CBHC_ASPFC
ID CBHC_ASPFC Reviewed; 454 AA.
AC B0XWL3;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Probable 1,4-beta-D-glucan cellobiohydrolase C;
DE EC=3.2.1.91;
DE AltName: Full=Beta-glucancellobiohydrolase C;
DE AltName: Full=Exocellobiohydrolase C;
DE AltName: Full=Exoglucanase C;
DE Flags: Precursor;
GN Name=cbhC; ORFNames=AFUB_046510;
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: The biological conversion of cellulose to glucose generally
CC requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC cut the disaccharide cellobiose from the non-reducing end of the
CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC cellobiose and other short cello-oligosaccharides to glucose.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC and cellotetraose, releasing cellobiose from the non-reducing ends of
CC the chains.; EC=3.2.1.91;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DOMAIN: Has a modular structure: a carbohydrate-binding module (CBM) at
CC the N-terminus, a linker rich in threonines, and a C-terminal
CC exocellobiohydrolase catalytic module. The genes for catalytic modules
CC and CBMs seem to have evolved separately and have been linked by gene
CC fusion.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
CC {ECO:0000305}.
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DR EMBL; DS499596; EDP53472.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XWL3; -.
DR SMR; B0XWL3; -.
DR EnsemblFungi; EDP53472; EDP53472; AFUB_046510.
DR VEuPathDB; FungiDB:AFUB_046510; -.
DR HOGENOM; CLU_015488_0_0_1; -.
DR PhylomeDB; B0XWL3; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase 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 Gene3D; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51989; SSF51989; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..454
FT /note="Probable 1,4-beta-D-glucan cellobiohydrolase C"
FT /id="PRO_0000394050"
FT DOMAIN 20..55
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 59..94
FT /note="Thr-rich linker"
FT REGION 68..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..454
FT /note="Thr-rich linker"
FT ACT_SITE 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT ACT_SITE 230
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT ACT_SITE 409
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..44
FT /evidence="ECO:0000250"
FT DISULFID 38..54
FT /evidence="ECO:0000250"
FT DISULFID 185..244
FT /evidence="ECO:0000250"
FT DISULFID 376..423
FT /evidence="ECO:0000250"
SQ SEQUENCE 454 AA; 47796 MW; 9EFFB0212288A576 CRC64;
MKHLASSIAL TLLLPAVQAQ QTVWGQCGGQ GWSGPTSCVA GAACSTLNPY YAQCIPGATA
TSTTLTTTTA ATTTSQTTTK PTTTGPTTSA PTVTASGNPF SGYQLYANPY YSSEVHTLAM
PSLPSSLQPK ASAVAEVPSF VWLDVAAKVP TMGTYLADIQ AKNKAGANPP IAGIFVVYDL
PDRDCAALAS NGEYSIANNG VANYKAYIDA IRAQLVKYSD VHTILVIEPD SLANLVTNLN
VAKCANAQSA YLECVDYALK QLNLPNVAMY LDAGHAGWLG WPANLGPAAT LFAKVYTDAG
SPAAVRGLAT NVANYNAWSL STCPSYTQGD PNCDEKKYIN AMAPLLKEAG FDAHFIMDTS
RNGVQPTKQN AWGDWCNVIG TGFGVRPSTN TGDPLQDAFV WIKPGGESDG TSNSTSPRYD
AHCGYSDALQ PAPEAGTWFQ AYFEQLLTNA NPSF
