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P14768

- XYNA_CELJU

UniProt

P14768 - XYNA_CELJU

Protein

Endo-1,4-beta-xylanase A

Gene

xynA

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 124 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      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 sitei391 – 3911Proton donor
    Active sitei510 – 5101Nucleophile

    GO - Molecular functioni

    1. cellulose binding Source: InterPro
    2. 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

    BioCyciCJAP498211:GHIT-2462-MONOMER.
    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiCBM10. Carbohydrate-Binding Module Family 10.
    CBM2. Carbohydrate-Binding Module Family 2.
    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
    Short name:
    XYLA
    Gene namesi
    Name:xynA
    Synonyms:xyn10A
    Ordered Locus Names:CJA_2471
    OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
    Taxonomic identifieri498211 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio
    ProteomesiUP000001036: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Add
    BLAST
    Chaini27 – 611585Endo-1,4-beta-xylanase APRO_0000007977Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 125By similarity
    Disulfide bondi184 ↔ 2151 Publication
    Disulfide bondi194 ↔ 2091 Publication

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    STRINGi498211.CJA_2471.

    Structurei

    Secondary structure

    1
    611
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi183 – 1864
    Beta strandi189 – 1935
    Beta strandi199 – 2046
    Beta strandi207 – 2104
    Helixi212 – 2154
    Helixi266 – 2694
    Beta strandi274 – 2796
    Beta strandi281 – 2833
    Turni287 – 2893
    Helixi291 – 30010
    Beta strandi302 – 3087
    Helixi312 – 3154
    Helixi324 – 33512
    Beta strandi339 – 3468
    Helixi350 – 3523
    Beta strandi358 – 3603
    Helixi364 – 37815
    Turni379 – 3824
    Beta strandi384 – 3907
    Helixi396 – 3983
    Helixi413 – 4186
    Helixi422 – 43413
    Beta strandi438 – 4469
    Helixi452 – 46615
    Beta strandi473 – 4764
    Beta strandi479 – 4857
    Helixi487 – 49812
    Beta strandi505 – 51511
    Helixi518 – 5203
    Beta strandi523 – 5253
    Helixi530 – 5334
    Helixi538 – 55720
    Helixi560 – 5623
    Beta strandi563 – 5697
    Helixi573 – 5753
    Beta strandi579 – 5813
    Beta strandi589 – 5913
    Helixi599 – 60911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CLXX-ray1.80A/B/C/D265-611[»]
    1E5NX-ray3.20A/B264-611[»]
    1E8RNMR-A180-228[»]
    1QLDNMR-A180-228[»]
    1W2PX-ray1.45A/B265-611[»]
    1W2VX-ray1.55A/B265-611[»]
    1W32X-ray1.20A/B265-611[»]
    1W3HX-ray1.50A/B265-611[»]
    1XYSX-ray2.50A/B265-611[»]
    ProteinModelPortaliP14768.
    SMRiP14768. Positions 180-228, 265-610.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14768.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 128102CBM2Add
    BLAST
    Domaini183 – 21028CBM10Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi131 – 17949Ser-rich (linker)Add
    BLAST
    Compositional biasi227 – 25933Ser-richAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000066328.
    KOiK01181.
    OMAiENIMKMS.
    OrthoDBiEOG6XQ3JG.

    Family and domain databases

    Gene3Di2.30.32.30. 1 hit.
    2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR002883. CBM10/Dockerin_dom.
    IPR018366. CBM2_CS.
    IPR009031. CBM_fam10.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF02013. CBM_10. 1 hit.
    PF00553. CBM_2. 1 hit.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00637. CBD_II. 1 hit.
    SM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    SSF57615. SSF57615. 1 hit.
    PROSITEiPS51173. CBM2. 1 hit.
    PS00561. CBM2_A. 1 hit.
    PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P14768-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRTAMAKSLG AAAFLGAALF AHTLAAQTAT CSYNITNEWN TGYTGDITIT    50
    NRGSSAINGW SVNWQYATNR LSSSWNANVS GSNPYSASNL SWNGNIQPGQ 100
    SVSFGFQVNK NGGSAERPSV GGSICSGSVA SSSAPASSVP SSIASSSPSS 150
    VASSVISSMA SSSPVSSSSV ASSTPGSSSG NQQCNWYGTL YPLCVTTTNG 200
    WGWEDQRSCI ARSTCAAQPA PFGIVGSGSS TPVSSSSSSL SSSSVVSSIR 250
    SSSSSSSSSV ATGNGLASLA DFPIGVAVAA SGGNADIFTS SARQNIVRAE 300
    FNQITAENIM KMSYMYSGSN FSFTNSDRLV SWAAQNGQTV HGHALVWHPS 350
    YQLPNWASDS NANFRQDFAR HIDTVAAHFA GQVKSWDVVN EALFDSADDP 400
    DGRGSANGYR QSVFYRQFGG PEYIDEAFRR ARAADPTAEL YYNDFNTEEN 450
    GAKTTALVNL VQRLLNNGVP IDGVGFQMHV MNDYPSIANI RQAMQKIVAL 500
    SPTLKIKITE LDVRLNNPYD GNSSNDYTNR NDCAVSCAGL DRQKARYKEI 550
    VQAYLEVVPP GRRGGITVWG IADPDSWLYT HQNLPDWPLL FNDNLQPKPA 600
    YQGVVEALSG R 611
    Length:611
    Mass (Da):64,804
    Last modified:November 1, 1997 - v2
    Checksum:i2CFAA3D453E6B68E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti432 – 4332RA → PR in CAA33469. (PubMed:2507868)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15429 Genomic DNA. Translation: CAA33469.1.
    CP000934 Genomic DNA. Translation: ACE85439.1.
    PIRiS06047.
    RefSeqiYP_001982932.1. NC_010995.1.

    Genome annotation databases

    EnsemblBacteriaiACE85439; ACE85439; CJA_2471.
    GeneIDi6414903.
    KEGGicja:CJA_2471.
    PATRICi21328304. VBICelJap122165_2421.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15429 Genomic DNA. Translation: CAA33469.1 .
    CP000934 Genomic DNA. Translation: ACE85439.1 .
    PIRi S06047.
    RefSeqi YP_001982932.1. NC_010995.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CLX X-ray 1.80 A/B/C/D 265-611 [» ]
    1E5N X-ray 3.20 A/B 264-611 [» ]
    1E8R NMR - A 180-228 [» ]
    1QLD NMR - A 180-228 [» ]
    1W2P X-ray 1.45 A/B 265-611 [» ]
    1W2V X-ray 1.55 A/B 265-611 [» ]
    1W32 X-ray 1.20 A/B 265-611 [» ]
    1W3H X-ray 1.50 A/B 265-611 [» ]
    1XYS X-ray 2.50 A/B 265-611 [» ]
    ProteinModelPortali P14768.
    SMRi P14768. Positions 180-228, 265-610.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 498211.CJA_2471.

    Protein family/group databases

    CAZyi CBM10. Carbohydrate-Binding Module Family 10.
    CBM2. Carbohydrate-Binding Module Family 2.
    GH10. Glycoside Hydrolase Family 10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACE85439 ; ACE85439 ; CJA_2471 .
    GeneIDi 6414903.
    KEGGi cja:CJA_2471.
    PATRICi 21328304. VBICelJap122165_2421.

    Phylogenomic databases

    HOGENOMi HOG000066328.
    KOi K01181.
    OMAi ENIMKMS.
    OrthoDBi EOG6XQ3JG.

    Enzyme and pathway databases

    UniPathwayi UPA00114 .
    BioCyci CJAP498211:GHIT-2462-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P14768.

    Family and domain databases

    Gene3Di 2.30.32.30. 1 hit.
    2.60.40.290. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR002883. CBM10/Dockerin_dom.
    IPR018366. CBM2_CS.
    IPR009031. CBM_fam10.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF02013. CBM_10. 1 hit.
    PF00553. CBM_2. 1 hit.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00637. CBD_II. 1 hit.
    SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 1 hit.
    SSF57615. SSF57615. 1 hit.
    PROSITEi PS51173. CBM2. 1 hit.
    PS00561. CBM2_A. 1 hit.
    PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conserved serine-rich sequences in xylanase and cellulase from Pseudomonas fluorescens subspecies cellulosa: internal signal sequence and unusual protein processing."
      Hall J., Hazlewood G.P., Huskisson N.S., Durrant A.J., Gilbert H.J.
      Mol. Microbiol. 3:1211-1219(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    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.
    3. "Structure of the catalytic core of the family F xylanase from Pseudomonas fluorescens and identification of the xylopentaose-binding sites."
      Harris G.W., Jenkins J.A., Connerton I., Cummings N., Lo Leggio L., Scott M., Hazlewood G.P., Laurie J.I., Gilbert H.J., Pickersgill R.W.
      Structure 2:1107-1116(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 265-611, SEQUENCE REVISION.
    4. "Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8-A resolution."
      Harris G.W., Jenkins J.A., Connerton I., Pickersgill R.W.
      Acta Crystallogr. D 52:393-401(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 265-611.
    5. "Solution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A."
      Raghothama S., Simpson P.J., Szabo L., Nagy T., Gilbert H.J., Williamson M.P.
      Biochemistry 39:978-984(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 180-228, DISULFIDE BONDS.

    Entry informationi

    Entry nameiXYNA_CELJU
    AccessioniPrimary (citable) accession number: P14768
    Secondary accession number(s): B3PKK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 124 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, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3