GUN5_THEFU
ID GUN5_THEFU Reviewed; 466 AA.
AC Q01786;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 02-JUN-2021, entry version 112.
DE RecName: Full=Endoglucanase E-5;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase E-5;
DE AltName: Full=Cellulase E5;
DE AltName: Full=Endo-1,4-beta-glucanase E-4;
DE Flags: Precursor;
GN Name=celE;
OS Thermobifida fusca (Thermomonospora fusca).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=2021;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=1904434; DOI=10.1128/jb.173.11.3397-3407.1991;
RA Lao G., Ghangas G.S., Jung E.D., Wilson D.B.;
RT "DNA sequences of three beta-1,4-endoglucanase genes from Thermomonospora
RT fusca.";
RL J. Bacteriol. 173:3397-3407(1991).
RN [2]
RP SEQUENCE REVISION.
RA Lao G., Ghangas G.S., Jung E.D., Wilson D.B.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 137-142 AND 157-166.
RC STRAIN=YX;
RA Irwin D.C., Spezio M., Walker L.P., Wilson D.B.;
RT "Activity studies of eight purified cellulases: specificity, synergism, and
RT binding domain effects.";
RL Biotechnol. Bioeng. 42:1002-1013(1993).
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; L01577; AAC09379.1; -; Genomic_DNA.
DR PIR; C42360; C42360.
DR PDB; 2CKR; X-ray; 1.77 A; A/B=161-466.
DR PDB; 2CKS; X-ray; 1.60 A; A/B=161-466.
DR PDBsum; 2CKR; -.
DR PDBsum; 2CKS; -.
DR SMR; Q01786; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR UniPathway; UPA00696; -.
DR EvolutionaryTrace; Q01786; -.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51173; CBM2; 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; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..36
FT CHAIN 37..466
FT /note="Endoglucanase E-5"
FT /id="PRO_0000007866"
FT DOMAIN 37..139
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 113..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 299
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT ACT_SITE 391
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:2CKS"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2CKS"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:2CKS"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:2CKS"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 235..250
FT /evidence="ECO:0007829|PDB:2CKS"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:2CKS"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 272..286
FT /evidence="ECO:0007829|PDB:2CKS"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 305..322
FT /evidence="ECO:0007829|PDB:2CKS"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 347..351
FT /evidence="ECO:0007829|PDB:2CKS"
FT STRAND 357..366
FT /evidence="ECO:0007829|PDB:2CKS"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:2CKS"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 405..418
FT /evidence="ECO:0007829|PDB:2CKS"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:2CKS"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:2CKS"
FT HELIX 455..465
FT /evidence="ECO:0007829|PDB:2CKS"
SQ SEQUENCE 466 AA; 49801 MW; 1CF0ADFBF2DEF82E CRC64;
MAKSPAARKG XPPVAVAVTA ALALLIALLS PGVAQAAGLT ATVTKESSWD NGYSASVTVR
NDTSSTVSQW EVVLTLPGGT TVAQVWNAQH TSSGNSHTFT GVSWNSTIPP GGTASSGFIA
SGSGEPTHCT INGAPCDEGS EPGGPGGPGT PSPDPGTQPG TGTPVERYGK VQVCGTQLCD
EHGNPVQLRG MSTHGIQWFD HCLTDSSLDA LAYDWKADII RLSMYIQEDG YETNPRGFTD
RMHQLIDMAT ARGLYVIVDW HILTPGDPHY NLDRAKTFFA EIAQRHASKT NVLYEIANEP
NGVSWASIKS YAEEVIPVIR QRDPDSVIIV GTRGWSSLGV SEGSGPAEIA ANPVNASNIM
YAFHFYAASH RDNYLNALRE ASELFPVFVT EFGTETYTGD GANDFQMADR YIDLMAERKI
GWTKWNYSDD FRSGAVFQPG TCASGGPWSG SSLKASGQWV RSKLQS
