GUN2_HYPJE
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 03-AUG-2022, entry version 127.
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}.
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; 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 BioCyc; MetaCyc:MON-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 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 Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF57180; SSF57180; 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
