ID   GUN4_RUMAL              Reviewed;         312 AA.
AC   Q07940;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Endoglucanase 4;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase 4;
DE   AltName: Full=Endo-1,4-beta-glucanase 4;
DE   AltName: Full=Endoglucanase IV;
DE            Short=EG-IV;
GN   Name=Eg IV;
OS   Ruminococcus albus.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-19.
RC   STRAIN=F-40;
RA   Karita S., Morioka K., Kajino T., Sakka K., Shimada K., Ohmiya K.;
RT   "Cloning and sequencing of a novel endo-1,4-beta-glucanase gene from
RT   Ruminococcus albus.";
RL   J. Ferment. Bioeng. 76:439-444(1993).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.;
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB016777; BAA32286.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07940; -.
DR   SMR; Q07940; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   OMA; THGIQWF; -.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
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   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation.
FT   CHAIN           1..312
FT                   /note="Endoglucanase 4"
FT                   /id="PRO_0000184050"
FT   ACT_SITE        135
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   ACT_SITE        222
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
SQ   SEQUENCE   312 AA;  35767 MW;  A8BAADD9F93A8CBC CRC64;
     MLDKLKVING KLTAGEKPVR LFGLSTHGIA WYPEYICEES FNALKKDWRT NCIRIAMYTD
     EFRGYCKDGN KQHLKELIEK GVVIAEKLDM YVIVDWHVLC DQDPMKYIDE AEEFFSDMSK
     RFANKTNVIY EICNEPNCSG TWDKITEYAD RIIPIIRSNS PDALIVTGTS TWSQDIHCAL
     EKPLKWDNVM YSLHFYAATH KGTLRSRLER CIEAGLPVFI NEFNLCEASG KGDIDIDEAN
     AWYEVIDRLG LSCISWCLSN SGDTCGVFTQ NCTKLSGWTD EDIKTSGKII KGWFEAFADE
     ENTNEQCFRI DK