GUNC_CELJU
ID GUNC_CELJU Reviewed; 747 AA.
AC P27033; B3PDK2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Endoglucanase C;
DE EC=3.2.1.4;
DE AltName: Full=Cellodextrinase C;
DE AltName: Full=Cellulase C;
DE AltName: Full=Endo-1,4-beta-glucanase C;
DE Short=EGC;
DE Flags: Precursor;
GN Name=celC; Synonyms=cel5A; OrderedLocusNames=CJA_1462;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 38-47.
RX PubMed=1953673; DOI=10.1042/bj2790793;
RA Ferreira L.M.A., Hazlewood G.P., Barker P.J., Gilbert H.J.;
RT "The cellodextrinase from Pseudomonas fluorescens subsp. cellulosa consists
RT of multiple functional domains.";
RL Biochem. J. 279:793-799(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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; X61299; CAA43597.1; -; Genomic_DNA.
DR EMBL; CP000934; ACE82870.1; -; Genomic_DNA.
DR PIR; S19652; S19652.
DR AlphaFoldDB; P27033; -.
DR SMR; P27033; -.
DR STRING; 498211.CJA_1462; -.
DR CAZy; CBM10; Carbohydrate-Binding Module Family 10.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR PRIDE; P27033; -.
DR EnsemblBacteria; ACE82870; ACE82870; CJA_1462.
DR KEGG; cja:CJA_1462; -.
DR eggNOG; COG2730; Bacteria.
DR HOGENOM; CLU_015313_0_0_6; -.
DR OMA; RTIQQTM; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.30.32.30; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR036601; CBM10_sf.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR009031; CBM_fam10.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF02013; CBM_10; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM01064; CBM_10; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF57615; SSF57615; 1.
DR PROSITE; PS51763; CBM10; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000269|PubMed:1953673"
FT CHAIN 38..747
FT /note="Endoglucanase C"
FT /id="PRO_0000007865"
FT DOMAIN 38..136
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT DOMAIN 182..211
FT /note="CBM10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT REGION 226..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..747
FT /note="Catalytic"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 652
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT DISULFID 39..133
FT /evidence="ECO:0000250"
FT DISULFID 183..214
FT /evidence="ECO:0000250"
FT DISULFID 193..208
FT /evidence="ECO:0000250"
FT CONFLICT 85
FT /note="A -> P (in Ref. 1; CAA43597)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="G -> GG (in Ref. 1; CAA43597)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="S -> C (in Ref. 1; CAA43597)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="Q -> K (in Ref. 1; CAA43597)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 80098 MW; 2A1D90E2612D361A CRC64;
MGHVTSPSKR YPASFKRAGS ILGVSIALAA FSNVAAAGCE YVVTNSWGSG FTAAIRITNS
TSSVINGWNV SWQYNSNRVT NLWNANLSGS NPYSASNLSW NGTIQPGQTV EFGFQGVTNS
GTVESPTVNG AACTGGTSSS VSSSSVVSSS SSSRSSVSSS SVVSSSSSVV SSSSSSVVSG
GQCNWYGTLY PLCVSTTSGW GYENNRSCIS PSTCSAQPAP YGIVGGSSSP SSISSSSVRS
SSSSSVVPPS SSSSSSVPSS SSSSVSSSSV VSSSSSSVSV PGTGVFRVNT QGNLTKDGQL
LPARCGNWFG LEGRHEPSND ADNPSGAPME LYAGNMWWVN NSQGSGRTIQ QTMTELKQQG
ITMLRLPIAP QTLDANDPQG RSPNLKNHQS IRQSNARQAL EDFIKLADQN DIQIFIDIHS
CSNYVGWRAG RLDARPPYVD ANRVGYDFTR EEYSCSATNN PSSVTRIHAY DKQKWLANLR
EIAGLSAKLG VSNLIGIDVF NEPYDYTWAE WKGMVEEAYQ AINEVNPNML IIVEGISANA
NTQDGTPDTS VPVPHGSTDL NPNWGENLYE AGANPPNIPK DRLLFSPHTY GPSVFVQRQF
MDPAQTECAG LEGDEAAQAR CRIVINPTVL EQGWEEHFGY LRELGYGILI GEFGGNMDWP
GAKSSQADRN AWSHITTNVD QQWQQAAASY FKRKGINACY WSMNPESADT MGWYLTPWDP
VTANDMWGQW TGFDPRKTQL LHNMWGL
