GUN3_EVAC2
ID GUN3_EVAC2 Reviewed; 825 AA.
AC P19570;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Endoglucanase C;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase C;
DE AltName: Full=Endo-1,4-beta-glucanase C;
DE Flags: Precursor;
GN Name=celC;
OS Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM
OS 9156 / N-4) (Bacillus cellulosilyticus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Evansella.
OX NCBI_TaxID=649639;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2666258; DOI=10.1016/0378-1119(89)90169-8;
RA Fukumori F., Kudo T., Sashihara N., Nagata Y., Ito K., Horikoshi K.;
RT "The third cellulase of alkalophilic Bacillus sp. strain N-4: evolutionary
RT relationships within the cel gene family.";
RL Gene 76:289-298(1989).
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; M25500; AAA22306.1; -; Genomic_DNA.
DR PIR; JS0174; JS0174.
DR AlphaFoldDB; P19570; -.
DR SMR; P19570; -.
DR STRING; 649639.Bcell_3370; -.
DR CAZy; CBM17; Carbohydrate-Binding Module Family 17.
DR CAZy; CBM28; Carbohydrate-Binding Module Family 28.
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 InterPro; IPR005086; CBM_fam_17/28.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF03424; CBM_17_28; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..825
FT /note="Endoglucanase C"
FT /id="PRO_0000007836"
FT REGION 607..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT ACT_SITE 335
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O85465"
SQ SEQUENCE 825 AA; 92015 MW; A1727DA3D7632617 CRC64;
MRNKLRRLLA IMMAVLLITS LFAPMVSAEE GDNGDDDDLV TPIEIEERPH ESNYEKYPAL
LDGGLDERRP SEAGALQLVE VDGQVTLADQ DGVPIQLRGM STHGLQWFGE IVNENAFAAL
ANDWGSNVIR LALYIGENAY RYNPDLIEKV YAGIELAKEN DMYVIIDWHV HAPGDPNADI
YQGGVNEDGE EYLGAKDFFL HIAEKYPNDP HLIYELANEP SSNSSGGPGI TNDEDGWEAV
REYAQPIVDA LRDSGNAEDN IIIVGSPNWS QRMDLAAADN PIDDHHTMYT LHFYTGTHEG
TNESYPEGIS SEDRSNVMAN AKYALDKGKA IFATEWGVSE ADGNNGPYLN EADVWLNFLN
ENNISWTNWS LTNKNETSGA FTPFILNESD ATDLDPGEDQ VWSMEELSVS GEYVRSRILG
EEYQPIDRTP REEFSEVIWD FNDGTTQGFV QNSDSPLDVT IENVNDALQI TGLDESNAIA
GEEEDYWSNV RISADEWEET FDILGAEELS MDVVVDDPTT VAIAAIPQSS AHEWANASNS
VLITEDDFEE QEDGTYKALL TITGEDAPNL TNIAEDPEGS ELNNIILFVG TENADVISLD
NITVTGDRES VPEPVEHDTK GDSALPSDFE DGTRQGWEWD SESAVRTALT IEEANGSNAL
SWEYAYPEVK PSDDWATAPR LTLYKDDLVR GDYEFVAFDF YIDPIEDRAT EGAIDINLIF
QPPAAGYWAQ ASETFEIDLE ELDSATVTDD GLYHYEVEIN IEDIENDIEL RNLMLIFADD
ESDFAGRVFL DNVRMDMSLE TKVEVLERNI NELQEQLVEV EALMR
