GUN_CLOSA
ID GUN_CLOSA Reviewed; 448 AA.
AC P15704;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Endoglucanase;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE Flags: Precursor;
GN Name=eglA;
OS Clostridium saccharobutylicum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=169679;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-117 / DSM 13864 / NCP 262;
RX PubMed=3389820; DOI=10.1128/aem.54.5.1289-1292.1988;
RA Zappe H., Jones W.A., Jones D.T., Woods D.R.;
RT "Structure of an endo-beta-1,4-glucanase gene from Clostridium
RT acetobutylicum P262 showing homology with endoglucanase genes from Bacillus
RT spp.";
RL Appl. Environ. Microbiol. 54:1289-1292(1988).
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 -!- MISCELLANEOUS: The C-terminal region of C.acetobutylicum is not
CC required for activity.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from C.acetobutylicum.
CC {ECO:0000305|PubMed:3389820}.
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DR EMBL; M31311; AAA23230.1; -; Genomic_DNA.
DR AlphaFoldDB; P15704; -.
DR SMR; P15704; -.
DR STRING; 169679.CSACC_09830; -.
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 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 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..34
FT CHAIN 35..448
FT /note="Endoglucanase"
FT /id="PRO_0000007844"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 74..75
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 269..270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT BINDING 302..304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O85465"
SQ SEQUENCE 448 AA; 49366 MW; 6FE6AC97C836A598 CRC64;
MFSKIKKINF FKKTFSFLIA VVMMLFTVLG TNTYKAEAAT TSFGGQLKVV GSQLCDSNGK
PIQLKGMSSH GLQWYVNFVN YDSMKFLRDK WGVNVIRAAM YTNEGGYISN PSSQKEKIKK
IVQDAIDLNM YVIIDWHILS DNNPNTYKEQ AKSFFQEMAE EYGKYSNVIY EICNEPNGGT
NWANDIKPYA NYIIPAIRAI DPNNIIIVGT STWSQDVDIA ADNPLRYSNI MYTCHFYAGT
HTQSLRDKIN YAMSKGIAIF VTEWGTSDAS GNGGPYLDES QKWVDFMASK NISWTNWALC
DKSEASAALK SGSSTTGGWT DSDLTTSGLF VKKSIGGSNT TSQTSAPTFS LQSGTYDSAQ
TVTLTSSDND SVIHYTTDGT TPTSSSPVYT SPITISKTTT VKAFTTKTGM TDSNITSAVY
TISNTDPVKQ VSAPTFSYNQ EHTIQLKL
