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P0C2S4

- GUND_CLOTM

UniProt

P0C2S4 - GUND_CLOTM

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Protein

Endoglucanase D

Gene

celD

Organism
Clostridium thermocellum (Ruminiclostridium 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

Sites

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

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 (Ruminiclostridium thermocellum)
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

Pathology & Biotechi

Mutagenesis

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 17›17Add
BLAST
Chaini18 – 625608Endoglucanase DPRO_0000007949Add
BLAST

Structurei

Secondary structure

1
625
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 374Combined sources
Beta strandi44 – 474Combined sources
Beta strandi53 – 586Combined sources
Beta strandi61 – 688Combined sources
Beta strandi70 – 745Combined sources
Turni75 – 784Combined sources
Beta strandi79 – 857Combined sources
Beta strandi93 – 997Combined sources
Turni100 – 1023Combined sources
Beta strandi108 – 1103Combined sources
Turni112 – 1154Combined sources
Helixi116 – 12813Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi142 – 1465Combined sources
Helixi157 – 1604Combined sources
Beta strandi175 – 1773Combined sources
Helixi182 – 19817Combined sources
Helixi200 – 2034Combined sources
Turni211 – 2144Combined sources
Beta strandi215 – 2173Combined sources
Helixi219 – 23113Combined sources
Helixi232 – 2343Combined sources
Beta strandi243 – 2486Combined sources
Helixi258 – 2603Combined sources
Beta strandi266 – 2705Combined sources
Helixi272 – 28918Combined sources
Turni290 – 2923Combined sources
Helixi294 – 31320Combined sources
Helixi336 – 35015Combined sources
Helixi353 – 36311Combined sources
Beta strandi367 – 3704Combined sources
Helixi380 – 38910Combined sources
Helixi397 – 42024Combined sources
Turni426 – 4294Combined sources
Helixi435 – 45218Combined sources
Helixi456 – 46914Combined sources
Beta strandi483 – 4864Combined sources
Helixi494 – 4985Combined sources
Helixi527 – 5304Combined sources
Helixi534 – 54512Combined sources
Turni546 – 5494Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0C2S4.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni561 – 620602 X 24 AA approximate repeatsAdd
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

        10         20         30         40         50
SLTGVFPSGL IETKVSAAKI TENYQFDSRI RLNSIGFIPN HSKKATIAAN
60 70 80 90 100
CSTFYVVKED GTIVYTGTAT SMFDNDTKET VYIADFSSVN EEGTYYLAVP
110 120 130 140 150
GVGKSVNFKI AMNVYEDAFK TAMLGMYLLR CGTSVSATYN GIHYSHGPCH
160 170 180 190 200
TNDAYLDYIN GQHTKKDSTK GWHDAGDYNK YVVNAGITVG SMFLAWEHFK
210 220 230 240 250
DQLEPVALEI PEKNNSIPDF LDELKYEIDW ILTMQYPDGS GRVAHKVSTR
260 270 280 290 300
NFGGFIMPEN EHDERFFVPW SSAATADFVA MTAMAARIFR PYDPQYAEKC
310 320 330 340 350
INAAKVSYEF LKNNPANVFA NQSGFSTGEY ATVSDADDRL WAAAEMWETL
360 370 380 390 400
GDEEYLRDFE NRAAQFSKKI EADFDWDNVA NLGMFTYLLS ERPGKNPALV
410 420 430 440 450
QSIKDSLLST ADSIVRTSQN HGYGRTLGTT YYWGCNGTVV RQTMILQVAN
460 470 480 490 500
KISPNNDYVN AALDAISHVF GRNYYNRSYV TGLGINPPMN PHDRRSGADG
510 520 530 540 550
IWEPWPGYLV GGGWPGPKDW VDIQDSYQTN EIAINWNAAL IYALAGFVNY
560 570 580 590 600
NSPQNEVLYG DVNDDGKVNS TDLTLLKRYV LKAVSTLPSS KAEKNADVNR
610 620
DGRVNSSDVT ILSRYLIRVI EKLPI
Length:625
Mass (Da):69,707
Last modified:April 17, 2007 - v1
Checksum:i6BFD88E2BDF1BD8F
GO

Experimental Info

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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 40 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.Curated

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