EGLD_ASPFU
ID EGLD_ASPFU Reviewed; 349 AA.
AC Q4WBU0;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Probable endo-beta-1,4-glucanase D;
DE Short=Endoglucanase D;
DE EC=3.2.1.4;
DE AltName: Full=Carboxymethylcellulase D;
DE AltName: Full=Cellulase D;
DE Flags: Precursor;
GN Name=eglD; ORFNames=AFUA_8G06830;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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 -!- DOMAIN: Has a modular structure: an endo-beta-1,4-glucanase catalytic
CC module at the N-terminus, a linker rich in serines and threonines, and
CC a C-terminal carbohydrate-binding module (CBM). The genes for catalytic
CC modules and CBMs seem to have evolved separately and have been linked
CC by gene fusion.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAHF01000013; EAL85444.1; -; Genomic_DNA.
DR RefSeq; XP_747482.1; XM_742389.1.
DR AlphaFoldDB; Q4WBU0; -.
DR SMR; Q4WBU0; -.
DR EnsemblFungi; EAL85444; EAL85444; AFUA_8G06830.
DR GeneID; 3504710; -.
DR KEGG; afm:AFUA_8G06830; -.
DR VEuPathDB; FungiDB:Afu8g06830; -.
DR eggNOG; ENOG502RXMI; Eukaryota.
DR HOGENOM; CLU_031730_0_0_1; -.
DR InParanoid; Q4WBU0; -.
DR OMA; YIDSPPN; -.
DR OrthoDB; 1307231at2759; -.
DR Proteomes; UP000002530; Chromosome 8.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR005103; AA9.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR Pfam; PF03443; AA9; 1.
DR Pfam; PF00734; CBM_1; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..349
FT /note="Probable endo-beta-1,4-glucanase D"
FT /id="PRO_0000394063"
FT DOMAIN 311..347
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 20..235
FT /note="Catalytic"
FT REGION 233..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..307
FT /note="Ser/Thr-rich linker"
FT ACT_SITE 164
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 210
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 319..336
FT /evidence="ECO:0000250"
FT DISULFID 330..346
FT /evidence="ECO:0000250"
SQ SEQUENCE 349 AA; 35735 MW; 19776990098D76C9 CRC64;
MKSTFGLLAL AAAAKLVSAH ATVHAVWIND VDQGAGNSAD GYIRSPPNNS PITDVTSTDM
TCNVNGKNPV AKTLSVKAGD KVTFEWHHDT RSDSDDIIAS SHMGPVMVYM APTEKGTAGN
GWVKIAEEGY SNGKWAVANL IANRGKHSIT VPDVPAGEYL LRPEIIALHE GNRQGGAQFY
MECVQVKVTS AGTKTLPAGV SIPGAYKATD PGVLFDMYNS FTSYPIPGPA VWDGSSSGSS
GSSGSSPATT TAPAVSVTAA PTKEAPVDTS ATPTTFVTAT KPATTAAPAA PSASSGSNSG
SDSCNSGSAS GSVKIYGQCG GQNYSGPTSC EAGLICKEWN PYYHQCVSA
