ID CBHA_ASPNG Reviewed; 452 AA. AC Q9UVS9; C7ENW1; DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 86. DE RecName: Full=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; OS Aspergillus niger. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=5061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION. RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732; RX PubMed=10508057; DOI=10.1128/aem.65.10.4340-4345.1999; RA Gielkens M.M., Dekkers E., Visser J., de Graaff L.H.; RT "Two cellobiohydrolase-encoding genes from Aspergillus niger require D- RT xylose and the xylanolytic transcriptional activator XlnR for their RT expression."; RL Appl. Environ. Microbiol. 65:4340-4345(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BCRC 31494; RA Hsing-Ren W., Trong-Rong Y.; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION, AND INDUCTION. RX PubMed=15182839; DOI=10.1016/j.biortech.2003.12.013; RA Hanif A., Yasmeen A., Rajoka M.I.; RT "Induction, production, repression, and de-repression of exoglucanase RT synthesis in Aspergillus niger."; RL Bioresour. Technol. 94:311-319(2004). 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:0000269|PubMed:15182839}. 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 -!- INDUCTION: Expression is under the control of the xylanolytic CC transcriptional activator xlnR. {ECO:0000269|PubMed:10508057, CC ECO:0000269|PubMed:15182839}. 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; AF156268; AAF04491.1; -; Genomic_DNA. DR EMBL; GQ281319; ACT65727.1; -; Genomic_DNA. DR AlphaFoldDB; Q9UVS9; -. DR SMR; Q9UVS9; -. DR CAZy; GH7; Glycoside Hydrolase Family 7. DR CLAE; CBH7A_ASPNG; -. DR GlyCosmos; Q9UVS9; 5 sites, No reported glycans. DR PaxDb; 5061-CADANGAP00006086; -. DR VEuPathDB; FungiDB:An07g09330; -. DR VEuPathDB; FungiDB:ASPNIDRAFT2_1164625; -. DR VEuPathDB; FungiDB:ATCC64974_49900; -. DR VEuPathDB; FungiDB:M747DRAFT_326184; -. DR eggNOG; ENOG502QPHV; Eukaryota. DR OrthoDB; 3014058at2759; -. 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 2: Evidence at transcript level; 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="1,4-beta-D-glucan cellobiohydrolase A" FT /id="PRO_5000056394" 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 62 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 285 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 335 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 402 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 445 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 101 FT /note="V -> I (in Ref. 2; ACT65727)" FT /evidence="ECO:0000305" FT CONFLICT 170 FT /note="V -> A (in Ref. 2; ACT65727)" FT /evidence="ECO:0000305" FT CONFLICT 359 FT /note="E -> D (in Ref. 2; ACT65727)" FT /evidence="ECO:0000305" SQ SEQUENCE 452 AA; 48258 MW; 6364A0F4BF7D254F CRC64; MHQRALLFSA LLTAVRAQQA GTLTEEVHPS LTWQKCTSEG SCTEQSGSVV IDSNWRWTHS VNDSTNCYTG NTWDATLCPD DETCAANCAL DGADYESTYG VTTDGDSLTL KFVTGSNVGS RLYLMDTSDE GYQTFNLLDA EFTFDVDVSN LPCGLNGALY FTAMDADGGV SKYPANKAGA KYGTGYCDSQ CPRDLKFIDG QANVDGWEPS SNNDNTGIGN HGSCCPEMDI WEANKISTAL TPHPCDSSEQ TMCEGNDCGG TYSDDRYGGT CDPDGCDFNP YRMGNDSFYG PGKTIDTGSK MTVVTQFITD GSGSLSEIKR YYVQNGNVIA NADSNISGVT GNSITTDFCT AQKKAFGDED IFAEHNGLAG ISDAMSSMVL ILSLWDDYYA SMEWLDSDYP ENATATDPGV ARGTCDSESG VPATVEGAHP DSSVTFSNIK FGPINSTFSA SA //