ID   GUN1_HYPJE              Reviewed;         459 AA.
AC   P07981;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   13-SEP-2023, entry version 144.
DE   RecName: Full=Endoglucanase EG-1;
DE            EC=3.2.1.4 {ECO:0000269|Ref.2};
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=egl1;
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].
RC   STRAIN=VTT-D-80133;
RX   PubMed=2948877; DOI=10.1016/0378-1119(86)90023-5;
RA   Penttilae M., Lehtovaara P., Nevalainen H., Bhikhabhai R., Knowles J.K.C.;
RT   "Homology between cellulase genes of Trichoderma reesei: complete
RT   nucleotide sequence of the endoglucanase I gene.";
RL   Gene 45:253-263(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=L27;
RX   DOI=10.1038/nbt0187-60;
RA   van Arsdell J.N., Kwok S., Schweickart V.L., Ladner M.B., Gelfand D.H.,
RA   Innis M.A.;
RT   "Cloning, characterization, and expression in Saccharomyces cerevisiae of
RT   endoglucanase I from Trichoderma reesei.";
RL   Biotechnology (N.Y.) 5:60-64(1987).
RN   [3]
RP   PROTEIN SEQUENCE OF 23-53, PYROGLUTAMATE FORMATION AT GLN-23, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=L27;
RX   DOI=10.1038/nbt1083-687;
RA   Shoemaker S., Watt K., Tsitovsky G., Cox R.;
RT   "Characterization and properties of cellulases purified from Trichoderma
RT   reesei strain L27.";
RL   Biotechnology (N.Y.) 1:687-690(1983).
RN   [4]
RP   PUTATIVE ACTIVE SITE GLU-149.
RX   DOI=10.1016/0014-5793(89)80136-X;
RA   Tomme P., Clayssens M.;
RT   "Identification of a functionally important carboxyl group in
RT   cellobiohydrolase I from Trichoderma reesei.";
RL   FEBS Lett. 243:239-243(1989).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 23-393, PYROGLUTAMATE FORMATION AT
RP   GLN-23, AND DISULFIDE BONDS.
RX   PubMed=9325098; DOI=10.1006/jmbi.1997.1243;
RA   Kleywegt G.J., Zou J.-Y., Divne C., Davies G.J., Sinning I., Staehlberg J.,
RA   Reinikainen T., Srisodsuk M., Teeri T.T., Jones T.A.;
RT   "The crystal structure of the catalytic core domain of endoglucanase I from
RT   Trichoderma reesei at 3.6-A resolution, and a comparison with related
RT   enzymes.";
RL   J. Mol. Biol. 272:383-397(1997).
RN   [6]
RP   STRUCTURE BY NMR OF 422-459, AND DISULFIDE BONDS.
RX   PubMed=9760165; DOI=10.1046/j.1432-1327.1998.2560279.x;
RA   Mattinen M.L., Linder M., Drakenberg T., Annila A.;
RT   "Solution structure of the cellulose-binding domain of endoglucanase I from
RT   Trichoderma reesei and its interaction with cello-oligosaccharides.";
RL   Eur. J. Biochem. 256:279-286(1998).
CC   -!- FUNCTION: Endoglucanase (EG) that cleaves the internal beta-1,4-
CC       glucosidic bonds in cellulose (PubMed:2948877). 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:2948877, 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|Ref.2};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}.
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:0000250|UniProtKB:P62694}.
CC   -!- PTM: Asn-204 contains mainly a high-mannose-type glycan (Hex(7-
CC       9)GlcNAc(2)), with a small fraction (8%) bearing a single GlcNAc at
CC       this site. {ECO:0000250|UniProtKB:A0A024SNB7}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally called endoglucanase EG-II. {ECO:0000305}.
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DR   EMBL; M15665; AAA34212.1; -; Genomic_DNA.
DR   PIR; A25928; A25928.
DR   PDB; 1EG1; X-ray; 3.60 A; A/C=24-393.
DR   PDB; 4BMF; NMR; -; A=422-459.
DR   PDBsum; 1EG1; -.
DR   PDBsum; 4BMF; -.
DR   AlphaFoldDB; P07981; -.
DR   BMRB; P07981; -.
DR   SMR; P07981; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   CLAE; EGL7A_TRIRE; -.
DR   GlyCosmos; P07981; 3 sites, No reported glycans.
DR   iPTMnet; P07981; -.
DR   VEuPathDB; FungiDB:TrQ_002418; -.
DR   OMA; GCVAQDT; -.
DR   BioCyc; MetaCyc:MONOMER-16501; -.
DR   BRENDA; 3.2.1.4; 6451.
DR   EvolutionaryTrace; P07981; -.
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   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR   PANTHER; PTHR33753:SF1; ENDO-BETA-1,4-GLUCANASE CELB; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 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..22
FT                   /evidence="ECO:0000269|Ref.3"
FT   CHAIN           23..459
FT                   /note="Endoglucanase EG-1"
FT                   /id="PRO_0000007915"
FT   DOMAIN          423..459
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          23..397
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000305|PubMed:9325098"
FT   REGION          390..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..423
FT                   /note="Linker"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        406..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        218
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:9325098"
FT   ACT_SITE        223
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000269|PubMed:9325098"
FT   SITE            164
FT                   /note="Not glycosylated"
FT                   /evidence="ECO:0000250|UniProtKB:A0A024SNB7"
FT   SITE            208
FT                   /note="Not glycosylated"
FT                   /evidence="ECO:0000250|UniProtKB:A0A024SNB7"
FT   SITE            281
FT                   /note="Not glycosylated"
FT                   /evidence="ECO:0000250|UniProtKB:A0A024SNB7"
FT   MOD_RES         23
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:9325098, ECO:0000269|Ref.3"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:A0A024SNB7,
FT                   ECO:0000305|PubMed:9325098"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:A0A024SNB7,
FT                   ECO:0000305|PubMed:9325098"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:A0A024SNB7"
FT   DISULFID        41..47
FT                   /evidence="ECO:0000269|PubMed:9325098,
FT                   ECO:0007744|PDB:1EG1"
FT   DISULFID        71..92
FT                   /evidence="ECO:0000269|PubMed:9325098,
FT                   ECO:0007744|PDB:1EG1"
FT   DISULFID        82..88
FT                   /evidence="ECO:0000269|PubMed:9325098,
FT                   ECO:0007744|PDB:1EG1"
FT   DISULFID        161..360
FT                   /evidence="ECO:0000269|PubMed:9325098,
FT                   ECO:0007744|PDB:1EG1"
FT   DISULFID        193..216
FT                   /evidence="ECO:0000269|PubMed:9325098,
FT                   ECO:0007744|PDB:1EG1"
FT   DISULFID        197..215
FT                   /evidence="ECO:0000269|PubMed:9325098,
FT                   ECO:0007744|PDB:1EG1"
FT   DISULFID        236..241
FT                   /evidence="ECO:0000269|PubMed:9325098,
FT                   ECO:0007744|PDB:1EG1"
FT   DISULFID        246..315
FT                   /evidence="ECO:0000269|PubMed:9325098,
FT                   ECO:0007744|PDB:1EG1"
FT   DISULFID        423..439
FT                   /evidence="ECO:0000269|PubMed:9760165,
FT                   ECO:0007744|PDB:4BMF"
FT   DISULFID        431..448
FT                   /evidence="ECO:0000269|PubMed:9760165,
FT                   ECO:0007744|PDB:4BMF"
FT   DISULFID        442..458
FT                   /evidence="ECO:0000269|PubMed:9760165,
FT                   ECO:0007744|PDB:4BMF"
FT   STRAND          448..454
FT                   /evidence="ECO:0007829|PDB:4BMF"
FT   STRAND          456..458
FT                   /evidence="ECO:0007829|PDB:4BMF"
SQ   SEQUENCE   459 AA;  48208 MW;  D235A256F808CBB9 CRC64;
     MAPSVTLPLT TAILAIARLV AAQQPGTSTP EVHPKLTTYK CTKSGGCVAQ DTSVVLDWNY
     RWMHDANYNS CTVNGGVNTT LCPDEATCGK NCFIEGVDYA ASGVTTSGSS LTMNQYMPSS
     SGGYSSVSPR LYLLDSDGEY VMLKLNGQEL SFDVDLSALP CGENGSLYLS QMDENGGANQ
     YNTAGANYGS GYCDAQCPVQ TWRNGTLNTS HQGFCCNEMD ILEGNSRANA LTPHSCTATA
     CDSAGCGFNP YGSGYKSYYG PGDTVDTSKT FTIITQFNTD NGSPSGNLVS ITRKYQQNGV
     DIPSAQPGGD TISSCPSASA YGGLATMGKA LSSGMVLVFS IWNDNSQYMN WLDSGNAGPC
     SSTEGNPSNI LANNPNTHVV FSNIRWGDIG STTNSTAPPP PPASSTTFST TRRSSTTSSS
     PSCTQTHWGQ CGGIGYSGCK TCTSGTTCQY SNDYYSQCL
//