CBHB_NEOFI
ID CBHB_NEOFI Reviewed; 530 AA.
AC A1DNL0;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=NFIA_057300;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027698; EAW16381.1; -; Genomic_DNA.
DR RefSeq; XP_001258278.1; XM_001258277.1.
DR AlphaFoldDB; A1DNL0; -.
DR SMR; A1DNL0; -.
DR STRING; 36630.CADNFIAP00004294; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH7; Glycoside Hydrolase Family 7.
DR EnsemblFungi; EAW16381; EAW16381; NFIA_057300.
DR GeneID; 4584793; -.
DR KEGG; nfi:NFIA_057300; -.
DR VEuPathDB; FungiDB:NFIA_057300; -.
DR eggNOG; ENOG502QPHV; Eukaryota.
DR HOGENOM; CLU_020817_3_2_1; -.
DR OMA; VYSNIKV; -.
DR OrthoDB; 875234at2759; -.
DR Proteomes; UP000006702; 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..530
FT /note="Probable 1,4-beta-D-glucan cellobiohydrolase B"
FT /id="PRO_0000393551"
FT DOMAIN 494..530
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 27..461
FT /note="Catalytic"
FT REGION 462..494
FT /note="Ser/Thr-rich linker"
FT REGION 462..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 502..519
FT /evidence="ECO:0000250"
FT DISULFID 513..529
FT /evidence="ECO:0000250"
SQ SEQUENCE 530 AA; 56046 MW; 0CEA2686BA4F4539 CRC64;
MLASTFSYRM YKTALILAAL LGSGQAQQVG TSQAEVHPSM TWQSCTAGGS CTTNNGKVVI
DANWRWVHKV GDYTNCYTGN TWDKTLCPDD ATCASNCALE GANYQSTYGA TTSGDSLRLN
FVTTSQQKNI GSRLYMMKDD TTYEMFKLLN QEFTFDVDVS NLPCGLNGAL YFVAMDADGG
MSKYPTNKAG AKYGTGYCDS QCPRDLKFIN GQANVEGWQP SSNDANAGTG NHGSCCAEMD
IWEANSISTA FTPHPCDTPG QVMCTGDACG GTYSSDRYGG TCDPDGCDFN SFRQGNKTFY
GPGMTVDTKS KFTVVTQFIT DDGTASGTLK EIKRFYVQNG KVIPNSESTW SGVGGNSITN
DYCTAQKSLF KDQNVFAKHG GMEGMGAALA QGMVLVMSLW DDHAANMLWL DSNYPTTASS
STPGVARGTC DISSGVPADV EANHPDASVV YSNIKVGPIG STFNSGGSNP GGGTTTTAKP
TTTTTTAGSP GGTGVAQHYG QCGGNGWQGP TTCASPYTCQ KLNDFYSQCL
