GUND_ACETH
ID GUND_ACETH Reviewed; 625 AA.
AC P0C2S4; P04954;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Endoglucanase D;
DE Short=EGD;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase D;
DE AltName: Full=Endo-1,4-beta-glucanase;
DE Flags: Precursor; Fragment;
GN Name=celD;
OS Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium
OS thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1515;
RN [1]
RP CALCIUM-BINDING DATA.
RX PubMed=2302168; DOI=10.1042/bj2650261;
RA Chauvaux S., Beguin P., Aubert J.-P., Bhat K.M., Gow L.A., Wood T.M.,
RA Bairoch A.;
RT "Calcium-binding affinity and calcium-enhanced activity of Clostridium
RT thermocellum endoglucanase D.";
RL Biochem. J. 265:261-265(1990).
RN [2]
RP ACTIVE SITE HIS-492, AND MUTAGENESIS OF HISTIDINE RESIDUES.
RX PubMed=2037583; DOI=10.1016/s0021-9258(18)99227-6;
RA Tomme P., Chauvaux S., Beguin P., Millet J., Aubert J.-P., Claeyssens M.;
RT "Identification of a histidyl residue in the active center of endoglucanase
RT D from Clostridium thermocellum.";
RL J. Biol. Chem. 266:10313-10318(1991).
RN [3]
RP ACTIVE SITE GLU-531, AND MUTAGENESIS OF ASPARTIC ACID AND GLUTAMIC ACID
RP RESIDUES.
RX PubMed=1537833; DOI=10.1016/s0021-9258(18)42857-8;
RA Chauvaux S., Beguin P., Aubert J.-P.;
RT "Site-directed mutagenesis of essential carboxylic residues in Clostridium
RT thermocellum endoglucanase CelD.";
RL J. Biol. Chem. 267:4472-4478(1992).
RN [4]
RP ACTIVE SITE ASP-522.
RX PubMed=1637316; DOI=10.1042/bj2850319;
RA Tomme P., van Beeumen J., Claeyssens M.;
RT "Modification of catalytically important carboxy residues in endoglucanase
RT D from Clostridium thermocellum.";
RL Biochem. J. 285:319-324(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RA Juy M., Amit A.G., Alzari P.M., Poljak R.J., Claeyssens M., Beguin P.,
RA Aubert J.-P.;
RT "Three-dimensional structure of a thermostable bacterial cellulase.";
RL Nature 357:89-91(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=7739036; DOI=10.1016/s0022-2836(95)80045-x;
RA Chitarra V., Souchon H., Spinelli S., Juy M., Beguin P., Alzari P.M.;
RT "Multiple crystal forms of endoglucanase CelD: signal peptide residues
RT modulate lattice formation.";
RL J. Mol. Biol. 248:225-232(1995).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 AND 2.3 ANGSTROMS) OF MUTANT GLN-116.
RX PubMed=8632467; DOI=10.1006/jmbi.1996.0222;
RA Dominguez R., Souchon H., Lascombe M.-B., Alzari P.M.;
RT "The crystal structure of a family 5 endoglucanase mutant in complexed and
RT uncomplexed forms reveals an induced fit activation mechanism.";
RL J. Mol. Biol. 257:1042-1051(1996).
CC -!- FUNCTION: This enzyme catalyzes the endohydrolysis of 1,4-beta-
CC glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
CC -!- CAUTION: The sequence shown here has been extracted from PDB entry
CC 1CLC. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A25535; CZCLDM.
DR PDB; 1CLC; X-ray; 1.90 A; A=1-625.
DR PDB; 4CJ0; X-ray; 1.10 A; A=1-625.
DR PDB; 4CJ1; X-ray; 1.63 A; A=1-625.
DR PDBsum; 1CLC; -.
DR PDBsum; 4CJ0; -.
DR PDBsum; 4CJ1; -.
DR AlphaFoldDB; P0C2S4; -.
DR SMR; P0C2S4; -.
DR EvolutionaryTrace; P0C2S4; -.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02850; E_set_Cellulase_N; 1.
DR Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR004197; Cellulase_Ig-like.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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 InterPro; IPR014756; Ig_E-set.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
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; Calcium; Carbohydrate metabolism; Cellulose degradation;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL <1..17
FT CHAIN 18..625
FT /note="Endoglucanase D"
FT /id="PRO_0000007949"
FT DOMAIN 555..625
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT ACT_SITE 177
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 492
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059,
FT ECO:0000269|PubMed:2037583"
FT ACT_SITE 522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060,
FT ECO:0000269|PubMed:1637316"
FT ACT_SITE 531
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060,
FT ECO:0000269|PubMed:1537833"
FT MUTAGEN 41
FT /note="H->A: 79% of wild-type activity."
FT MUTAGEN 143
FT /note="H->A: 104% of wild-type activity."
FT MUTAGEN 146
FT /note="H->A: 77% of wild-type activity."
FT MUTAGEN 150
FT /note="H->A: 2% of wild-type activity."
FT MUTAGEN 163
FT /note="H->A: 124% of wild-type activity."
FT MUTAGEN 173
FT /note="H->A: 8% of wild-type activity."
FT MUTAGEN 174
FT /note="D->A: 0.08% of wild-type activity."
FT MUTAGEN 177
FT /note="D->A: 0.2% of wild-type activity."
FT MUTAGEN 198
FT /note="H->S: 17% of wild-type activity."
FT MUTAGEN 222
FT /note="D->A: 72% of wild-type activity."
FT MUTAGEN 245
FT /note="H->A: 90% of wild-type activity."
FT MUTAGEN 262
FT /note="H->A: 19% of wild-type activity."
FT MUTAGEN 293
FT /note="D->A: 98% of wild-type activity."
FT MUTAGEN 337
FT /note="D->A: 86% of wild-type activity."
FT MUTAGEN 421
FT /note="H->S: 32% of wild-type activity."
FT MUTAGEN 468
FT /note="H->A: 9% of wild-type activity."
FT MUTAGEN 492
FT /note="H->S: 25% of wild-type activity."
FT MUTAGEN 493
FT /note="D->A: 0.8% of wild-type activity."
FT MUTAGEN 499
FT /note="D->A: 224% of wild-type activity."
FT MUTAGEN 503
FT /note="E->A: 127% of wild-type activity."
FT MUTAGEN 519
FT /note="D->A: 91% of wild-type activity."
FT MUTAGEN 522
FT /note="D->A: 1% of wild-type activity."
FT MUTAGEN 525
FT /note="D->A: 118% of wild-type activity."
FT MUTAGEN 531
FT /note="E->A: 0.3% of wild-type activity."
FT NON_TER 1
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:4CJ0"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:4CJ0"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4CJ0"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 182..198
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:4CJ0"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:1CLC"
FT HELIX 272..289
FT /evidence="ECO:0007829|PDB:4CJ0"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 294..313
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 336..350
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 380..389
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 397..420
FT /evidence="ECO:0007829|PDB:4CJ0"
FT TURN 426..429
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 435..452
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 456..469
FT /evidence="ECO:0007829|PDB:4CJ0"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 494..498
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 527..530
FT /evidence="ECO:0007829|PDB:4CJ0"
FT HELIX 534..545
FT /evidence="ECO:0007829|PDB:4CJ0"
FT TURN 546..549
FT /evidence="ECO:0007829|PDB:4CJ0"
SQ SEQUENCE 625 AA; 69707 MW; 6BFD88E2BDF1BD8F CRC64;
SLTGVFPSGL IETKVSAAKI TENYQFDSRI RLNSIGFIPN HSKKATIAAN CSTFYVVKED
GTIVYTGTAT SMFDNDTKET VYIADFSSVN EEGTYYLAVP GVGKSVNFKI AMNVYEDAFK
TAMLGMYLLR CGTSVSATYN GIHYSHGPCH TNDAYLDYIN GQHTKKDSTK GWHDAGDYNK
YVVNAGITVG SMFLAWEHFK DQLEPVALEI PEKNNSIPDF LDELKYEIDW ILTMQYPDGS
GRVAHKVSTR NFGGFIMPEN EHDERFFVPW SSAATADFVA MTAMAARIFR PYDPQYAEKC
INAAKVSYEF LKNNPANVFA NQSGFSTGEY ATVSDADDRL WAAAEMWETL GDEEYLRDFE
NRAAQFSKKI EADFDWDNVA NLGMFTYLLS ERPGKNPALV QSIKDSLLST ADSIVRTSQN
HGYGRTLGTT YYWGCNGTVV RQTMILQVAN KISPNNDYVN AALDAISHVF GRNYYNRSYV
TGLGINPPMN PHDRRSGADG IWEPWPGYLV GGGWPGPKDW VDIQDSYQTN EIAINWNAAL
IYALAGFVNY NSPQNEVLYG DVNDDGKVNS TDLTLLKRYV LKAVSTLPSS KAEKNADVNR
DGRVNSSDVT ILSRYLIRVI EKLPI
