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)

P17901

- GUNA_CLOCE

UniProt

P17901 - GUNA_CLOCE

Protein

Endoglucanase A

Gene

celCCA

Organism
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

    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 sitei147 – 1471Curated
    Active sitei195 – 1951Proton donor
    Active sitei332 – 3321Nucleophile

    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

    BioCyciCCEL394503:GJET-1124-MONOMER.

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase A (EC:3.2.1.4)
    Alternative name(s):
    Cellulase A
    EGCCA
    Endo-1,4-beta-glucanase A
    Gene namesi
    Name:celCCA
    Ordered Locus Names:Ccel_1099
    OrganismiClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
    Taxonomic identifieri394503 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000001349: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi104 – 1041R → K: Small loss of activity. 1 Publication
    Mutagenesisi104 – 1041R → S or V: Large decrease of activity. 1 Publication
    Mutagenesisi147 – 1471H → S, E, G or F: Total loss of activity. 1 Publication
    Mutagenesisi148 – 1481H → V: Large decrease of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26261 PublicationAdd
    BLAST
    Chaini27 – 475449Endoglucanase APRO_0000007845Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi394503.Ccel_1099.

    Structurei

    Secondary structure

    1
    475
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi29 – 313
    Helixi46 – 549
    Beta strandi56 – 594
    Helixi75 – 773
    Helixi78 – 814
    Helixi89 – 9810
    Beta strandi102 – 1054
    Helixi110 – 1123
    Turni115 – 1184
    Helixi122 – 13615
    Turni137 – 1393
    Beta strandi141 – 1455
    Turni152 – 1543
    Helixi160 – 1623
    Helixi163 – 18018
    Turni181 – 1833
    Beta strandi188 – 1914
    Turni202 – 2054
    Helixi212 – 23423
    Helixi237 – 2404
    Beta strandi244 – 2474
    Helixi249 – 2513
    Helixi253 – 2575
    Beta strandi274 – 2796
    Helixi284 – 2874
    Helixi291 – 2933
    Helixi304 – 32017
    Helixi322 – 3243
    Beta strandi328 – 3336
    Helixi341 – 35717
    Beta strandi361 – 3644
    Beta strandi371 – 3744
    Turni382 – 3854
    Beta strandi386 – 3894
    Helixi390 – 39910
    Beta strandi418 – 4203
    Helixi424 – 43512
    Helixi443 – 4453
    Helixi455 – 46511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EDGX-ray1.60A27-401[»]
    2VN5X-ray1.90B/D410-475[»]
    2VN6X-ray1.49B410-472[»]
    ProteinModelPortaliP17901.
    SMRiP17901. Positions 27-401, 410-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17901.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati415 – 438241Add
    BLAST
    Repeati446 – 469242Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni415 – 469552 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

    eggNOGiCOG2730.
    HOGENOMiHOG000027405.
    KOiK01179.
    OMAiTWGEEAT.
    OrthoDBiEOG6KHFWF.

    Family and domain databases

    Gene3Di1.10.1330.10. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR016134. Cellulos_enz_dockerin_1.
    IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
    IPR018242. Dockerin_1.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    PF00404. Dockerin_1. 2 hits.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF63446. SSF63446. 1 hit.
    PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00018. EF_HAND_1. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P17901-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKTTAFLLC FLMIFTALLP MQNANAYDAS LIPNLQIPQK NIPNNDGMNF    50
    VKGLRLGWNL GNTFDAFNGT NITNELDYET SWSGIKTTKQ MIDAIKQKGF 100
    NTVRIPVSWH PHVSGSDYKI SDVWMNRVQE VVNYCIDNKM YVILNTHHDV 150
    DKVKGYFPSS QYMASSKKYI TSVWAQIAAR FANYDEHLIF EGMNEPRLVG 200
    HANEWWPELT NSDVVDSINC INQLNQDFVN TVRATGGKNA SRYLMCPGYV 250
    ASPDGATNDY FRMPNDISGN NNKIIVSVHA YCPWNFAGLA MADGGTNAWN 300
    INDSKDQSEV TWFMDNIYNK YTSRGIPVII GECGAVDKNN LKTRVEYMSY 350
    YVAQAKARGI LCILWDNNNF SGTGELFGFF DRRSCQFKFP EIIDGMVKYA 400
    FEAKTDPDPV IVYGDYNNDG NVDALDFAGL KKYIMAADHA YVKNLDVNLD 450
    NEVNAFDLAI LKKYLLGMVS KLPSN 475
    Length:475
    Mass (Da):53,625
    Last modified:November 1, 1990 - v1
    Checksum:i1AF20EA2C0A132F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93096 Genomic DNA. Translation: AAA51444.1.
    M32362 Genomic DNA. Translation: AAA23221.1.
    CP001348 Genomic DNA. Translation: ACL75458.1.
    RefSeqiWP_015924614.1. NC_011898.1.
    YP_002505438.1. NC_011898.1.

    Genome annotation databases

    EnsemblBacteriaiACL75458; ACL75458; Ccel_1099.
    GeneIDi7309912.
    KEGGicce:Ccel_1099.
    PATRICi19433019. VBICloCel57783_1132.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93096 Genomic DNA. Translation: AAA51444.1 .
    M32362 Genomic DNA. Translation: AAA23221.1 .
    CP001348 Genomic DNA. Translation: ACL75458.1 .
    RefSeqi WP_015924614.1. NC_011898.1.
    YP_002505438.1. NC_011898.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EDG X-ray 1.60 A 27-401 [» ]
    2VN5 X-ray 1.90 B/D 410-475 [» ]
    2VN6 X-ray 1.49 B 410-472 [» ]
    ProteinModelPortali P17901.
    SMRi P17901. Positions 27-401, 410-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 394503.Ccel_1099.

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACL75458 ; ACL75458 ; Ccel_1099 .
    GeneIDi 7309912.
    KEGGi cce:Ccel_1099.
    PATRICi 19433019. VBICloCel57783_1132.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000027405.
    KOi K01179.
    OMAi TWGEEAT.
    OrthoDBi EOG6KHFWF.

    Enzyme and pathway databases

    BioCyci CCEL394503:GJET-1124-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P17901.

    Family and domain databases

    Gene3Di 1.10.1330.10. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR016134. Cellulos_enz_dockerin_1.
    IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
    IPR018242. Dockerin_1.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    PF00404. Dockerin_1. 2 hits.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF63446. SSF63446. 1 hit.
    PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00018. EF_HAND_1. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the Clostridium cellulolyticum endoglucanase-A-encoding gene, celCCA."
      Faure E., Belaich A., Bagnara C., Gaudin C., Belaich J.-P.
      Gene 84:39-46(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-39.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.
    3. "Characterization of endoglucanase A from Clostridium cellulolyticum."
      Fierobe H.-P., Gaudin C., Belaich A., Loufti M., Faure E., Bagnara C., Baty D., Belaich J.-P.
      J. Bacteriol. 173:7956-7962(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    4. "The catalytic domain of endoglucanase A from Clostridium cellulolyticum: effects of arginine 79 and histidine 122 mutations on catalysis."
      Belaich A., Fierobe H.-P., Baty D., Busetta B., Bagnara-Tardif C., Gaudin C., Belaich J.-P.
      J. Bacteriol. 174:4677-4682(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-104; HIS-147 AND HIS-148.
    5. "Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5."
      Ducros V., Czjzek M., Belaich A., Gaudin C., Fierobe H.P., Belaich J.-P., Davies G.J., Haser R.
      Structure 3:939-949(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 27-406.

    Entry informationi

    Entry nameiGUNA_CLOCE
    AccessioniPrimary (citable) accession number: P17901
    Secondary accession number(s): B8HZV8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The C-terminus (AA 411-475) may play a role in organizing the cellulosome complex.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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