GUN2_EVAC2
ID GUN2_EVAC2 Reviewed; 409 AA.
AC P06565;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Endoglucanase B;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase B;
DE AltName: Full=Endo-1,4-beta-glucanase B;
GN Name=celB;
OS Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM
OS 9156 / N-4) (Bacillus cellulosilyticus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Evansella.
OX NCBI_TaxID=649639;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3782013; DOI=10.1128/jb.168.2.479-485.1986;
RA Fukumori F., Sashihara N., Kudo T., Horikoshi K.;
RT "Nucleotide sequences of two cellulase genes from alkalophilic Bacillus sp.
RT strain N-4 and their strong homology.";
RL J. Bacteriol. 168:479-485(1986).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; M14729; AAA22299.1; -; Genomic_DNA.
DR PIR; B25156; B25156.
DR AlphaFoldDB; P06565; -.
DR SMR; P06565; -.
DR STRING; 649639.Bcell_0437; -.
DR eggNOG; COG2730; Bacteria.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SUPFAM; SSF51055; SSF51055; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW Polysaccharide degradation.
FT CHAIN 1..409
FT /note="Endoglucanase B"
FT /id="PRO_0000184045"
FT REGION 326..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT ACT_SITE 254
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 65..66
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 260..261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 293..295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
SQ SEQUENCE 409 AA; 45690 MW; 9888660E66B4DA3F CRC64;
MKKITTIFVV LLMTLALFII GNTTAADDYS VVEEHGQLSI SNGELVNDRG EPVQLKGMSS
HGLQWYGQFV NYESMKWLRD DWGITVFRAA MYTSSGGYIE DPSVKEKVKE AVEAAIDLGI
YVIIDWHILS DNDPNIYKEE AKDFFDEMSE LYGDYPNVIY EIANEPNGSD VTWDNQIKPY
AEEVIPVIRN NDPNNIIIVG TGTWSQDVHH AADNQLTDPN VMYAFHFYAG THGQNLRDQV
DYALDQGAAI FVSEWGTSEA TGDGGVFLDE AQVWIDFMDE RNLSWANWSL THKDESSAAL
MPGASPTGGW TEAELSPSGT FVREKIRESA TTPPSDPTPP SDPDPGEPEP DPGEPDPTPP
SDPGDYPAWD PNTIYTDEIV YHNGQLWQAK WWTQNQEPGD PYGPWEPLN
