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P82593 (EABF_STRCX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
Alpha-L-AFase
Extracellular arabinan exo-alpha-L-arabinosidase
Short name=Arabinosidase
OrganismStreptomyces chartreusis
Taxonomic identifier1969 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length825 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 the cleavage of terminal alpha-L-arabinofuranosyl residues of arabinan present in the arabinofuranosyl polysaccharides or oligosaccharides. It cannot act on other arabinose-containing polysaccharides and arabinoxylo-oligosaccharides. It leaves most of the polymer intact, including most of the main-chain residues and the arabinose side chains. It acts preferentially on the linear alpha-(1->2)-linked arabinofuranobiosides and alpha-(1->3)-linked arabinofuranobiosides, and is much less effective on alpha-(1->5)-linked arabinofuranobiosides. It also hydrolyzes the terminal alpha-(1->3)-linked arabinofuranotriosides in preference to the alpha-(1->5)-linked arabinofuranotriosides. Ref.1

Catalytic activity

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

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 51 family.

Contains 1 CBM-cenC (cenC-type cellulose-binding) domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5. The enzyme is slowly inactivated above pH 8.5 and below pH 5.5. Ref.1

Temperature dependence:

Optimum temperature is 55 degrees Celsius. The enzyme is inactivated at temperatures above 45 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   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-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 – 2929 Ref.1
Chain30 – 825796Extracellular exo-alpha-L-arabinofuranosidase
PRO_0000012217

Regions

Domain70 – 215146CBM-cenC
Region379 – 3802Alpha-L-arabinofuranose binding By similarity

Sites

Active site3801Proton donor/acceptor By similarity
Binding site581Alpha-L-arabinofuranose By similarity
Binding site2471Alpha-L-arabinofuranose; via amide nitrogen By similarity
Site6071Important for substrate recognition By similarity

Sequences

Sequence LengthMass (Da)Tools
P82593 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 9FF4EE99BE0C696E

FASTA82590,184
        10         20         30         40         50         60 
MSRIRWRYGT AATALLVAAG LVPTATAHAE DVTDYSITVD PAAKGAAIDD TMYGVFFEDI 

        70         80         90        100        110        120 
NRAADGGLYA ELVQNRSFEY STDDNRSYTP LTSWIVDGTG EVVNDAGRLN ERNRNYLSLG 

       130        140        150        160        170        180 
AGSSVTNAGY NTGIRVEQGK RYDFSVWARA GSASTLTVAL KDAAGTLATA RQVAVEGGWA 

       190        200        210        220        230        240 
KYRATFTATR TSNRGRLAVA ANDAAALDMV SLFPRDTYRN QQNGLRKDLA EKIAALHPGF 

       250        260        270        280        290        300 
VRFPGGCLVN TGSMEDYSAA SGWQRKRSYQ WKDTVGPVEE RATNANFWGY NQSYGLGYYE 

       310        320        330        340        350        360 
YFRFSEDIGA MPLPVVPALV TGCGQNKAVD DEALLKRHIQ DTLDLIEFAN GPATSKWGKV 

       370        380        390        400        410        420 
RAEMGHPRPF RLTHLEVGNE ENLPDEFFDR FKQFRAAIEA EYPDITVVSN SGPDDAGTTF 

       430        440        450        460        470        480 
DTAWKLNREA NVEMVDEHYY NSPNWFLQNN DRYDSYDRGG PKVFLGEYAS QGNAWKNGLS 

       490        500        510        520        530        540 
EAAFMTGLER NADVVKLASY APLLANEDYV QWRPDLVWFN NRASWNSANY EVQKLFMNNV 

       550        560        570        580        590        600 
GDRVVPSKAT TTPDVSGPIT GAVGLSTWAT GTAYDDVKVT AADGATLLSD DFSGDASKWT 

       610        620        630        640        650        660 
HTGAGSWSVQ DGQYVQTDAA AENTMVQAGD PSWHDYDLHV KATKKSGKEG FLVAFGVKDT 

       670        680        690        700        710        720 
GNYYWWNLGG WNNTQSAVEQ AVDGGKGTLL TKAGSIETGR AYDIDVKVRG RQVTLYLDGQ 

       730        740        750        760        770        780 
EWGGFTDDKP AEPFRQVVTK DARTGDLIVK VVNAQPAEAR TAIDLGGARV ASTARVTTLA 

       790        800        810        820 
ADQDAVNTET DAPVTPATST FSGVTDRFTY TFPANSVTFL RLKQR 

« 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 30-75, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
Strain: GS901.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB023625 Genomic DNA. Translation: BAA90771.1.
PIRA59296.

3D structure databases

ProteinModelPortalP82593.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH51. Glycoside Hydrolase Family 51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.260. 1 hit.
InterProIPR010720. Alpha-L-AF_C.
IPR003305. CenC_carb-bd.
IPR008985. ConA-like_lec_gl_sf.
IPR008979. Galactose-bd-like.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF06964. Alpha-L-AF_C. 1 hit.
PF02018. CBM_4_9. 1 hit.
[Graphical view]
SMARTSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameEABF_STRCX
AccessionPrimary (citable) accession number: P82593
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 60 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries