GUNC_ACETH
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 25-MAY-2022, entry version 61.
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; Firmicutes; 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}.
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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 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 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
