GUNC_CLOSF
ID GUNC_CLOSF Reviewed; 343 AA.
AC P23340;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Endoglucanase C307;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase C307;
DE AltName: Full=Endo-1,4-beta-glucanase C307;
DE Flags: Precursor;
GN Name=celC307;
OS Clostridium sp. (strain F1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1508;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-19 (PRECURSOR
RP PROTEIN).
RX PubMed=1368690; DOI=10.1271/bbb1961.55.347;
RA Sakka K., Shimanuki T., Shimada K.;
RT "Nucleotide sequence of celC307 encoding endoglucanase C307 of Clostridium
RT sp. strain F1.";
RL Agric. Biol. Chem. 55:347-350(1991).
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 -!- PTM: The signal sequence was not cleaved in the protein expressed in
CC E.coli.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; D00945; BAA00793.1; -; Genomic_DNA.
DR PIR; JE0409; JE0409.
DR AlphaFoldDB; P23340; -.
DR SMR; P23340; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR UniPathway; UPA00696; -.
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 Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..343
FT /note="Endoglucanase C307"
FT /id="PRO_0000007851"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 280
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 343 AA; 40905 MW; 72DD9BEA01A0DD05 CRC64;
MVSFKAGINL GGWISQYQVF SKEHFDTFIT EKDIETIAEA GFDHVRLPFD YPIIESDDNV
GEYKEDGLSY IDRCLEWCKK YNLGLVLDMH HAPGYRFQDF KTSTLFEDPN QQKRFVDIWR
FLAKRYINER EHIAFELLNE VVEPDSTRWN KLMLECVKAI REIDSTRWLY IGGNNYNSPD
ELKNLADIDD DYIVYNFHFY NPFFFTHQKA HWSESAMAYN RTVKYPGQYE GIEEFVKNNP
KYSFMMELNN LKLNKELLRK DLKPAIEFRE KKKCKLYCGE FGVIAIADLE SRIKWHEDYI
SLLEEYDIGG AVWNYKKMDF EIYNEDRKPV SQELVNILAR RKT