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Q8NK89 (ABFB_ASPKW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Alpha-L-arabinofuranosidase B

Short name=ABF B
Short name=Arabinosidase B
EC=3.2.1.55
Gene names
Name:abfB
ORF Names:AKAW_08685
OrganismAspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi) [Complete proteome]
Taxonomic identifier1033177 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length499 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. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. Ref.1 Ref.3

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 Ref.1.

Induction

Expressed in the presence of L-arabitol and L-arabinose, and repressed in the presence of sucrose and glucose. Ref.1

Domain

Organized into two domains: an N-terminal catalytic domain and a C-terminal arabinose-binding domain (ABD). Ref.3

Biotechnological use

Contribute to an increase in cereal utilization and formation of aroma in shochu brewing. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 54 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.76 mM for L-arabinofuranose Ref.1 Ref.3

pH dependence:

Optimum pH is 4.0. Stable between pH 3.0 and 7.0.

Temperature dependence:

Optimum temperature is 55 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 499482Alpha-L-arabinofuranosidase B
PRO_0000394606

Regions

Region18 – 335318Catalytic
Region336 – 499164ABD

Sites

Active site2211Nucleophile Ref.3
Active site2971Proton donor Ref.3
Binding site2191Substrate
Binding site2221Substrate; via amide nitrogen
Binding site2231Substrate; via amide nitrogen
Binding site2961Substrate; via amide nitrogen
Binding site4161Substrate
Binding site4181Substrate; via amide nitrogen
Binding site4191Substrate; via amide nitrogen
Binding site4351Substrate
Binding site4631Substrate
Binding site4651Substrate; via amide nitrogen
Binding site4681Substrate; via amide nitrogen
Binding site4881Substrate
Site176 – 1772Cis-peptide bond

Amino acid modifications

Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Ref.3
Disulfide bond21 ↔ 31 Ref.3
Disulfide bond81 ↔ 86 Ref.3
Disulfide bond176 ↔ 177 Ref.3
Disulfide bond401 ↔ 439 Ref.3

Experimental info

Mutagenesis176 – 1772CC → AA: Decreases the affinity toward the substrate.
Mutagenesis2041T → A: Reduces thermostability and catalytic activity. Ref.3
Mutagenesis2211E → A: Impairs catalytic activity. Ref.3
Mutagenesis2971D → A: Impairs catalytic activity. Ref.3

Secondary structure

............................................................................................. 499
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8NK89 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 94B340130BB18746

FASTA49952,598
        10         20         30         40         50         60 
MFSRRNLLAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY QLQRGSDDTT 

        70         80         90        100        110        120 
TTISPLTAGG IADASAQDTF CANTTCLITI IYDQSGNGNH LTQAPPGGFD GPDTDGYDNL 

       130        140        150        160        170        180 
ASAIGAPVTL NGQKAYGVFM SPGTGYRNNE ATGTATGDEA EGMYAVLDGT HYNDACCFDY 

       190        200        210        220        230        240 
GNAETSSTDT GAGHMEAIYL GNSTTWGYGA GDGPWIMVDM ENNLFSGADE GYNSGDPSIS 

       250        260        270        280        290        300 
YRFVTAAVKG GADKWAIRGA NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGDNSN 

       310        320        330        340        350        360 
GAQGTFYEGV MTSGYPSDDT ENSVQENIVA AKYVVGSLVS GPSFTSGEVV SLRVTTPGYT 

       370        380        390        400        410        420 
TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ CFSFESVDTP GSYIRHYNFE 

       430        440        450        460        470        480 
LLLNANDGTK QFHEDATFCP QAALNGEGTS LRSWSYPTRY FRHYENVLYA ASNGGVQTFD 

       490 
SKTSFNNDVS FEIETAFAS 

« Hide

References

« Hide 'large scale' 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 18-27 AND 421-432, SUBCELLULAR LOCATION, INDUCTION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY.
Strain: NBRC 4308.
[2]"Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used for brewing the Japanese distilled spirit shochu."
Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H., Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.
Eukaryot. Cell 10:1586-1587(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBRC 4308.
[3]"Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose."
Miyanaga A., Koseki T., Matsuzawa H., Wakagi T., Shoun H., Fushinobu S.
J. Biol. Chem. 279:44907-44914(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 19-499 IN COMPLEX WITH SUBSTRATE, DOMAIN, ACTIVE SITE, DISULFIDE BONDS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION AT ASN-202, MUTAGENESIS OF 176-CYS-CYS-177; THR-204; GLU-221 AND ASP-297.
Strain: NBRC 4308.
[4]"The family 42 carbohydrate-binding module of family 54 alpha-L-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose."
Miyanaga A., Koseki T., Miwa Y., Mese Y., Nakamura S., Kuno A., Hirabayashi J., Matsuzawa H., Wakagi T., Shoun H., Fushinobu S.
Biochem. J. 399:503-511(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 19-499 OF THE ALA-221 MUTANT IN COMPLEX WITH SUBSTRATE.
Strain: NBRC 4308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB085904 Genomic DNA. Translation: BAB96816.1.
DF126474 Genomic DNA. Translation: GAA90571.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WD3X-ray1.75A19-499[»]
1WD4X-ray2.07A19-499[»]
2D43X-ray2.80A19-499[»]
2D44X-ray2.30A19-499[»]
ProteinModelPortalQ8NK89.
SMRQ8NK89. Positions 19-499.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM42. Carbohydrate-Binding Module Family 42.
GH54. Glycoside Hydrolase Family 54.
mycoCLAPABF54B_ASPKA.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OrthoDBEOG7DFXNQ.

Enzyme and pathway databases

SABIO-RKQ8NK89.
UniPathwayUPA00667.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR015289. A-L-arabinofuranosidase_B_cat.
IPR007934. AbfB.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]
PfamPF05270. AbfB. 1 hit.
PF09206. ArabFuran-catal. 1 hit.
[Graphical view]
SUPFAMSSF110221. SSF110221. 1 hit.
SSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8NK89.

Entry information

Entry nameABFB_ASPKW
AccessionPrimary (citable) accession number: Q8NK89
Secondary accession number(s): G7XUM7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 54 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries