CEL6B_PODAN
ID CEL6B_PODAN Reviewed; 419 AA.
AC B2AC20;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=1,4-beta-D-glucan cellobiohydrolase CEL6B {ECO:0000305};
DE EC=3.2.1.91 {ECO:0000269|PubMed:23645193};
DE AltName: Full=Beta-glucancellobiohydrolase CEL6B {ECO:0000305};
DE AltName: Full=Exocellobiohydrolase CEL6B {ECO:0000305};
DE AltName: Full=Exoglucanase CEL6B {ECO:0000305};
DE Flags: Precursor;
GN Name=CEL6B {ECO:0000303|PubMed:23645193}; OrderedLocusNames=Pa_2_13800;
GN ORFNames=PODANS_2_13800;
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=43 uM for cellotetraose {ECO:0000269|PubMed:23645193};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:23645193};
CC Temperature dependence:
CC Optimum temperature is 45 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; CU633447; CAP60981.1; -; Genomic_DNA.
DR EMBL; FO904937; CDP26446.1; -; Genomic_DNA.
DR RefSeq; XP_001903209.1; XM_001903174.1.
DR AlphaFoldDB; B2AC20; -.
DR SMR; B2AC20; -.
DR STRING; 5145.XP_001903209.1; -.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR CLAE; EGL6B_PODAN; -.
DR EnsemblFungi; CAP60981; CAP60981; PODANS_2_13800.
DR GeneID; 6187311; -.
DR KEGG; pan:PODANSg221; -.
DR VEuPathDB; FungiDB:PODANS_2_13800; -.
DR eggNOG; ENOG502SATK; Eukaryota.
DR HOGENOM; CLU_015488_0_0_1; -.
DR OrthoDB; 957754at2759; -.
DR Proteomes; UP000001197; Chromosome 2.
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; 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..47
FT /evidence="ECO:0000255"
FT CHAIN 48..419
FT /note="1,4-beta-D-glucan cellobiohydrolase CEL6B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432650"
FT ACT_SITE 152
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 419 AA; 45948 MW; E6F1D2D56EBFEF5B CRC64;
MGESFLLLQP ASPALSPTPS SLLLGPTITM RADVLIAALA TGALVAAVPT SPKKPTPPKG
DVSNPFVGKT QFVNPEWSNK LTQTYKSFLK KGDVKNAFRT LQAQKVSTFV WVSRLSELSR
IDEAIATARR VQKTTGKKQI VGLVLYNLPD RDCSAGESAG ELLSGENGFE RYKEEFVKPY
AQKVAAAKDL EFAIVLEPDS LGNLVTNLNI PLCAGAVDTY RDGIAHAITQ LQQDHVHLYI
DAAHGGWLGW NDNLPLAADE FAEVLKRADE ASGKKNKIRG FATNVSNYNP LHAVVRENYT
EWSNSWDESH YASSLAPHLE ERGLPAHFIV DQGRVANPGA RKEWGEWCNV APSGFGPAPS
TNTNNTVVDA IVWIKPGGES DGECGYFNAP RAGHWHDEFA QQLVQNAHPS VYENWWKFW
