ID   EGLB_NEOFI              Reviewed;         329 AA.
AC   A1DME8;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=NFIA_053150;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027698; EAW15969.1; -; Genomic_DNA.
DR   RefSeq; XP_001257866.1; XM_001257865.1.
DR   AlphaFoldDB; A1DME8; -.
DR   SMR; A1DME8; -.
DR   STRING; 36630.CADNFIAP00005314; -.
DR   EnsemblFungi; EAW15969; EAW15969; NFIA_053150.
DR   GeneID; 4584381; -.
DR   KEGG; nfi:NFIA_053150; -.
DR   VEuPathDB; FungiDB:NFIA_053150; -.
DR   eggNOG; ENOG502QXN4; Eukaryota.
DR   HOGENOM; CLU_029718_0_2_1; -.
DR   OMA; NEPHDIK; -.
DR   OrthoDB; 722981at2759; -.
DR   Proteomes; UP000006702; 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; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..329
FT                   /note="Probable endo-beta-1,4-glucanase B"
FT                   /id="PRO_0000394059"
FT   ACT_SITE        156
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   329 AA;  35875 MW;  DFA67E1E6BFA5E3F CRC64;
     MKFGSIVLIA AAAGSAVAAP AKRASVFQWF GSNESGAEFG QNTIPGSYGK EFIFPDPSTI
     STLIGKGMNI FRVQFLMERL VPSSMTGSYN EEYLANLTSV VDAVTKAGSY AILDPHNFGR
     YNGQIISSTD DFKTFWQNLA GKFKSNNLVI FDTNNEYHDM DQALVLNLNQ AAINGIRAAG
     ATSQYIFVEG NSWSGAWTWV DVNDNLKALT DPQDKIVYEM HQYLDSDGSG TSESCVSTTI
     GKERVTAATK WLKDNGKVGI IGEFAGGVND QCRTAISGML EYLAQNTDVW KGALWWAAGP
     WWGNYMFNME PPSGAAYVGM LDILEPYLG