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Protein

Endoglucanase D

Gene

celD

Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
Status
Reviewed-Annotation score: Annotation score: 3 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.By similarity

Catalytic activityi

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

Cofactori

Ca2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei201NucleophilePROSITE-ProRule annotation1
Active sitei516By similarity1
Active sitei546By similarity1
Active sitei555Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16416.

Protein family/group databases

CAZyiGH9. Glycoside Hydrolase Family 9.

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
Ordered Locus Names:Cthe_0825
OrganismiClostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
Taxonomic identifieri203119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
Proteomesi
  • UP000002145 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 41By similarityAdd BLAST41
ChainiPRO_000028472242 – 649Endoglucanase DAdd BLAST608

Proteomic databases

PRIDEiA3DDN1.

Interactioni

Protein-protein interaction databases

STRINGi203119.Cthe_0825.

Structurei

Secondary structure

1649
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi594 – 604Combined sources11
Helixi614 – 620Combined sources7
Helixi630 – 640Combined sources11
Beta strandi643 – 645Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FL4X-ray2.90A/D/G/J584-649[»]
ProteinModelPortaliA3DDN1.
SMRiA3DDN1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA3DDN1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini579 – 649DockerinPROSITE-ProRule annotationAdd BLAST71

Sequence similaritiesi

Contains 1 dockerin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105E08. Bacteria.
ENOG410XNTA. LUCA.
HOGENOMiHOG000245359.
KOiK01179.
OMAiCSYASNE.
OrthoDBiPOG091H04TS.

Family and domain databases

CDDicd02850. E_set_Cellulase_N. 1 hit.
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.
IPR004197. Cellulase_Ig-like.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR001701. Glyco_hydro_9.
IPR033126. Glyco_hydro_9_Asp/Glu_AS.
IPR018221. Glyco_hydro_9_His_AS.
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.
PS51766. DOCKERIN. 1 hit.
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: Complete.

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

A3DDN1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRMTLKSSM KKRVLSLLIA VVFLSLTGVF PSGLIETKVS AAKITENYQF
60 70 80 90 100
DSRIRLNSIG FIPNHSKKAT IAANCSTFYV VKEDGTIVYT GTATSMFDND
110 120 130 140 150
TKETVYIADF SSVNEEGTYY LAVPGVGKSV NFKIAMNVYE DAFKTAMLGM
160 170 180 190 200
YLLRCGTSVS ATYNGIHYSH GPCHTNDAYL DYINGQHTKK DSTKGWHDAG
210 220 230 240 250
DYNKYVVNAG ITVGSMFLAW EHFKDQLEPV ALEIPEKNNS IPDFLDELKY
260 270 280 290 300
EIDWILTMQY PDGSGRVAHK VSTRNFGGFI MPENEHDERF FVPWSSAATA
310 320 330 340 350
DFVAMTAMAA RIFRPYDPQY AEKCINAAKV SYEFLKNNPA NVFANQSGFS
360 370 380 390 400
TGEYATVSDA DDRLWAAAEM WETLGDEEYL RDFENRAAQF SKKIEADFDW
410 420 430 440 450
DNVANLGMFT YLLSERPGKN PALVQSIKDS LLSTADSIVR TSQNHGYGRT
460 470 480 490 500
LGTTYYWGCN GTVVRQTMIL QVANKISPNN DYVNAALDAI SHVFGRNYYN
510 520 530 540 550
RSYVTGLGIN PPMNPHDRRS GADGIWEPWP GYLVGGGWPG PKDWVDIQDS
560 570 580 590 600
YQTNEIAINW NAALIYALAG FVNYNSAQNE VLYGDVNDDG KVNSTDLTLL
610 620 630 640
KRYVLKAVST LPSSKAEKNA DVNRDGRVNS SDVTILSRYL IRVIEKLPI
Length:649
Mass (Da):72,415
Last modified:March 20, 2007 - v1
Checksum:i3A6A44735B29D3F4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti577A → P in CAA28255 (PubMed:3024110).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04584 Genomic DNA. Translation: CAA28255.1.
CP000568 Genomic DNA. Translation: ABN52060.1.
PIRiA25535. CZCLDM.
RefSeqiWP_011837914.1. NC_009012.1.

Genome annotation databases

EnsemblBacteriaiABN52060; ABN52060; Cthe_0825.
KEGGicth:Cthe_0825.
PATRICi19515357. VBICloThe47081_0867.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04584 Genomic DNA. Translation: CAA28255.1.
CP000568 Genomic DNA. Translation: ABN52060.1.
PIRiA25535. CZCLDM.
RefSeqiWP_011837914.1. NC_009012.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FL4X-ray2.90A/D/G/J584-649[»]
ProteinModelPortaliA3DDN1.
SMRiA3DDN1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi203119.Cthe_0825.

Protein family/group databases

CAZyiGH9. Glycoside Hydrolase Family 9.

Proteomic databases

PRIDEiA3DDN1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN52060; ABN52060; Cthe_0825.
KEGGicth:Cthe_0825.
PATRICi19515357. VBICloThe47081_0867.

Phylogenomic databases

eggNOGiENOG4105E08. Bacteria.
ENOG410XNTA. LUCA.
HOGENOMiHOG000245359.
KOiK01179.
OMAiCSYASNE.
OrthoDBiPOG091H04TS.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16416.

Miscellaneous databases

EvolutionaryTraceiA3DDN1.

Family and domain databases

CDDicd02850. E_set_Cellulase_N. 1 hit.
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.
IPR004197. Cellulase_Ig-like.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR001701. Glyco_hydro_9.
IPR033126. Glyco_hydro_9_Asp/Glu_AS.
IPR018221. Glyco_hydro_9_His_AS.
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.
PS51766. DOCKERIN. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUND_CLOTH
AccessioniPrimary (citable) accession number: A3DDN1
Secondary accession number(s): P04954
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: March 20, 2007
Last modified: November 2, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.