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P29127

- XYNA_NEOPA

UniProt

P29127 - XYNA_NEOPA

Protein

Bifunctional endo-1,4-beta-xylanase A

Gene

XYNA

Organism
Neocallimastix patriciarum (Rumen fungus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    Hydrolyzes xylans into xylobiose and xylose.

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei141 – 1411NucleophilePROSITE-ProRule annotation
    Active sitei223 – 2231Proton donorPROSITE-ProRule annotation
    Active sitei386 – 3861NucleophilePROSITE-ProRule annotation
    Active sitei474 – 4741Proton donorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BRENDAi3.2.1.8. 6834.
    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiGH11. Glycoside Hydrolase Family 11.
    mycoCLAPiXYN11A_NEOPA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional endo-1,4-beta-xylanase A (EC:3.2.1.8)
    Short name:
    XYLA
    Gene namesi
    Name:XYNA
    OrganismiNeocallimastix patriciarum (Rumen fungus)
    Taxonomic identifieri4758 [NCBI]
    Taxonomic lineageiEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaeNeocallimastix

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 607589Bifunctional endo-1,4-beta-xylanase APRO_0000008016Add
    BLAST

    Structurei

    Secondary structure

    1
    607
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi275 – 2817
    Beta strandi283 – 2897
    Beta strandi292 – 2976
    Beta strandi305 – 3095
    Beta strandi315 – 3206
    Beta strandi327 – 3359
    Helixi342 – 3443
    Beta strandi345 – 37531
    Beta strandi385 – 39511
    Beta strandi403 – 4075
    Beta strandi410 – 42314
    Beta strandi426 – 44015
    Beta strandi443 – 4486
    Helixi449 – 4579
    Turni458 – 4603
    Beta strandi468 – 49225

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C1FX-ray2.10A275-499[»]
    2VG9X-ray2.00A275-492[»]
    ProteinModelPortaliP29127.
    SMRiP29127. Positions 30-247, 275-492, 529-562, 572-605.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29127.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini524 – 56239CBM10 1Add
    BLAST
    Domaini566 – 60540CBM10 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 255226Catalytic 1Add
    BLAST
    Regioni275 – 499225Catalytic 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi256 – 27419Ser/Thr-rich (linker)Add
    BLAST
    Compositional biasi500 – 52324Ser/Thr-rich (linker)Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.60.120.180. 2 hits.
    3.90.1220.10. 2 hits.
    InterProiIPR002883. CBM10/Dockerin_dom.
    IPR008985. ConA-like_lec_gl_sf.
    IPR009034. Dockerin_dom_fun.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    [Graphical view]
    PfamiPF02013. CBM_10. 2 hits.
    PF00457. Glyco_hydro_11. 2 hits.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SUPFAMiSSF49899. SSF49899. 2 hits.
    SSF64571. SSF64571. 2 hits.
    PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 2 hits.
    PS00777. GLYCOSYL_HYDROL_F11_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P29127-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRTIKFFFAV AIATVAKAQW GGGGASAGQR LTVGNGQTQH KGVADGYSYE    50
    IWLDNTGGSG SMTLGSGATF KAEWNASVNR GNFLARRGLD FGSQKKATDY 100
    SYIGLDYTAT YRQTGSASGN SRLCVYGWFQ NRGVQGVPLV EYYIIEDWVD 150
    WVSDAQGRMV TIDGAQYKIF QMDHTGPTIN GGSETFKQYF SVRQQKRTSG 200
    HITVSDHFKE WAKQGWGIGN LYEVALNAEG WQSSGIADVT KLDVYTTQKG 250
    SNPAPTSTGT VPSSSAGGST ANGKKFTVGN GQNQHKGVND GFSYEIWLDN 300
    TGGNGSMTLG SGATFKAEWN AAVNRGNFLA RRGLDFGSQK KATDYDYIGL 350
    DYAATYKQTA SASGNSRLCV YGWFQNRGLN GVPLVEYYII EDWVDWVPDA 400
    QGKMVTIDGA QYKIFQMDHT GPTINGGSET FKQYFSVRQQ KRTSGHITVS 450
    DHFKEWAKQG WGIGNLYEVA LNAEGWQSSG VADVTLLDVY TTPKGSSPAT 500
    SAAPRTTTRT TTRTKSLPTN YNKCSARITA QGYKCCSDPN CVVYYTDEDG 550
    TWGVENNDWC GCGVEQCSSK ITSQGYKCCS DPNCVVFYTD DDGKWGVENN 600
    DWCGCGF 607
    Length:607
    Mass (Da):66,175
    Last modified:December 1, 1992 - v1
    Checksum:i9C5B73A67D0CC780
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65526 mRNA. Translation: CAA46498.1.
    PIRiS24754.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65526 mRNA. Translation: CAA46498.1 .
    PIRi S24754.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C1F X-ray 2.10 A 275-499 [» ]
    2VG9 X-ray 2.00 A 275-492 [» ]
    ProteinModelPortali P29127.
    SMRi P29127. Positions 30-247, 275-492, 529-562, 572-605.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH11. Glycoside Hydrolase Family 11.
    mycoCLAPi XYN11A_NEOPA.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .
    BRENDAi 3.2.1.8. 6834.

    Miscellaneous databases

    EvolutionaryTracei P29127.

    Family and domain databases

    Gene3Di 2.60.120.180. 2 hits.
    3.90.1220.10. 2 hits.
    InterProi IPR002883. CBM10/Dockerin_dom.
    IPR008985. ConA-like_lec_gl_sf.
    IPR009034. Dockerin_dom_fun.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    [Graphical view ]
    Pfami PF02013. CBM_10. 2 hits.
    PF00457. Glyco_hydro_11. 2 hits.
    [Graphical view ]
    PRINTSi PR00911. GLHYDRLASE11.
    SUPFAMi SSF49899. SSF49899. 2 hits.
    SSF64571. SSF64571. 2 hits.
    PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 2 hits.
    PS00777. GLYCOSYL_HYDROL_F11_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Homologous catalytic domains in a rumen fungal xylanase: evidence for gene duplication and prokaryotic origin."
      Gilbert H.J., Hazlewood G.P., Laurie J.I., Orpin C.G., Xue G.P.
      Mol. Microbiol. 6:2065-2072(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiXYNA_NEOPA
    AccessioniPrimary (citable) accession number: P29127
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Multifunctional enzyme

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3