GUN1_HYPJE
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 03-AUG-2022, entry version 140.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 iPTMnet; P07981; -.
DR VEuPathDB; FungiDB:TrQ_002418; -.
DR OMA; NEMDILE; -.
DR BioCyc; MetaCyc:MON-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; -; 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; PTHR33753; 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; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 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
