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A3DDN1

- GUND_CLOTH

UniProt

A3DDN1 - GUND_CLOTH

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: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (20 Mar 2007)
      Previous versions | rss
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    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

    Calcium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei201 – 2011NucleophilePROSITE-ProRule annotation
    Active sitei516 – 5161By similarity
    Active sitei546 – 5461By similarity
    Active sitei555 – 5551Proton donorPROSITE-ProRule annotation

    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

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    BioCyciCTHE203119:GIW8-854-MONOMER.
    MetaCyc: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
    ProteomesiUP000002145: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141By similarityAdd
    BLAST
    Chaini42 – 649608Endoglucanase DPRO_0000284722Add
    BLAST

    Proteomic databases

    PRIDEiA3DDN1.

    Interactioni

    Protein-protein interaction databases

    STRINGi203119.Cthe_0825.

    Structurei

    Secondary structure

    1
    649
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi594 – 60411
    Helixi614 – 6207
    Helixi630 – 64011
    Beta strandi643 – 6453

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4FL4X-ray2.90A/D/G/J584-649[»]
    ProteinModelPortaliA3DDN1.
    SMRiA3DDN1. Positions 35-575, 580-649.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiA3DDN1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati585 – 608241Add
    BLAST
    Repeati621 – 644242Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni585 – 644602 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 By similarity.By similarity

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG05134.
    HOGENOMiHOG000245359.
    KOiK01179.
    OMAiQQDAKEC.
    OrthoDBiEOG6BCSN2.

    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: Complete.

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

    A3DDN1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRMTLKSSM KKRVLSLLIA VVFLSLTGVF PSGLIETKVS AAKITENYQF    50
    DSRIRLNSIG FIPNHSKKAT IAANCSTFYV VKEDGTIVYT GTATSMFDND 100
    TKETVYIADF SSVNEEGTYY LAVPGVGKSV NFKIAMNVYE DAFKTAMLGM 150
    YLLRCGTSVS ATYNGIHYSH GPCHTNDAYL DYINGQHTKK DSTKGWHDAG 200
    DYNKYVVNAG ITVGSMFLAW EHFKDQLEPV ALEIPEKNNS IPDFLDELKY 250
    EIDWILTMQY PDGSGRVAHK VSTRNFGGFI MPENEHDERF FVPWSSAATA 300
    DFVAMTAMAA RIFRPYDPQY AEKCINAAKV SYEFLKNNPA NVFANQSGFS 350
    TGEYATVSDA DDRLWAAAEM WETLGDEEYL RDFENRAAQF SKKIEADFDW 400
    DNVANLGMFT YLLSERPGKN PALVQSIKDS LLSTADSIVR TSQNHGYGRT 450
    LGTTYYWGCN GTVVRQTMIL QVANKISPNN DYVNAALDAI SHVFGRNYYN 500
    RSYVTGLGIN PPMNPHDRRS GADGIWEPWP GYLVGGGWPG PKDWVDIQDS 550
    YQTNEIAINW NAALIYALAG FVNYNSAQNE VLYGDVNDDG KVNSTDLTLL 600
    KRYVLKAVST LPSSKAEKNA DVNRDGRVNS SDVTILSRYL IRVIEKLPI 649
    Length:649
    Mass (Da):72,415
    Last modified:March 20, 2007 - v1
    Checksum:i3A6A44735B29D3F4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti577 – 5771A → P in CAA28255. (PubMed:3024110)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04584 Genomic DNA. Translation: CAA28255.1.
    CP000568 Genomic DNA. Translation: ABN52060.1.
    PIRiA25535. CZCLDM.
    RefSeqiYP_001037253.1. NC_009012.1.

    Genome annotation databases

    EnsemblBacteriaiABN52060; ABN52060; Cthe_0825.
    GeneIDi4810443.
    KEGGicth:Cthe_0825.
    PATRICi19515357. VBICloThe47081_0867.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04584 Genomic DNA. Translation: CAA28255.1 .
    CP000568 Genomic DNA. Translation: ABN52060.1 .
    PIRi A25535. CZCLDM.
    RefSeqi YP_001037253.1. NC_009012.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4FL4 X-ray 2.90 A/D/G/J 584-649 [» ]
    ProteinModelPortali A3DDN1.
    SMRi A3DDN1. Positions 35-575, 580-649.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 203119.Cthe_0825.

    Protein family/group databases

    CAZyi GH9. Glycoside Hydrolase Family 9.

    Proteomic databases

    PRIDEi A3DDN1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABN52060 ; ABN52060 ; Cthe_0825 .
    GeneIDi 4810443.
    KEGGi cth:Cthe_0825.
    PATRICi 19515357. VBICloThe47081_0867.

    Phylogenomic databases

    eggNOGi NOG05134.
    HOGENOMi HOG000245359.
    KOi K01179.
    OMAi QQDAKEC.
    OrthoDBi EOG6BCSN2.

    Enzyme and pathway databases

    BioCyci CTHE203119:GIW8-854-MONOMER.
    MetaCyc:MONOMER-16416.

    Miscellaneous databases

    EvolutionaryTracei A3DDN1.

    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. "Nucleotide sequence of the cellulase gene celD encoding endoglucanase D of Clostridium thermocellum."
      Joliff G., Beguin P., Aubert J.-P.
      Nucleic Acids Res. 14:8605-8613(1986) [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.

    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: October 1, 2014
    This is version 51 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