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P82594 (IABF_STRCX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 58. 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-(1->5)-L-arabinofuranosidase

Short name=ABF
EC=3.2.1.55
Alternative name(s):
Alpha-L-AFase
Extracellular arabinan exo-alpha-(1->5)-L-arabinosidase
Short name=Arabinosidase
OrganismStreptomyces chartreusis
Taxonomic identifier1969 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length328 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 arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes only the cleavage of terminal alpha-(1->5) arabinofuranosyl bonds of arabinan present in the arabinofuranosyl polysaccharides or oligosaccharides. It cannot act on other arabinose-containing polysaccharides and arabinoxylo-oligosaccharides. Ref.1

Catalytic activity

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

Pathway

Glycan metabolism; L-arabinan degradation.

Subcellular location

Secreted.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Sequence similarities

Belongs to the glycosyl hydrolase 43 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0. The enzyme is slowly inactivated above pH 9 and below pH 5. Ref.1

Temperature dependence:

Optimum temperature is 50 degrees Celsius. The enzyme is inactivated at temperatures above 40 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processarabinan 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 – 4343Tat-tyPE signal Ref.1
Chain44 – 328285Extracellular exo-alpha-(1->5)-L-arabinofuranosidase
PRO_0000012203

Sequences

Sequence LengthMass (Da)Tools
P82594 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: AA7D5C1D2ABF38D5

FASTA32836,774
        10         20         30         40         50         60 
MCTREAVRMS REHDLPEIPS RRLLLKGAAA AGALTAVPGV AHAAPRPAPY ENPLVRQRAD 

        70         80         90        100        110        120 
PHIHRHTDGR YYFTATAPEY DRIVLRRSRT LGGLSTAAES VIWRAHPTGD MAAHIWAPEL 

       130        140        150        160        170        180 
HRIGGKWYVY FAAAPAEDVW RIRIWVLENS HPDPFKGTWE EKGQVRTAWE TFSLDATTFT 

       190        200        210        220        230        240 
HRGARYLCWA QHEPGADNNT GLFLSEMANP WTLTGPQIRL STPEYDWECV GYKVNEGPYA 

       250        260        270        280        290        300 
LKRNGRIFLT YSASATDHHY CVGMFTADAG GNLMDPGNWS KSPIPVFTGN ETTKQYGPGH 

       310        320 
NCFTVAEDGR SDVLVYHARQ YKEIVGDP 

« Hide

References

[1]"Purification, characterization and gene cloning of two alpha-L-arabinofuranosidases from Streptomyces chartreusis GS901."
Matsuo N., Kaneko S., Kuno A., Kobayashi H., Kusakabe I.
Biochem. J. 346:9-15(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 44-72, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
Strain: GS901.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB023626 Genomic DNA. Translation: BAA90772.1.
PIRB59296.

3D structure databases

ProteinModelPortalP82594.
SMRP82594. Positions 51-326.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH43. Glycoside Hydrolase Family 43.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00667.

Family and domain databases

Gene3D2.115.10.20. 1 hit.
InterProIPR016828. Alpha-L-arabinofuranosidase.
IPR006710. Glyco_hydro_43.
IPR023296. Glyco_hydro_beta-prop.
IPR006311. TAT_signal.
[Graphical view]
PANTHERPTHR22925. PTHR22925. 1 hit.
PfamPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFPIRSF025414. Alpha-L-arabinofuranosidase. 1 hit.
SUPFAMSSF75005. SSF75005. 1 hit.
PROSITEPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIABF_STRCX
AccessionPrimary (citable) accession number: P82594
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: October 1, 2000
Last modified: October 16, 2013
This is version 58 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries