CBHA_ASPNG
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 25-MAY-2022, entry version 81.
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}.
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DR EMBL; AF156268; AAF04491.1; -; Genomic_DNA.
DR EMBL; GQ281319; ACT65727.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UVS9; -.
DR SMR; Q9UVS9; -.
DR STRING; 5061.CADANGAP00006086; -.
DR CAZy; GH7; Glycoside Hydrolase Family 7.
DR CLAE; CBH7A_ASPNG; -.
DR VEuPathDB; FungiDB:An07g09330; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1164625; -.
DR VEuPathDB; FungiDB:ATCC64974_49900; -.
DR VEuPathDB; FungiDB:M747DRAFT_326184; -.
DR eggNOG; ENOG502QPHV; Eukaryota.
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 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
