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P96463 (EABF_STRLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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:
Extracellular exo-alpha-L-arabinofuranosidase

Short name=ABF
EC=3.2.1.55
Alternative name(s):
Arabinosidase
Arabinoxylan arabinofuranohydrolase
Gene names
Name:abfB
OrganismStreptomyces lividans
Taxonomic identifier1916 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

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. Ref.1

Catalytic activity

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. Ref.1

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted Ref.1.

Miscellaneous

These dual activities might be explained by a rotation about the alpha-(1->3)-glycosidic bond of the arabinofuranose group to the xylose moiety of xylan, which produces a bond conformation resembling that of a beta-(1->4) bond found in xylosides. Thus a single catalytic site could perform the double activity (Ref.1).

Sequence similarities

Belongs to the glycosyl hydrolase 62 family.

Contains 1 ricin B-type lectin domain.

Biophysicochemical properties

Kinetic parameters:

KM=1.17 mM for wheat arabinoxylan (at 55 degrees Celsius) Ref.1

KM=5.12 mM for oat xylan (at 55 degrees Celsius)

Vmax=17.2 µmol/min/mg enzyme with oat xylan as substrate (at 55 degrees Celsius)

Vmax=18.5 µmol/min/mg enzyme with wheat arabinoxylan as substrate (at 55 degrees Celsius)

pH dependence:

Optimum pH is 6.

Temperature dependence:

Optimum temperature is 55 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   LigandLectin
   Molecular functionGlycosidase
Hydrolase
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_0000008037

Regions

Domain39 – 166128Ricin B-type lectin

Sequences

Sequence LengthMass (Da)Tools
P96463 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: C3CB14EE7BF85AAD

FASTA47550,369
        10         20         30         40         50         60 
MHRGSLSRGQ HVRGTRRRGA ALAALAALLV ATAPAQAAGS GALRGAGSNR CLDVLGGSQD 

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

       130        140        150        160        170        180 
RVNSDGTVVG VESGLCLEAA GAGTPNGTAV 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 QGKAPNAGGH YNSLPWRPGV LTLRH 

« Hide

References

[1]"New alpha-L-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme."
Vincent P., Shareck F., Dupont C., Morosoli R., Kluepfel D.
Biochem. J. 322:845-852(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBSTRATE SPECIFICITY.
Strain: 66 / 1326.
[2]Shareck F.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64551 Genomic DNA. Translation: AAC26524.1.

3D structure databases

ProteinModelPortalP96463.
SMRP96463. Positions 38-164.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_STRLI
AccessionPrimary (citable) accession number: P96463
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: May 14, 2014
This is version 80 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