CBHB_ASPCL
ID CBHB_ASPCL Reviewed; 539 AA.
AC A1CU44;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Probable 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; ORFNames=ACLA_085260;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR EMBL; DS027060; EAW06831.1; -; Genomic_DNA.
DR RefSeq; XP_001268257.1; XM_001268256.1.
DR AlphaFoldDB; A1CU44; -.
DR SMR; A1CU44; -.
DR STRING; 5057.CADACLAP00007326; -.
DR EnsemblFungi; EAW06831; EAW06831; ACLA_085260.
DR GeneID; 4699868; -.
DR KEGG; act:ACLA_085260; -.
DR VEuPathDB; FungiDB:ACLA_085260; -.
DR eggNOG; ENOG502QPHV; Eukaryota.
DR HOGENOM; CLU_020817_3_2_1; -.
DR OMA; VYSNIKV; -.
DR OrthoDB; 875234at2759; -.
DR Proteomes; UP000006701; 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: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 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..539
FT /note="Probable 1,4-beta-D-glucan cellobiohydrolase B"
FT /id="PRO_0000393546"
FT DOMAIN 503..539
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 27..461
FT /note="Catalytic"
FT REGION 462..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..503
FT /note="Thr-rich linker"
FT ACT_SITE 238
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 243
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 511..528
FT /evidence="ECO:0000250"
FT DISULFID 522..538
FT /evidence="ECO:0000250"
SQ SEQUENCE 539 AA; 57042 MW; 27D7BD8E58C17687 CRC64;
MLPSTISYRI YKNALFFAAL FGAVQAQKVG TSKAEVHPSM AWQTCAADGT CTTKNGKVVI
DANWRWVHDV KGYTNCYTGN TWNAELCPDN ESCAENCALE GADYAATYGA TTSGNALSLK
FVTQSQQKNI GSRLYMMKDD NTYETFKLLN QEFTFDVDVS NLPCGLNGAL YFVSMDADGG
LSRYTGNEAG AKYGTGYCDS QCPRDLKFIN GLANVEGWTP SSSDANAGNG GHGSCCAEMD
IWEANSISTA YTPHPCDTPG QAMCNGDSCG GTYSSDRYGG TCDPDGCDFN SYRQGNKSFY
GPGMTVDTKK KMTVVTQFLT NDGTATGTLS EIKRFYVQDG KVIANSESTW PNLGGNSLTN
DFCKAQKTVF GDMDTFSKHG GMEGMGAALA EGMVLVMSLW DDHNSNMLWL DSNSPTTGTS
TTPGVARGSC DISSGDPKDL EANHPDASVV YSNIKVGPIG STFNSGGSNP GGSTTTTKPA
TSTTTTKATT TATTNTTGPT GTGVAQPWAQ CGGIGYSGPT QCAAPYTCTK QNDYYSQCL
