GUN1_HUMIN
ID GUN1_HUMIN Reviewed; 402 AA.
AC P56680;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Endoglucanase 1;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase 1;
DE AltName: Full=Endo-1,4-beta-glucanase 1;
DE AltName: Full=Endoglucanase I;
GN Name=CEL7B;
OS Humicola insolens (Soft-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Humicola.
OX NCBI_TaxID=34413;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT TRP-37/TRP-39, AND
RP PYROGLUTAMATE FORMATION AT GLN-1.
RX PubMed=9335168; DOI=10.1016/s0168-1656(97)00092-8;
RA Davies G.J., Ducros V., Lewis R.J., Borchert T.V., Schuelein M.;
RT "Oligosaccharide specificity of a family 7 endoglucanase: insertion of
RT potential sugar-binding subsites.";
RL J. Biotechnol. 57:91-100(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND MUTAGENESIS.
RX PubMed=9761741; DOI=10.1042/bj3350409;
RA MacKenzie L.F., Sulzenbacher G., Divne C., Jones T.A., Woeldike H.F.,
RA Schuelein M., Withers S.G., Davies G.J.;
RT "Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola
RT insolens at 2.2 A resolution and identification of the catalytic
RT nucleophile by trapping of the covalent glycosyl-enzyme intermediate.";
RL Biochem. J. 335:409-416(1998).
CC -!- FUNCTION: The biological conversion of cellulose to glucose generally
CC requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC cut the disaccharide cellobiose from the non-reducing end of the
CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC cellobiose and other short cello-oligosaccharides to glucose.
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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000305}.
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DR PDB; 1A39; X-ray; 2.20 A; A=2-402.
DR PDB; 1DYM; X-ray; 1.75 A; A=2-402.
DR PDB; 1OJI; X-ray; 2.15 A; A=2-402.
DR PDB; 1OJJ; X-ray; 1.40 A; A/B=2-402.
DR PDB; 1OJK; X-ray; 1.50 A; A/B=2-402.
DR PDB; 2A39; X-ray; 2.20 A; A/B=2-398.
DR PDB; 6YOZ; X-ray; 1.88 A; AAA/BBB=2-400.
DR PDB; 6YP1; X-ray; 1.20 A; AAA=1-402.
DR PDBsum; 1A39; -.
DR PDBsum; 1DYM; -.
DR PDBsum; 1OJI; -.
DR PDBsum; 1OJJ; -.
DR PDBsum; 1OJK; -.
DR PDBsum; 2A39; -.
DR PDBsum; 6YOZ; -.
DR PDBsum; 6YP1; -.
DR AlphaFoldDB; P56680; -.
DR SMR; P56680; -.
DR Allergome; 8280; Hum in Cellulase.
DR CAZy; GH7; Glycoside Hydrolase Family 7.
DR CLAE; EGL7B_HUMIN; -.
DR BioCyc; MetaCyc:MON-17623; -.
DR EvolutionaryTrace; P56680; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
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; 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; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Pyrrolidone carboxylic acid; Secreted.
FT CHAIN 1..402
FT /note="Endoglucanase 1"
FT /id="PRO_0000184057"
FT ACT_SITE 197
FT /note="Nucleophile"
FT ACT_SITE 202
FT /note="Proton donor"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:9335168"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 18..24
FT DISULFID 51..73
FT DISULFID 63..69
FT DISULFID 140..365
FT DISULFID 172..195
FT DISULFID 176..194
FT DISULFID 215..234
FT DISULFID 223..228
FT DISULFID 239..315
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1OJJ"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 23..33
FT /evidence="ECO:0007829|PDB:1OJJ"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1OJJ"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1OJJ"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1OJJ"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:1OJJ"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:1OJI"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1OJJ"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1OJJ"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 280..289
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1OJJ"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:1OJJ"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:1OJJ"
FT HELIX 328..338
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:1OJJ"
FT TURN 350..354
FT /evidence="ECO:0007829|PDB:1OJJ"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:1OJJ"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:1OJJ"
FT TURN 367..370
FT /evidence="ECO:0007829|PDB:1OJJ"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:1OJJ"
FT STRAND 383..393
FT /evidence="ECO:0007829|PDB:1OJJ"
SQ SEQUENCE 402 AA; 44577 MW; E0C6D31375D1635F CRC64;
QKPGETKEVH PQLTTFRCTK RGGCKPATNF IVLDSLSHPI HRAEGLGPGG CGDWGNPPPK
DVCPDVESCA KNCIMEGIPD YSQYGVTTNG TSLRLQHILP DGRVPSPRVY LLDKTKRRYE
MLHLTGFEFT FDVDATKLPC GMNSALYLSE MHPTGAKSKY NPGGAYYGTG YCDAQCFVTP
FINGLGNIEG KGSCCNEMDI WEANSRASHV APHTCNKKGL YLCEGEECAF EGVCDKNGCG
WNNYRVNVTD YYGRGEEFKV NTLKPFTVVT QFLANRRGKL EKIHRFYVQD GKVIESFYTN
KEGVPYTNMI DDEFCEATGS RKYMELGATQ GMGEALTRGM VLAMSIWWDQ GGNMEWLDHG
EAGPCAKGEG APSNIVQVEP FPEVTYTNLR WGEIGSTYQE LQ
