GUN4_THEFU
ID GUN4_THEFU Reviewed; 880 AA.
AC P26221; Q08167;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Endoglucanase E-4;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase E-4;
DE AltName: Full=Cellulase E4;
DE AltName: Full=Endo-1,4-beta-glucanase E-4;
DE Flags: Precursor;
GN Name=celD;
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=8215374; DOI=10.1128/aem.59.9.3032-3043.1993;
RA Jung E.D., Lao G., Irwin D., Barr B.K., Benjamin A., Wilson D.B.;
RT "DNA sequences and expression in Streptomyces lividans of an exoglucanase
RT gene and an endoglucanase gene from Thermomonospora fusca.";
RL Appl. Environ. Microbiol. 59:3032-3043(1993).
RN [2]
RP SEQUENCE REVISION.
RA Wilson D.B.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PARTIAL 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 [4]
RP PROTEIN SEQUENCE OF 47-67.
RA Wilson D.B.;
RT "Cellulases of Thermomonospora fusca.";
RL Methods Enzymol. 160:314-323(1988).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 47-651.
RX PubMed=9334746; DOI=10.1038/nsb1097-810;
RA Sakon J., Irwin D., Wilson D.B., Karplus P.A.;
RT "Structure and mechanism of endo/exocellulase E4 from Thermomonospora
RT fusca.";
RL Nat. Struct. Biol. 4:810-818(1997).
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 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
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DR EMBL; L20093; AAB42155.1; -; Genomic_DNA.
DR PIR; B42360; B42360.
DR RefSeq; WP_011292599.1; NZ_JEMR01000003.1.
DR PDB; 1JS4; X-ray; 2.00 A; A/B=47-651.
DR PDB; 1TF4; X-ray; 1.90 A; A/B=47-651.
DR PDB; 3TF4; X-ray; 2.20 A; A/B=47-651.
DR PDB; 4TF4; X-ray; 2.00 A; A/B=47-651.
DR PDBsum; 1JS4; -.
DR PDBsum; 1TF4; -.
DR PDBsum; 3TF4; -.
DR PDBsum; 4TF4; -.
DR AlphaFoldDB; P26221; -.
DR SMR; P26221; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR OMA; RWLDYWT; -.
DR BRENDA; 3.2.1.4; 6298.
DR BRENDA; 3.2.1.B42; 6298.
DR UniPathway; UPA00696; -.
DR EvolutionaryTrace; P26221; -.
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-UniPathway.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.40.710; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_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; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM01067; CBM_3; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49384; SSF49384; 2.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS51172; CBM3; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 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..46
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 47..880
FT /note="Endoglucanase E-4"
FT /id="PRO_0000007959"
FT DOMAIN 504..652
FT /note="CBM3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT DOMAIN 678..770
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 771..880
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 647..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 427
FT /evidence="ECO:0000250"
FT ACT_SITE 461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:1TF4"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 109..125
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 196..213
FT /evidence="ECO:0007829|PDB:1TF4"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 218..237
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 259..273
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1JS4"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:1TF4"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 361..378
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 382..400
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:1TF4"
FT TURN 466..469
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 473..476
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 477..490
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 508..517
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 520..531
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 542..550
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:1JS4"
FT STRAND 582..588
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:1TF4"
FT TURN 599..602
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 603..611
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:1TF4"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 637..641
FT /evidence="ECO:0007829|PDB:1TF4"
FT STRAND 644..648
FT /evidence="ECO:0007829|PDB:1TF4"
SQ SEQUENCE 880 AA; 95203 MW; 5EA9A6ABF45A4D9A CRC64;
MSVTEPPPRR RGRHSRARRF LTSLGATAAL TAGMLGVPLA TGTAHAEPAF NYAEALQKSM
FFYEAQRSGK LPENNRVSWR GDSGLNDGAD VGLDLTGGWY DAGDHVKFGF PMAFTATMLA
WGAIESPEGY IRSGQMPYLK DNLRWVNDYF IKAHPSPNVL YVQVGDGDAD HKWWGPAEVM
PMERPSFKVD PSCPGSDVAA ETAAAMAASS IVFADDDPAY AATLVQHAKQ LYTFADTYRG
VYSDCVPAGA FYNSWSGYQD ELVWGAYWLY KATGDDSYLA KAEYEYDFLS TEQQTDLRSY
RWTIAWDDKS YGTYVLLAKE TGKQKYIDDA NRWLDYWTVG VNGQRVPYSP GGMAVLDTWG
ALRYAANTAF VALVYAKVID DPVRKQRYHD FAVRQINYAL GDNPRNSSYV VGFGNNPPRN
PHHRTAHGSW TDSIASPAEN RHVLYGALVG GPGSPNDAYT DDRQDYVANE VATDYNAGFS
SALAMLVEEY GGTPLADFPP TEEPDGPEIF VEAQINTPGT TFTEIKAMIR NQSGWPARML
DKGTFRYWFT LDEGVDPADI TVSSAYNQCA TPEDVHHVSG DLYYVEIDCT GEKIFPGGQS
EHRREVQFRI AGGPGWDPSN DWSFQGIGNE LAPAPYIVLY DDGVPVWGTA PEEGEEPGGG
EGPGGGEEPG EDVTPPSAPG SPAVRDVTST SAVLTWSASS DTGGSGVAGY DVFLRAGTGQ
EQKVGSTTRT SFTLTGLEPD TTYIAAVVAR DNAGNVSQRS TVSFTTLAEN GGGPDASCTV
GYSTNDWDSG FTASIRITYH GTAPLSSWEL SFTFPAGQQV THGWNATWRQ DGAAVTATPM
SWNSSLAPGA TVEVGFNGSW SGSNTPPTDF TLNGEPCALA
