ID E0RKV9_PAEP6 Unreviewed; 537 AA.
AC E0RKV9;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN OrderedLocusNames=PPE_03499 {ECO:0000313|EMBL:ADM71316.1};
OS Paenibacillus polymyxa (strain E681).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=349520 {ECO:0000313|EMBL:ADM71316.1, ECO:0000313|Proteomes:UP000002227};
RN [1] {ECO:0000313|EMBL:ADM71316.1, ECO:0000313|Proteomes:UP000002227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E681 {ECO:0000313|EMBL:ADM71316.1,
RC ECO:0000313|Proteomes:UP000002227};
RX PubMed=20851896; DOI=10.1128/JB.00983-10;
RA Kim J.F., Jeong H., Park S.Y., Kim S.B., Park Y.K., Choi S.K., Ryu C.M.,
RA Hur C.G., Ghim S.Y., Oh T.K., Kim J.J., Park C.S., Park S.H.;
RT "Genome sequence of the polymyxin-producing plant-probiotic rhizobacterium
RT Paenibacillus polymyxa E681.";
RL J. Bacteriol. 192:6103-6104(2010).
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 ECO:0000256|RuleBase:RU361153};
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; CP000154; ADM71316.1; -; Genomic_DNA.
DR RefSeq; WP_013311450.1; NZ_CP048794.1.
DR AlphaFoldDB; E0RKV9; -.
DR SMR; E0RKV9; -.
DR CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR KEGG; ppy:PPE_03499; -.
DR eggNOG; COG2730; Bacteria.
DR HOGENOM; CLU_012932_1_1_9; -.
DR Proteomes; UP000002227; Chromosome.
DR GO; GO:0008810; F:cellulase 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; 2.60.40.710; Endoglucanase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
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; PF00942; CBM_3; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM01067; CBM_3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51172; CBM3; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361153};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361153};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361153}.
FT REGION 344..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 58557 MW; 9EF56F86A3B2DC5A CRC64;
MMNGQWVLPR IAKRVAVMLT AVLLLTLTNG FNWNTQTAEA AGTTPMERYG QLSVKNGKLV
DKNGKPVQLK GISSHGVQWF GDLVNQDSMR WLRDDWGISV FRVALYTEEG GYIANPSLKN
KVKEAIEAAQ KLGLYVIIDW HILSDGDPNI HKNEAKAFFN EFSTQYGHLP NVIYELANEP
NGNVNWNNQI RPYASEVSQV IRAKDPDNII IVGTGTWSQD VHDAADHPLP DKNTMYTVHF
YAGTHGQFLR DRVDYALNKG VGIFATEWGT SDASGNGGPF LNESKVWTDF LASRGISWAN
WSLSDKNETS AALLPGADRK GGWPDSQLSA SGKFVKQAIL EGSSNIGGGG NNGGDNGGDG
NTGGNNGGSN NGGDNGNGGS TPGSNDQGIV LQYRTGDTNA KDNAIRPEFN IKNTGKTAVK
LSDLKIRYYY TDESKQAQQF FVDWARIGTE KVKATFVTLP KPKAKADKYV EISFTDGAGT
IQPGGESGEI QPRIHAANWS NFDETNDYSY GATQKAFADW DHGTVYQQGK LVWGIEP
//