CELB_ASPCL
ID CELB_ASPCL Reviewed; 418 AA.
AC A1CG87;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=ACLA_066030;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027053; EAW10967.1; -; Genomic_DNA.
DR RefSeq; XP_001272393.1; XM_001272392.1.
DR AlphaFoldDB; A1CG87; -.
DR SMR; A1CG87; -.
DR STRING; 5057.CADACLAP00006191; -.
DR EnsemblFungi; EAW10967; EAW10967; ACLA_066030.
DR GeneID; 4704573; -.
DR KEGG; act:ACLA_066030; -.
DR VEuPathDB; FungiDB:ACLA_066030; -.
DR eggNOG; ENOG502SJT6; Eukaryota.
DR HOGENOM; CLU_020817_0_1_1; -.
DR OMA; NEMDIFE; -.
DR OrthoDB; 875234at2759; -.
DR Proteomes; UP000006701; 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; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..418
FT /note="Probable endo-beta-1,4-glucanase celB"
FT /id="PRO_0000395153"
FT ACT_SITE 215
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 418 AA; 44827 MW; C9607BB9C58EC80B CRC64;
MVRTFAVTAL ALLPLVAAQQ IGSTKEVHPQ LTTYKCTSQG GCVKQNTSIV LDSGSHWIHA
KGGEVSCTTS SGLDPALCPD KETCAENCVV EGITDYSQYG VQTRGDAMLL REYIKQNNQT
KAPSPRVYLL DEDGENYSML RLLNQEFTFD VDVSKLPCGM NGALYFSEMS ASGGRSALNP
AGAAYGTGYC DAQCYTNAWI NGEANTAKAG LCCQEMDIWE ANARANAFTP HPCNSTGLLG
CAGDECNSVC DKAGCGFNPY ALGARDYYGT AMTVDTTKPF TVVTQFLTAD NSTTGALREI
RRLYVQAGQV IQNAVVKVDG RTVNSITEPY CASQGVFEGL GGLRRMGEAL GRGMVLSMSI
WNDAGGFMHW LDSGNSGPCS STEGDPSLIE NKYPDTAVTF SKIRWGDLGT TFATRRLH