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   03-MAY-2023, entry version 94.
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; Bacillota; 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   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   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
//