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Q96X54 (ABFA_ASPAW) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. 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:
Probable alpha-L-arabinofuranosidase A

Short name=ABF A
Short name=Arabinosidase A
EC=3.2.1.55
Gene names
Name:abfA
OrganismAspergillus awamori (Black koji mold)
Taxonomic identifier105351 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length628 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides By similarity.

Catalytic activity

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

Pathway

Glycan metabolism; L-arabinan degradation.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 51 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.1
Chain26 – 628603Probable alpha-L-arabinofuranosidase A
PRO_0000394596

Amino acid modifications

Glycosylation361N-linked (GlcNAc...) Potential
Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation1521N-linked (GlcNAc...) Potential
Glycosylation1711N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential
Glycosylation4931N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q96X54 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 84E4AF25C4805BE4

FASTA62868,007
        10         20         30         40         50         60 
MVAFSALSGV SALSLLLCLV QHAHGVSLKV STQGGNSSSP ILYGFMFEDI NHSGDGGIYG 

        70         80         90        100        110        120 
QLLQNPGLQG TTPNLTAWAA VGDATIAIDG DSPLTSAIPS TIKLDVADDA TGAVGLTNEG 

       130        140        150        160        170        180 
YWGIPVDGSE FQSSFWIKGD YSGDITVRLV GNYTGTEYGS ATITHTSTAD NFTQASVKFP 

       190        200        210        220        230        240 
TTKAPDGNVL YELTVDGSVA AGSSLNFGYL TLFGETYKSR ENGLKPQLAN VLADMKGSFL 

       250        260        270        280        290        300 
RFPGGNNLEG NSAENRWKWN ETIGDLWDRP GREGTWTYYN TDGLGLHEYF YWCEDLGLVP 

       310        320        330        340        350        360 
VLGVWDGFAL ESGGNTPITG DALTPYIDDV LNELEYILGD TSTTYGAWRA ANGQEEPWNL 

       370        380        390        400        410        420 
TMVEIGNEDM LGGGCESYAE RFTAFYDAIH AAYPDLILIA STSEADCLPE SMPEGSWVDY 

       430        440        450        460        470        480 
HDYSTPDGLV GQFNYFDNLY RSVPYFIGEY SRWEIDWPNM KGSVSEAVFM IGFERNSDVV 

       490        500        510        520        530        540 
KMAAYAPLLQ LVNSTQWTPD LIGYTQSPDD IFLSTSYYVQ EMFSRNRGDT IKEVTSDSDF 

       550        560        570        580        590        600 
GPLYWVASSA GDSYYVKLAN YGSETQDLTV SIPGTSTGKL TVLADNDPDA YNSDTQTLVT 

       610        620 
PSESTVQASN GTFTFSLPAW AVAVLAAN 

« Hide

References

[1]"Role of two alpha-L-arabinofuranosidases in arabinoxylan degradation and characteristics of the encoding genes from shochu koji molds, Aspergillus kawachii and Aspergillus awamori."
Koseki T., Okuda M., Sudoh S., Kizaki Y., Iwano K., Aramaki I., Matsuzawa H.
J. Biosci. Bioeng. 96:232-241(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-43.
Strain: ATCC 38854 / NBRC 4033.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB046702 Genomic DNA. Translation: BAB21568.2.

3D structure databases

ProteinModelPortalQ96X54.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH51. Glycoside Hydrolase Family 51.
mycoCLAPABF51A_ASPAW.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00667.

Family and domain databases

InterProIPR010720. Alpha-L-AF_C.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF06964. Alpha-L-AF_C. 1 hit.
[Graphical view]
SMARTSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameABFA_ASPAW
AccessionPrimary (citable) accession number: Q96X54
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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