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A3DC29

- GUNA_CLOTH

UniProt

A3DC29 - GUNA_CLOTH

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Protein

Endoglucanase A

Gene

celA

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

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 – 1521NucleophileCurated

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 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
Taxonomic identifieri203119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
ProteomesiUP000002145: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232By 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 – 443Combined sources
Beta strandi48 – 503Combined sources
Helixi52 – 7019Combined sources
Helixi86 – 883Combined sources
Helixi94 – 10613Combined sources
Helixi110 – 12112Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi132 – 1343Combined sources
Turni142 – 1476Combined sources
Helixi151 – 16818Combined sources
Beta strandi170 – 1745Combined sources
Helixi176 – 19116Combined sources
Turni194 – 1963Combined sources
Beta strandi201 – 2055Combined sources
Helixi213 – 2153Combined sources
Helixi218 – 22811Combined sources
Helixi232 – 24716Combined sources
Turni248 – 2503Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi274 – 2763Combined sources
Helixi279 – 2813Combined sources
Helixi282 – 29312Combined sources
Helixi296 – 31015Combined sources
Helixi314 – 3163Combined sources
Turni334 – 3363Combined sources
Helixi337 – 3448Combined sources
Helixi350 – 36213Combined sources
Helixi367 – 3693Combined sources
Helixi372 – 38413Combined sources

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.
ModBaseiSearch...
MobiDBiSearch...

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKNVKKRVGV VLLILAVLGV YMLAMPANTV SAAGVPFNTK YPYGPTSIAD
60 70 80 90 100
NQSEVTAMLK AEWEDWKSKR ITSNGAGGYK RVQRDASTNY DTVSEGMGYG
110 120 130 140 150
LLLAVCFNEQ ALFDDLYRYV KSHFNGNGLM HWHIDANNNV TSHDGGDGAA
160 170 180 190 200
TDADEDIALA LIFADKLWGS SGAINYGQEA RTLINNLYNH CVEHGSYVLK
210 220 230 240 250
PGDRWGGSSV TNPSYFAPAW YKVYAQYTGD TRWNQVADKC YQIVEEVKKY
260 270 280 290 300
NNGTGLVPDW CTASGTPASG QSYDYKYDAT RYGWRTAVDY SWFGDQRAKA
310 320 330 340 350
NCDMLTKFFA RDGAKGIVDG YTIQGSKISN NHNASFIGPV AAASMTGYDL
360 370 380 390 400
NFAKELYRET VAVKDSEYYG YYGNSLRLLT LLYITGNFPN PLSDLSGQPT
410 420 430 440 450
PPSNPTPSLP PQVVYGDVNG DGNVNSTDLT MLKRYLLKSV TNINREAADV
460 470
NRDGAINSSD MTILKRYLIK SIPHLPY
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 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372.
  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: October 29, 2014
This is version 54 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

External Data

Dasty 3