CBHA_ASPFN
ID CBHA_ASPFN Reviewed; 455 AA.
AC B8N7G5;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=AFLA_021870;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963474; EED54935.1; -; Genomic_DNA.
DR RefSeq; XP_002376207.1; XM_002376166.1.
DR AlphaFoldDB; B8N7G5; -.
DR SMR; B8N7G5; -.
DR STRING; 5059.CADAFLAP00004072; -.
DR EnsemblFungi; EED54935; EED54935; AFLA_021870.
DR VEuPathDB; FungiDB:AFLA_021870; -.
DR eggNOG; ENOG502QPHV; Eukaryota.
DR HOGENOM; CLU_020817_3_2_1; -.
DR OMA; ALTWSKC; -.
DR Proteomes; UP000001875; 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; -; 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; Secreted; 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_0000393540"
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"
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