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C6CRV0 (XYNA1_PAESJ) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase A

EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Gene names
Name:xynA1
Synonyms:xynA
Ordered Locus Names:Pjdr2_0221
OrganismPaenibacillus sp. (strain JDR-2) [Complete proteome] [HAMAP]
Taxonomic identifier324057 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length1462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secretedcell wall Ref.1.

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Contains 3 CBM-cenC (cenC-type cellulose-binding) domains.

Contains 3 SLH (S-layer homology) domains.

Biophysicochemical properties

Kinetic parameters:

Vmax=8.0 µmol/min/mg enzyme with sweet gum methylglucuronoxylan as substrate Ref.1

pH dependence:

Optimum pH is 6.5 with sweet gum methylglucuronoxylan as substrate.

Temperature dependence:

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentCell wall
Secreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcell wall

Inferred from direct assay Ref.1. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

endo-1,4-beta-xylanase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 14621432Endo-1,4-beta-xylanase A
PRO_5000484609

Regions

Domain64 – 165102CBM-cenC 1
Domain207 – 319113CBM-cenC 2
Domain360 – 490131CBM-cenC 3
Domain1279 – 134264SLH 1
Domain1345 – 140460SLH 2
Domain1407 – 146256SLH 3
Compositional bias186 – 1916Poly-Thr

Sites

Active site6511Proton donor By similarity
Active site7061 By similarity
Active site7751Nucleophile By similarity

Experimental info

Sequence conflict3131S → T in CAI79477. Ref.1
Sequence conflict454 – 4618SLASKTIT → TPTTQAWQARRLP in CAI79477. Ref.1

Secondary structure

.............................................................. 1462
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
C6CRV0 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: AE29664CDEA3BF3E

FASTA1,462157,322
        10         20         30         40         50         60 
MSRSLKKFVS ILLAAALLIP IGRLAPVAEA AENPTIVYHE DFAIDKGKAI QSGGASLTQV 

        70         80         90        100        110        120 
TGKVFDGNND GSALYVSNRA NTWDAADFKF ADIGLQNGKT YTVTVKGYVD QDATVPSGAQ 

       130        140        150        160        170        180 
AFLQAVDSNN YGFLASANFA AGTAFTLTKE FTVDTSVSTQ LRVQSSEEGK AVPFYIGDIL 

       190        200        210        220        230        240 
ITANPTTTTN TVYHEDFATD KGKAVQSGGA NLAQVADKVF DGNDDGKALY VSNRANTWDA 

       250        260        270        280        290        300 
ADFKFADIGL QNGKTYTVTV KGYVDQDATV PSGAQAFLQA VDSNNYGFLA SANFAARSAF 

       310        320        330        340        350        360 
TLTKEFTVDT SVSTQLRVQS SEEGKAVPFY IGDILITETV NSGGGQEDPP RPPALPFNTI 

       370        380        390        400        410        420 
TFEDQTAGGF TGRAGTETLT VTNESNHTAD GSYSLKVEGR TTSWHGPSLR VEKYVDKGYE 

       430        440        450        460        470        480 
YKVTAWVKLL SPETSTKLEL ASQVGDGGSA NYPSLASKTI TAADGWVQLQ GNYRYNSVGG 

       490        500        510        520        530        540 
EYLTIYVQSS NATASYYIDD ISFESTGSGP VGIQKDLAPL KDVYKNDFLI GNAISAEDLE 

       550        560        570        580        590        600 
GTRLELLKMH HDVVTAGNAM KPDALQPTKG NFTFTAADAM IDKVLAEGMK MHGHVLVWHQ 

       610        620        630        640        650        660 
QSPAWLNTKK DDNNNTVPLG RDEALDNLRT HIQTVMKHFG NKVISWDVVN EAMNDNPSNP 

       670        680        690        700        710        720 
ADYKASLRQT PWYQAIGSDY VEQAFLAARE VLDENPSWNI KLYYNDYNED NQNKATAIYN 

       730        740        750        760        770        780 
MVKDINDRYA AAHNGKLLID GVGMQGHYNI NTNPDNVKLS LEKFISLGVE VSVSELDVTA 

       790        800        810        820        830        840 
GNNYTLPENL AVGQAYLYAQ LFKLYKEHAD HIARVTFWGM DDNTSWRAEN NPLLFDKNLQ 

       850        860        870        880        890        900 
AKPAYYGVID PDKYMEEHAP ESKDANQAEA QYGTPVIDGT VDSIWSNAQA MPVNRYQMAW 

       910        920        930        940        950        960 
QGATGTAKAL WDDQNLYVLI QVSDSQLNKA NENAWEQDSV EVFLDQNNGK TTFYQNDDGQ 

       970        980        990       1000       1010       1020 
YRVNFDNETS FSPASIAAGF ESQTKKTANS YTVELKIPLT AVTPANQKKL GFDVQINDAT 

      1030       1040       1050       1060       1070       1080 
DGARTSVAAW NDTTGNGYQD TSVYGELTLA GKGTGGTGTV GTTVPQTGNV VKNPDGSTTL 

      1090       1100       1110       1120       1130       1140 
KPEVKTTNGN AVGTVTGDDL KKALDQAAPA AGGKKQVIID VPLQANAATY AVQLPTQSLK 

      1150       1160       1170       1180       1190       1200 
SQDGYQLTAK IANAFIQIPS NMLANTNVTT DQVSIRVAKA SLDNVDAATR ELIGNRPVID 

      1210       1220       1230       1240       1250       1260 
LSLVAGGNVI AWNNPTAPVT VAVPYAPTAE ELKHPEHILI WYIDGSGKAT PVPNSRYDAA 

      1270       1280       1290       1300       1310       1320 
LGAVVFQTTH FSTYAAVSVF TTFGDLAKVP WAKEAIDAMA SRGVIKGTGE NTFSPAASIK 

      1330       1340       1350       1360       1370       1380 
RADFIALLVR ALELHGTGTT DTAMFSDVPA NAYYYNELAV AKQLGIATGF EDNTFKPDSS 

      1390       1400       1410       1420       1430       1440 
ISRQDMMVLT TRALAVLGKQ LPAGGSLNAF SDAASVAGYA QDSVAALVKA GVVQGSGSKL 

      1450       1460 
APNDQLTRAE AAVILYRIWK LQ 

« Hide

References

« Hide 'large scale' references
[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]"Complete genome sequence of Paenibacillus sp. strain JDR-2."
Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O., Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S., Nolan M., Pati A., Martin J., Copeland A., Land M.L., Goodwin L. expand/collapse author list , Jones J.B., Ingram L.O., Shanmugam K.T., Preston J.F.
Stand. Genomic Sci. 6:1-10(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JDR-2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ938162 Genomic DNA. Translation: CAI79477.1.
CP001656 Genomic DNA. Translation: ACS98901.1.
RefSeqYP_003008988.1. NC_012914.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RDKX-ray1.49A/B518-851[»]
3RO8X-ray1.34A/B/C/D/E/F/G/H518-851[»]
4E4PX-ray1.92A/B518-851[»]
ProteinModelPortalC6CRV0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING324057.Pjdr2_0221.

Protein family/group databases

CAZyCBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS98901; ACS98901; Pjdr2_0221.
GeneID8127565.
KEGGpjd:Pjdr2_0221.
PATRIC22830917. VBIPaeSp118865_0225.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3693.
HOGENOMHOG000049670.
KOK01181.
OMAHVLVWHQ.
OrthoDBEOG6WMHV1.
ProtClustDBCLSK2482236.

Enzyme and pathway databases

BioCycPSP324057:GH5H-261-MONOMER.
UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.260. 3 hits.
2.60.40.1190. 1 hit.
3.20.20.80. 1 hit.
InterProIPR010502. 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]
PfamPF02018. CBM_4_9. 3 hits.
PF06452. DUF1083. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 3 hits.
SSF51445. SSF51445. 1 hit.
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS51272. SLH. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA1_PAESJ
AccessionPrimary (citable) accession number: C6CRV0
Secondary accession number(s): Q53I45
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: September 1, 2009
Last modified: November 13, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries