ID S8BGM3_PENO1 Unreviewed; 413 AA.
AC S8BGM3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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};
GN ORFNames=PDE_09226 {ECO:0000313|EMBL:EPS34262.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS34262.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS34262.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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}.
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DR EMBL; KB644415; EPS34262.1; -; Genomic_DNA.
DR AlphaFoldDB; S8BGM3; -.
DR SMR; S8BGM3; -.
DR STRING; 933388.S8BGM3; -.
DR eggNOG; ENOG502QXN4; Eukaryota.
DR HOGENOM; CLU_029718_0_2_1; -.
DR OrthoDB; 1638835at2759; -.
DR PhylomeDB; S8BGM3; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
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.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..413
FT /note="cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004548380"
FT DOMAIN 377..413
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 339..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 44001 MW; 8CAC4FDF378D12AD CRC64;
MRYDLILAAG ATLALAVPQG ISKRAGGFVW FGASESCGEF GETHLPGVLG TDYTWPDQSA
IKTLYDGGMN IFRVPFRMER LIPTSMTASP DAAYLQGLKS TVNYITSIGA HAIIDPHNYG
RYYGNIITST SDFKAFWTTV AKEFASNDKV IFDTNNEFNT EDQSVVYDMN QAAIDAIRAA
GATSQYIFVE GNSWTGAWTW VSVNSGLGNL TDPQNKIVYE MHQYLDSDGS GTSGTCASST
IGKERVQSAT QWLKDNNKLG FLGEFAGGAN SVCQTAITGM LDYMQDNSDV WLGASWWAAG
PWWGNYFASM EPPSGAGYAY YFKILSAYFP SSSSGGGSGG STTATTTAAQ TTTTKAPVTT
TKTTTTAAPP TTTAGGATAG HWAQCGGVGY SGPTACASPY TCKKQNDYYS QCL
//
