CBHB_ASPNG
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 25-MAY-2022, entry version 88.
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 STRING; 5061.CADANGAP00001127; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH7; Glycoside Hydrolase Family 7.
DR CLAE; CBH7B_ASPNG; -.
DR VEuPathDB; FungiDB:An01g11660; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1117716; -.
DR VEuPathDB; FungiDB:ATCC64974_14090; -.
DR VEuPathDB; FungiDB:M747DRAFT_286038; -.
DR eggNOG; ENOG502QPHV; Eukaryota.
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; -; 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; PTHR33753; 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; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 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
