CEL6C_PODAN
ID CEL6C_PODAN Reviewed; 398 AA.
AC B2AE04;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=1,4-beta-D-glucan cellobiohydrolase CEL6C {ECO:0000305};
DE EC=3.2.1.91 {ECO:0000269|PubMed:23645193};
DE AltName: Full=Beta-glucancellobiohydrolase CEL6C {ECO:0000305};
DE AltName: Full=Exocellobiohydrolase CEL6C {ECO:0000305};
DE AltName: Full=Exoglucanase CEL6C {ECO:0000305};
DE Flags: Precursor;
GN Name=CEL6C {ECO:0000303|PubMed:23645193}; OrderedLocusNames=Pa_4_2420;
GN ORFNames=PODANS_4_2420;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP GLYCOSYLATION.
RX PubMed=23645193; DOI=10.1128/aem.00327-13;
RA Poidevin L., Feliu J., Doan A., Berrin J.G., Bey M., Coutinho P.M.,
RA Henrissat B., Record E., Heiss-Blanquet S.;
RT "Insights into exo- and endoglucanase activities of family 6 glycoside
RT hydrolases from Podospora anserina.";
RL Appl. Environ. Microbiol. 79:4220-4229(2013).
CC -!- FUNCTION: Exoglucanase that plays an important function in biomass
CC degradation by catalyzing the hydrolysis of the non-reducing end beta-
CC 1,4-glucosidic linkages in cellulose and cellotetraose to release
CC cellobiose. Hydrolyzes crystalline and amorphous cellulose but is
CC inactive on hydroxyethyl cellulose, mannan, galactomannan, xyloglucan,
CC arabinoxylan, arabinan, xylan, and pectin.
CC {ECO:0000269|PubMed:23645193}.
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; Evidence={ECO:0000269|PubMed:23645193};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.59 uM for cellotetraose {ECO:0000269|PubMed:23645193};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:23645193};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:23645193};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- PTM: Both N- and O-glycosylated. {ECO:0000269|PubMed:23645193}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
CC {ECO:0000305}.
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DR EMBL; CU633455; CAP61669.1; -; Genomic_DNA.
DR EMBL; FO904939; CDP28020.1; -; Genomic_DNA.
DR RefSeq; XP_001903893.1; XM_001903858.1.
DR AlphaFoldDB; B2AE04; -.
DR SMR; B2AE04; -.
DR STRING; 5145.XP_001903893.1; -.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR CLAE; CBH6C_PODAN; -.
DR EnsemblFungi; CAP61669; CAP61669; PODANS_4_2420.
DR GeneID; 6188027; -.
DR KEGG; pan:PODANSg909; -.
DR VEuPathDB; FungiDB:PODANS_4_2420; -.
DR eggNOG; ENOG502QWHE; Eukaryota.
DR HOGENOM; CLU_015488_0_0_1; -.
DR OrthoDB; 957754at2759; -.
DR Proteomes; UP000001197; Chromosome 4.
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 Gene3D; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SUPFAM; SSF51989; SSF51989; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..398
FT /note="1,4-beta-D-glucan cellobiohydrolase CEL6C"
FT /id="PRO_5001338839"
FT ACT_SITE 125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT ACT_SITE 170
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 398 AA; 42570 MW; D1D8B3CABA06AB41 CRC64;
MKITSSAAAL ALVASAVAAP SPTTQDKPTK RQAGCASAVS LNAQTNVFKQ YTLHANNFYR
KEIEELAIPN LSDPSLEAAA RKVADTGSFV WLDTIANVDR LEPALAEVPC NEILGVVVYD
LPGRDCAAKA SNGELKVGEL NRYKTEFIDR IASILKAHPN TAVALVIEPD SLPNLVTNSD
VQACRNSAAG YRDGVAYALK TLNLPNVVQY IDAGHGGWLG WDANLKPGAE ELAKAYKAAG
SPKQFRGIAT NVAGWNAWDL SPGEFSSASD AKYNSCQNER TYVNTFGQRL KAAGMPNHAI
VDTGRNGVQG LREEWGNWCN VDGAGFGRPP SADTGLELAD AFVWVKPGGE SDGTSDSSAV
RYDSFCGKPD AFQPSPEAGA WHQEYFEMLL RNSNPSLL
