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P0C2S4

- GUND_CLOTM

UniProt

P0C2S4 - GUND_CLOTM

Protein

Endoglucanase D

Gene

celD

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 39 (01 Oct 2014)
      Sequence version 1 (17 Apr 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.

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

    Cofactori

    Calcium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei177 – 1771Nucleophile
    Active sitei492 – 49211 Publication
    Active sitei522 – 52211 Publication
    Active sitei531 – 5311Proton donor1 PublicationPROSITE-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

    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
    OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)
    Taxonomic identifieri1515 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi41 – 411H → A: 79% of wild-type activity.
    Mutagenesisi143 – 1431H → A: 104% of wild-type activity.
    Mutagenesisi146 – 1461H → A: 77% of wild-type activity.
    Mutagenesisi150 – 1501H → A: 2% of wild-type activity.
    Mutagenesisi163 – 1631H → A: 124% of wild-type activity.
    Mutagenesisi173 – 1731H → A: 8% of wild-type activity.
    Mutagenesisi174 – 1741D → A: 0.08% of wild-type activity.
    Mutagenesisi177 – 1771D → A: 0.2% of wild-type activity.
    Mutagenesisi198 – 1981H → S: 17% of wild-type activity.
    Mutagenesisi222 – 2221D → A: 72% of wild-type activity.
    Mutagenesisi245 – 2451H → A: 90% of wild-type activity.
    Mutagenesisi262 – 2621H → A: 19% of wild-type activity.
    Mutagenesisi293 – 2931D → A: 98% of wild-type activity.
    Mutagenesisi337 – 3371D → A: 86% of wild-type activity.
    Mutagenesisi421 – 4211H → S: 32% of wild-type activity.
    Mutagenesisi468 – 4681H → A: 9% of wild-type activity.
    Mutagenesisi492 – 4921H → S: 25% of wild-type activity.
    Mutagenesisi493 – 4931D → A: 0.8% of wild-type activity.
    Mutagenesisi499 – 4991D → A: 224% of wild-type activity.
    Mutagenesisi503 – 5031E → A: 127% of wild-type activity.
    Mutagenesisi519 – 5191D → A: 91% of wild-type activity.
    Mutagenesisi522 – 5221D → A: 1% of wild-type activity.
    Mutagenesisi525 – 5251D → A: 118% of wild-type activity.
    Mutagenesisi531 – 5311E → A: 0.3% of wild-type activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei‹1 – 17›17Add
    BLAST
    Chaini18 – 625608Endoglucanase DPRO_0000007949Add
    BLAST

    Structurei

    Secondary structure

    1
    625
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 374
    Beta strandi44 – 474
    Beta strandi53 – 586
    Beta strandi61 – 688
    Beta strandi70 – 745
    Turni75 – 784
    Beta strandi79 – 857
    Beta strandi93 – 997
    Turni100 – 1023
    Beta strandi108 – 1103
    Turni112 – 1154
    Helixi116 – 12813
    Beta strandi135 – 1395
    Beta strandi142 – 1465
    Helixi157 – 1604
    Beta strandi175 – 1773
    Helixi182 – 19817
    Helixi200 – 2034
    Turni211 – 2144
    Beta strandi215 – 2173
    Helixi219 – 23113
    Helixi232 – 2343
    Beta strandi243 – 2486
    Helixi258 – 2603
    Beta strandi266 – 2705
    Helixi272 – 28918
    Turni290 – 2923
    Helixi294 – 31320
    Helixi336 – 35015
    Helixi353 – 36311
    Beta strandi367 – 3704
    Helixi380 – 38910
    Helixi397 – 42024
    Turni426 – 4294
    Helixi435 – 45218
    Helixi456 – 46914
    Beta strandi483 – 4864
    Helixi494 – 4985
    Helixi527 – 5304
    Helixi534 – 54512
    Turni546 – 5494

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CLCX-ray1.90A1-625[»]
    4CJ0X-ray1.10A1-625[»]
    4CJ1X-ray1.63A1-625[»]
    ProteinModelPortaliP0C2S4.
    SMRiP0C2S4. Positions 11-551, 556-625.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C2S4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati561 – 584241Add
    BLAST
    Repeati597 – 620242Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni561 – 620602 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

    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: Fragment.

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

    P0C2S4-1 [UniParc]FASTAAdd to Basket

    « Hide

    SLTGVFPSGL IETKVSAAKI TENYQFDSRI RLNSIGFIPN HSKKATIAAN    50
    CSTFYVVKED GTIVYTGTAT SMFDNDTKET VYIADFSSVN EEGTYYLAVP 100
    GVGKSVNFKI AMNVYEDAFK TAMLGMYLLR CGTSVSATYN GIHYSHGPCH 150
    TNDAYLDYIN GQHTKKDSTK GWHDAGDYNK YVVNAGITVG SMFLAWEHFK 200
    DQLEPVALEI PEKNNSIPDF LDELKYEIDW ILTMQYPDGS GRVAHKVSTR 250
    NFGGFIMPEN EHDERFFVPW SSAATADFVA MTAMAARIFR PYDPQYAEKC 300
    INAAKVSYEF LKNNPANVFA NQSGFSTGEY ATVSDADDRL WAAAEMWETL 350
    GDEEYLRDFE NRAAQFSKKI EADFDWDNVA NLGMFTYLLS ERPGKNPALV 400
    QSIKDSLLST ADSIVRTSQN HGYGRTLGTT YYWGCNGTVV RQTMILQVAN 450
    KISPNNDYVN AALDAISHVF GRNYYNRSYV TGLGINPPMN PHDRRSGADG 500
    IWEPWPGYLV GGGWPGPKDW VDIQDSYQTN EIAINWNAAL IYALAGFVNY 550
    NSPQNEVLYG DVNDDGKVNS TDLTLLKRYV LKAVSTLPSS KAEKNADVNR 600
    DGRVNSSDVT ILSRYLIRVI EKLPI 625
    Length:625
    Mass (Da):69,707
    Last modified:April 17, 2007 - v1
    Checksum:i6BFD88E2BDF1BD8F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    PIRiA25535. CZCLDM.

    Cross-referencesi

    Sequence databases

    PIRi A25535. CZCLDM.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CLC X-ray 1.90 A 1-625 [» ]
    4CJ0 X-ray 1.10 A 1-625 [» ]
    4CJ1 X-ray 1.63 A 1-625 [» ]
    ProteinModelPortali P0C2S4.
    SMRi P0C2S4. Positions 11-551, 556-625.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P0C2S4.

    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. "Calcium-binding affinity and calcium-enhanced activity of Clostridium thermocellum endoglucanase D."
      Chauvaux S., Beguin P., Aubert J.-P., Bhat K.M., Gow L.A., Wood T.M., Bairoch A.
      Biochem. J. 265:261-265(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CALCIUM-BINDING DATA.
    2. "Identification of a histidyl residue in the active center of endoglucanase D from Clostridium thermocellum."
      Tomme P., Chauvaux S., Beguin P., Millet J., Aubert J.-P., Claeyssens M.
      J. Biol. Chem. 266:10313-10318(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE HIS-492, MUTAGENESIS OF HISTIDINE RESIDUES.
    3. "Site-directed mutagenesis of essential carboxylic residues in Clostridium thermocellum endoglucanase CelD."
      Chauvaux S., Beguin P., Aubert J.-P.
      J. Biol. Chem. 267:4472-4478(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE GLU-531, MUTAGENESIS OF ASPARTIC ACID AND GLUTAMIC ACID RESIDUES.
    4. "Modification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum."
      Tomme P., van Beeumen J., Claeyssens M.
      Biochem. J. 285:319-324(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE ASP-522.
    5. "Three-dimensional structure of a thermostable bacterial cellulase."
      Juy M., Amit A.G., Alzari P.M., Poljak R.J., Claeyssens M., Beguin P., Aubert J.-P.
      Nature 357:89-91(1992)
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    6. "Multiple crystal forms of endoglucanase CelD: signal peptide residues modulate lattice formation."
      Chitarra V., Souchon H., Spinelli S., Juy M., Beguin P., Alzari P.M.
      J. Mol. Biol. 248:225-232(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    7. "The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism."
      Dominguez R., Souchon H., Lascombe M.-B., Alzari P.M.
      J. Mol. Biol. 257:1042-1051(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 AND 2.3 ANGSTROMS) OF MUTANT GLN-116.

    Entry informationi

    Entry nameiGUND_CLOTM
    AccessioniPrimary (citable) accession number: P0C2S4
    Secondary accession number(s): P04954
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 17, 2007
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 39 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    The sequence shown here has been extracted from PDB entry 1CLC.Curated

    Keywords - Technical termi

    3D-structure

    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