ID CBHB_ASPNG Reviewed; 536 AA. AC Q9UVS8; DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 93. DE RecName: Full=1,4-beta-D-glucan cellobiohydrolase B; DE EC=3.2.1.91; DE AltName: Full=Beta-glucancellobiohydrolase B; DE AltName: Full=Exocellobiohydrolase B; DE AltName: Full=Exoglucanase B; DE Flags: Precursor; GN Name=cbhB; 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 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:0000250, 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; AF156269; AAF04492.1; -; Genomic_DNA. DR AlphaFoldDB; Q9UVS8; -. DR SMR; Q9UVS8; -. DR CAZy; CBM1; Carbohydrate-Binding Module Family 1. DR CAZy; GH7; Glycoside Hydrolase Family 7. DR CLAE; CBH7B_ASPNG; -. DR GlyCosmos; Q9UVS8; 2 sites, No reported glycans. DR PaxDb; 5061-CADANGAP00001127; -. DR VEuPathDB; FungiDB:An01g11660; -. DR VEuPathDB; FungiDB:ASPNIDRAFT2_1117716; -. DR VEuPathDB; FungiDB:ATCC64974_14090; -. DR VEuPathDB; FungiDB:M747DRAFT_286038; -. DR eggNOG; ENOG502QPHV; Eukaryota. DR OrthoDB; 3014058at2759; -. DR BRENDA; 3.2.1.91; 518. 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:0030248; F:cellulose binding; IEA:InterPro. 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; IPR035971; CBD_sf. DR InterPro; IPR000254; Cellulose-bd_dom_fun. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR001722; Glyco_hydro_7. DR InterPro; IPR037019; Glyco_hydro_7_sf. DR PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1. DR PANTHER; PTHR33753:SF2; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1. DR Pfam; PF00734; CBM_1; 1. DR Pfam; PF00840; Glyco_hydro_7; 1. DR PRINTS; PR00734; GLHYDRLASE7. DR SMART; SM00236; fCBD; 1. DR SUPFAM; SSF57180; Cellulose-binding domain; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS00562; CBM1_1; 1. DR PROSITE; PS51164; CBM1_2; 1. PE 2: Evidence at transcript level; KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond; KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; KW Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..536 FT /note="1,4-beta-D-glucan cellobiohydrolase B" FT /id="PRO_5000056395" FT DOMAIN 500..536 FT /note="CBM1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597" FT REGION 22..458 FT /note="Catalytic" FT REGION 459..500 FT /note="Ser/Thr-rich linker" FT REGION 464..499 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 233 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 238 FT /note="Proton donor" FT /evidence="ECO:0000250" FT CARBOHYD 351 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 414 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 508..525 FT /evidence="ECO:0000250" FT DISULFID 519..535 FT /evidence="ECO:0000250" SQ SEQUENCE 536 AA; 56219 MW; EB904612E2FA3A60 CRC64; MSSFQIYRAA LLLSILATAN AQQVGTYTTE THPSLTWQTC TSDGSCTTND GEVVIDANWR WVHSTSSATN CYTGNEWDTS ICTDDVTCAA NCALDGATYE ATYGVTTSGS ELRLNFVTQG SSKNIGSRLY LMSDDSNYEL FKLLGQEFTF DVDVSNLPCG LNGALYFVAM DADGGTSEYS GNKAGAKYGT GYCDSQCPRD LKFINGEANC DGWEPSSNNV NTGVGDHGSC CAEMDVWEAN SISNAFTAHP CDSVSQTMCD GDSCGGTYSA SGDRYSGTCD PDGCDYNPYR LGNTDFYGPG LTVDTNSPFT VVTQFITDDG TSSGTLTEIK RLYVQNGEVI ANGASTYSSV NGSSITSAFC ESEKTLFGDE NVFDKHGGLE GMGEAMAKGM VLVLSLWDDY AADMLWLDSD YPVNSSASTP GVARGTCSTD SGVPATVEAE SPNAYVTYSN IKFGPIGSTY SSGSSSGSGS SSSSSSTTTK ATSTTLKTTS TTSSGSSSTS AAQAYGQCGG QGWTGPTTCV SGYTCTYENA YYSQCL //