ID   GUNA_BUTFI              Reviewed;         429 AA.
AC   P22541;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-MAY-2023, entry version 86.
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   Flags: Precursor;
GN   Name=celA;
OS   Butyrivibrio fibrisolvens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 35-50.
RC   STRAIN=A46;
RX   PubMed=2269875; DOI=10.1099/00221287-136-10-2089;
RA   Hazlewood G.P., Davidson K., Laurie J.I., Romaniec M.P.M., Gilbert H.J.;
RT   "Cloning and sequencing of the celA gene encoding endoglucanase A of
RT   Butyrivibrio fibrisolvens strain A46.";
RL   J. Gen. Microbiol. 136:2089-2097(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; M37031; AAA20893.1; -; Genomic_DNA.
DR   PIR; S29044; S29044.
DR   AlphaFoldDB; P22541; -.
DR   SMR; P22541; -.
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; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 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..34
FT                   /evidence="ECO:0000269|PubMed:2269875"
FT   CHAIN           35..429
FT                   /note="Endoglucanase A"
FT                   /id="PRO_0000007842"
FT   REGION          46..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        249
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
SQ   SEQUENCE   429 AA;  48859 MW;  7144A574505E2EAE CRC64;
     MVSKKQKFLT VILVIVLAIV IVGGVFGISF VKGRVTFPWQ LQNSEAKTEQ VKEPAKEEPK
     LVIKEKKQDE SAKKEQELKK AKEEAEAAVE KETEKTEEEP VDNLLNDMKL KYYGKLAVEG
     SHLVDADGHE VLLMGVSTHG INWYPEYASA ETIKSLRDTW GINVIRLAMY TSDYNGYCVA
     GKENQEKLKD IIDDAVEAAT DNDMYVIIDW HTLNDADPNE YKADAIQFFG EMVRKYKDNE
     NVIYEICNEP NGDTTWNDVR RYANEVIPVI RNVDAIILVG TPKWATDLDS VLDKPLDFDN
     IMYTYHFYAG THHKAERNAL RDALDEGLPV FISEYGLVDA DGDGNLNEKE ADYWYDMIRK
     EYGVSSCMWN LSNKDEGSAM INADCDKLSD FTEEDLSESA MWLIDQISQL KHSDLEQGVD
     WITPENNNR
//