Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A3DC29

- GUNA_CLOTH

UniProt

A3DC29 - GUNA_CLOTH

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (20 Mar 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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 – 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.
    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.

    A3DC29-1 [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

    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 1, 2014
    This is version 53 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