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Q00177

- XYNC_EMENI

UniProt

Q00177 - XYNC_EMENI

Protein

Endo-1,4-beta-xylanase C

Gene

xlnC

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.2 Publications

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 4.9.1 Publication

    Temperature dependencei

    Optimum temperature is 52 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei154 – 1541Proton donorBy similarity
    Active sitei262 – 2621NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BioCyciRETL1328306-WGS:GSTH-3265-MONOMER.
    BRENDAi3.2.1.8. 9578.
    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiGH10. Glycoside Hydrolase Family 10.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase C (EC:3.2.1.8)
    Short name:
    Xylanase C
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase C
    34 kDa xylanase
    Xylanase X34
    Gene namesi
    Name:xlnC
    ORF Names:AN1818
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome VII

    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 – 2424By similarityAdd
    BLAST
    Chaini25 – 327303Endo-1,4-beta-xylanase CPRO_0000007974Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251Pyrrolidone carboxylic acidBy similarity
    Disulfide bondi280 ↔ 2861 Publication

    Keywords - PTMi

    Disulfide bond, Pyrrolidone carboxylic acid

    Expressioni

    Inductioni

    Expressed in presence of xylan and repressed by glucose.1 Publication

    Structurei

    Secondary structure

    1
    327
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi29 – 357
    Beta strandi39 – 457
    Helixi47 – 515
    Helixi53 – 6210
    Beta strandi64 – 707
    Helixi74 – 774
    Helixi87 – 9812
    Beta strandi102 – 1098
    Beta strandi111 – 1133
    Helixi116 – 1194
    Helixi124 – 14118
    Turni142 – 1443
    Beta strandi147 – 1548
    Beta strandi160 – 1623
    Helixi166 – 1716
    Helixi174 – 18613
    Beta strandi190 – 1978
    Helixi205 – 21915
    Beta strandi226 – 2294
    Helixi240 – 2423
    Helixi243 – 2519
    Beta strandi256 – 26510
    Helixi270 – 28112
    Beta strandi286 – 2927
    Helixi296 – 2983
    Helixi302 – 3043
    Beta strandi307 – 3093
    Helixi317 – 32610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TA3X-ray1.70B25-327[»]
    ProteinModelPortaliQ00177.
    SMRiQ00177. Positions 27-327.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00177.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3693.
    HOGENOMiHOG000019847.
    KOiK01181.
    OrthoDBiEOG7GJ6PM.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q00177-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVHLKTLAGS AVFASLATAA VLPRQSASLN DLFVAAGKSY FGTCSDQALL    50
    QNSQNEAIVA SQFGVITPEN SMKWDALEPS QGNFGWSGAD YLVDYATQHN 100
    KKVRGHTLVW HSQLPSWVSS IGDANTLRSV MTNHINEVVG RYKGKIMHWD 150
    VVNEIFNEDG TFRNSVFYNL LGEDFVRIAF ETARAADPDA KLYINDYNLD 200
    SASYAKTQAM ASYVKKWLAE GVPIDGIGSQ AHYSSSHWSS TEAAGALSSL 250
    ANTGVSEVAI TELDIAGAAS SDYLNLLNAC LNEQKCVGIT VWGVSDKDSW 300
    RASDSPLLFD GNYQPKDAYN AIVNALS 327
    Length:327
    Mass (Da):35,441
    Last modified:November 1, 1996 - v1
    Checksum:iB59CF4DE435F6F20
    GO

    Sequence cautioni

    The sequence CBF85620.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAA64983.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49894 Genomic DNA. Translation: CAA90075.1.
    DQ490475 mRNA. Translation: ABF50851.1.
    AACD01000029 Genomic DNA. Translation: EAA64983.1. Sequence problems.
    BN001307 Genomic DNA. Translation: CBF85620.1. Sequence problems.
    PIRiJC5034.
    RefSeqiXP_659422.1. XM_654330.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00008467; CADANIAP00008467; CADANIAG00008467.
    GeneIDi2874673.
    KEGGiani:AN1818.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49894 Genomic DNA. Translation: CAA90075.1 .
    DQ490475 mRNA. Translation: ABF50851.1 .
    AACD01000029 Genomic DNA. Translation: EAA64983.1 . Sequence problems.
    BN001307 Genomic DNA. Translation: CBF85620.1 . Sequence problems.
    PIRi JC5034.
    RefSeqi XP_659422.1. XM_654330.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TA3 X-ray 1.70 B 25-327 [» ]
    ProteinModelPortali Q00177.
    SMRi Q00177. Positions 27-327.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH10. Glycoside Hydrolase Family 10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00008467 ; CADANIAP00008467 ; CADANIAG00008467 .
    GeneIDi 2874673.
    KEGGi ani:AN1818.2.

    Phylogenomic databases

    eggNOGi COG3693.
    HOGENOMi HOG000019847.
    KOi K01181.
    OrthoDBi EOG7GJ6PM.

    Enzyme and pathway databases

    UniPathwayi UPA00114 .
    BioCyci RETL1328306-WGS:GSTH-3265-MONOMER.
    BRENDAi 3.2.1.8. 9578.

    Miscellaneous databases

    EvolutionaryTracei Q00177.

    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.
    [Graphical view ]
    Pfami PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification, isolation and sequence of the Aspergillus nidulans xlnC gene encoding the 34-kDa xylanase."
      Maccabe A.P., Fernandez-Espinar M.-T., de Graaff L.H., Visser J., Ramon D.
      Gene 175:29-33(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
    2. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
      Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
      Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    4. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    5. "The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases."
      Payan F., Leone P., Porciero S., Furniss C., Tahir T., Williamson G., Durand A., Manzanares P., Gilbert H.J., Juge N., Roussel A.
      J. Biol. Chem. 279:36029-36037(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 25-327 IN COMPLEX WITH WHEAT XIP-1, DISULFIDE BOND.

    Entry informationi

    Entry nameiXYNC_EMENI
    AccessioniPrimary (citable) accession number: Q00177
    Secondary accession number(s): C8VPM8, Q1HFU9, Q5BCB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 101 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, Complete proteome, 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