CBHC_ASPNC
ID CBHC_ASPNC Reviewed; 459 AA.
AC A2QYR9;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=An12g02220;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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}.
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; AM270264; CAK41068.1; -; Genomic_DNA.
DR RefSeq; XP_001395308.1; XM_001395271.2.
DR AlphaFoldDB; A2QYR9; -.
DR SMR; A2QYR9; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR PaxDb; A2QYR9; -.
DR EnsemblFungi; CAK41068; CAK41068; An12g02220.
DR GeneID; 4985573; -.
DR KEGG; ang:ANI_1_300104; -.
DR VEuPathDB; FungiDB:An12g02220; -.
DR HOGENOM; CLU_015488_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 3L.
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;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..459
FT /note="Probable 1,4-beta-D-glucan cellobiohydrolase C"
FT /id="PRO_5000220698"
FT DOMAIN 19..54
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 54..94
FT /note="Thr-rich linker"
FT REGION 76..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..459
FT /note="Catalytic"
FT ACT_SITE 189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT ACT_SITE 414
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..43
FT /evidence="ECO:0000250"
FT DISULFID 37..53
FT /evidence="ECO:0000250"
FT DISULFID 190..249
FT /evidence="ECO:0000250"
FT DISULFID 381..428
FT /evidence="ECO:0000250"
SQ SEQUENCE 459 AA; 48126 MW; A584E983E58DCE87 CRC64;
MHYPLSLALA FLPFGIQAQQ TLWGQCGGQG YSGATSCVAG ATCATVNEYY AQCTPAAGTS
SATTLKTTTS STTAAVTTTT TTQSPTGSAS PTTTASASGN PFSGYQLYVN PYYSSEVASL
AIPSLTGSLS SLQAAATAAA KVPSFVWLDT AAKVPTMGDY LADIQSQNAA GANPPIAGQF
VVYDLPDRDC AALASNGEYS IADNGVEHYK SYIDSIREIL VQYSDVHTLL VIEPDSLANL
VTNLNVAKCA NAESAYLECT NYALTQLNLP NVAMYLDAGH AGWLGWPANQ QPAADLFASV
YKNASSPAAV RGLATNVANY NAWTISSCPS YTQGNSVCDE QQYINAIAPL LQAQGFDAHF
IVDTGRNGKQ PTGQQAWGDW CNVINTGFGE RPTTDTGDAL VDAFVWVKPG GESDGTSDSS
ATRYDAHCGY SDALQPAPEA GTWFQAYFVQ LLTNANPAF
