CBHA_ASPOR
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 25-MAY-2022, entry version 83.
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 RefSeq; XP_001727881.2; XM_001727829.2.
DR AlphaFoldDB; Q2UBM3; -.
DR SMR; Q2UBM3; -.
DR STRING; 510516.Q2UBM3; -.
DR CAZy; GH7; Glycoside Hydrolase Family 7.
DR EnsemblFungi; BAE61042; BAE61042; AO090012000941.
DR GeneID; 5988355; -.
DR KEGG; aor:AO090012000941; -.
DR VEuPathDB; FungiDB:AO090012000941; -.
DR HOGENOM; CLU_020817_3_2_1; -.
DR OMA; ALTWSKC; -.
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; -; 1.
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; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SUPFAM; SSF49899; SSF49899; 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
