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P18429

- XYNA_BACSU

UniProt

P18429 - XYNA_BACSU

Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei106 – 1061Nucleophile1 PublicationPROSITE-ProRule annotation
    Active sitei200 – 2001Proton 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

    BioCyciBSUB:BSU18840-MONOMER.
    BRENDAi3.2.1.8. 700.
    SABIO-RKP18429.
    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiGH11. Glycoside Hydrolase Family 11.

    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:xynA
    Ordered Locus Names:BSU18840
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU18840. [Micado]

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1061E → S: Drastically reduced activity. 1 Publication
    Mutagenesisi200 – 2001E → S: Drastically reduced activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Add
    BLAST
    Chaini29 – 213185Endo-1,4-beta-xylanase APRO_0000007999Add
    BLAST

    Proteomic databases

    PaxDbiP18429.

    Interactioni

    Protein-protein interaction databases

    IntActiP18429. 2 interactions.
    MINTiMINT-7101863.
    STRINGi224308.BSU18840.

    Structurei

    Secondary structure

    1
    213
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 386
    Beta strandi42 – 487
    Beta strandi53 – 608
    Beta strandi62 – 7211
    Beta strandi78 – 10124
    Turni102 – 1043
    Beta strandi105 – 11511
    Beta strandi121 – 1288
    Beta strandi131 – 14515
    Beta strandi148 – 16215
    Beta strandi170 – 1734
    Helixi174 – 18310
    Beta strandi190 – 20314
    Beta strandi205 – 2139

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AXKX-ray2.10A/B29-213[»]
    1XXNX-ray1.70A29-213[»]
    2B42X-ray2.50B29-213[»]
    2B45X-ray2.00X29-213[»]
    2B46X-ray2.21X29-213[»]
    2DCYX-ray1.40A/B/C/D/E29-213[»]
    2DCZX-ray1.90A/B29-213[»]
    2QZ3X-ray1.80A/B29-213[»]
    2Z79X-ray1.30A/B29-213[»]
    3EXUX-ray1.81A/B29-213[»]
    3HD8X-ray2.39B/D29-213[»]
    ProteinModelPortaliP18429.
    SMRiP18429. Positions 29-213.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18429.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG05353.
    HOGENOMiHOG000179135.
    KOiK01181.
    OMAiTYDIYTT.
    OrthoDBiEOG63VBWG.
    PhylomeDBiP18429.

    Family and domain databases

    Gene3Di2.60.120.180. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    [Graphical view]
    PfamiPF00457. Glyco_hydro_11. 1 hit.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P18429-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKFKKNFLV GLSAALMSIS LFSATASAAS TDYWQNWTDG GGIVNAVNGS    50
    GGNYSVNWSN TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NGYLTLYGWT 100
    RSPLIEYYVV DSWGTYRPTG TYKGTVKSDG GTYDIYTTTR YNAPSIDGDR 150
    TTFTQYWSVR QSKRPTGSNA TITFSNHVNA WKSHGMNLGS NWAYQVMATE 200
    GYQSSGSSNV TVW 213
    Length:213
    Mass (Da):23,345
    Last modified:November 1, 1990 - v1
    Checksum:i20CBA35238CC0564
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36648 Genomic DNA. Translation: AAA22897.1.
    AF027868 Genomic DNA. Translation: AAB84458.1.
    AL009126 Genomic DNA. Translation: CAB13776.1.
    PIRiI40569.
    RefSeqiNP_389765.1. NC_000964.3.
    WP_003231377.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB13776; CAB13776; BSU18840.
    GeneIDi939861.
    KEGGibsu:BSU18840.
    PATRICi18975607. VBIBacSub10457_1994.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36648 Genomic DNA. Translation: AAA22897.1 .
    AF027868 Genomic DNA. Translation: AAB84458.1 .
    AL009126 Genomic DNA. Translation: CAB13776.1 .
    PIRi I40569.
    RefSeqi NP_389765.1. NC_000964.3.
    WP_003231377.1. NZ_CM000487.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AXK X-ray 2.10 A/B 29-213 [» ]
    1XXN X-ray 1.70 A 29-213 [» ]
    2B42 X-ray 2.50 B 29-213 [» ]
    2B45 X-ray 2.00 X 29-213 [» ]
    2B46 X-ray 2.21 X 29-213 [» ]
    2DCY X-ray 1.40 A/B/C/D/E 29-213 [» ]
    2DCZ X-ray 1.90 A/B 29-213 [» ]
    2QZ3 X-ray 1.80 A/B 29-213 [» ]
    2Z79 X-ray 1.30 A/B 29-213 [» ]
    3EXU X-ray 1.81 A/B 29-213 [» ]
    3HD8 X-ray 2.39 B/D 29-213 [» ]
    ProteinModelPortali P18429.
    SMRi P18429. Positions 29-213.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P18429. 2 interactions.
    MINTi MINT-7101863.
    STRINGi 224308.BSU18840.

    Protein family/group databases

    CAZyi GH11. Glycoside Hydrolase Family 11.

    Proteomic databases

    PaxDbi P18429.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13776 ; CAB13776 ; BSU18840 .
    GeneIDi 939861.
    KEGGi bsu:BSU18840.
    PATRICi 18975607. VBIBacSub10457_1994.

    Organism-specific databases

    GenoListi BSU18840. [Micado ]

    Phylogenomic databases

    eggNOGi NOG05353.
    HOGENOMi HOG000179135.
    KOi K01181.
    OMAi TYDIYTT.
    OrthoDBi EOG63VBWG.
    PhylomeDBi P18429.

    Enzyme and pathway databases

    UniPathwayi UPA00114 .
    BioCyci BSUB:BSU18840-MONOMER.
    BRENDAi 3.2.1.8. 700.
    SABIO-RK P18429.

    Miscellaneous databases

    EvolutionaryTracei P18429.

    Family and domain databases

    Gene3Di 2.60.120.180. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    [Graphical view ]
    Pfami PF00457. Glyco_hydro_11. 1 hit.
    [Graphical view ]
    PRINTSi PR00911. GLHYDRLASE11.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A xylanase gene from Bacillus subtilis: nucleotide sequence and comparison with B. pumilus gene."
      Paice M.G., Bourbonnais R., Desrochers M., Jurasek L., Yaguchi M.
      Arch. Microbiol. 144:201-206(1986)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequence analysis of the Bacillus subtilis chromosome region between the terC and odhAB loci cloned in a yeast artificial chromosome."
      Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    4. Wakarchuk W., Methot N., Lanthier P., Sung W., Seligy V., Yaguchi M., To R., Campbell R., Rose D.
      (In) Visser J., Beldman G., Kusters-van Someren M.A., Voragen A.G.J. (eds.); Xylans and xylanases, pp.439-442, Elsevier, Amsterdam (1992)
      Cited for: MUTAGENESIS.
    5. "Identification of glutamic acid 78 as the active site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry."
      Miao S., Ziser L., Aebersold R., Withers S.G.
      Biochemistry 33:7027-7032(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE GLU-106.

    Entry informationi

    Entry nameiXYNA_BACSU
    AccessioniPrimary (citable) accession number: P18429
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3