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P19487

- GUNA_XANCP

UniProt

P19487 - GUNA_XANCP

Protein

Major extracellular endoglucanase

Gene

engXCA

Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (11 Jul 2002)
      Previous versions | rss
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    Functioni

    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 sitei182 – 1821Proton 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

    BioCyciXCAM190485:GIXZ-3519-MONOMER.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Major extracellular endoglucanase (EC:3.2.1.4)
    Alternative name(s):
    Cellulase
    Endo-1,4-beta-glucanase
    Gene namesi
    Name:engXCA
    Ordered Locus Names:XCC3521
    OrganismiXanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568)
    Taxonomic identifieri190485 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
    ProteomesiUP000001010: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25251 PublicationAdd
    BLAST
    Chaini26 – 484459Major extracellular endoglucanasePRO_0000007875Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi190485.XCC3521.

    Structurei

    3D structure databases

    ProteinModelPortaliP19487.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni375 – 39925Thr-Pro repeats ("hinge") (Pro-Thr box)Add
    BLAST

    Domaini

    The C-terminal region of the protein is not crucial for activity.
    The Thr/Pro-rich region (also termed "hinge") may be a potential site for proteolysis.

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000225207.
    KOiK01179.
    OMAiDCAAISE.
    OrthoDBiEOG6FRCSN.

    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.

    P19487-1 [UniParc]FASTAAdd to Basket

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    MSIFRTASTL ALATALALAA GPAFSYSINN SRQIVDDSGK VVQLKGVNVF    50
    GFETGNHVMH GLWARNWKDM IVQMQGLGFN AVRLPFCPAT LRSDTMPASI 100
    DYSRNADLQG LTSLQILDKV IAEFNARGMY VLLDHHTPDC AGISELWYTG 150
    SYTEAQWLAD LRFVANRYKN VPYVLGLDLK NEPHGAATWG TGNAATDWNK 200
    AAERGSAAVL AVAPKWLIAV EGITDNPVCS TNGGIFWGGN LQPLACTPLN 250
    IPANRLLLAP HVYGPDVFVQ SYFNDSNFPN NMPAIWERHF GQFAGTHALL 300
    LGEFGGKYGE GDARDKTWQD ALVKYLRSKG INQGFYWSWN PNSGDTGGIL 350
    RDDWTSVRQD KMTLLRTLWG TAGNTTPTPT PTPTPTPTPT PTPTPTPTPG 400
    TSTFSTKVIV DNSWNGGYCN RVQVTNTGTA SGTWSIAVPV TGTVNNAWNA 450
    TWSQSGSTLR ASGVDFNRTL AAGATAEFGF CAAS 484
    Length:484
    Mass (Da):52,242
    Last modified:July 11, 2002 - v2
    Checksum:i6671AE5BF1B7602A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti410 – 48475VDNSW…FCAAS → ASPVVGSAARKLPAASRLAC HWPASSTGWRVWVIAAPSVT WKRPHAARAIERRMRVTRLR RATRLNRGPLPAPAHTTQHA PRL in AAA27612. (PubMed:2373365)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32700 Genomic DNA. Translation: AAA27612.1.
    AE008922 Genomic DNA. Translation: AAM42791.1.
    PIRiJH0158.
    RefSeqiNP_638867.1. NC_003902.1.

    Genome annotation databases

    EnsemblBacteriaiAAM42791; AAM42791; XCC3521.
    GeneIDi1000085.
    KEGGixcc:XCC3521.
    PATRICi24078160. VBIXanCam115730_3766.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32700 Genomic DNA. Translation: AAA27612.1 .
    AE008922 Genomic DNA. Translation: AAM42791.1 .
    PIRi JH0158.
    RefSeqi NP_638867.1. NC_003902.1.

    3D structure databases

    ProteinModelPortali P19487.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 190485.XCC3521.

    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 AAM42791 ; AAM42791 ; XCC3521 .
    GeneIDi 1000085.
    KEGGi xcc:XCC3521.
    PATRICi 24078160. VBIXanCam115730_3766.

    Phylogenomic databases

    eggNOGi COG2730.
    HOGENOMi HOG000225207.
    KOi K01179.
    OMAi DCAAISE.
    OrthoDBi EOG6FRCSN.

    Enzyme and pathway databases

    BioCyci XCAM190485:GIXZ-3519-MONOMER.

    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. "Nucleotide sequence of the engXCA gene encoding the major endoglucanase of Xanthomonas campestris pv. campestris."
      Gough C.L., Dow J.M., Keen J., Henrissat B., Daniels M.J.
      Gene 89:53-59(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-61.
    2. "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
      da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.
      , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
      Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33913 / NCPPB 528 / LMG 568.

    Entry informationi

    Entry nameiGUNA_XANCP
    AccessioniPrimary (citable) accession number: P19487
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: July 11, 2002
    Last modified: October 1, 2014
    This is version 112 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

    Complete proteome, Direct protein sequencing, Reference proteome

    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