GUN5_HUMIN
ID GUN5_HUMIN Reviewed; 213 AA.
AC P43316;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Endoglucanase-5;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase V;
DE AltName: Full=Endo-1,4-beta-glucanase V;
DE Short=EG V;
DE AltName: Full=Endoglucanase V;
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 NUCLEOTIDE SEQUENCE.
RA Rasmussen G., Mikkelsen J.-M., Schuelein M., Patkar S.A., Hagen F.,
RA Hjort C.M., Hastrup S.;
RT "A cellulase preparation comprising an endoglucanase enzyme.";
RL Patent number WO9117243, 14-NOV-1991.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=8377830; DOI=10.1038/365362a0;
RA Davies G.J., Dodson G.G., Hubbard R.E., Tolley S.P., Dauter Z.,
RA Wilson K.S., Hjort C., Mikkelsen J.M., Rasmussen G., Schuelein M.;
RT "Structure and function of endoglucanase V.";
RL Nature 365:362-364(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=8519779; DOI=10.1021/bi00049a037;
RA Davies G.J., Tolley S.P., Henrissat B., Hjort C., Schuelein M.;
RT "Structures of oligosaccharide-bound forms of the endoglucanase V from
RT Humicola insolens at 1.9-A resolution.";
RL Biochemistry 34:16210-16220(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=15299721; DOI=10.1107/s0907444995009280;
RA Davies G.J., Dodson G.G., Moore M.H., Tolley S.P., Dauter Z., Wilson K.S.,
RA Rasmussen G., Schuelein M.;
RT "Structure determination and refinement of the Humicola insolens
RT endoglucanase V at 1.5-A resolution.";
RL Acta Crystallogr. D 52:7-17(1996).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family.
CC {ECO:0000305}.
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DR PDB; 1HD5; X-ray; 1.66 A; A=5-213.
DR PDB; 2ENG; X-ray; 1.50 A; A=1-210.
DR PDB; 3ENG; X-ray; 1.90 A; A=1-213.
DR PDB; 4ENG; X-ray; 1.90 A; A=1-210.
DR PDBsum; 1HD5; -.
DR PDBsum; 2ENG; -.
DR PDBsum; 3ENG; -.
DR PDBsum; 4ENG; -.
DR AlphaFoldDB; P43316; -.
DR SMR; P43316; -.
DR BindingDB; P43316; -.
DR ChEMBL; CHEMBL1795107; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH45; Glycoside Hydrolase Family 45.
DR EvolutionaryTrace; P43316; -.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.40.40.10; -; 1.
DR InterPro; IPR000334; Glyco_hydro_45.
DR InterPro; IPR036908; RlpA-like_sf.
DR Pfam; PF02015; Glyco_hydro_45; 1.
DR SUPFAM; SSF50685; SSF50685; 1.
DR PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase;
KW Hydrolase; Polysaccharide degradation.
FT CHAIN 1..213
FT /note="Endoglucanase-5"
FT /id="PRO_0000184074"
FT ACT_SITE 10
FT /note="Nucleophile"
FT ACT_SITE 121
FT /note="Proton donor"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2ENG"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2ENG"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2ENG"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2ENG"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:2ENG"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2ENG"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:2ENG"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2ENG"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:2ENG"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:2ENG"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1HD5"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:2ENG"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2ENG"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2ENG"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:2ENG"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:2ENG"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:2ENG"
FT TURN 172..176
FT /evidence="ECO:0007829|PDB:3ENG"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:2ENG"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:2ENG"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2ENG"
SQ SEQUENCE 213 AA; 22864 MW; 24334301BA3BC804 CRC64;
ADGRSTRYWD CCKPSCGWAK KAPVNQPVFS CNANFQRITD FDAKSGCEPG GVAYSCADQT
PWAVNDDFAL GFAATSIAGS NEAGWCCACY ELTFTSGPVA GKKMVVQSTS TGGDLGSNHF
DLNIPGGGVG IFDGCTPQFG GLPGQRYGGI SSRNECDRFP DALKPGCYWR FDWFKNADNP
SFSFRQVQCP AELVARTGCR RNDDGNFPAV QIP
