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P14768 (XYNA_CELJU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 123. 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

Short name=Xylanase A
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Short name=XYLA
Gene names
Name:xynA
Synonyms:xyn10A
Ordered Locus Names:CJA_2471
OrganismCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) [Complete proteome] [HAMAP]
Taxonomic identifier498211 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Sequence similarities

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

Contains 1 CBM10 (carbohydrate binding type-10) domain.

Contains 1 CBM2 (carbohydrate binding type-2) domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626
Chain27 – 611585Endo-1,4-beta-xylanase A
PRO_0000007977

Regions

Domain27 – 128102CBM2
Domain183 – 21028CBM10
Compositional bias131 – 17949Ser-rich (linker)
Compositional bias227 – 25933Ser-rich

Sites

Active site3911Proton donor
Active site5101Nucleophile

Amino acid modifications

Disulfide bond31 ↔ 125 By similarity
Disulfide bond184 ↔ 215 Ref.5
Disulfide bond194 ↔ 209 Ref.5

Experimental info

Sequence conflict432 – 4332RA → PR in CAA33469. Ref.1

Secondary structure

........................................................................... 611
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14768 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 2CFAA3D453E6B68E

FASTA61164,804
        10         20         30         40         50         60 
MRTAMAKSLG AAAFLGAALF AHTLAAQTAT CSYNITNEWN TGYTGDITIT NRGSSAINGW 

        70         80         90        100        110        120 
SVNWQYATNR LSSSWNANVS GSNPYSASNL SWNGNIQPGQ SVSFGFQVNK NGGSAERPSV 

       130        140        150        160        170        180 
GGSICSGSVA SSSAPASSVP SSIASSSPSS VASSVISSMA SSSPVSSSSV ASSTPGSSSG 

       190        200        210        220        230        240 
NQQCNWYGTL YPLCVTTTNG WGWEDQRSCI ARSTCAAQPA PFGIVGSGSS TPVSSSSSSL 

       250        260        270        280        290        300 
SSSSVVSSIR SSSSSSSSSV ATGNGLASLA DFPIGVAVAA SGGNADIFTS SARQNIVRAE 

       310        320        330        340        350        360 
FNQITAENIM KMSYMYSGSN FSFTNSDRLV SWAAQNGQTV HGHALVWHPS YQLPNWASDS 

       370        380        390        400        410        420 
NANFRQDFAR HIDTVAAHFA GQVKSWDVVN EALFDSADDP DGRGSANGYR QSVFYRQFGG 

       430        440        450        460        470        480 
PEYIDEAFRR ARAADPTAEL YYNDFNTEEN GAKTTALVNL VQRLLNNGVP IDGVGFQMHV 

       490        500        510        520        530        540 
MNDYPSIANI RQAMQKIVAL SPTLKIKITE LDVRLNNPYD GNSSNDYTNR NDCAVSCAGL 

       550        560        570        580        590        600 
DRQKARYKEI VQAYLEVVPP GRRGGITVWG IADPDSWLYT HQNLPDWPLL FNDNLQPKPA 

       610 
YQGVVEALSG R 

« Hide

References

« Hide 'large scale' references
[1]"Conserved serine-rich sequences in xylanase and cellulase from Pseudomonas fluorescens subspecies cellulosa: internal signal sequence and unusual protein processing."
Hall J., Hazlewood G.P., Huskisson N.S., Durrant A.J., Gilbert H.J.
Mol. Microbiol. 3:1211-1219(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ueda107.
[3]"Structure of the catalytic core of the family F xylanase from Pseudomonas fluorescens and identification of the xylopentaose-binding sites."
Harris G.W., Jenkins J.A., Connerton I., Cummings N., Lo Leggio L., Scott M., Hazlewood G.P., Laurie J.I., Gilbert H.J., Pickersgill R.W.
Structure 2:1107-1116(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 265-611, SEQUENCE REVISION.
[4]"Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8-A resolution."
Harris G.W., Jenkins J.A., Connerton I., Pickersgill R.W.
Acta Crystallogr. D 52:393-401(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 265-611.
[5]"Solution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A."
Raghothama S., Simpson P.J., Szabo L., Nagy T., Gilbert H.J., Williamson M.P.
Biochemistry 39:978-984(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 180-228, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15429 Genomic DNA. Translation: CAA33469.1.
CP000934 Genomic DNA. Translation: ACE85439.1.
PIRS06047.
RefSeqYP_001982932.1. NC_010995.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CLXX-ray1.80A/B/C/D265-611[»]
1E5NX-ray3.20A/B264-611[»]
1E8RNMR-A180-228[»]
1QLDNMR-A180-228[»]
1W2PX-ray1.45A/B265-611[»]
1W2VX-ray1.55A/B265-611[»]
1W32X-ray1.20A/B265-611[»]
1W3HX-ray1.50A/B265-611[»]
1XYSX-ray2.50A/B265-611[»]
ProteinModelPortalP14768.
SMRP14768. Positions 180-228, 265-610.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING498211.CJA_2471.

Protein family/group databases

CAZyCBM10. Carbohydrate-Binding Module Family 10.
CBM2. Carbohydrate-Binding Module Family 2.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE85439; ACE85439; CJA_2471.
GeneID6414903.
KEGGcja:CJA_2471.
PATRIC21328304. VBICelJap122165_2421.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000066328.
KOK01181.
OMAENIMKMS.
OrthoDBEOG6XQ3JG.

Enzyme and pathway databases

BioCycCJAP498211:GHIT-2462-MONOMER.
UniPathwayUPA00114.

Family and domain databases

Gene3D2.30.32.30. 1 hit.
2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR002883. CBM10/Dockerin_dom.
IPR018366. CBM2_CS.
IPR009031. CBM_fam10.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00637. CBD_II. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF57615. SSF57615. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14768.

Entry information

Entry nameXYNA_CELJU
AccessionPrimary (citable) accession number: P14768
Secondary accession number(s): B3PKK3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1997
Last modified: May 14, 2014
This is version 123 of the entry and version 2 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