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O69230

- XYNC_PAEBA

UniProt

O69230 - XYNC_PAEBA

Protein

Endo-1,4-beta-xylanase C

Gene

xynC

Organism
Paenibacillus barcinonensis
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Endoxylanase with high hydrolytic activity on birchwood and oat spelt xylan. Xylotetraose, xylotriose, xylobiose and xylose are the main products from birchwood xylan hydrolysis. Shows increasing activity on xylo-oligosaccharides of increasing length. Displays very low hydrolytic activity on Avicel, carboxymethylcellulose (CMC) and p-nitrophenyl-beta-xylopyranoside. Also shows transxylosidase activity, allowing the formation of xylo-oligosaccharides of higher degreee of polymerization than the starting substrate.1 Publication

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 5. Retains at least 50% of its maximum activity between pH 4.5 and 8.0. Is not active at pH values below 4.5, while at least 35% of maximum activity is found in the pH range 8.5-11.0.1 Publication

    Temperature dependencei

    Optimum temperature is 45 degrees Celsius. Is only stable at 55 degrees Celsius or lower temperatures. Retains more than 77% activity after 2 hours incubation at 55 degrees Celsius and pH 7.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei502 – 5021Proton donorBy similarity
    Active sitei556 – 5561By similarity
    Active sitei620 – 6201NucleophilePROSITE-ProRule annotation

    GO - Molecular functioni

    1. carbohydrate 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

    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiCBM22. Carbohydrate-Binding Module Family 22.
    CBM9. Carbohydrate-Binding Module Family 9.
    GH10. 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
    Gene namesi
    Name:xynC
    OrganismiPaenibacillus barcinonensis
    Taxonomic identifieri198119 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 10861055Endo-1,4-beta-xylanase CPRO_0000371420Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliO69230.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 183149CBM-cenC 1Add
    BLAST
    Domaini197 – 359163CBM-cenC 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni370 – 711342CatalyticAdd
    BLAST

    Domaini

    Consists of three different domains. The central region of the enzyme is the catalytic domain. The N-terminal region contains cenC-type cellulose-binding domains and seems to act as a thermostabilizing domain: a derivative lacking this region shows a lower optimum temperature for activity (35 degrees Celsius) than the full-length enzyme, and a reduced thermal stability that results in a complete inactivation of the enzyme after 2 hours incubation at 55 degrees Celsius. The C-terminal region contains family 9 carbohydrate-binding modules.

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.60.120.260. 2 hits.
    2.60.40.1190. 2 hits.
    3.20.20.80. 1 hit.
    InterProiIPR010502. Carb-bd_dom_fam9.
    IPR003305. CenC_carb-bd.
    IPR008979. Galactose-bd-like.
    IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF02018. CBM_4_9. 2 hits.
    PF06452. DUF1083. 2 hits.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O69230-1 [UniParc]FASTAAdd to Basket

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    MRGKWLRLCL AAVLIVSLLP GLGAGEWKAS AAKAGDILLS HSFEEGTTQG     50
    WTARGGVKVD VTAEQAYQGK QSLQTTGRTE AWNGPSLSLT DVVHKNEVVE 100
    ISGYVKLVAG SAPPDLKFTV ERRDRNGDTQ YDQVNAAEQV TDQKWVKLQG 150
    QYSYEQGSSL LLYLESTDAK AAYLLDEFQI RLVKAAPENP GEPGEAGQAL 200
    FKAYFEDGNI GNWRARGTEK LEVVSGIGHN SNRSLKTSSR SETYHGPLVE 250
    VLPYLQKGST VHISFWAMYD EGPATQVING SLEKEFNRDT ANLEYAMFAS 300
    TTLNKGQWKK IEADIIVPAE STGISGLRMY AETPWKQSSE VTETDTIPFY 350
    VDDVQITATE AIAIEKNIPD LAKKLGSSYA LGAAIDQTAL DPKDPHSELL 400
    TKHFNSITAG NFMKMDAMQP TEGKFVWSEA DKLVNFAAAN NMQVRGHTLL 450
    WHSQVPDWFF TDPNDPSKPA TREQLMQRMK THIQTIVSRY KGKVHTWDVV 500
    NEVISDGGGL RNQASGSKWR DIIGDVDGDG DDSDYIELAF RYAREADPDA 550
    VLVINDYGIE GSVSKMNDMV KLVEKLLAKG TPIDAIGFQM HVSMYGPDIK 600
    QIREAFNRAA ALGVHIQVTE LDMSIYSGNS EQEKPVTDEM MLEQAYRYRA 650
    LFDLFKEFDD RGVMDSVTLW GLADDGTWLD DFPVKGRKDA PLLFDRKLKA 700
    KPAYWALVDP STLPVYRNEW TASQAKVSLP DRKGQEDIIW GAVRALPFSH 750
    VIEGAVGTTG EVKTLWDGKQ LNLRIEVKDA TRLKGDQVEV FVSPEDMTAG 800
    KKNSTPKDGQ YIFNRDGGKG KDQKLYQVKE NKSGYVVYAS LPLSSADLAA 850
    GKVLSLDFRI TDKQPNGKTS IVVWNDVNNQ QPQKTENRGK LKLGFDLKHA 900
    KVMYGTPTVD GKEDKLWKKA VTITTDVKVT GNSGAKAKAK LLWDEKYLYV 950
    LAEVKDPLLS KKSANAHEQD SIELFIDLNK NQTNSYEEDD AQYRVNFDNE 1000
    TSFGGSPRKE LFKSATRLTK EGYIVEAAIP LENVRTKESK WIGFDLQVND 1050
    DGAGDGKRSS VFMWSDPSGN SYRDTSGFGS LLLMKK 1086
    Length:1,086
    Mass (Da):120,586
    Last modified:August 1, 1998 - v1
    Checksum:i4378361F1801A326
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006645 Genomic DNA. Translation: CAA07173.1.
    PIRiT17628.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006645 Genomic DNA. Translation: CAA07173.1 .
    PIRi T17628.

    3D structure databases

    ProteinModelPortali O69230.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM22. Carbohydrate-Binding Module Family 22.
    CBM9. Carbohydrate-Binding Module Family 9.
    GH10. Glycoside Hydrolase Family 10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .

    Family and domain databases

    Gene3Di 2.60.120.260. 2 hits.
    2.60.40.1190. 2 hits.
    3.20.20.80. 1 hit.
    InterProi IPR010502. Carb-bd_dom_fam9.
    IPR003305. CenC_carb-bd.
    IPR008979. Galactose-bd-like.
    IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF02018. CBM_4_9. 2 hits.
    PF06452. DUF1083. 2 hits.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes."
      Blanco A., Diaz P., Zueco J., Parascandola P., Pastor F.I.J.
      Microbiology 145:2163-2170(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: DSM 15478 / CECT 7022 / BP-23.

    Entry informationi

    Entry nameiXYNC_PAEBA
    AccessioniPrimary (citable) accession number: O69230
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3