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; ORFNames=AFLA_087870;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963472; EED58088.1; -; Genomic_DNA.
DR   RefSeq; XP_002373700.1; XM_002373659.1.
DR   AlphaFoldDB; B8MW97; -.
DR   SMR; B8MW97; -.
DR   STRING; 5059.CADAFLAP00001565; -.
DR   EnsemblFungi; EED58088; EED58088; AFLA_087870.
DR   VEuPathDB; FungiDB:AFLA_087870; -.
DR   eggNOG; ENOG502QXN4; Eukaryota.
DR   HOGENOM; CLU_029718_0_2_1; -.
DR   OMA; GVNDDCK; -.
DR   Proteomes; UP000001875; 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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..333
FT                   /note="probable endo-beta-1,4-glucanase B"
FT                   /id="PRO_0000394055"
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"
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