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Reviewed, UniProtKB/Swiss-Prot Q9XBQ3 (ABFA_BACST)

Last modified June 16, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Alpha-N-arabinofuranosidase
      Short name=Arabinosidase
    EC=3.2.1.55
Gene names
Name: abfA
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

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Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Enzyme regulation

Strongly inhibited by Hg2+.

Subunit structure

Homotetramer Probable.

Induction

By L-arabinose, sugar beet arabinan or oat spelt xylan.

Sequence similarities

Belongs to the glycosyl hydrolase 51 family.

biophysicochemical properties

pH dependence:

Optimum pH is 5.5-6.0.

Temperature dependence:

Optimum temperature is 70 degrees Celsius.

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Ontologies

Keywords
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processL-arabinose metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionalpha-N-arabinofuranosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 502501Alpha-N-arabinofuranosidase
PRO_0000057700

Secondary structure

1 ...................................................................................... 502
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9XBQ3-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 37C048AE29DBB230

FASTA50257,212
        10         20         30         40         50         60 
MATKKATMII EKDFKIAEID KRIYGSFIEH LGRAVYGGIY EPGHPQADEN GFRQDVIELV 

        70         80         90        100        110        120 
KELQVPIIRY PGGNFVSGYN WEDGVGPKEQ RPRRLDLAWK SVETNEIGLN EFMDWAKMVG 

       130        140        150        160        170        180 
AEVNMAVNLG TRGIDAARNL VEYCNHPSGS YYSDLRIAHG YKEPHKIKTW CLGNEMDGPW 

       190        200        210        220        230        240 
QIGHKTAVEY GRIACEAAKV MKWVDPTIEL VVCGSSNRNM PTFAEWEATV LDHTYDHVDY 

       250        260        270        280        290        300 
ISLHQYYGNR DNDTANYLAL SLEMDDFIRS VVAIADYVKA KKRSKKTIHL SFDEWNVWYH 

       310        320        330        340        350        360 
SNEADKLIEP WTVAPPLLED IYNFEDALLV GCMLITLMKH ADRVKIACLA QLVNVIAPIM 

       370        380        390        400        410        420 
TEKNGPAWKQ TIYYPFMHAS VYGRGVALHP VISSPKYDSK DFTDVPYLES IAVYNEEKEE 

       430        440        450        460        470        480 
VTIFAVNRDM EDALLLECDV RSFEDYRVIE HIVLEHDNVK QTNSAQSSPV VPHRNGDAQL 

       490        500 
SDRKVSATLP KLSWNVIRLG KR

« Hide

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References

[1]Gilead-Gropper S., Gat O., Alchanati I., Yaron S., Bren A., Shoham Y.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: T-6 / NCIMB 40222.
[2]"Purification and characterization of alpha-L-arabinofuranosidase from Bacillus stearothermophilus T-6."
Gilead S., Shoham Y.
Appl. Environ. Microbiol. 61:170-174(1995) [PubMed: 7887599] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-51, CHARACTERIZATION.
Strain: T-6 / NCIMB 40222.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF159625 Genomic DNA. Translation: AAD45520.2.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1PZ2X-ray2.00A/B1-502[»]
1PZ3X-ray1.75A/B1-502[»]
1QW8X-ray1.80A/B1-502[»]
1QW9X-ray1.20A/B1-502[»]
ModBaseSearch...

Protein family/group databases

CAZyGH51. Glycoside Hydrolase Family 51.

Family and domain databases

InterProIPR010720. Alpha-L-AF_C.
[Graphical view]
PfamPF06964. Alpha-L-AF_C. 1 hit.
[Graphical view]
SMARTSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameABFA_BACST
AccessionPrimary (citable) accession number: Q9XBQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 40 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents