GUX3_AGABI
ID GUX3_AGABI Reviewed; 438 AA.
AC P49075;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Exoglucanase 3;
DE EC=3.2.1.91;
DE AltName: Full=1,4-beta-cellobiohydrolase 3;
DE AltName: Full=Exocellobiohydrolase 3;
DE Flags: Precursor;
GN Name=cel3;
OS Agaricus bisporus (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX NCBI_TaxID=5341;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 255-277 AND 331-351.
RC STRAIN=D649;
RX PubMed=8085821; DOI=10.1128/aem.60.8.2779-2785.1994;
RA Chow C.-M., Yague E., Raguz S., Wood D.A., Thurston C.F.;
RT "The cel3 gene of Agaricus bisporus codes for a modular cellulase and is
RT transcriptionally regulated by the carbon source.";
RL Appl. Environ. Microbiol. 60:2779-2785(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Mycelium;
RX PubMed=8662210; DOI=10.1007/s002940050100;
RA Yague E., Chow C.-M., Challen M.P., Thurston C.F.;
RT "Correlation of exons with functional domains and folding regions in a
RT cellulase from Agaricus bisporus.";
RL Curr. Genet. 30:56-61(1996).
CC -!- FUNCTION: Shows enzymatic activity towards crystalline cellulose. At
CC long reaction times. It is also able to degrade carboxymethyl cellulose
CC and barley B-glucan.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
CC {ECO:0000305}.
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DR EMBL; L24519; AAA50607.1; -; mRNA.
DR EMBL; L24520; AAA50608.1; -; mRNA.
DR EMBL; Z34007; CAA83971.1; -; Genomic_DNA.
DR PIR; S70602; S70602.
DR AlphaFoldDB; P49075; -.
DR SMR; P49075; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR CLAE; CBH6C_AGABI; -.
DR BioCyc; MetaCyc:MON-17626; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..438
FT /note="Exoglucanase 3"
FT /id="PRO_0000007902"
FT DOMAIN 21..59
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 57..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..87
FT /note="Linker"
FT REGION 88..438
FT /note="Catalytic"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT DISULFID 28..45
FT /evidence="ECO:0000250"
FT DISULFID 39..55
FT /evidence="ECO:0000250"
FT DISULFID 170..229
FT /evidence="ECO:0000250"
FT DISULFID 360..407
FT /evidence="ECO:0000250"
FT VARIANT 133
FT /note="V -> T"
FT VARIANT 152
FT /note="R -> Q"
FT VARIANT 244
FT /note="V -> I"
FT VARIANT 248
FT /note="N -> D"
FT VARIANT 398
FT /note="N -> S"
SQ SEQUENCE 438 AA; 46210 MW; 002C973544893794 CRC64;
MFKFAALLAL ASLVPGFVQA QSPVWGQCGG NGWTGPTTCA SGSTCVKQND FYSQCLPNNQ
APPSTTTQPG TTPPATTTSG GTGPTSGAGN PYTGKTVWLS PFYADEVAQA AADISNPSLA
TKAASVAKIP TFVWFDTVAK VPDLGGYLAD ARSKNQLVQI VVYDLPDRDC AALASNGEFS
LANDGLNKYK NYVDQIAAQI KQFPDVSVVA VIEPDSLANL VTNLNVQKCA NAQSAYKEGV
IYAVQKLNAV GVTMYIDAGH AGWLGWPANL SPAAQLFAQI YRDAGSPRNL RGIATNVANF
NALRASSPDP ITQGNSNYDE IHYIEALAPM LSNAGFPAHF IVDQGRSGVQ NIRDQWGDWC
NVKGAGFGQR PTTNTGSSLI DAIVWVKPGG ECDGTSDNSS PRFDSHCSLS DAHQPAPEAG
TWFQAYFETL VANANPAL
