GUN2_THEFU
ID GUN2_THEFU Reviewed; 441 AA.
AC P26222;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Endoglucanase E-2;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase E-2;
DE AltName: Full=Cellulase E2;
DE AltName: Full=Endo-1,4-beta-glucanase E-2;
DE Flags: Precursor;
GN Name=celB;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=YX;
RA Jung E.D., Lao G., Irwin D., Barr B., Benjamin A., Wilson D.B.;
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 32-47.
RA Wilson D.B.;
RT "Cellulases of Thermomonospora fusca.";
RL Methods Enzymol. 160:314-323(1988).
RN [4]
RP SUBUNIT, AND MUTAGENESIS OF GLU-163.
RX PubMed=8347613; DOI=10.1021/bi00083a013;
RA McGinnis K., Kroupis C., Wilson D.B.;
RT "Dimerization of Thermomonospora fusca beta-1,4-endoglucanase E2.";
RL Biochemistry 32:8146-8150(1993).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 32-317.
RX PubMed=8399160; DOI=10.1021/bi00089a006;
RA Spezio M., Wilson D.B., Karplus P.A.;
RT "Crystal structure of the catalytic domain of a thermophilic
RT endocellulase.";
RL Biochemistry 32:9906-9916(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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8347613}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
CC {ECO:0000305}.
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DR EMBL; M73321; AAC06388.1; -; mRNA.
DR PIR; A42360; A42360.
DR PIR; T12011; T12011.
DR RefSeq; WP_011291521.1; NZ_JEMR01000002.1.
DR PDB; 1TML; X-ray; 1.80 A; A=32-317.
DR PDB; 2BOD; X-ray; 1.50 A; X=32-317.
DR PDB; 2BOE; X-ray; 1.15 A; X=32-317.
DR PDB; 2BOF; X-ray; 1.64 A; X=32-317.
DR PDB; 2BOG; X-ray; 1.04 A; X=32-317.
DR PDB; 3RPT; X-ray; 1.30 A; A/X=33-103, A/X=128-145, A/X=169-317.
DR PDBsum; 1TML; -.
DR PDBsum; 2BOD; -.
DR PDBsum; 2BOE; -.
DR PDBsum; 2BOF; -.
DR PDBsum; 2BOG; -.
DR PDBsum; 3RPT; -.
DR AlphaFoldDB; P26222; -.
DR SMR; P26222; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR OMA; SNVSNFH; -.
DR UniPathway; UPA00696; -.
DR EvolutionaryTrace; P26222; -.
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 Gene3D; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF51989; SSF51989; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..31
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|Ref.3"
FT CHAIN 32..441
FT /note="Endoglucanase E-2"
FT /id="PRO_0000007909"
FT DOMAIN 339..441
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 32..320
FT /note="Catalytic"
FT REGION 317..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..340
FT /note="Linker"
FT COMPBIAS 323..341
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 110
FT ACT_SITE 148
FT /note="Proton donor"
FT ACT_SITE 296
FT /note="Nucleophile"
FT DISULFID 111..156
FT DISULFID 263..298
FT DISULFID 346..438
FT /evidence="ECO:0000255"
FT MUTAGEN 163
FT /note="E->G: Loss of ability to form dimers."
FT /evidence="ECO:0000269|PubMed:8347613"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2BOG"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:2BOG"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:2BOG"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2BOG"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2BOG"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:2BOG"
FT HELIX 81..95
FT /evidence="ECO:0007829|PDB:2BOG"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2BOG"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2BOD"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1TML"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2BOE"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:2BOG"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:2BOG"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2BOG"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:2BOG"
FT HELIX 158..178
FT /evidence="ECO:0007829|PDB:2BOG"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:2BOG"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:2BOG"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:2BOG"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:2BOG"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:2BOG"
FT HELIX 225..239
FT /evidence="ECO:0007829|PDB:2BOG"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:2BOG"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:2BOG"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:2BOG"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:2BOG"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:2BOG"
SQ SEQUENCE 441 AA; 45844 MW; 87218E4537092AE5 CRC64;
MSPRPLRALL GAAAAALVSA AALAFPSQAA ANDSPFYVNP NMSSAEWVRN NPNDPRTPVI
RDRIASVPQG TWFAHHNPGQ ITGQVDALMS AAQAAGKIPI LVVYNAPGRD CGNHSSGGAP
SHSAYRSWID EFAAGLKNRP AYIIVEPDLI SLMSSCMQHV QQEVLETMAY AGKALKAGSS
QARIYFDAGH SAWHSPAQMA SWLQQADISN SAHGIATNTS NYRWTADEVA YAKAVLSAIG
NPSLRAVIDT SRNGNGPAGN EWCDPSGRAI GTPSTTNTGD PMIDAFLWIK LPGEADGCIA
GAGQFVPQAA YEMAIAAGGT NPNPNPNPTP TPTPTPTPPP GSSGACTATY TIANEWNDGF
QATVTVTANQ NITGWTVTWT FTDGQTITNA WNADVSTSGS SVTARNVGHN GTLSQGASTE
FGFVGSKGNS NSVPTLTCAA S
