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O54161 (EABF_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 97. 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:
Extracellular exo-alpha-L-arabinofuranosidase

Short name=ABF
EC=3.2.1.55
Alternative name(s):
Arabinosidase
Arabinoxylan arabinofuranohydrolase
Gene names
Name:abfB
Ordered Locus Names:SCO5932
ORF Names:SC7H1.02
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. Acts synergistically with the xylanases and binds specifically to xylan. From small arabinoxylo-oligosides (ranging from arabinoxylotriose to arabinoxylohexaose), it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well By similarity.

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydr olase 62 family.

Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   LigandLectin
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-arabinose metabolic process

Inferred from electronic annotation. Source: InterPro

xylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-L-arabinofuranosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737 Potential
Chain38 – 475438Extracellular exo-alpha-L-arabinofuranosidase
PRO_0000008036

Regions

Domain39 – 166128Ricin B-type lectin

Secondary structure

...................................................... 475
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O54161 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 47E707FE543CA60D

FASTA47550,046
        10         20         30         40         50         60 
MHRGSLSRGH TSAVLAAVVA ALAALAALLV ATTPAQAAGS GALRGAGSNR CLDVLGGSQD 

        70         80         90        100        110        120 
DGALLQLYDC WGGTNQQWTS TDTGRLTVYG DKCLDVPGHA TAPGTRVQIW SCSGGANQQW 

       130        140        150        160        170        180 
RVNSDGTVVG VESGLCLEAA GAGTANGTAV QLWTCNGGGN QKWTGLTGTP PTDGTCALPS 

       190        200        210        220        230        240 
TYRWSSTGVL AQPKSGWVAL KDFTTVTHNG RHLVYGSTSS GSSYGSMVFS PFTNWSDMAS 

       250        260        270        280        290        300 
AGQNAMNQAA VAPTLFYFAP KNIWVLAYQW GSWPFIYRTS SDPTDPNGWS APQPLFTGSI 

       310        320        330        340        350        360 
SGSDTGPIDQ TLIADGQNMY LFFAGDNGKI YRASMPIGNF PGNFGSSYTT IMSDTKANLF 

       370        380        390        400        410        420 
EGVQVYKVQG QNQYLMIVEA MGANGRYFRS FTASSLSGSW TPQAASEGNP FAGKANSGAT 

       430        440        450        460        470 
WTNDISHGDL VRDNPDQTMT VDPCNLQFLY QGKSPNAGGD YNSLPWRPGV LTLRR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939125 Genomic DNA. Translation: CAA16189.1.
PIRT35697.
RefSeqNP_630049.1. NC_003888.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3WMYX-ray1.40A38-475[»]
3WMZX-ray1.90A38-475[»]
3WN0X-ray1.90A38-475[»]
3WN1X-ray2.00A38-475[»]
3WN2X-ray2.10A38-475[»]
ProteinModelPortalO54161.
SMRO54161. Positions 39-164.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO5932.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GH62. Glycoside Hydrolase Family 62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA16189; CAA16189; CAA16189.
GeneID1101374.
KEGGsco:SCO5932.
PATRIC23741764. VBIStrCoe124346_6029.

Phylogenomic databases

eggNOGNOG81570.
HOGENOMHOG000025219.
OMATGCIDQT.
OrthoDBEOG6ZH2FF.
PhylomeDBO54161.

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

InterProIPR005193. GH62_arabinosidase.
IPR023296. Glyco_hydro_beta-prop.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF03664. Glyco_hydro_62. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEABF_STRCO
AccessionPrimary (citable) accession number: O54161
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: May 14, 2014
This is version 97 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