CBHC_NEOFI
ID CBHC_NEOFI Reviewed; 450 AA.
AC A1DJQ7;
DT 18-MAY-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 C;
DE EC=3.2.1.91;
DE AltName: Full=Beta-glucancellobiohydrolase C;
DE AltName: Full=Exocellobiohydrolase C;
DE AltName: Full=Exoglucanase C;
DE Flags: Precursor;
GN Name=cbhC; ORFNames=NFIA_002990;
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:0000250}.
CC -!- DOMAIN: Has a modular structure: a carbohydrate-binding module (CBM) at
CC the N-terminus, a linker rich in threonines, and a C-terminal
CC exocellobiohydrolase catalytic module. The genes for catalytic modules
CC and CBMs seem to have evolved separately and have been linked by gene
CC fusion.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
CC {ECO:0000305}.
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DR EMBL; DS027697; EAW16946.1; -; Genomic_DNA.
DR RefSeq; XP_001258843.1; XM_001258842.1.
DR AlphaFoldDB; A1DJQ7; -.
DR SMR; A1DJQ7; -.
DR STRING; 36630.CADNFIAP00000041; -.
DR EnsemblFungi; EAW16946; EAW16946; NFIA_002990.
DR GeneID; 4585216; -.
DR KEGG; nfi:NFIA_002990; -.
DR VEuPathDB; FungiDB:NFIA_002990; -.
DR eggNOG; ENOG502QWHE; Eukaryota.
DR HOGENOM; CLU_015488_0_0_1; -.
DR OMA; NTPQAYW; -.
DR OrthoDB; 957754at2759; -.
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 Gene3D; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51989; SSF51989; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..450
FT /note="Probable 1,4-beta-D-glucan cellobiohydrolase C"
FT /id="PRO_0000394054"
FT DOMAIN 20..55
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 59..90
FT /note="Thr-rich linker"
FT REGION 63..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..450
FT /note="Catalytic"
FT ACT_SITE 180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT ACT_SITE 226
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT ACT_SITE 405
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..44
FT /evidence="ECO:0000250"
FT DISULFID 38..54
FT /evidence="ECO:0000250"
FT DISULFID 181..240
FT /evidence="ECO:0000250"
FT DISULFID 372..419
FT /evidence="ECO:0000250"
SQ SEQUENCE 450 AA; 47383 MW; 591EB3C96C03AB8A CRC64;
MKHLASSIAL TLLLPAVQAQ QTVWGQCGGQ GWSGPTNCVA GAACSTLNPY YAQCIPGATA
TSTTLSTTTT TQTTTKPTTT GPTTSAPTVT ASGNPFSGYQ LYANPYYSSE VHTLAMPSLP
SSLQPKASAV AEVPSFVWLD VAAKVPTMGT YLADIQAKNK AGASPPIAGI FVVYDLPDRD
CAALASNGEY SIANNGVANY KAYIDAIRAQ LVKYSDVHTI LVIEPDSLAN LVTNLNVAKC
ANAQSAYLEC VDYALKQLNL PNVAMYLDAG HAGWLGWPAN LGPAATLFAK VYTDAGSPAA
LRGLATNVAN YNAWSLSTCP SYTQGDPNCD EKKYINAMAP LLKNAGFDAH FIMDTSRNGV
QPTKQSAWGD WCNVIGTGFG VRPSTNTGDP LQDAFVWIKP GGESDGTSNS SSARYDAHCG
YSDALQPAPE AGTWFQAYFE QLLTNANPSF
