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Reviewed, UniProtKB/Swiss-Prot P14768 (XYNA_PSEFL)

Last modified June 16, 2009. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
OrganismPseudomonas fluorescens
Taxonomic identifier294 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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Protein attributes

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

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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 CBM2 (carbohydrate binding type-2) domain.

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Ontologies

Keywords
   Biological processXylan degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

endo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: EC

polysaccharide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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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
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.4
Disulfide bond194 ↔ 209 Ref.4

Experimental info

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

Secondary structure

1 .................................................................... 611
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P14768-1 [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

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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: 2507868] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: Sp. Cellulosa.
[2]"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: 7881909] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 265-611, SEQUENCE REVISION.
Strain: Sp. Cellulosa.
[3]"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: 15299710] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 265-611.
[4]"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: 10653641] [Abstract]
Cited for: STRUCTURE BY NMR OF 180-228, DISULFIDE BONDS.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X15429 Genomic DNA. Translation: CAA33469.1.
PIRS06047.

3D structure databases

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[»]
ModBaseSearch...

Protein family/group databases

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

Enzyme and pathway databases

BRENDA3.2.1.8. 329.

Family and domain databases

InterProIPR001919. CBD_bac.
IPR012291. CBD_carb_bd.
IPR018366. CBM2_CS.
IPR002883. Dockerin_CBD_5.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sg_catalytic.
IPR009031. TypeX_cellulose-bd_reg_CBDX.
[Graphical view]
Gene3DG3DSA:2.60.40.290. CBD_carb_bd. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.30.32.30. TypeX_cellulose-bd_reg_CBDX. 1 hit.
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]
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameXYNA_PSEFL
AccessionPrimary (citable) accession number: P14768
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents