ID   CBHA_ASPFC              Reviewed;         452 AA.
AC   B0Y793;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-MAY-2023, entry version 58.
DE   RecName: Full=Probable 1,4-beta-D-glucan cellobiohydrolase A;
DE            EC=3.2.1.91;
DE   AltName: Full=Beta-glucancellobiohydrolase A;
DE   AltName: Full=Cellobiohydrolase D;
DE   AltName: Full=Exocellobiohydrolase A;
DE   AltName: Full=Exoglucanase A;
DE   Flags: Precursor;
GN   Name=cbhA; Synonyms=celD; ORFNames=AFUB_073010;
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
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=CBS 144.89 / FGSC A1163 / CEA10;
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:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
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DR   EMBL; DS499599; EDP49274.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y793; -.
DR   SMR; B0Y793; -.
DR   GlyCosmos; B0Y793; 2 sites, No reported glycans.
DR   EnsemblFungi; EDP49274; EDP49274; AFUB_073010.
DR   VEuPathDB; FungiDB:AFUB_073010; -.
DR   HOGENOM; CLU_020817_3_2_1; -.
DR   PhylomeDB; B0Y793; -.
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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753:SF6; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE A-RELATED; 1.
DR   PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..452
FT                   /note="Probable 1,4-beta-D-glucan cellobiohydrolase A"
FT                   /id="PRO_0000393539"
FT   REGION          405..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        226
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        231
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   452 AA;  48135 MW;  B62A9D4115A45295 CRC64;
     MHQRALLFSA LAVAANAQQV GTQTPETHPP LTWQKCTAAG SCSQQSGSVV IDANWRWLHS
     TKDTTNCYTG NTWNTELCPD NESCAQNCAL DGADYAGTYG VTTSGSELKL SFVTGANVGS
     RLYLMQDDET YQHFNLLNHE FTFDVDVSNL PCGLNGALYF VAMDADGGMS KYPSNKAGAK
     YGTGYCDSQC PRDLKFINGM ANVEGWEPSS SDKNAGVGGH GSCCPEMDIW EANSISTAVT
     PHPCDDVSQT MCSGDACGGT YSESRYAGTC DPDGCDFNPF RMGNESFYGP GKIVDTKSKM
     TVVTQFITAD GTDSGALSEI KRLYVQNGKV IANSVSNVAG VSGNSITSDF CTAQKKAFGD
     EDIFAKHGGL SGMGKALSEM VLIMSIWDDH HSSMMWLDST YPTDADPSKP GVARGTCEHG
     AGDPENVESQ HPDASVTFSN IKFGPIGSTY EG
//