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Q0CEE5 (ABFB_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 41. 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 B

Short name=ABF B
Short name=Arabinosidase B
EC=3.2.1.55
Gene names
Name:abfB
ORF Names:ATEG_07939
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length506 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 506480Probable alpha-L-arabinofuranosidase B
PRO_0000394608

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 site4271Substrate; via amide nitrogen By similarity
Binding site4431Substrate By similarity
Binding site4711Substrate By similarity
Binding site4761Substrate; via amide nitrogen By similarity
Binding site4961Substrate By similarity
Site184 – 1852Cis-peptide bond By similarity

Amino acid modifications

Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation3751N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 39 By similarity
Disulfide bond89 ↔ 94 By similarity
Disulfide bond184 ↔ 185 By similarity
Disulfide bond409 ↔ 447 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0CEE5 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 10913205A0B91DE1

FASTA50652,197
        10         20         30         40         50         60 
MLLPRGFNRA VVTALGVVGT GTLVAAGPCD IYSSGGTPCV AAHSTTRALY SAYTGPLYQV 

        70         80         90        100        110        120 
KRGSDGATTN IAPLSAGGVA NAAAQDSFCA GTTCLITIIY DQSGRGNHLT QAPPGGFKGP 

       130        140        150        160        170        180 
EANGYDNLAS AIGAPVTLNG QKAYGVFISP GTGYRNNAAS GTATGDAPEG MYAVLDGTHY 

       190        200        210        220        230        240 
NGGCCFDYGN AETSSTDTGN GHMEAIYFGD NTVWGSGSGS GPWIMADLEN GLFSGSSTKN 

       250        260        270        280        290        300 
NAGDPSVSYR FLTAIVKGKP NQWAIRGANA ASGSLSTYYN GARPNASGYN PMSKEGAIIL 

       310        320        330        340        350        360 
GIGGDNSIGA QGTFYEGVMT SGYPSDATEN SVQANIVAAK YAVAPLTSGP SLTVGSSISL 

       370        380        390        400        410        420 
RATTSCCTTR YLAHNGSTVN TQVVSSSSST ALKQQASWTV RAGLANSACF SFESKDTPGS 

       430        440        450        460        470        480 
FIRHYDFVLQ LSANDGTKQF YEDATFCPQS GLNGQGSSIR SWNYPTRYFR HYNNVLYAAS 

       490        500 
NGGVHTFDAT GSFNDDVSWV VSTSFA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476604 Genomic DNA. Translation: EAU32201.1.
RefSeqXP_001216560.1. XM_001216560.1.

3D structure databases

ProteinModelPortalQ0CEE5.
SMRQ0CEE5. Positions 27-506.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33178.CADATEAP00002379.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADATEAT00002379; CADATEAP00002379; CADATEAG00002379.
GeneID4322793.

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_ASPTN
AccessionPrimary (citable) accession number: Q0CEE5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 41 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