ID   GUN2_RUMJO              Reviewed;         460 AA.
AC   P37701;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Endoglucanase 2;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase 2;
DE   AltName: Full=Endo-1,4-beta-glucanase 2;
DE   Flags: Precursor;
GN   Name=celB;
OS   Ruminiclostridium josui (Clostridium josui).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=1499;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Fujino T., Karita S., Ohmiya K.;
RL   Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
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 8 (cellulase D) family.
CC       {ECO:0000305}.
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DR   EMBL; D16670; BAA04078.1; -; Genomic_DNA.
DR   PIR; I40799; I40799.
DR   AlphaFoldDB; P37701; -.
DR   SMR; P37701; -.
DR   CAZy; GH8; Glycoside Hydrolase Family 8.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1330.10; -; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002037; Glyco_hydro_8.
DR   InterPro; IPR019834; Glyco_hydro_8_CS.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF01270; Glyco_hydro_8; 1.
DR   PRINTS; PR00735; GLHYDRLASE8.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF63446; SSF63446; 1.
DR   PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS00812; GLYCOSYL_HYDROL_F8; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..460
FT                   /note="Endoglucanase 2"
FT                   /id="PRO_0000007934"
FT   DOMAIN          400..460
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT   ACT_SITE        99
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        155
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10058"
SQ   SEQUENCE   460 AA;  50599 MW;  65EEAABCD82B7BD4 CRC64;
     MIKGSSLKRI KSLVMMAIFS VSIITTAIVS SAADQIPFPY NATYPYGAYS CLADSQSSAN
     NLLKSEWEQW KSAHITSNGA RGYKRVQRDA STNYDTVSEG LGYGMLLAVY FGEQQLFDDL
     YRYVKVFLNS NGLMSWRIDA NGNIMGQNAI GAATDADEDI AVSLVFAHKK WGTSGGFNYQ
     TEAKNYINNI YNKMVEPGTY VLKPGDMWGG SDVTNPSYFA PAWYRIFADF TGNSGWINVA
     NKCYEIADKA RNSNTGLVPD WCTANGTPAS GQGYDFYYDA IRYQWRTAID YSWYGTAKAK
     THCDAISNFF KNIGYPNIKD GYTLSGSQIS ANHTATFVSC AAAAAMTGTD ATYAKNIYNE
     CVKVKDTGNY TYFGNTLRMM ILLYTTGNFP NLYSYSSQPQ QGLKGDVNND GAIDALDIAA
     LKKAILTQST SNINLTNADM NNDGNIDAID FAQLKVKLLN