ID   CBHB_ASPAC              Reviewed;         540 AA.
AC   O59843;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=1,4-beta-D-glucan cellobiohydrolase B;
DE            EC=3.2.1.91;
DE   AltName: Full=1,4-beta-D-glucan cellobiohydrolase I;
DE   AltName: Full=Beta-glucancellobiohydrolase B;
DE   AltName: Full=Exocellobiohydrolase B;
DE   AltName: Full=Exoglucanase B;
DE   Flags: Precursor;
GN   Name=cbhB; Synonyms=cbhI;
OS   Aspergillus aculeatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=F-50;
RX   DOI=10.1016/S0922-338X(97)80345-5;
RA   Takada G., Kawaguchi T., Sumitani J., Arai M.;
RT   "Cloning, nucleotide sequence, and transcriptional analysis of Aspergillus
RT   aculeatus No.F-50 cellobiohydrolase I (cbhI) gene.";
RL   J. Ferment. Bioeng. 85:1-9(1998).
RN   [2]
RP   FUNCTION.
RX   PubMed=16233469; DOI=10.1263/jbb.95.627;
RA   Kanamasa S., Mochizuki M., Takada G., Kawaguchi T., Sumitani J., Araii M.;
RT   "Overexpression of Aspergillus aculeatus cellobiohydrolase I in Aspergillus
RT   oryzae.";
RL   J. Biosci. Bioeng. 95:627-629(2003).
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:0000269|PubMed:16233469}.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
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DR   EMBL; AB002821; BAA25183.1; -; mRNA.
DR   AlphaFoldDB; O59843; -.
DR   SMR; O59843; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   CLAE; CBH7A_ASPAC; -.
DR   VEuPathDB; FungiDB:ASPACDRAFT_1901759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; -; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..540
FT                   /note="1,4-beta-D-glucan cellobiohydrolase B"
FT                   /id="PRO_0000007918"
FT   DOMAIN          505..540
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          23..459
FT                   /note="Catalytic"
FT   REGION          460..505
FT                   /note="Ser/Thr-rich linker"
FT   REGION          464..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        234
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        239
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        513..529
FT                   /evidence="ECO:0000250"
FT   DISULFID        524..539
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   540 AA;  57099 MW;  002D7FD28DF194D0 CRC64;
     MVDSFSIYKT ALLLSMLATS NAQQVGTYTA ETHPSLTWQT CSGSGSCTTT SGSVVIDANW
     RWVHEVGGYT NCYSGNTWDS SICSTDTTCA SECALEGATY ESTYGVTTSG SSLRLNFVTT
     ASQKNIGSRL YLLADDSTYE TFKLFNREFT FDVDVSNLPC GLNGALYFVS MDADGGVSRF
     PTNKAGAKYG TGYCDSQCPR DLKFIDGQAN IEGWEPSSTD VNAGTGNHGS CCPEMDIWEA
     NSISSAFTAH PCDSVQQTMC TGDTCGGTYS DTTDRYSGTC DPDGCDFNPY RFGNTNFYGP
     GKTVDNSKPF TVVTQFITHD GTDTGTLTEI RRLYVQNGVV IGNGPSTYTA ASGNSITESF
     CKAEKTLFGD TNVFETHGGL SAMGDALGDG MVLVLSLWDD HAADMLWLDS DYPTTSCASS
     PGVARGTCPT TTGNATYVEA NYPNSYVTYS NIKFGTLNST YSGTSSGGSS SSSTTLTTKA
     STSTTSSKTT TTTSKTSTTS SSSTNVAQLY GQCGGQGWTG PTTCASGTCT KQNDYYSQCL