ID   GUN_PAEPO               Reviewed;         397 AA.
AC   P23548;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=Endoglucanase;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
OS   Paenibacillus polymyxa (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2307659; DOI=10.1128/jb.172.3.1576-1586.1990;
RA   Baird S.D., Johnson D.A., Seligy V.L.;
RT   "Molecular cloning, expression, and characterization of endo-beta-1,4-
RT   glucanase genes from Bacillus polymyxa and Bacillus circulans.";
RL   J. Bacteriol. 172:1576-1586(1990).
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; M33791; AAA22631.1; -; Genomic_DNA.
DR   PIR; A35136; A35136.
DR   AlphaFoldDB; P23548; -.
DR   SMR; P23548; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   eggNOG; COG2730; Bacteria.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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..397
FT                   /note="Endoglucanase"
FT                   /id="PRO_0000184042"
FT   ACT_SITE        194
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        317
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  44357 MW;  B9C2E802C04F0A2A CRC64;
     MKKKGLKKTF FVIASLVMGF TLYGYTPVSA DAASVKGYYH TQGNKIVDES GKEAAFNGLN
     WFGLETPNYT LHGLWSRSMD DMLDQVKKEG YNLIRLPYSN QLFDSSSRPD SIDYHKNPDL
     VGLNPIQIMD KLIEKAGQRG IQIILDRHRP GSGGQSELWY TSQYPESRWI SDWKMLADRY
     KNNPTVIGAD LHNEPHGQAS WGTGNASTDW RLAAQRAGNA ILSVNPNWLI LVEGVDHNVQ
     GNNSQYWWGG NLTGVANYPV VLDVPNRVVY SPHDYGPGVS SQPWFNDPAF PSNLPAIWDQ
     TWGYISKQNI APVLVGEFGG RNVDLSCPEG KWQNALVHYI GANNLYFTYW SLNPNSGDTG
     GLLLDDWTTW NRPKQDMLGR IMKPVVSVAQ QAEAAAE
//