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CELB_ASPFC
ID   CELB_ASPFC              Reviewed;         407 AA.
AC   B0YBX0;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Probable endo-beta-1,4-glucanase celB;
DE            Short=Endoglucanase celB;
DE            EC=3.2.1.4;
DE   AltName: Full=Carboxymethylcellulase celB;
DE   AltName: Full=Cellulase B;
DE   Flags: Precursor;
GN   Name=celB; ORFNames=AFUB_088110;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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 7 (cellulase C) family.
CC       {ECO:0000305}.
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DR   EMBL; DS499601; EDP48101.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0YBX0; -.
DR   SMR; B0YBX0; -.
DR   EnsemblFungi; EDP48101; EDP48101; AFUB_088110.
DR   VEuPathDB; FungiDB:AFUB_088110; -.
DR   HOGENOM; CLU_020817_0_1_1; -.
DR   PhylomeDB; B0YBX0; -.
DR   Proteomes; UP000001699; 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   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; PTHR33753; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SUPFAM; SSF49899; SSF49899; 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..407
FT                   /note="Probable endo-beta-1,4-glucanase celB"
FT                   /id="PRO_0000395154"
FT   ACT_SITE        216
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        221
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   407 AA;  43448 MW;  133126CA3F0BAE75 CRC64;
     MAQTLAAASL VLVPLVTAQQ IGSIAENHPE LKTYRCGSQA GCVAQSTSVV LDINAHWIHQ
     MGAQTSCTTS SGLDPSLCPD KVTCSQNCVV EGITDYSSFG VQNSGDAITL RQYQVQNGQI
     KTLRPRVYLL AEDGINYSKL QLLNQEFTFD VDASKLPCGM NGALYLSEMD ASGGRSALNP
     AGATYGTGYC DAQCFNPGPW INGEANTLGA GACCQEMDLW EANSRSTIFS PHPCTTAGLY
     ACTGAECYSI CDGYGCTYNP YELGAKDYYG YGLTVDTAKP ITVVMQFVTA DNTATGTLAE
     IRRLYVQEGM VIGNSAVAMT EAFCSSSRTF EALGGLQRMG EALGRGMVPV FSIWDDPSLW
     MHWLDSDGAG PCGSTEGDPA FIQANYPNTA VTFSKVRWGD IDSTYSV
 
 
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