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P23031

- XYNC_CELJU

UniProt

P23031 - XYNC_CELJU

Protein

Alpha-L-arabinofuranosidase C

Gene

xynC

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (20 Apr 2010)
      Previous versions | rss
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    Functioni

    Xylanase C contributes to hydrolyse hemicellulose, the major component of plant cell-walls.

    Catalytic activityi

    Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

    Pathwayi

    GO - Molecular functioni

    1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC
    2. polysaccharide binding Source: InterPro

    GO - Biological processi

    1. L-arabinose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciCJAP498211:GHIT-3270-MONOMER.
    UniPathwayiUPA00697.

    Protein family/group databases

    CAZyiCBM2. Carbohydrate-Binding Module Family 2.
    CBM35. Carbohydrate-Binding Module Family 35.
    GH62. Glycoside Hydrolase Family 62.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-L-arabinofuranosidase C (EC:3.2.1.55)
    Alternative name(s):
    Xylanase C
    Gene namesi
    Name:xynC
    Synonyms:abf62A
    Ordered Locus Names:CJA_3281
    OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
    Taxonomic identifieri498211 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio
    ProteomesiUP000001036: Chromosome

    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 – 37371 PublicationAdd
    BLAST
    Chaini38 – 619582Alpha-L-arabinofuranosidase CPRO_0000008033Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi39 ↔ 133By similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    STRINGi498211.CJA_3281.

    Structurei

    3D structure databases

    ProteinModelPortaliP23031.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 13699CBM2Add
    BLAST
    Domaini163 – 289127CBM6PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi135 – 16228Ser-rich (linker)Add
    BLAST
    Compositional biasi300 – 32021Ser-rich (linker)Add
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 62 family.Curated
    Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    OMAiWYLITQW.
    OrthoDBiEOG6ZH2FF.

    Family and domain databases

    Gene3Di2.115.10.20. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.290. 1 hit.
    InterProiIPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR018366. CBM2_CS.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR005084. CMB_fam6.
    IPR008979. Galactose-bd-like.
    IPR005193. GH62_arabinosidase.
    IPR023296. Glyco_hydro_beta-prop.
    [Graphical view]
    PfamiPF00553. CBM_2. 1 hit.
    PF03422. CBM_6. 1 hit.
    PF03664. Glyco_hydro_62. 1 hit.
    [Graphical view]
    SMARTiSM00637. CBD_II. 1 hit.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF75005. SSF75005. 1 hit.
    PROSITEiPS51173. CBM2. 1 hit.
    PS00561. CBM2_A. 1 hit.
    PS51175. CBM6. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23031-1 [UniParc]FASTAAdd to Basket

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    MINHNKTPNI LAKVFKRTCG LVSTGAALAI LSQAASAACT YTIDSEWSTG    50
    FTANITLKND TGAAINNWNV NWQYSSNRMT SGWNANFSGT NPYNATNMSW 100
    NGSIAPGQSI SFGLQGEKNG STAERPTVTG AACNSATTSS VASSSSTPTT 150
    SSSSASSVAS ALLLQEAQAG FCRVDGTIDN NHTGFTGSGF ANTNNAQGAA 200
    VVWAIDATSS GRRTLTIRYA NGGTANRNGS LVINGGSNGN YTVSLPTTGA 250
    WTTWQTATID VDLVQGNNIV QLSATTAEGL PNIDSLSVVG GTVRAGNCGS 300
    VSSSSSVQSS SSSSSTPSQT CELKAPLRWT STGPLISPKN PGWISIKDPS 350
    IVKYNDTYHV YATYYDTAYR SMYTSFTDWN TAQQAPHISM NGSRVGNTVA 400
    PQVFYFRPHN KWYLITQWAG AYATTDDIRN PNWSAKQKLL QGEPNGALDF 450
    WVICNDTHCY LYFSRDDGVL YVSKTTLANF PNFSGYSIVM EDHRGNGNSY 500
    LFEAANVYKL DGQNRYLLMV EAYISGPRFF RSWTATSLDG PWTPLADTEA 550
    NPFAGNNNVE WSTGKWADGI SHGELIRSGH DEKMTVDPCN LEFLYQGASG 600
    PGSTYNTIPY KLGLLRLKK 619
    Length:619
    Mass (Da):66,440
    Last modified:April 20, 2010 - v2
    Checksum:i9CA48261A2D0FD0F
    GO

    Sequence cautioni

    The sequence CAA38390.1 differs from that shown. Reason: Frameshift at positions 527 and 544.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti556 – 59035NNNVE…VDPCN → MMFCFTMASSLKVYTCY in CAA38390. (PubMed:2125205)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54523 Genomic DNA. Translation: CAA38390.1. Frameshift.
    CP000934 Genomic DNA. Translation: ACE85320.1.
    RefSeqiYP_001983735.1. NC_010995.1.

    Genome annotation databases

    EnsemblBacteriaiACE85320; ACE85320; CJA_3281.
    GeneIDi6413842.
    KEGGicja:CJA_3281.
    PATRICi21329953. VBICelJap122165_3241.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54523 Genomic DNA. Translation: CAA38390.1 . Frameshift.
    CP000934 Genomic DNA. Translation: ACE85320.1 .
    RefSeqi YP_001983735.1. NC_010995.1.

    3D structure databases

    ProteinModelPortali P23031.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 498211.CJA_3281.

    Protein family/group databases

    CAZyi CBM2. Carbohydrate-Binding Module Family 2.
    CBM35. Carbohydrate-Binding Module Family 35.
    GH62. Glycoside Hydrolase Family 62.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACE85320 ; ACE85320 ; CJA_3281 .
    GeneIDi 6413842.
    KEGGi cja:CJA_3281.
    PATRICi 21329953. VBICelJap122165_3241.

    Phylogenomic databases

    OMAi WYLITQW.
    OrthoDBi EOG6ZH2FF.

    Enzyme and pathway databases

    UniPathwayi UPA00697 .
    BioCyci CJAP498211:GHIT-3270-MONOMER.

    Family and domain databases

    Gene3Di 2.115.10.20. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.290. 1 hit.
    InterProi IPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR018366. CBM2_CS.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR005084. CMB_fam6.
    IPR008979. Galactose-bd-like.
    IPR005193. GH62_arabinosidase.
    IPR023296. Glyco_hydro_beta-prop.
    [Graphical view ]
    Pfami PF00553. CBM_2. 1 hit.
    PF03422. CBM_6. 1 hit.
    PF03664. Glyco_hydro_62. 1 hit.
    [Graphical view ]
    SMARTi SM00637. CBD_II. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF75005. SSF75005. 1 hit.
    PROSITEi PS51173. CBM2. 1 hit.
    PS00561. CBM2_A. 1 hit.
    PS51175. CBM6. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Xylanase B and an arabinofuranosidase from Pseudomonas fluorescens subsp. cellulosa contain identical cellulose-binding domains and are encoded by adjacent genes."
      Kellett L.E., Poole D.M., Ferreira L.M.A., Durrant A.J., Hazlewood G.P., Gilbert H.J.
      Biochem. J. 272:369-376(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 38-46.
    2. "Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
      DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
      J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ueda107.

    Entry informationi

    Entry nameiXYNC_CELJU
    AccessioniPrimary (citable) accession number: P23031
    Secondary accession number(s): B3PEH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Acts only on high MW substrates, in which arabinose is linked to a polymeric backbone.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3