CBHC_ASPTN
ID CBHC_ASPTN Reviewed; 468 AA.
AC Q0CFP1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 65.
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=ATEG_07493;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476604; EAU31755.1; -; Genomic_DNA.
DR RefSeq; XP_001216114.1; XM_001216114.1.
DR AlphaFoldDB; Q0CFP1; -.
DR SMR; Q0CFP1; -.
DR STRING; 341663.Q0CFP1; -.
DR EnsemblFungi; EAU31755; EAU31755; ATEG_07493.
DR GeneID; 4322742; -.
DR VEuPathDB; FungiDB:ATEG_07493; -.
DR eggNOG; ENOG502QWHE; Eukaryota.
DR HOGENOM; CLU_015488_0_0_1; -.
DR OMA; NTPQAYW; -.
DR OrthoDB; 957754at2759; -.
DR Proteomes; UP000007963; 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 Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..468
FT /note="Probable 1,4-beta-D-glucan cellobiohydrolase C"
FT /id="PRO_0000394052"
FT DOMAIN 19..54
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 57..106
FT /note="Thr-rich linker"
FT REGION 68..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..468
FT /note="Catalytic"
FT ACT_SITE 198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT ACT_SITE 244
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT ACT_SITE 423
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT DISULFID 26..43
FT /evidence="ECO:0000250"
FT DISULFID 37..53
FT /evidence="ECO:0000250"
FT DISULFID 199..258
FT /evidence="ECO:0000250"
FT DISULFID 390..437
FT /evidence="ECO:0000250"
SQ SEQUENCE 468 AA; 48846 MW; 8FA36060121BF2AB CRC64;
MGRVSSLALA LLLPAVQAQQ TLWGQCGGIG WTGPTNCVAG AACSTQNPYY AQCLPGTATT
STTLTTTTRV TTTTTSTTSK SSSTGSTTTT KSTGTTTTSG SSTTITSAPS GNPFSGYQLY
ANPYYSSEVH TLAMPSLASS LLPAASAAAK VPSFTWLDTA AKVPTMGTYL ADIKAKNAAG
ANPPIAAQFV VYDLPDRDCA ALASNGEYSI ANGGVANYKK YIDAIRAQLL NYPDVHTILV
IEPDSLANLV TNLNVAKCAN AQSAYLECVN YALIQLNLPN VAMYIDAGHA GWLGWPANIG
PAAQLFAGVY KDAGAPAALR GLATNVANYN AFSISTCPSY TSGDANCDEN RYINAIAPLL
KDQGWDAHFI VDTGRNGVQP TKQNAWGDWC NVIGTGFGVR PTTNTGNSLV DAFVWVKPGG
ESDGTSDSSS ARYDAHCGYS DALQPAPEAG TWFQAYFEQL LKNANPAF
