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P0C2S4

- GUND_CLOTM

UniProt

P0C2S4 - GUND_CLOTM

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Protein
Endoglucanase D
Gene
celD
Organism
Clostridium thermocellum
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Cofactori

Calcium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei177 – 1771Nucleophile
Active sitei492 – 49211 Publication
Active sitei522 – 52211 Publication
Active sitei531 – 5311Proton donor1 Publication

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase D (EC:3.2.1.4)
Short name:
EGD
Alternative name(s):
Cellulase D
Endo-1,4-beta-glucanase
Gene namesi
Name:celD
OrganismiClostridium thermocellum
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411H → A: 79% of wild-type activity. 2 Publications
Mutagenesisi143 – 1431H → A: 104% of wild-type activity. 2 Publications
Mutagenesisi146 – 1461H → A: 77% of wild-type activity. 2 Publications
Mutagenesisi150 – 1501H → A: 2% of wild-type activity. 2 Publications
Mutagenesisi163 – 1631H → A: 124% of wild-type activity. 2 Publications
Mutagenesisi173 – 1731H → A: 8% of wild-type activity. 2 Publications
Mutagenesisi174 – 1741D → A: 0.08% of wild-type activity. 2 Publications
Mutagenesisi177 – 1771D → A: 0.2% of wild-type activity. 2 Publications
Mutagenesisi198 – 1981H → S: 17% of wild-type activity. 2 Publications
Mutagenesisi222 – 2221D → A: 72% of wild-type activity. 2 Publications
Mutagenesisi245 – 2451H → A: 90% of wild-type activity. 2 Publications
Mutagenesisi262 – 2621H → A: 19% of wild-type activity. 2 Publications
Mutagenesisi293 – 2931D → A: 98% of wild-type activity. 2 Publications
Mutagenesisi337 – 3371D → A: 86% of wild-type activity. 2 Publications
Mutagenesisi421 – 4211H → S: 32% of wild-type activity. 2 Publications
Mutagenesisi468 – 4681H → A: 9% of wild-type activity. 2 Publications
Mutagenesisi492 – 4921H → S: 25% of wild-type activity. 2 Publications
Mutagenesisi493 – 4931D → A: 0.8% of wild-type activity. 2 Publications
Mutagenesisi499 – 4991D → A: 224% of wild-type activity. 2 Publications
Mutagenesisi503 – 5031E → A: 127% of wild-type activity. 2 Publications
Mutagenesisi519 – 5191D → A: 91% of wild-type activity. 2 Publications
Mutagenesisi522 – 5221D → A: 1% of wild-type activity. 2 Publications
Mutagenesisi525 – 5251D → A: 118% of wild-type activity. 2 Publications
Mutagenesisi531 – 5311E → A: 0.3% of wild-type activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 17›17
Add
BLAST
Chaini18 – 625608Endoglucanase D
PRO_0000007949Add
BLAST

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 374
Beta strandi44 – 474
Beta strandi53 – 586
Beta strandi61 – 688
Beta strandi70 – 745
Turni75 – 784
Beta strandi79 – 857
Beta strandi93 – 997
Turni100 – 1023
Beta strandi108 – 1103
Turni112 – 1154
Helixi116 – 12813
Beta strandi135 – 1395
Beta strandi142 – 1465
Helixi157 – 1604
Beta strandi175 – 1773
Helixi182 – 19817
Helixi200 – 2034
Turni211 – 2144
Beta strandi215 – 2173
Helixi219 – 23113
Helixi232 – 2343
Beta strandi243 – 2486
Helixi258 – 2603
Beta strandi266 – 2705
Helixi272 – 28918
Turni290 – 2923
Helixi294 – 31320
Helixi336 – 35015
Helixi353 – 36311
Beta strandi367 – 3704
Helixi380 – 38910
Helixi397 – 42024
Turni426 – 4294
Helixi435 – 45218
Helixi456 – 46914
Beta strandi483 – 4864
Helixi494 – 4985
Helixi527 – 5304
Helixi534 – 54512
Turni546 – 5494

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CLCX-ray1.90A1-625[»]
4CJ0X-ray1.10A1-625[»]
4CJ1X-ray1.63A1-625[»]
ProteinModelPortaliP0C2S4.
SMRiP0C2S4. Positions 11-551, 556-625.

Miscellaneous databases

EvolutionaryTraceiP0C2S4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati561 – 584241
Add
BLAST
Repeati597 – 620242
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni561 – 620602 X 24 AA approximate repeats
Add
BLAST

Domaini

A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR004197. Glyco_hydro_9_Ig-like.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF02927. CelD_N. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C2S4-1 [UniParc]FASTAAdd to Basket

« Hide

SLTGVFPSGL IETKVSAAKI TENYQFDSRI RLNSIGFIPN HSKKATIAAN    50
CSTFYVVKED GTIVYTGTAT SMFDNDTKET VYIADFSSVN EEGTYYLAVP 100
GVGKSVNFKI AMNVYEDAFK TAMLGMYLLR CGTSVSATYN GIHYSHGPCH 150
TNDAYLDYIN GQHTKKDSTK GWHDAGDYNK YVVNAGITVG SMFLAWEHFK 200
DQLEPVALEI PEKNNSIPDF LDELKYEIDW ILTMQYPDGS GRVAHKVSTR 250
NFGGFIMPEN EHDERFFVPW SSAATADFVA MTAMAARIFR PYDPQYAEKC 300
INAAKVSYEF LKNNPANVFA NQSGFSTGEY ATVSDADDRL WAAAEMWETL 350
GDEEYLRDFE NRAAQFSKKI EADFDWDNVA NLGMFTYLLS ERPGKNPALV 400
QSIKDSLLST ADSIVRTSQN HGYGRTLGTT YYWGCNGTVV RQTMILQVAN 450
KISPNNDYVN AALDAISHVF GRNYYNRSYV TGLGINPPMN PHDRRSGADG 500
IWEPWPGYLV GGGWPGPKDW VDIQDSYQTN EIAINWNAAL IYALAGFVNY 550
NSPQNEVLYG DVNDDGKVNS TDLTLLKRYV LKAVSTLPSS KAEKNADVNR 600
DGRVNSSDVT ILSRYLIRVI EKLPI 625
Length:625
Mass (Da):69,707
Last modified:April 17, 2007 - v1
Checksum:i6BFD88E2BDF1BD8F
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

PIRiA25535. CZCLDM.

Cross-referencesi

Sequence databases

PIRi A25535. CZCLDM.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CLC X-ray 1.90 A 1-625 [» ]
4CJ0 X-ray 1.10 A 1-625 [» ]
4CJ1 X-ray 1.63 A 1-625 [» ]
ProteinModelPortali P0C2S4.
SMRi P0C2S4. Positions 11-551, 556-625.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P0C2S4.

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR018242. Dockerin_1.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR004197. Glyco_hydro_9_Ig-like.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view ]
Pfami PF02927. CelD_N. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Calcium-binding affinity and calcium-enhanced activity of Clostridium thermocellum endoglucanase D."
    Chauvaux S., Beguin P., Aubert J.-P., Bhat K.M., Gow L.A., Wood T.M., Bairoch A.
    Biochem. J. 265:261-265(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING DATA.
  2. "Identification of a histidyl residue in the active center of endoglucanase D from Clostridium thermocellum."
    Tomme P., Chauvaux S., Beguin P., Millet J., Aubert J.-P., Claeyssens M.
    J. Biol. Chem. 266:10313-10318(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE HIS-492, MUTAGENESIS OF HISTIDINE RESIDUES.
  3. "Site-directed mutagenesis of essential carboxylic residues in Clostridium thermocellum endoglucanase CelD."
    Chauvaux S., Beguin P., Aubert J.-P.
    J. Biol. Chem. 267:4472-4478(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE GLU-531, MUTAGENESIS OF ASPARTIC ACID AND GLUTAMIC ACID RESIDUES.
  4. "Modification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum."
    Tomme P., van Beeumen J., Claeyssens M.
    Biochem. J. 285:319-324(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE ASP-522.
  5. "Three-dimensional structure of a thermostable bacterial cellulase."
    Juy M., Amit A.G., Alzari P.M., Poljak R.J., Claeyssens M., Beguin P., Aubert J.-P.
    Nature 357:89-91(1992)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  6. "Multiple crystal forms of endoglucanase CelD: signal peptide residues modulate lattice formation."
    Chitarra V., Souchon H., Spinelli S., Juy M., Beguin P., Alzari P.M.
    J. Mol. Biol. 248:225-232(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  7. "The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism."
    Dominguez R., Souchon H., Lascombe M.-B., Alzari P.M.
    J. Mol. Biol. 257:1042-1051(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 AND 2.3 ANGSTROMS) OF MUTANT GLN-116.

Entry informationi

Entry nameiGUND_CLOTM
AccessioniPrimary (citable) accession number: P0C2S4
Secondary accession number(s): P04954
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: September 3, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The sequence shown here has been extracted from PDB entry 1CLC.

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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