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A3DC29

- GUNA_CLOTH

UniProt

A3DC29 - GUNA_CLOTH

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Protein

Endoglucanase A

Gene
celA, Cthe_0269
Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237)
Status
Reviewed - Annotation score: 4 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951Proton donor
Active sitei152 – 1521Nucleophile Inferred

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

Enzyme and pathway databases

BioCyciCTHE203119:GIW8-276-MONOMER.
MetaCyc:MONOMER-16413.

Protein family/group databases

CAZyiGH8. Glycoside Hydrolase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase A (EC:3.2.1.4)
Short name:
EGA
Alternative name(s):
Cellulase A
Endo-1,4-beta-glucanase
Gene namesi
Name:celA
Ordered Locus Names:Cthe_0269
OrganismiClostridium thermocellum (strain ATCC 27405 / DSM 1237)
Taxonomic identifieri203119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
ProteomesiUP000002145: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232 By similarityAdd
BLAST
Chaini33 – 477445Endoglucanase APRO_0000284721Add
BLAST

Proteomic databases

PRIDEiA3DC29.

Interactioni

Protein-protein interaction databases

STRINGi203119.Cthe_0269.

Structurei

Secondary structure

1
477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 443
Beta strandi48 – 503
Helixi52 – 7019
Helixi86 – 883
Helixi94 – 10613
Helixi110 – 12112
Beta strandi128 – 1303
Beta strandi132 – 1343
Turni142 – 1476
Helixi151 – 16818
Beta strandi170 – 1745
Helixi176 – 19116
Turni194 – 1963
Beta strandi201 – 2055
Helixi213 – 2153
Helixi218 – 22811
Helixi232 – 24716
Turni248 – 2503
Beta strandi259 – 2613
Beta strandi274 – 2763
Helixi279 – 2813
Helixi282 – 29312
Helixi296 – 31015
Helixi314 – 3163
Turni334 – 3363
Helixi337 – 3448
Helixi350 – 36213
Helixi367 – 3693
Helixi372 – 38413

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CEMX-ray1.65A33-395[»]
1IS9X-ray1.03A33-395[»]
1KWFX-ray0.94A33-395[»]
ProteinModelPortaliA3DC29.
SMRiA3DC29. Positions 33-395, 412-477.

Miscellaneous databases

EvolutionaryTraceiA3DC29.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati417 – 440241Add
BLAST
Repeati449 – 472242Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni417 – 472562 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

Phylogenomic databases

eggNOGiCOG3405.
HOGENOMiHOG000069581.
OMAiDMDIAYA.
OrthoDBiEOG67Q9BX.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
1.50.10.10. 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.
IPR018247. EF_Hand_1_Ca_BS.
IPR002037. Glyco_hydro_8.
IPR019834. Glyco_hydro_8_CS.
[Graphical view]
PfamiPF00404. Dockerin_1. 2 hits.
PF01270. Glyco_hydro_8. 1 hit.
[Graphical view]
PRINTSiPR00735. GLHYDRLASE8.
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS00812. GLYCOSYL_HYDROL_F8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A3DC29-1 [UniParc]FASTAAdd to Basket

« Hide

MKNVKKRVGV VLLILAVLGV YMLAMPANTV SAAGVPFNTK YPYGPTSIAD    50
NQSEVTAMLK AEWEDWKSKR ITSNGAGGYK RVQRDASTNY DTVSEGMGYG 100
LLLAVCFNEQ ALFDDLYRYV KSHFNGNGLM HWHIDANNNV TSHDGGDGAA 150
TDADEDIALA LIFADKLWGS SGAINYGQEA RTLINNLYNH CVEHGSYVLK 200
PGDRWGGSSV TNPSYFAPAW YKVYAQYTGD TRWNQVADKC YQIVEEVKKY 250
NNGTGLVPDW CTASGTPASG QSYDYKYDAT RYGWRTAVDY SWFGDQRAKA 300
NCDMLTKFFA RDGAKGIVDG YTIQGSKISN NHNASFIGPV AAASMTGYDL 350
NFAKELYRET VAVKDSEYYG YYGNSLRLLT LLYITGNFPN PLSDLSGQPT 400
PPSNPTPSLP PQVVYGDVNG DGNVNSTDLT MLKRYLLKSV TNINREAADV 450
NRDGAINSSD MTILKRYLIK SIPHLPY 477
Length:477
Mass (Da):52,594
Last modified:March 20, 2007 - v1
Checksum:iBA5A0AD5022E8A51
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K03088 Genomic DNA. Translation: AAA83521.1.
CP000568 Genomic DNA. Translation: ABN51508.1.
PIRiA23100. CZCLAM.
RefSeqiWP_003512420.1. NC_009012.1.
YP_001036701.1. NC_009012.1.

Genome annotation databases

EnsemblBacteriaiABN51508; ABN51508; Cthe_0269.
GeneIDi4808552.
KEGGicth:Cthe_0269.
PATRICi19514173. VBICloThe47081_0284.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K03088 Genomic DNA. Translation: AAA83521.1 .
CP000568 Genomic DNA. Translation: ABN51508.1 .
PIRi A23100. CZCLAM.
RefSeqi WP_003512420.1. NC_009012.1.
YP_001036701.1. NC_009012.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CEM X-ray 1.65 A 33-395 [» ]
1IS9 X-ray 1.03 A 33-395 [» ]
1KWF X-ray 0.94 A 33-395 [» ]
ProteinModelPortali A3DC29.
SMRi A3DC29. Positions 33-395, 412-477.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 203119.Cthe_0269.

Protein family/group databases

CAZyi GH8. Glycoside Hydrolase Family 8.

Proteomic databases

PRIDEi A3DC29.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABN51508 ; ABN51508 ; Cthe_0269 .
GeneIDi 4808552.
KEGGi cth:Cthe_0269.
PATRICi 19514173. VBICloThe47081_0284.

Phylogenomic databases

eggNOGi COG3405.
HOGENOMi HOG000069581.
OMAi DMDIAYA.
OrthoDBi EOG67Q9BX.

Enzyme and pathway databases

BioCyci CTHE203119:GIW8-276-MONOMER.
MetaCyc:MONOMER-16413.

Miscellaneous databases

EvolutionaryTracei A3DC29.

Family and domain databases

Gene3Di 1.10.1330.10. 1 hit.
1.50.10.10. 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.
IPR018247. EF_Hand_1_Ca_BS.
IPR002037. Glyco_hydro_8.
IPR019834. Glyco_hydro_8_CS.
[Graphical view ]
Pfami PF00404. Dockerin_1. 2 hits.
PF01270. Glyco_hydro_8. 1 hit.
[Graphical view ]
PRINTSi PR00735. GLHYDRLASE8.
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS00812. GLYCOSYL_HYDROL_F8. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a cellulase gene of the thermophilic bacterium Clostridium thermocellum."
    Beguin P., Cornet P., Aubert J.-P.
    J. Bacteriol. 162:102-105(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27405 / DSM 1237.
  3. "The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum."
    Alzari P.M., Souchon H., Dominguez R.
    Structure 4:265-275(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 33-395.
  4. "Advantages of high-resolution phasing: MAD to atomic resolution."
    Schmidt A., Gonzalez A., Morris R.J., Costabel M., Alzari P.M., Lamzin V.S.
    Acta Crystallogr. D 58:1433-1441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) OF 33-395.
  5. "Atomic (0.94 A) resolution structure of an inverting glycosidase in complex with substrate."
    Guerin D.M., Lascombe M.B., Costabel M., Souchon H., Lamzin V., Beguin P., Alzari P.M.
    J. Mol. Biol. 316:1061-1069(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.94 ANGSTROMS) OF 33-395.

Entry informationi

Entry nameiGUNA_CLOTH
AccessioniPrimary (citable) accession number: A3DC29
Secondary accession number(s): P04955
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: March 20, 2007
Last modified: September 3, 2014
This is version 52 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

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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