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C6CRV0

- XYNA1_PAESJ

UniProt

C6CRV0 - XYNA1_PAESJ

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Protein

Endo-1,4-beta-xylanase A

Gene
xynA1, xynA, Pjdr2_0221
Organism
Paenibacillus sp. (strain JDR-2)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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.

    Temperature dependencei

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei651 – 6511Proton donor By similarity
    Active sitei706 – 7061 By similarity
    Active sitei775 – 7751Nucleophile By similarity

    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
    Complete GO annotation...

    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
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell wall, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030 Reviewed predictionAdd
    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.

    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 1Add
    BLAST
    Domaini1345 – 140460SLH 2Add
    BLAST
    Domaini1407 – 146256SLH 3Add
    BLAST

    Compositional bias

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

    Sequence similaritiesi

    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

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti313 – 3131S → T in CAI79477. 1 Publication
    Sequence conflicti454 – 4618SLASKTIT → TPTTQAWQARRLP in CAI79477. 1 Publication

    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

    « Hide 'large scale' publications
    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: September 3, 2014
    This is version 37 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

    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

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