ID   GUN_MYTED               Reviewed;         181 AA.
AC   P82186;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Endoglucanase;
DE            EC=3.2.1.4;
DE   AltName: Full=CMCase;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
OS   Mytilus edulis (Blue mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC   Mytilus.
OX   NCBI_TaxID=6550;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Digestive gland;
RX   PubMed=10931178; DOI=10.1046/j.1432-1327.2000.01533.x;
RA   Xu B., Hellman U., Ersson B., Janson J.-C.;
RT   "Purification, characterization and amino-acid sequence analysis of a
RT   thermostable, low molecular mass endo-beta-1,4-glucanase from blue mussel,
RT   Mytilus edulis.";
RL   Eur. J. Biochem. 267:4970-4977(2000).
CC   -!- FUNCTION: Active towards the soluble carboxymethylcellulose (CMC).
CC       Possesses expansin activity too. {ECO:0000269|PubMed:10931178}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.6.;
CC       Temperature dependence:
CC         Optimum temperature is 30-50 degrees Celsius.;
CC   -!- TISSUE SPECIFICITY: Digestive gland.
CC   -!- MASS SPECTROMETRY: Mass=19702; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10931178};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family.
CC       {ECO:0000305}.
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DR   PDB; 1WC2; X-ray; 1.20 A; A=1-181.
DR   PDBsum; 1WC2; -.
DR   AlphaFoldDB; P82186; -.
DR   SMR; P82186; -.
DR   CAZy; GH45; Glycoside Hydrolase Family 45.
DR   EvolutionaryTrace; P82186; -.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.40.10; -; 1.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   SUPFAM; SSF50685; SSF50685; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..181
FT                   /note="Endoglucanase"
FT                   /id="PRO_0000184075"
FT   ACT_SITE        24
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   DISULFID        4..16
FT   DISULFID        30..69
FT   DISULFID        32..176
FT   DISULFID        65..178
FT   DISULFID        72..157
FT   DISULFID        103..113
FT   TURN            6..9
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   STRAND          14..22
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   TURN            28..31
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   HELIX           54..57
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   TURN            67..70
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   STRAND          72..81
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   STRAND          94..103
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   TURN            110..112
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   STRAND          128..134
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   HELIX           141..143
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   STRAND          146..155
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   HELIX           157..163
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   HELIX           170..173
FT                   /evidence="ECO:0007829|PDB:1WC2"
FT   HELIX           177..179
FT                   /evidence="ECO:0007829|PDB:1WC2"
SQ   SEQUENCE   181 AA;  19711 MW;  E00A8C57203823F6 CRC64;
     NQKCSGNPRR YNGKSCASTT NYHDSHKGAC GCGPASGDAQ FGWNAGSFVA AASQMYFDSG
     NKGWCGQHCG QCIKLTTTGG YVPGQGGPVR EGLSKTFMIT NLCPNIYPNQ DWCNQGSQYG
     GHNKYGYELH LDLENGRSQV TGMGWNNPET TWEVVNCDSE HNHDHRTPSN SMYGQCQCAH
     Q