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Reviewed, UniProtKB/Swiss-Prot P23031 (XYNC_PSEFL)

Last modified February 9, 2010. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
    Alpha-L-arabinofuranosidase C
    EC=3.2.1.55
Alternative name(s):
    Xylanase C
Gene names
Name: xynC
OrganismPseudomonas fluorescens
Taxonomic identifier294 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length571 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Xylanase C contributes to hydrolyse hemicellulose, the major component of plant cell-walls.

Catalytic activity

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

Pathway

Glycan metabolism; hemicellulose degradation.

Subcellular location

Secreted.

Miscellaneous

Acts only on high MW substrates, in which arabinose is linked to a polymeric backbone.

Sequence similarities

Belongs to the glycosyl hydrolase 62 family.

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

Contains 1 CBM6 (carbohydrate binding type-6) domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processL-arabinose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha-N-arabinofuranosidase activity

Inferred from electronic annotation. Source: EC

polysaccharide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737 Ref.1
Chain38 – 571534Alpha-L-arabinofuranosidase C
PRO_0000008033

Regions

Domain38 – 13699CBM2
Domain163 – 289127CBM6
Compositional bias135 – 16228Ser-rich (linker)
Compositional bias300 – 32021Ser-rich (linker)

Amino acid modifications

Disulfide bond39 ↔ 133 By similarity

Sequences

Sequence LengthMass (Da)Tools
P23031-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: AD19585F5E3D5555

FASTA57161,073
        10         20         30         40         50         60 
MINHNKTPNI LAKVFKRTCG LVSTGAALAI LSQAASAACT YTIDSEWSTG FTANITLKND 

        70         80         90        100        110        120 
TGAAINNWNV NWQYSSNRMT SGWNANFSGT NPYNATNMSW NGSIAPGQSI SFGLQGEKNG 

       130        140        150        160        170        180 
STAERPTVTG AACNSATTSS VASSSSTPTT SSSSASSVAS ALLLQEAQAG FCRVDGTIDN 

       190        200        210        220        230        240 
NHTGFTGSGF ANTNNAQGAA VVWAIDATSS GRRTLTIRYA NGGTANRNGS LVINGGSNGN 

       250        260        270        280        290        300 
YTVSLPTTGA WTTWQTATID VDLVQGNNIV QLSATTAEGL PNIDSLSVVG GTVRAGNCGS 

       310        320        330        340        350        360 
VSSSSSVQSS SSSSSTPSQT CELKAPLRWT STGPLISPKN PGWISIKDPS IVKYNDTYHV 

       370        380        390        400        410        420 
YATYYDTAYR SMYTSFTDWN TAQQAPHISM NGSRVGNTVA PQVFYFRPHN KWYLITQWAG 

       430        440        450        460        470        480 
AYATTDDIRN PNWSAKQKLL QGEPNGALDF WVICNDTHCY LYFSRDDGVL YVSKTTLANF 

       490        500        510        520        530        540 
PNFSGYSIVM EDHRGNGNSY LFEAANVYKL DGQNRYLLMV EAYISGRAFS APGQRPAWMA 

       550        560        570 
HGPLADTEAN PFAGMMFCFT MASSLKVYTC Y 

« Hide

References

[1]"Xylanase B and an arabinofuranosidase from Pseudomonas fluorescens subsp. cellulosa contain identical cellulose-binding domains and are encoded by adjacent genes."
Kellett L.E., Poole D.M., Ferreira L.M.A., Durrant A.J., Hazlewood G.P., Gilbert H.J.
Biochem. J. 272:369-376(1990) [PubMed: 2125205] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 38-46.
Strain: Sp. Cellulosa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54523 Genomic DNA. Translation: CAA38390.1.

3D structure databases

SMRP23031. Positions 33-134, 180-289, 344-521.
ModBaseSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
CBM35. Carbohydrate-Binding Module Family 35.
GH62. Glycoside Hydrolase Family 62.

Enzyme and pathway databases

BRENDA3.2.1.55. 329.

Family and domain databases

InterProIPR005084. Carb-bd_dom_fam6.
IPR008965. Carb_bd.
IPR012291. CBD_carb_bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR008979. Galactose-bd-like.
[Graphical view]
Gene3DG3DSA:2.60.40.290. CBD_carb_bd. 1 hit.
PfamPF00553. CBM_2. 1 hit.
PF03422. CBM_6. 1 hit.
[Graphical view]
SMARTSM00637. CBD_II. 1 hit.
[Graphical view]
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51175. CBM6. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNC_PSEFL
AccessionPrimary (citable) accession number: P23031
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: February 9, 2010
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

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