ID   GUN1_RUMAL              Reviewed;         406 AA.
AC   P16216;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-MAY-2023, entry version 90.
DE   RecName: Full=Endoglucanase 1;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   AltName: Full=Endoglucanase I;
DE            Short=EG-I;
DE   Flags: Precursor;
GN   Name=Eg I;
OS   Ruminococcus albus.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 44-58.
RC   STRAIN=F-40;
RX   PubMed=2687251; DOI=10.1128/jb.171.12.6771-6775.1989;
RA   Ohmiya K., Kajino T., Kato A., Shimizu S.;
RT   "Structure of a Ruminococcus albus endo-1,4-beta-glucanase gene.";
RL   J. Bacteriol. 171:6771-6775(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 44-70.
RX   PubMed=1987156; DOI=10.1128/jb.173.2.636-641.1991;
RA   Ohmiya K., Deguchi H., Shimizu S.;
RT   "Modification of the properties of a Ruminococcus albus endo-1,4-beta-
RT   glucanase by gene truncation.";
RL   J. Bacteriol. 173:636-641(1991).
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; M30928; AAA26469.1; -; Genomic_DNA.
DR   PIR; A43722; A43722.
DR   AlphaFoldDB; P16216; -.
DR   SMR; P16216; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
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; PTHR31297:SF17; ENDOGLUCANASE; 1.
DR   PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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; Signal.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000269|PubMed:1987156,
FT                   ECO:0000269|PubMed:2687251"
FT   CHAIN           44..406
FT                   /note="Endoglucanase 1"
FT                   /id="PRO_0000007871"
FT   REGION          30..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        330
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   406 AA;  45390 MW;  2E0172437B14FEA8 CRC64;
     MNSKKIGAMI AAAVLSLIVM TPAATRKIVQ RQTRNSSTAV ENSAADESET ENVPVSQTHT
     NDTMTVTSAK DLVAKMTNGW NLGNTMDATA QGLGSEVSWL PLKVTTNKYM IDMLPEAGFN
     VLRIPVSWGN HIIDDKYTSD PAWMDRVQEI VNYGIDNGLY VILNTHHEEW YMPKPSEKDG
     DIEEIKAVWA QIADRFKGYD EHLIFEGLNE PRLRGEGAEW TGTSEAREII NEYEKAFVET
     VRASGGNNGD RCLMITGYAA SSAYNNLSAI ELPEDSDKLI ISVHAYLPYS FALDTKGTDK
     YDPEDTAIPE LFEHLNELFI SKGIPVIVGE FGTMNKENTE DRVKCLEDYL AAAAKYDIPC
     VWWDNYARIG NGENFGLMNR ADLEWYFPDL IETFKTYAEK DPASAE
//