ID   GUNA_RUMAL              Reviewed;         364 AA.
AC   P23660;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   24-JAN-2024, entry version 93.
DE   RecName: Full=Endoglucanase A;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase A;
DE   AltName: Full=Endo-1,4-beta-glucanase A;
DE            Short=EGA;
DE   AltName: Full=Endo-1,4-beta-xylanase;
DE            EC=3.2.1.8;
GN   Name=celA;
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 1-14.
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   -!- FUNCTION: Hydrolyzes both carboxymethylcellulose and xylan. Probably
CC       has a role in hydrolyzing oligosaccharides derived from cellulose,
CC       which are transported across the cell wall.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; X54931; CAA38692.1; -; Genomic_DNA.
DR   PIR; S12017; S12017.
DR   AlphaFoldDB; P23660; -.
DR   SMR; P23660; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   eggNOG; COG2730; Bacteria.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan 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; Cytoplasm;
KW   Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Xylan degradation.
FT   CHAIN           1..364
FT                   /note="Endoglucanase A"
FT                   /id="PRO_0000184051"
FT   ACT_SITE        169
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        293
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  41218 MW;  F8DCD2E2E55781F7 CRC64;
     MRKPDKDADR LTTLDLARSG EVRDISAMEL VGEMKTGWNL GNSLDATGAP GNASEVNWGN
     PKTTKEMIDA VYNKGFDVIR IPVTWGGHVG DAPDYKIDDE WIARVQEVVN YAYDDGAYVI
     INSHHEEDWR IPDNEHIDAV DEKTAAIWKQ VAERFKDYGD HLIFEGLNEP RVKGSPQEWN
     GGTEEGRRCV DRLNKTFLDT VRATGGNNEK RLLLMTTYAS SSMSNVIKDT AIPEDDHIGF
     SIHAYTPYAF TYNANADWEL FHWDDSHDGE LVSLMTNLKE NYLDKDIPVI ITEYGAVNKD
     NNDEDRAKWV SSYIEYAELL GGIPCVWWDN GYYSSGNELF GIFDRNTCTW FTDTVTDAII
     ENAK
//