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 24-JAN-2024, entry version 73. 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 / RC SRRC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EQ963474; EED54935.1; -; Genomic_DNA. DR RefSeq; XP_002376207.1; XM_002376166.1. DR AlphaFoldDB; B8N7G5; -. DR SMR; B8N7G5; -. DR STRING; 332952.B8N7G5; -. DR GlyCosmos; B8N7G5; 2 sites, No reported glycans. DR EnsemblFungi; EED54935; EED54935; AFLA_021870. DR VEuPathDB; FungiDB:AFLA_002665; -. DR eggNOG; ENOG502QPHV; Eukaryota. DR HOGENOM; CLU_020817_3_2_1; -. DR OMA; NTYQMFQ; -. DR OrthoDB; 3014058at2759; -. 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; 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..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 //