GUNA_BUTFI
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 25-MAY-2022, entry version 82.
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; Firmicutes; 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 PRIDE; P22541; -.
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; 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