ID K4MQD1_PENDI Unreviewed; 484 AA.
AC K4MQD1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
DE AltName: Full=Endo-beta-1,4-mannanase F {ECO:0000256|ARBA:ARBA00033295};
OS Penicillium digitatum (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36651 {ECO:0000313|EMBL:AFV30215.1};
RN [1] {ECO:0000313|EMBL:AFV30215.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Pd01 {ECO:0000313|EMBL:AFV30215.1};
RA Cotter K.A., Callard G.V.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has endoglucanase activity on substrates containing beta-1,4
CC glycosidic bonds, like in carboxymethylcellulose (CMC),
CC hydroxyethylcellulose (HEC) and beta-glucan. Involved in the
CC degradation of complex natural cellulosic substrates.
CC {ECO:0000256|ARBA:ARBA00025192}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000966};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JX495172; AFV30215.1; -; mRNA.
DR AlphaFoldDB; K4MQD1; -.
DR OMA; YTDNKLM; -.
DR PhylomeDB; K4MQD1; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..484
FT /note="cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003880828"
FT DOMAIN 447..483
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 484 AA; 51668 MW; 8E5E4677165EAE0C CRC64;
MKFTNIVLAA SAASVACAYP RDRNVVPSKQ SAEIKKRAAN GFTWVGVSES GAEFGSNIPG
TLGQDYAWPK TSQIQILRDA GMNIFRVPFL MERLVPTSIT GAPDATYLAD LKSTIKFITD
SGAYAVLDPH NYGRYHGNII SSTSDFKAFW TTVATEFASN EKVIFDTNNE YHDLDQTLVL
DLNQAAIDAI RAAGATSQYI FVEGNAWTGA WSWTDHNDNL KALTDSEDKI VYEMHQYLDG
DSSGTSESCA SPTIGKERLQ SATAWLQENN KRGFIGEFAG GVNADCQAAV EGMLAYMSEN
SDVWMGAEWW SAGPMWGSYM YNLEPSNGPA YASYLPILEK YFVDSVASII SPSSSSSSGS
KAAAKPSTTA AGVEITSIPS SNVQAFSSVI EPSSATVSAS AEVSVAVAPV VSSATTAAPT
TLVTVTATAK PHTAKPSNAK PYTAKPYTAK PFTQCGGINW TGPTVCEAGT TCVKQNPFYY
QCVN
//
