ID   CBHA_ASPOR              Reviewed;         455 AA.
AC   Q2UBM3; Q8NK81;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   08-NOV-2023, entry version 88.
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=AO090012000941;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kitamoto N., Yoshino-Yasuda S.;
RT   "Molecular cloning of two cellobiohydrolases from Aspergillus oryzae
RT   KBN616.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC07256.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB089437; BAC07256.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP007161; BAE61042.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UBM3; -.
DR   SMR; Q2UBM3; -.
DR   STRING; 510516.Q2UBM3; -.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   GlyCosmos; Q2UBM3; 2 sites, No reported glycans.
DR   EnsemblFungi; BAE61042; BAE61042; AO090012000941.
DR   VEuPathDB; FungiDB:AO090012000941; -.
DR   HOGENOM; CLU_020817_3_2_1; -.
DR   OMA; NTYQMFQ; -.
DR   OrthoDB; 3014058at2759; -.
DR   Proteomes; UP000006564; Chromosome 4.
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; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..455
FT                   /note="Probable 1,4-beta-D-glucan cellobiohydrolase A"
FT                   /id="PRO_0000393542"
FT   ACT_SITE        227
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        232
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        227
FT                   /note="E -> Q (in Ref. 1; BAC07256)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   455 AA;  48135 MW;  BE240033EABD0ADB CRC64;
     MHQRALLFSA FWTAVQAQQA GTLTAETHPS LTWQKCAAGG TCTEQKGSVV LDSNWRWLHS
     VDGSTNCYTG NTWDATLCPD NESCASNCAL DGADYEGTYG VTTSGDALTL QFVTGANIGS
     RLYLMADDDE SYQTFNLLNN EFTFDVDASK LPCGLNGAVY FVSMDADGGV AKYSTNKAGA
     KYGTGYCDSQ CPRDLKFING QANVEGWEPS DSDKNAGVGG HGSCCPEMDI WEANSISTAY
     TPHPCDDTAQ TMCEGDTCGG TYSSERYAGT CDPDGCDFNA YRMGNESFYG PSKLVDSSSP
     VTVVTQFITA DGTDSGALSE IKRFYVQGGK VIANAASNVD GVTGNSITAD FCTAQKKAFG
     DDDIFAQHGG LQGMGNALSS MVLTLSIWDD HHSSMMWLDS SYPEDADATA PGVARGTCEP
     HAGDPEKVES QSGSATVTYS NIKYGPIGST FDAPA
//