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Q47096

- GUNV_PECCC

UniProt

Q47096 - GUNV_PECCC

Protein

Endoglucanase 5

Gene

celV

Organism
Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Endoglucanase with some exoglucanase activity.

    Catalytic activityi

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

    pH dependencei

    Optimum pH is about 7.0.

    Temperature dependencei

    Optimum temperature is about 42 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei168 – 1681Proton donorBy similarity
    Active sitei256 – 2561NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. cellulose 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

    Protein family/group databases

    CAZyiCBM3. Carbohydrate-Binding Module Family 3.
    GH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase 5 (EC:3.2.1.4)
    Alternative name(s):
    Cellulase V
    Endo-1,4-beta-glucanase V
    Endoglucanase V
    Gene namesi
    Name:celV
    OrganismiPectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora)
    Taxonomic identifieri555 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 505474Endoglucanase 5PRO_0000007858Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ47096.
    SMRiQ47096. Positions 35-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini353 – 505153CBM3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni32 – 334303CatalyticAdd
    BLAST
    Regioni335 – 35218LinkerAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CBM3 (carbohydrate binding type-3) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.40.710. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00942. CBM_3. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view]
    SMARTiSM01067. CBM_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS51172. CBM3. 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.

    Q47096-1 [UniParc]FASTAAdd to Basket

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    MWMRRNQIVR KLTLGVVTTV LGMSLSFSAL SATPVETHGQ LSIENGRLVD    50
    EQGKRVQLRG ISSHGLQWFG DYVNKDSMKW LRDDWGINVF RVAMYTAADG 100
    YISNPSLANK VKEAVAAAQS LGVYIIIDWH ILSDNDPNIY KAQAKTFFAE 150
    MAGLYGSSPN VIYEIANEPN GGVTWNGQIR PYALEVTDTI RSKDPDNLII 200
    VGTGTWSQDI HDAADNQLPD PNTMYALHFY AGTHGQFLRD RIDYAQSRGA 250
    AIFVSEWGTS DASGNGGPFL PESQTWIDFL NNRGVSWVNW SLTDKSEASA 300
    ALAPGASKSG GWTEQNLSTS GKFVREQIRA GANLGGGDTP TTPTEPTNPG 350
    NGTTGDVVLQ YRNVDNNPSD DAIRMAVNIK NTGSTPIKLS DLQVRYYFHD 400
    DGKPGANLFV DWANVGPNNI VTSTGTPAAS TDKANRYVLV TFSSGAGSLQ 450
    PGAETGEVQV RIHAGDWSNV NETNDYSYGA NVTSYANWDK ITVHDKGTLV 500
    WGVEP 505
    Length:505
    Mass (Da):54,900
    Last modified:November 1, 1996 - v1
    Checksum:iDBEA9337BB4D2623
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76000 Genomic DNA. Translation: CAA53592.1.
    PIRiS39962.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76000 Genomic DNA. Translation: CAA53592.1 .
    PIRi S39962.

    3D structure databases

    ProteinModelPortali Q47096.
    SMRi Q47096. Positions 35-333.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM3. Carbohydrate-Binding Module Family 3.
    GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.40.710. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00942. CBM_3. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SMARTi SM01067. CBM_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS51172. CBM3. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular analysis of the major cellulase (CelV) of Erwinia carotovora: evidence for an evolutionary 'mix-and-match' of enzyme domains."
      Cooper V.J.C., Salmond G.P.C.
      Mol. Gen. Genet. 241:341-350(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SCRI 193.

    Entry informationi

    Entry nameiGUNV_PECCC
    AccessioniPrimary (citable) accession number: Q47096
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3