GUNC_RUMCH
ID GUNC_RUMCH Reviewed; 460 AA.
AC P37699; B8I7V2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Endoglucanase C;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase C;
DE AltName: Full=EGCCC;
DE AltName: Full=Endo-1,4-beta-glucanase C;
DE Flags: Precursor;
GN Name=celCCC; OrderedLocusNames=Ccel_0730;
OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10) (Clostridium cellulolyticum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RX PubMed=1398087; DOI=10.1016/0378-1119(92)90062-t;
RA Bagnara-Tardif C., Gaudin C., Belaich A., Hoest P., Citard T.,
RA Belaich J.-P.;
RT "Sequence analysis of a gene cluster encoding cellulases from Clostridium
RT cellulolyticum.";
RL Gene 119:17-28(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 33-37, AND CHARACTERIZATION.
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RX PubMed=8223599; DOI=10.1111/j.1432-1033.1993.tb18277.x;
RA Fierobe H.-P., Bagnara-Tardif C., Gaudin C., Guerlesquin F., Sauve P.,
RA Belaich A., Belaich J.-P.;
RT "Purification and characterization of endoglucanase C from Clostridium
RT cellulolyticum. Catalytic comparison with endoglucanase A.";
RL Eur. J. Biochem. 217:557-565(1993).
CC -!- FUNCTION: The biological conversion of cellulose to glucose generally
CC requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC cut the disaccharide cellobiose from the non-reducing end of the
CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC cellobiose and other short cello-oligosaccharides to glucose.
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC -!- SUBUNIT: Monomer.
CC -!- PTM: There are two forms of the cellulase. The shorter form lacks
CC probably the C-terminal reiterated domains.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family.
CC {ECO:0000305}.
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DR EMBL; M87018; AAA73867.1; -; Genomic_DNA.
DR EMBL; CP001348; ACL75109.1; -; Genomic_DNA.
DR PIR; JC1299; JC1299.
DR RefSeq; WP_015924276.1; NC_011898.1.
DR AlphaFoldDB; P37699; -.
DR SMR; P37699; -.
DR STRING; 394503.Ccel_0730; -.
DR CAZy; GH8; Glycoside Hydrolase Family 8.
DR EnsemblBacteria; ACL75109; ACL75109; Ccel_0730.
DR KEGG; cce:Ccel_0730; -.
DR eggNOG; COG3405; Bacteria.
DR HOGENOM; CLU_036185_0_0_9; -.
DR OMA; CRTPWRL; -.
DR OrthoDB; 636673at2; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000001349; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002037; Glyco_hydro_8.
DR InterPro; IPR019834; Glyco_hydro_8_CS.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF01270; Glyco_hydro_8; 1.
DR PRINTS; PR00735; GLHYDRLASE8.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS00812; GLYCOSYL_HYDROL_F8; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:8223599"
FT CHAIN 33..460
FT /note="Endoglucanase C"
FT /id="PRO_0000007936"
FT DOMAIN 400..460
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 155
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10058"
FT CONFLICT 91
FT /note="S -> T (in Ref. 1; AAA73867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 50483 MW; 2F31E1F6CB41504F CRC64;
MIKGSSLKRF KSLVMAAIFS VSIISTAIAS SAADQIPFPY DAKYPNGAYS CLADSQSIGN
NLVRSEWEQW KSAHITSNGA RGYKRVQRDA STNYDTVSEG LGYGLLLSVY FGEQQLFDDL
YRYVKVFLNS NGLMSWRIDS SGNIMGKDSI GAATDADEDI AVSLVFAHKK WGTSGGFNYQ
TEAKNYINNI YNKMVEPGTY VIKAGDTWGG SNVTNPSYFA PAWYRIFADF TGNSGWINVA
NKCYEIADKA RNSNTGLVPD WCTANGTPAS GQGFDFYYDA IRYQWRAAID YSWYGTAKAK
THCDAISNFF KNIGYANIKD GYTISGSQIS SNHTATFVSC AAAAAMTGTD TTYAKNIYNE
CVKVKDSGNY TYFGNTLRMM VLLYTTGNFP NLYTYNSQPK PDLKGDVNND GAIDALDIAA
LKKAILTQTT SNISLTNADM NNDGNIDAID FAQLKVKLLN
