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C6CRV0

- XYNA1_PAESJ

UniProt

C6CRV0 - XYNA1_PAESJ

Protein

Endo-1,4-beta-xylanase A

Gene

xynA1

Organism
Paenibacillus sp. (strain JDR-2)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (01 Sep 2009)
      Previous versions | rss
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    Functioni

    Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn), a beta-1,4 xylan in which 10% to 20% of the xylose residues are substituted with alpha-1,2-4-O-methylglucuronate (MeGA) residues, which is predominant in hemicellulose fractions of hardwood and crop residues. Generates xylobiose (X2) and aldotetrauronate (MeGAX3) as the predominant products of MeGAXn hydrolysis; these products are then directly assimilated by the bacterium for subsequent metabolism. Thus, allows the bacterium to efficiently use polymeric MeGAXn as a growth substrate.1 Publication

    Catalytic activityi

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

    Kineticsi

      Vmax=8.0 µmol/min/mg enzyme with sweet gum methylglucuronoxylan as substrate1 Publication

      pH dependencei

      Optimum pH is 6.5 with sweet gum methylglucuronoxylan as substrate.1 Publication

      Temperature dependencei

      Optimum temperature is 45 degrees Celsius with sweet gum methylglucuronoxylan as substrate.1 Publication

      Pathwayi

      Sites

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Active sitei651 – 6511Proton donorBy similarity
      Active sitei706 – 7061By similarity
      Active sitei775 – 7751NucleophilePROSITE-ProRule annotation

      GO - Molecular functioni

      1. carbohydrate binding Source: InterPro
      2. 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

      BioCyciPSP324057:GH5H-261-MONOMER.
      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 A (EC:3.2.1.8)
      Alternative name(s):
      1,4-beta-D-xylan xylanohydrolase A
      Gene namesi
      Name:xynA1
      Synonyms:xynA
      Ordered Locus Names:Pjdr2_0221
      OrganismiPaenibacillus sp. (strain JDR-2)
      Taxonomic identifieri324057 [NCBI]
      Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus
      ProteomesiUP000002510: Chromosome

      Subcellular locationi

      Secretedcell wall 1 Publication

      GO - Cellular componenti

      1. cell wall Source: UniProtKB
      2. extracellular region Source: UniProtKB-KW

      Keywords - Cellular componenti

      Cell wall, Secreted

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Signal peptidei1 – 3030Sequence AnalysisAdd
      BLAST
      Chaini31 – 14621432Endo-1,4-beta-xylanase APRO_5000484609Add
      BLAST

      Interactioni

      Protein-protein interaction databases

      STRINGi324057.Pjdr2_0221.

      Structurei

      Secondary structure

      1
      1462
      Legend: HelixTurnBeta strand
      Show more details
      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Helixi520 – 5234
      Turni524 – 5274
      Beta strandi529 – 5346
      Helixi536 – 5394
      Helixi541 – 55010
      Beta strandi552 – 5587
      Helixi562 – 5654
      Helixi575 – 58612
      Beta strandi590 – 5978
      Beta strandi599 – 6013
      Helixi604 – 6063
      Beta strandi608 – 6103
      Beta strandi616 – 6183
      Helixi621 – 63919
      Helixi640 – 6423
      Beta strandi643 – 6508
      Helixi664 – 6663
      Helixi671 – 6766
      Helixi680 – 69415
      Beta strandi701 – 7077
      Helixi712 – 73221
      Turni733 – 7353
      Beta strandi741 – 7444
      Beta strandi747 – 7493
      Helixi754 – 76512
      Turni766 – 7683
      Beta strandi770 – 77910
      Helixi787 – 80721
      Helixi808 – 8114
      Beta strandi812 – 8176
      Helixi822 – 8243
      Helixi828 – 8303
      Beta strandi833 – 8353
      Helixi843 – 8497

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      EntryMethodResolution (Å)ChainPositionsPDBsum
      3RDKX-ray1.49A/B518-851[»]
      3RO8X-ray1.34A/B/C/D/E/F/G/H518-851[»]
      4E4PX-ray1.92A/B518-851[»]
      ProteinModelPortaliC6CRV0.
      ModBaseiSearch...
      MobiDBiSearch...

      Family & Domainsi

      Domains and Repeats

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Domaini64 – 165102CBM-cenC 1Add
      BLAST
      Domaini207 – 319113CBM-cenC 2Add
      BLAST
      Domaini360 – 490131CBM-cenC 3Add
      BLAST
      Domaini1279 – 134264SLH 1PROSITE-ProRule annotationAdd
      BLAST
      Domaini1345 – 140460SLH 2PROSITE-ProRule annotationAdd
      BLAST
      Domaini1407 – 146256SLH 3PROSITE-ProRule annotationAdd
      BLAST

      Compositional bias

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Compositional biasi186 – 1916Poly-Thr

      Sequence similaritiesi

      Contains 3 SLH (S-layer homology) domains.PROSITE-ProRule annotation

      Keywords - Domaini

      Repeat, Signal

      Phylogenomic databases

      eggNOGiCOG3693.
      HOGENOMiHOG000049670.
      KOiK01181.
      OMAiHVLVWHQ.
      OrthoDBiEOG6WMHV1.

      Family and domain databases

      Gene3Di2.60.120.260. 3 hits.
      2.60.40.1190. 1 hit.
      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.
      IPR001119. S-layer_homology_dom.
      [Graphical view]
      PfamiPF02018. CBM_4_9. 3 hits.
      PF06452. DUF1083. 1 hit.
      PF00331. Glyco_hydro_10. 1 hit.
      PF00395. SLH. 3 hits.
      [Graphical view]
      PRINTSiPR00134. GLHYDRLASE10.
      SMARTiSM00633. Glyco_10. 1 hit.
      [Graphical view]
      SUPFAMiSSF49785. SSF49785. 3 hits.
      SSF51445. SSF51445. 1 hit.
      PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
      PS51272. SLH. 3 hits.
      [Graphical view]

      Sequencei

      Sequence statusi: Complete.

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

      C6CRV0-1 [UniParc]FASTAAdd to Basket

      « Hide

      MSRSLKKFVS ILLAAALLIP IGRLAPVAEA AENPTIVYHE DFAIDKGKAI     50
      QSGGASLTQV TGKVFDGNND GSALYVSNRA NTWDAADFKF ADIGLQNGKT 100
      YTVTVKGYVD QDATVPSGAQ AFLQAVDSNN YGFLASANFA AGTAFTLTKE 150
      FTVDTSVSTQ LRVQSSEEGK AVPFYIGDIL ITANPTTTTN TVYHEDFATD 200
      KGKAVQSGGA NLAQVADKVF DGNDDGKALY VSNRANTWDA ADFKFADIGL 250
      QNGKTYTVTV KGYVDQDATV PSGAQAFLQA VDSNNYGFLA SANFAARSAF 300
      TLTKEFTVDT SVSTQLRVQS SEEGKAVPFY IGDILITETV NSGGGQEDPP 350
      RPPALPFNTI TFEDQTAGGF TGRAGTETLT VTNESNHTAD GSYSLKVEGR 400
      TTSWHGPSLR VEKYVDKGYE YKVTAWVKLL SPETSTKLEL ASQVGDGGSA 450
      NYPSLASKTI TAADGWVQLQ GNYRYNSVGG EYLTIYVQSS NATASYYIDD 500
      ISFESTGSGP VGIQKDLAPL KDVYKNDFLI GNAISAEDLE GTRLELLKMH 550
      HDVVTAGNAM KPDALQPTKG NFTFTAADAM IDKVLAEGMK MHGHVLVWHQ 600
      QSPAWLNTKK DDNNNTVPLG RDEALDNLRT HIQTVMKHFG NKVISWDVVN 650
      EAMNDNPSNP ADYKASLRQT PWYQAIGSDY VEQAFLAARE VLDENPSWNI 700
      KLYYNDYNED NQNKATAIYN MVKDINDRYA AAHNGKLLID GVGMQGHYNI 750
      NTNPDNVKLS LEKFISLGVE VSVSELDVTA GNNYTLPENL AVGQAYLYAQ 800
      LFKLYKEHAD HIARVTFWGM DDNTSWRAEN NPLLFDKNLQ AKPAYYGVID 850
      PDKYMEEHAP ESKDANQAEA QYGTPVIDGT VDSIWSNAQA MPVNRYQMAW 900
      QGATGTAKAL WDDQNLYVLI QVSDSQLNKA NENAWEQDSV EVFLDQNNGK 950
      TTFYQNDDGQ YRVNFDNETS FSPASIAAGF ESQTKKTANS YTVELKIPLT 1000
      AVTPANQKKL GFDVQINDAT DGARTSVAAW NDTTGNGYQD TSVYGELTLA 1050
      GKGTGGTGTV GTTVPQTGNV VKNPDGSTTL KPEVKTTNGN AVGTVTGDDL 1100
      KKALDQAAPA AGGKKQVIID VPLQANAATY AVQLPTQSLK SQDGYQLTAK 1150
      IANAFIQIPS NMLANTNVTT DQVSIRVAKA SLDNVDAATR ELIGNRPVID 1200
      LSLVAGGNVI AWNNPTAPVT VAVPYAPTAE ELKHPEHILI WYIDGSGKAT 1250
      PVPNSRYDAA LGAVVFQTTH FSTYAAVSVF TTFGDLAKVP WAKEAIDAMA 1300
      SRGVIKGTGE NTFSPAASIK RADFIALLVR ALELHGTGTT DTAMFSDVPA 1350
      NAYYYNELAV AKQLGIATGF EDNTFKPDSS ISRQDMMVLT TRALAVLGKQ 1400
      LPAGGSLNAF SDAASVAGYA QDSVAALVKA GVVQGSGSKL APNDQLTRAE 1450
      AAVILYRIWK LQ 1462
      Length:1,462
      Mass (Da):157,322
      Last modified:September 1, 2009 - v1
      Checksum:iAE29664CDEA3BF3E
      GO

      Experimental Info

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Sequence conflicti313 – 3131S → T in CAI79477. (PubMed:16461704)Curated
      Sequence conflicti454 – 4618SLASKTIT → TPTTQAWQARRLP in CAI79477. (PubMed:16461704)Curated

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      AJ938162 Genomic DNA. Translation: CAI79477.1.
      CP001656 Genomic DNA. Translation: ACS98901.1.
      RefSeqiWP_012772223.1. NC_012914.1.
      YP_003008988.1. NC_012914.1.

      Genome annotation databases

      EnsemblBacteriaiACS98901; ACS98901; Pjdr2_0221.
      GeneIDi8127565.
      KEGGipjd:Pjdr2_0221.
      PATRICi22830917. VBIPaeSp118865_0225.

      Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      AJ938162 Genomic DNA. Translation: CAI79477.1 .
      CP001656 Genomic DNA. Translation: ACS98901.1 .
      RefSeqi WP_012772223.1. NC_012914.1.
      YP_003008988.1. NC_012914.1.

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      Entry Method Resolution (Å) Chain Positions PDBsum
      3RDK X-ray 1.49 A/B 518-851 [» ]
      3RO8 X-ray 1.34 A/B/C/D/E/F/G/H 518-851 [» ]
      4E4P X-ray 1.92 A/B 518-851 [» ]
      ProteinModelPortali C6CRV0.
      ModBasei Search...
      MobiDBi Search...

      Protein-protein interaction databases

      STRINGi 324057.Pjdr2_0221.

      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...

      Genome annotation databases

      EnsemblBacteriai ACS98901 ; ACS98901 ; Pjdr2_0221 .
      GeneIDi 8127565.
      KEGGi pjd:Pjdr2_0221.
      PATRICi 22830917. VBIPaeSp118865_0225.

      Phylogenomic databases

      eggNOGi COG3693.
      HOGENOMi HOG000049670.
      KOi K01181.
      OMAi HVLVWHQ.
      OrthoDBi EOG6WMHV1.

      Enzyme and pathway databases

      UniPathwayi UPA00114 .
      BioCyci PSP324057:GH5H-261-MONOMER.

      Family and domain databases

      Gene3Di 2.60.120.260. 3 hits.
      2.60.40.1190. 1 hit.
      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.
      IPR001119. S-layer_homology_dom.
      [Graphical view ]
      Pfami PF02018. CBM_4_9. 3 hits.
      PF06452. DUF1083. 1 hit.
      PF00331. Glyco_hydro_10. 1 hit.
      PF00395. SLH. 3 hits.
      [Graphical view ]
      PRINTSi PR00134. GLHYDRLASE10.
      SMARTi SM00633. Glyco_10. 1 hit.
      [Graphical view ]
      SUPFAMi SSF49785. SSF49785. 3 hits.
      SSF51445. SSF51445. 1 hit.
      PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
      PS51272. SLH. 3 hits.
      [Graphical view ]
      ProtoNeti Search...

      Publicationsi

      1. "Paenibacillus sp. strain JDR-2 and XynA1: a novel system for methylglucuronoxylan utilization."
        Stjohn F.J., Rice J.D., Preston J.F.
        Appl. Environ. Microbiol. 72:1496-1506(2006) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
        Strain: JDR-2.
      2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
        Strain: JDR-2.

      Entry informationi

      Entry nameiXYNA1_PAESJ
      AccessioniPrimary (citable) accession number: C6CRV0
      Secondary accession number(s): Q53I45
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: May 31, 2011
      Last sequence update: September 1, 2009
      Last modified: October 1, 2014
      This is version 38 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. 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