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)

P28623

- GUND_CLOC7

UniProt

P28623 - GUND_CLOC7

Protein

Endoglucanase D

Gene

engD

Organism
Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Has endoglucanase activity on carboxymethyl-cellulose (CMC), cellobiosidase activity on p-nitrophenyl-cellobioside (p-NPC), and partial hydrolytic activity on crystalline cellulose (Avicel).

    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 sitei180 – 1801Proton donorBy similarity
    Active sitei303 – 3031NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. polysaccharide binding Source: InterPro

    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

    BioCyciCCEL573061:GIXD-3329-MONOMER.

    Protein family/group databases

    CAZyiCBM2. Carbohydrate-Binding Module Family 2.
    GH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase D (EC:3.2.1.4)
    Alternative name(s):
    Cellulase D
    Endo-1,4-beta-glucanase D
    Gene namesi
    Name:engD
    Ordered Locus Names:Clocel_3242
    OrganismiClostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B)
    Taxonomic identifieri573061 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000002730: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 31311 PublicationAdd
    BLAST
    Chaini32 – 515484Endoglucanase DPRO_0000007848Add
    BLAST

    Structurei

    Secondary structure

    1
    515
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi43 – 508
    Beta strandi52 – 565
    Turni57 – 615
    Turni66 – 694
    Helixi76 – 8510
    Beta strandi89 – 924
    Turni103 – 1053
    Helixi110 – 12415
    Turni125 – 1273
    Beta strandi129 – 1324
    Turni138 – 1403
    Turni145 – 1473
    Helixi148 – 16518
    Turni166 – 1683
    Beta strandi173 – 1775
    Helixi186 – 1883
    Helixi195 – 21420
    Helixi217 – 2204
    Beta strandi224 – 2274
    Helixi229 – 2313
    Helixi235 – 2406
    Helixi244 – 2463
    Beta strandi250 – 2556
    Helixi260 – 2634
    Helixi275 – 29117
    Helixi293 – 2953
    Beta strandi299 – 3046
    Helixi312 – 32716
    Turni328 – 3303
    Beta strandi332 – 3376
    Turni354 – 3574
    Beta strandi358 – 3614
    Helixi362 – 37211
    Beta strandi411 – 42010
    Beta strandi422 – 43312
    Beta strandi435 – 4373
    Beta strandi439 – 4413
    Beta strandi443 – 4475
    Beta strandi452 – 46514
    Beta strandi468 – 4736
    Turni482 – 4843
    Beta strandi485 – 49511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NDYX-ray2.10A/B/C/D32-376[»]
    E/F/G/H409-515[»]
    3NDZX-ray2.08A/B/C/D32-376[»]
    E/F/G/H409-515[»]
    ProteinModelPortaliP28623.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28623.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini404 – 515112CBM2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni32 – 376345CatalyticBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi377 – 40731Pro/Thr-rich (linker)Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000027405.
    KOiK01179.
    OMAiACINDYN.

    Family and domain databases

    Gene3Di2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00553. CBM_2. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view]
    SMARTiSM00637. CBD_II. 1 hit.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS51173. CBM2. 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.

    P28623-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIKHLLSRGK LLLFVSVMAT SSIIAGGNAY GSTAFTGVRD VPAQQIVNEM    50
    KVGWNLGNTM DAIGGETNWG NPMTTHAMIN KIKEAGFNTL RLPVTWDGHM 100
    GAAPEYTIDQ TWMKRVEEIA NYAFDNDMYV IINLHHENEW LKPFYANEAQ 150
    VKAQLTKVWT QIANNFKKYG DHLIFETMNE PRPVGASNEW TGGSYENREV 200
    VNRYNLTAVN AIRATGGNNA TRYIMVPTLA ASAMSTTIND LVIPNNDSKV 250
    IVSLHMYSPY FFAMDINGTS SWGSDYDKSS LDSEFDAVYN KFVKNGRAVV 300
    IGEMGSINKN NTAARVTHAE YYAKSAKARG LTPIWWDNGY SVAGKAETFG 350
    IFNRSNLTWD APEVMKAFIK GIGGSSTTTP TTPTTPTTPT TPTTPTTPTT 400
    PTTPTTPQSA VEVTYAITNS WGSGASVNVT IKNNGTTPIN GWTLKWTMPI 450
    NQTITNMWSA SFVASGTTLS VTNAGYNGTI AANGGTQSFG FNINYSGVLS 500
    KPTGFTVNGT ECTVK 515
    Length:515
    Mass (Da):55,978
    Last modified:November 30, 2010 - v2
    Checksum:i57F15B035856008E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1892NE → LQ in AAA23233. (PubMed:1538700)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37434 Genomic DNA. Translation: AAA23233.1.
    CP002160 Genomic DNA. Translation: ADL52928.1.
    PIRiS20493.
    RefSeqiYP_003844692.1. NC_014393.1.

    Genome annotation databases

    EnsemblBacteriaiADL52928; ADL52928; Clocel_3242.
    GeneIDi9610136.
    KEGGiccb:Clocel_3242.
    PATRICi41732687. VBICloCel81632203721_0262.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37434 Genomic DNA. Translation: AAA23233.1 .
    CP002160 Genomic DNA. Translation: ADL52928.1 .
    PIRi S20493.
    RefSeqi YP_003844692.1. NC_014393.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3NDY X-ray 2.10 A/B/C/D 32-376 [» ]
    E/F/G/H 409-515 [» ]
    3NDZ X-ray 2.08 A/B/C/D 32-376 [» ]
    E/F/G/H 409-515 [» ]
    ProteinModelPortali P28623.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM2. Carbohydrate-Binding Module Family 2.
    GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADL52928 ; ADL52928 ; Clocel_3242 .
    GeneIDi 9610136.
    KEGGi ccb:Clocel_3242.
    PATRICi 41732687. VBICloCel81632203721_0262.

    Phylogenomic databases

    HOGENOMi HOG000027405.
    KOi K01179.
    OMAi ACINDYN.

    Enzyme and pathway databases

    BioCyci CCEL573061:GIXD-3329-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P28623.

    Family and domain databases

    Gene3Di 2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00553. CBM_2. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SMARTi SM00637. CBD_II. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS51173. CBM2. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of functional domains of endoglucanases from Clostridium cellulovorans by gene cloning, nucleotide sequencing and chimeric protein construction."
      Hamamoto T., Foong F., Shoseyov O., Doi R.H.
      Mol. Gen. Genet. 231:472-479(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-44.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35296 / DSM 3052 / OCM 3 / 743B.

    Entry informationi

    Entry nameiGUND_CLOC7
    AccessioniPrimary (citable) accession number: P28623
    Secondary accession number(s): D9SUH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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