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P26514

- XYNA_STRLI

UniProt

P26514 - XYNA_STRLI

Protein

Endo-1,4-beta-xylanase A

Gene

xlnA

Organism
Streptomyces lividans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources.

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei169 – 1691Proton donor
    Active sitei277 – 2771Nucleophile

    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

    Keywords - Ligandi

    Lectin

    Enzyme and pathway databases

    BRENDAi3.2.1.8. 6052.
    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.
    GH10. Glycoside Hydrolase Family 10.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase A (EC:3.2.1.8)
    Short name:
    Xylanase A
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase A
    Gene namesi
    Name:xlnA
    OrganismiStreptomyces lividans
    Taxonomic identifieri1916 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    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 – 41411 PublicationAdd
    BLAST
    Chaini42 – 477436Endo-1,4-beta-xylanase APRO_0000007979Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi364 ↔ 3831 PublicationPROSITE-ProRule annotation
    Disulfide bondi406 ↔ 4231 PublicationPROSITE-ProRule annotation
    Disulfide bondi447 ↔ 4661 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    477
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi46 – 516
    Turni52 – 543
    Beta strandi56 – 616
    Helixi63 – 653
    Helixi69 – 7810
    Beta strandi80 – 867
    Helixi90 – 934
    Helixi103 – 11412
    Beta strandi118 – 1258
    Beta strandi127 – 1293
    Helixi132 – 1354
    Helixi139 – 15618
    Turni157 – 1604
    Beta strandi162 – 1687
    Beta strandi173 – 1764
    Helixi183 – 1864
    Helixi191 – 20212
    Beta strandi206 – 2149
    Helixi221 – 23616
    Beta strandi242 – 2454
    Beta strandi248 – 2503
    Beta strandi251 – 2533
    Helixi259 – 2679
    Turni268 – 2703
    Beta strandi272 – 2809
    Helixi285 – 29612
    Beta strandi301 – 3077
    Helixi311 – 3133
    Helixi317 – 3193
    Beta strandi322 – 3243
    Helixi332 – 34110
    Turni359 – 3613
    Beta strandi364 – 3663
    Helixi368 – 3703
    Beta strandi379 – 3813
    Helixi387 – 3893
    Beta strandi391 – 3933
    Beta strandi399 – 4013
    Turni402 – 4043
    Beta strandi405 – 4106
    Beta strandi417 – 4226
    Helixi427 – 4293
    Beta strandi431 – 4333
    Beta strandi439 – 4413
    Turni442 – 4443
    Beta strandi447 – 4504
    Helixi451 – 4533
    Beta strandi460 – 4645
    Helixi470 – 4723

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E0VX-ray1.70A42-343[»]
    1E0WX-ray1.20A42-343[»]
    1E0XX-ray1.65A/B42-350[»]
    1KNLX-ray1.20A348-477[»]
    1KNMX-ray1.20A348-477[»]
    1MC9X-ray1.70A348-477[»]
    1OD8X-ray1.05A42-354[»]
    1V0KX-ray1.03A42-354[»]
    1V0LX-ray0.98A42-354[»]
    1V0MX-ray1.07A42-354[»]
    1V0NX-ray1.10A42-354[»]
    1XASX-ray2.60A42-340[»]
    ProteinModelPortaliP26514.
    SMRiP26514. Positions 42-477.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26514.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini361 – 477117Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF00331. Glyco_hydro_10. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00633. Glyco_10. 1 hit.
    SM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P26514-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSYALPRSG VRRSIRVLLL ALVVGVLGTA TALIAPPGAH AAESTLGAAA    50
    AQSGRYFGTA IASGRLSDST YTSIAGREFN MVTAENEMKI DATEPQRGQF 100
    NFSSADRVYN WAVQNGKQVR GHTLAWHSQQ PGWMQSLSGS ALRQAMIDHI 150
    NGVMAHYKGK IVQWDVVNEA FADGSSGARR DSNLQRSGND WIEVAFRTAR 200
    AADPSAKLCY NDYNVENWTW AKTQAMYNMV RDFKQRGVPI DCVGFQSHFN 250
    SGSPYNSNFR TTLQNFAALG VDVAITELDI QGAPASTYAN VTNDCLAVSR 300
    CLGITVWGVR DSDSWRSEQT PLLFNNDGSK KAAYTAVLDA LNGGDSSEPP 350
    ADGGQIKGVG SGRCLDVPDA STSDGTQLQL WDCHSGTNQQ WAATDAGELR 400
    VYGDKCLDAA GTSNGSKVQI YSCWGGDNQK WRLNSDGSVV GVQSGLCLDA 450
    VGNGTANGTL IQLYTCSNGS NQRWTRT 477
    Length:477
    Mass (Da):51,163
    Last modified:May 30, 2000 - v2
    Checksum:iE14A7FE37BDC68CC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64551 Genomic DNA. Translation: AAC26525.1.
    PIRiJS0589.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64551 Genomic DNA. Translation: AAC26525.1 .
    PIRi JS0589.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E0V X-ray 1.70 A 42-343 [» ]
    1E0W X-ray 1.20 A 42-343 [» ]
    1E0X X-ray 1.65 A/B 42-350 [» ]
    1KNL X-ray 1.20 A 348-477 [» ]
    1KNM X-ray 1.20 A 348-477 [» ]
    1MC9 X-ray 1.70 A 348-477 [» ]
    1OD8 X-ray 1.05 A 42-354 [» ]
    1V0K X-ray 1.03 A 42-354 [» ]
    1V0L X-ray 0.98 A 42-354 [» ]
    1V0M X-ray 1.07 A 42-354 [» ]
    1V0N X-ray 1.10 A 42-354 [» ]
    1XAS X-ray 2.60 A 42-340 [» ]
    ProteinModelPortali P26514.
    SMRi P26514. Positions 42-477.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM13. Carbohydrate-Binding Module Family 13.
    GH10. Glycoside Hydrolase Family 10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .
    BRENDAi 3.2.1.8. 6052.

    Miscellaneous databases

    EvolutionaryTracei P26514.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF00331. Glyco_hydro_10. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00633. Glyco_10. 1 hit.
    SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequences of three genes specifying xylanases in Streptomyces lividans."
      Shareck F., Roy C., Yaguchi M., Morosoli R., Kluepfel D.
      Gene 107:75-82(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 42-92.
      Strain: 66 / 1326.
    2. Shareck F.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 20 AND 140-141.
    3. "Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases."
      Derewenda U., Swenson L., Green R., Wei Y.Y., Morosoli R., Shareck F., Kluepfel D., Derewenda Z.S.
      J. Biol. Chem. 269:20811-20814(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 42-340.
    4. "High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding."
      Notenboom V., Boraston A.B., Williams S.J., Kilburn D.G., Rose D.R.
      Biochemistry 41:4246-4254(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 348-477, DISULFIDE BONDS.

    Entry informationi

    Entry nameiXYNA_STRLI
    AccessioniPrimary (citable) accession number: P26514
    Secondary accession number(s): P96464
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 100 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, Direct protein sequencing

    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