CEL6A_PODAN
ID CEL6A_PODAN Reviewed; 484 AA.
AC B2ABX7;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=1,4-beta-D-glucan cellobiohydrolase CEL6A {ECO:0000305};
DE EC=3.2.1.91 {ECO:0000269|PubMed:23645193};
DE AltName: Full=Beta-glucancellobiohydrolase CEL6A {ECO:0000305};
DE AltName: Full=Exocellobiohydrolase CEL6A {ECO:0000305};
DE AltName: Full=Exoglucanase CEL6A {ECO:0000305};
DE Flags: Precursor;
GN Name=CEL6A {ECO:0000303|PubMed:23645193}; OrderedLocusNames=Pa_0_1250;
GN ORFNames=PODANS_0_1250;
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=4.7 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 55 degrees Celsius.
CC {ECO:0000269|PubMed:23645193};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9C1S9}.
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; CU633446; CAP60942.1; -; Genomic_DNA.
DR EMBL; FO904937; CDP24957.1; -; Genomic_DNA.
DR RefSeq; XP_001903170.1; XM_001903135.1.
DR AlphaFoldDB; B2ABX7; -.
DR SMR; B2ABX7; -.
DR STRING; 5145.XP_001903170.1; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR CLAE; CBH6A_PODAN; -.
DR EnsemblFungi; CAP60942; CAP60942; PODANS_0_1250.
DR GeneID; 6187194; -.
DR KEGG; pan:PODANSg182; -.
DR VEuPathDB; FungiDB:PODANS_0_1250; -.
DR eggNOG; ENOG502QWHE; 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: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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..484
FT /note="1,4-beta-D-glucan cellobiohydrolase CEL6A"
FT /id="PRO_5001338834"
FT DOMAIN 26..62
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 68..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..230
FT /note="Substrate binding loop 1"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT REGION 431..469
FT /note="Substrate binding loop 2"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT ACT_SITE 260
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9,
FT ECO:0000255|PROSITE-ProRule:PRU10057"
FT ACT_SITE 439
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9,
FT ECO:0000255|PROSITE-ProRule:PRU10056"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 433
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT BINDING 437
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 34..51
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
FT DISULFID 45..61
FT /evidence="ECO:0000250|UniProtKB:Q9C1S9"
SQ SEQUENCE 484 AA; 51054 MW; DD57EDE0BEB4D3AD CRC64;
MAKRLLLTAA LAATTLAAPV IEERQNCGSV WSQCGGQGWT GATCCASGST CVAQNQWYSQ
CLPGSQVTTT AQAPSSTRTT TSSSSRPTSS SISTSAVNVP TTTTSAGASV TVPPGGGASS
TASYSGNPFL GVQQWANSYY SSEVHTLAIP SLTGPMATKA AAVAKVPSFQ WMDRNVTVDT
LFSGTLADIR AANRAGANPP YAGIFVVYDL PDRDCAAAAS NGEWAIADGG AAKYKAYIDR
IRHHLVQYSD IRTILVIEPD SLANMVTNMN VPKCQGAANT YKELTVYALK QLNLPNVAMY
LDAGHAGWLG WPANIGPAAE LFAGIYKDAG RPTSLRGLAT NVANYNGWSL SSAPSYTTPN
PNFDEKRFVQ AFSPLLTAAG FPAHFITDTG RSGKQPTGQL EWGHWCNAIG TGFGPRPTTD
TGLDIEDAFV WIKPGGECDG TSDTTAARYD HHCGFADALK PAPEAGQWFQ AYFEQLLTNA
NPPF
