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P23031 (XYNC_CELJU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Alpha-L-arabinofuranosidase C

EC=3.2.1.55
Alternative name(s):
Xylanase C
Gene names
Name:xynC
Synonyms:abf62A
Ordered Locus Names:CJA_3281
OrganismCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) [Complete proteome] [HAMAP]
Taxonomic identifier498211 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio

Protein attributes

Sequence length619 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.

Sequence caution

The sequence CAA38390.1 differs from that shown. Reason: Frameshift at positions 527 and 544.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Direct 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-L-arabinofuranosidase activity

Inferred from electronic annotation. Source: UniProtKB-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 – 619582Alpha-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

Experimental info

Sequence conflict556 – 59035NNNVE…VDPCN → MMFCFTMASSLKVYTCY in CAA38390. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P23031 [UniParc].

Last modified April 20, 2010. Version 2.
Checksum: 9CA48261A2D0FD0F

FASTA61966,440
        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 EAYISGPRFF RSWTATSLDG 

       550        560        570        580        590        600 
PWTPLADTEA NPFAGNNNVE WSTGKWADGI SHGELIRSGH DEKMTVDPCN LEFLYQGASG 

       610 
PGSTYNTIPY KLGLLRLKK 

« Hide

References

« Hide 'large scale' 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 38-46.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54523 Genomic DNA. Translation: CAA38390.1. Frameshift.
CP000934 Genomic DNA. Translation: ACE85320.1.
RefSeqYP_001983735.1. NC_010995.1.

3D structure databases

ProteinModelPortalP23031.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING498211.CJA_3281.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE85320; ACE85320; CJA_3281.
GeneID6413842.
KEGGcja:CJA_3281.
PATRIC21329953. VBICelJap122165_3241.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAWYLITQW.
OrthoDBEOG6ZH2FF.
ProtClustDBCLSK2544292.

Enzyme and pathway databases

BioCycCJAP498211:GHIT-3270-MONOMER.
UniPathwayUPA00697.

Family and domain databases

Gene3D2.115.10.20. 1 hit.
2.60.120.260. 1 hit.
2.60.40.290. 1 hit.
InterProIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR005193. GH62_arabinosidase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamPF00553. CBM_2. 1 hit.
PF03422. CBM_6. 1 hit.
PF03664. Glyco_hydro_62. 1 hit.
[Graphical view]
SMARTSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51175. CBM6. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNC_CELJU
AccessionPrimary (citable) accession number: P23031
Secondary accession number(s): B3PEH9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 20, 2010
Last modified: November 13, 2013
This is version 89 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries