ID GUNC_ACETH Reviewed; 343 AA. AC P0C2S3; P07985; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 1. DT 03-MAY-2023, entry version 64. 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 Short=EgC; GN Name=celC; OS Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium OS thermocellum). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Acetivibrio. OX NCBI_TaxID=1515; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3384335; DOI=10.1016/0378-1119(88)90542-2; RA Schwarz W.H., Schimming S., Ruecknagel K.P., Burgschwaiger S., Kreil G., RA Staudenbauer W.L.; RT "Nucleotide sequence of the celC gene encoding endoglucanase C of RT Clostridium thermocellum."; RL Gene 63:23-30(1988). RN [2] RP ACTIVE SITE GLU-280. RX PubMed=8100226; DOI=10.1016/s0021-9258(19)85213-4; RA Wang Q., Tull D., Meinke A., Gilkes N.R., Warren R.A., Aebersold R., RA Withers S.G.; RT "Glu280 is the nucleophile in the active site of Clostridium thermocellum RT CelC, a family A endo-beta-1,4-glucanase."; RL J. Biol. Chem. 268:14096-14102(1993). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). RX PubMed=7664125; DOI=10.1038/nsb0795-569; RA Dominguez R., Souchon H., Spinelli S., Dauter Z., Wilson K.S., Chauvaux S., RA Beguin P., Alzari P.M.; RT "A common protein fold and similar active site in two distinct families of RT beta-glycanases."; RL Nat. Struct. Biol. 2:569-576(1995). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT GLN-140. RX PubMed=8632467; DOI=10.1006/jmbi.1996.0222; RA Dominguez R., Souchon H., Lascombe M.-B., Alzari P.M.; RT "The crystal structure of a family 5 endoglucanase mutant in complexed and RT uncomplexed forms reveals an induced fit activation mechanism."; RL J. Mol. Biol. 257:1042-1051(1996). CC -!- FUNCTION: This enzyme catalyzes the endohydrolysis of 1,4-beta- CC glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. 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 -!- MISCELLANEOUS: CelC has an unusual substrate range and displays CC features common to cellobiohydrolases by being able to cleave the CC agluconic bond of aryl-beta-glucosides. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M19422; AAA23220.1; -; Genomic_DNA. DR PIR; JT0268; JT0268. DR PDB; 1CEC; X-ray; 2.15 A; A=1-343. DR PDB; 1CEN; X-ray; 2.30 A; A=1-343. DR PDB; 1CEO; X-ray; 1.90 A; A=1-343. DR PDBsum; 1CEC; -. DR PDBsum; 1CEN; -. DR PDBsum; 1CEO; -. DR AlphaFoldDB; P0C2S3; -. DR SMR; P0C2S3; -. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR UniPathway; UPA00696; -. DR EvolutionaryTrace; P0C2S3; -. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR001547; Glyco_hydro_5. DR InterPro; IPR018087; Glyco_hydro_5_CS. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR31297:SF41; ENDOGLUCANASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G01830)-RELATED; 1. DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1. DR Pfam; PF00150; Cellulase; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase; KW Hydrolase; Polysaccharide degradation. FT CHAIN 1..343 FT /note="Endoglucanase C" FT /id="PRO_0000184047" FT ACT_SITE 140 FT /note="Proton donor" FT ACT_SITE 280 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:8100226" FT STRAND 5..9 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 13..16 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 22..28 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 31..40 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 44..50 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 51..53 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 65..80 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 84..91 FT /evidence="ECO:0007829|PDB:1CEO" FT TURN 105..107 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 109..125 FT /evidence="ECO:0007829|PDB:1CEO" FT TURN 126..128 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 131..136 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 147..163 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 169..172 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 174..177 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 179..184 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 191..199 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 203..206 FT /evidence="ECO:0007829|PDB:1CEO" FT TURN 207..209 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 214..219 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 225..228 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 232..238 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 240..248 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 255..272 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 275..281 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 289..305 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 309..313 FT /evidence="ECO:0007829|PDB:1CEO" FT STRAND 315..317 FT /evidence="ECO:0007829|PDB:1CEO" FT HELIX 332..339 FT /evidence="ECO:0007829|PDB:1CEO" SQ SEQUENCE 343 AA; 40954 MW; BD24763F548C726E CRC64; MVSFKAGINL GGWISQYQVF SKEHFDTFIT EKDIETIAEA GFDHVRLPFD YPIIESDDNV GEYKEDGLSY IDRCLEWCKK YNLGLVLDMH HAPGYRFQDF KTSTLFEDPN QQKRFVDIWR FLAKRYINER EHIAFELLNE VVEPDSTRWN KLMLEYIKAI REIDSTMWLY IGGNNYNSPD ELKNLADIDD DYIVYNFHFY NPFFFTHQKA HWSESAMAYN RTVKYPGQYE GIEEFVKNNP KYSFMMELNN LKLNKELLRK DLKPAIEFRE KKKCKLYCGE FGVIAIADLE SRIKWHEDYI SLLEEYDIGG AVWNYKKMDF EIYNEDRKPV SQELVNILAR RKT //