ID   GUNB_RUMAL              Reviewed;         409 AA.
AC   P23661;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   24-JAN-2024, entry version 88.
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;
DE            Short=EGB;
DE   Flags: Precursor;
GN   Name=celB;
OS   Ruminococcus albus.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SY3;
RX   PubMed=2250649; DOI=10.1007/bf00265057;
RA   Poole D.M., Hazlewood G.P., Laurie J.I., Barker P.J., Gilbert H.J.;
RT   "Nucleotide sequence of the Ruminococcus albus SY3 endoglucanase genes celA
RT   and celB.";
RL   Mol. Gen. Genet. 223:217-223(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; X54932; CAA38693.1; -; Genomic_DNA.
DR   PIR; S12018; S12018.
DR   AlphaFoldDB; P23661; -.
DR   SMR; P23661; -.
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; PTHR31297:SF41; ENDOGLUCANASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G01830)-RELATED; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           22..409
FT                   /note="Endoglucanase B"
FT                   /id="PRO_0000007872"
FT   REGION          23..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  45524 MW;  119081DFA3BFDD54 CRC64;
     MKLKRIAALL TAAVMSVGVM ASCGGSKSDD KSKADTKSAA ETSGAEGDSS ESEEIPVSQT
     HTNDPMTVTS AKDLVAKMSN GWNLGNTMDA TGEGLESEIS WLPTKVYTNK FMIDMLPEAG
     FNVLRIPVSW GNHLIDNNYT IDPAWMDRVQ EIVNYGIDDG MYVILNTHHE EWYMPKPSEK
     DGDIEELKAI WSQIADRFKG YDEHLIFEGL NEPRLRGEGA EWTGTSEARE IINEYEKAFV
     ETVRASGGNN GDRCLMITGY AASSGYNNLS AIELPEDSDK LIISVHAYLP YSFALDTKGT
     DKYDPEDTAI PTLFESLNEL FISRDIPVIV GEFGSMNKDN IDDRVKCLDD YLGNAAKYDI
     PCVWWDNYAR IGNGENFGLL NRQEYDWYFP KLMDVFKKYA ESDPSAAAA
//