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Q2UIM2 (ABFB_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:
Alpha-L-arabinofuranosidase B

Short name=ABF B
Short name=Arabinosidase B
EC=3.2.1.55
Gene names
Name:abfB
ORF Names:AO090023000001
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length506 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

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

Repressed by glucose. Ref.1

Domain

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

Sequence similarities

Belongs to the glycosyl hydrolase 54 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5. Stable between pH 4.0 and 6.5. Ref.1

Temperature dependence:

Optimum temperature is 60 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 506480Alpha-L-arabinofuranosidase B
PRO_0000394607

Regions

Region27 – 343317Catalytic By similarity
Region344 – 506163ABD By similarity

Sites

Active site2291Nucleophile By similarity
Active site3051Proton donor By similarity
Binding site2271Substrate By similarity
Binding site2301Substrate; via amide nitrogen By similarity
Binding site3041Substrate; via amide nitrogen By similarity
Binding site4241Substrate By similarity
Binding site4261Substrate; via amide nitrogen By similarity
Binding site4271Substrate; via amide nitrogen By similarity
Binding site4431Substrate By similarity
Binding site4711Substrate By similarity
Binding site4731Substrate; via amide nitrogen By similarity
Binding site4761Substrate; via amide nitrogen By similarity
Binding site4961Substrate By similarity
Site184 – 1852Cis-peptide bond By similarity

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 39 By similarity
Disulfide bond89 ↔ 94 By similarity
Disulfide bond184 ↔ 185 By similarity
Disulfide bond409 ↔ 447 By similarity

Experimental info

Sequence conflict461T → A in BAB71804. Ref.1
Sequence conflict841I → T in BAB71803. Ref.1
Sequence conflict1671K → E in BAB71803. Ref.1
Sequence conflict3871S → T in BAB71803. Ref.1
Sequence conflict3901T → K in BAB71803. Ref.1
Sequence conflict3931R → K in BAB71803. Ref.1
Sequence conflict4101L → F in BAB71803. Ref.1
Sequence conflict4291L → H in BAB71803. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q2UIM2 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: A0D6B300C19C9420

FASTA50652,195
        10         20         30         40         50         60 
MSSGLSLERA CAVALGIVAS ASLVAAGPCD IYSSGGTPCV AAHSTTRALY SAYTGALYQV 

        70         80         90        100        110        120 
KRGSDGSTTD IAPLSAGGVA DAAIQDSFCA NTTCLITIIY DQSGRGNHLT QAPPGGFNGP 

       130        140        150        160        170        180 
ESNGYDNLAS AVGAPVTLNG KKAYGVFMSP GTGYRNNAAS GTATGDKAEG MYAVLDGTHY 

       190        200        210        220        230        240 
NSACCFDYGN AEVSNTDTGN GHMEAIYYGD NTVWGSGAGS GPWIMADLEN GLFSGLSSTN 

       250        260        270        280        290        300 
NAGDPSISYR FVTAVVKGEA NQWSIRGANA ASGSLSTYYS GARPSASGYN PMSKEGAIIL 

       310        320        330        340        350        360 
GIGGDNSNGA QGTFYEGVMT SGYPSDATEN SVQADIVAAK YAIASLTSGP ALTVGSSISL 

       370        380        390        400        410        420 
QVTTAGYTTR YLAHDGSTVN TQVVSSSSTT ALRQQASWTV RTGLANSACL SFESVDTPGS 

       430        440        450        460        470        480 
YIRHYNFALL LNANDGTKQF YEDATFCPQA GLNGQGNSIR SWSYPTRYFR HYENVLYVAS 

       490        500 
NGGVQTFDAT TSFNDDVSWV VSTGFA 

« Hide

References

« Hide 'large scale' references
[1]"Synergistic degradation of arabinoxylan with alpha-L-arabinofuranosidase, xylanase and beta-xylosidase from soy sauce koji mold, Aspergillus oryzae, in high salt condition."
Hashimoto T., Nakata Y.
J. Biosci. Bioeng. 95:164-169(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 42149 / RIB 40 and HL15.
[2]"Genome sequencing and analysis of Aspergillus oryzae."
Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. expand/collapse author list , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB073860 Genomic DNA. Translation: BAB71803.1.
AB073861 Genomic DNA. Translation: BAB71804.1.
AP007157 Genomic DNA. Translation: BAE58593.1.
RefSeqXP_001820595.1. XM_001820543.1.

3D structure databases

ProteinModelPortalQ2UIM2.
SMRQ2UIM2. Positions 27-506.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00007019.

Protein family/group databases

CAZyCBM42. Carbohydrate-Binding Module Family 42.
GH54. Glycoside Hydrolase Family 54.
mycoCLAPABF54B_ASPOR.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00007157; CADAORAP00007019; CADAORAG00007157.
GeneID5993498.
KEGGaor:AOR_1_144.

Phylogenomic databases

eggNOGNOG83819.
HOGENOMHOG000187007.
OMANIVAAKY.
OrthoDBEOG7DFXNQ.

Enzyme and pathway databases

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...

Entry information

Entry nameABFB_ASPOR
AccessionPrimary (citable) accession number: Q2UIM2
Secondary accession number(s): Q96VA0, Q96VA1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 55 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