ID   GUN2_HYPJE              Reviewed;         418 AA.
AC   P07982;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   13-SEP-2023, entry version 130.
DE   RecName: Full=Endoglucanase EG-II;
DE            Short=EGII;
DE            EC=3.2.1.4 {ECO:0000269|PubMed:3356188, ECO:0000269|PubMed:3384334};
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=egl2;
OS   Hypocrea jecorina (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-58, FUNCTION,
RP   CATALYTIC ACTIVITY, AND PYROGLUTAMATE FORMATION AT GLN-22.
RC   STRAIN=VTT-D-80133;
RX   PubMed=3384334; DOI=10.1016/0378-1119(88)90541-0;
RA   Saloheimo M., Lehtovaara P., Penttilae M., Teeri T.T., Staahlberg J.,
RA   Johansson G., Pettersson G., Clayssens M., Tomme P., Knowles J.K.C.;
RT   "EGIII, a new endoglucanase from Trichoderma reesei: the characterization
RT   of both gene and enzyme.";
RL   Gene 63:11-21(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 87-99, CATALYTIC ACTIVITY, AND DOMAIN.
RC   STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX   PubMed=3356188; DOI=10.1111/j.1432-1033.1988.tb13982.x;
RA   Stahlberg J., Johansson G., Pettersson G.;
RT   "A binding-site-deficient, catalytically active, core protein of
RT   endoglucanase III from the culture filtrate of Trichoderma reesei.";
RL   Eur. J. Biochem. 173:179-183(1988).
RN   [3]
RP   ACTIVE SITE GLU-350.
RC   STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX   PubMed=8093602; DOI=10.1016/0014-5793(93)81202-b;
RA   Macarron R., van Beeumen J., Henrissat B., de la Mata I., Claeyssens M.;
RT   "Identification of an essential glutamate residue in the active site of
RT   endoglucanase III from Trichoderma reesei.";
RL   FEBS Lett. 316:137-140(1993).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 92-418, ACTIVE SITE, AND
RP   DISULFIDE BONDS.
RX   PubMed=21898652; DOI=10.1002/pro.730;
RA   Lee T.M., Farrow M.F., Arnold F.H., Mayo S.L.;
RT   "A structural study of Hypocrea jecorina Cel5A.";
RL   Protein Sci. 20:1935-1940(2011).
CC   -!- FUNCTION: Endoglucanase (EG) that cleaves the internal beta-1,4-
CC       glucosidic bonds in cellulose (PubMed:3384334). The degradation of
CC       cellulose involves an interplay between different cellulolytic enzymes.
CC       Hydrolysis starts with EGs, which cut internal glycosidic linkages to
CC       reduce the polymerization degree of the substrate and creates new chain
CC       ends for exocellobiohydrolases (CBHs). The CBH release the disaccharide
CC       cellobiose from the non-reducing end of the cellulose polymer chain.
CC       Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short
CC       cello-oligosaccharides into glucose units (Probable).
CC       {ECO:0000269|PubMed:3384334, ECO:0000305}.
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         Evidence={ECO:0000269|PubMed:3356188, ECO:0000269|PubMed:3384334};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:3384334}.
CC   -!- DOMAIN: The enzyme consists of two functional domains, a catalytic core
CC       joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-,
CC       and proline-rich, highly glycosylated linker sequence.
CC       {ECO:0000305|PubMed:21898652, ECO:0000305|PubMed:3356188}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally called endoglucanase EG-III.
CC       {ECO:0000305|PubMed:3384334}.
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DR   EMBL; M19373; AAA34213.1; -; Genomic_DNA.
DR   PIR; S28372; S28372.
DR   PDB; 3QR3; X-ray; 2.05 A; A/B=92-418.
DR   PDBsum; 3QR3; -.
DR   AlphaFoldDB; P07982; -.
DR   SMR; P07982; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   CLAE; EGL5C_TRIRE; -.
DR   GlyCosmos; P07982; 1 site, No reported glycans.
DR   BioCyc; MetaCyc:MONOMER-16502; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34142:SF5; CBM1 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Pyrrolidone carboxylic acid;
KW   Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:3384334"
FT   CHAIN           22..418
FT                   /note="Endoglucanase EG-II"
FT                   /id="PRO_0000007874"
FT   DOMAIN          22..57
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          58..91
FT                   /note="Linker"
FT                   /evidence="ECO:0000305"
FT   REGION          63..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..418
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000305|PubMed:21898652"
FT   ACT_SITE        239
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000305|PubMed:21898652,
FT                   ECO:0000305|PubMed:8093602"
FT   ACT_SITE        350
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:8093602,
FT                   ECO:0000305|PubMed:21898652"
FT   MOD_RES         22
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:3384334"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:A0A024SH20"
FT   DISULFID        107..113
FT                   /evidence="ECO:0000269|PubMed:21898652,
FT                   ECO:0007744|PDB:3QR3"
FT   DISULFID        183..190
FT                   /evidence="ECO:0000269|PubMed:21898652,
FT                   ECO:0007744|PDB:3QR3"
FT   DISULFID        323..359
FT                   /evidence="ECO:0000269|PubMed:21898652,
FT                   ECO:0007744|PDB:3QR3"
FT   DISULFID        364..414
FT                   /evidence="ECO:0000269|PubMed:21898652,
FT                   ECO:0007744|PDB:3QR3"
FT   STRAND          94..102
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   TURN            103..106
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   STRAND          125..129
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   HELIX           134..145
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   HELIX           156..159
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   TURN            160..162
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   HELIX           170..185
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   STRAND          189..194
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   TURN            205..208
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   HELIX           212..226
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   STRAND          232..235
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   HELIX           245..261
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   STRAND          269..272
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   HELIX           275..277
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   TURN            279..285
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   HELIX           287..291
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   STRAND          304..309
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   STRAND          316..318
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   STRAND          320..322
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   TURN            328..331
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   HELIX           332..341
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   STRAND          346..351
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   HELIX           357..371
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   TURN            372..376
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   STRAND          377..386
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   STRAND          399..403
FT                   /evidence="ECO:0007829|PDB:3QR3"
FT   HELIX           409..414
FT                   /evidence="ECO:0007829|PDB:3QR3"
SQ   SEQUENCE   418 AA;  44227 MW;  26A492D55237A49B CRC64;
     MNKSVAPLLL AASILYGGAV AQQTVWGQCG GIGWSGPTNC APGSACSTLN PYYAQCIPGA
     TTITTSTRPP SGPTTTTRAT STSSSTPPTS SGVRFAGVNI AGFDFGCTTD GTCVTSKVYP
     PLKNFTGSNN YPDGIGQMQH FVNEDGMTIF RLPVGWQYLV NNNLGGNLDS TSISKYDQLV
     QGCLSLGAYC IVDIHNYARW NGGIIGQGGP TNAQFTSLWS QLASKYASQS RVWFGIMNEP
     HDVNINTWAA TVQEVVTAIR NAGATSQFIS LPGNDWQSAG AFISDGSAAA LSQVTNPDGS
     TTNLIFDVHK YLDSDNSGTH AECTTNNIDG AFSPLATWLR QNNRQAILTE TGGGNVQSCI
     QDMCQQIQYL NQNSDVYLGY VGWGAGSFDS TYVLTETPTS SGNSWTDTSL VSSCLARK
//