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A2R511 (ABFB_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 50. 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:An15g02300
OrganismAspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]
Taxonomic identifier425011 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length499 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 – 1818 Potential
Chain19 – 499481Probable alpha-L-arabinofuranosidase B
PRO_5000221024

Regions

Region19 – 335317Catalytic By similarity
Region336 – 499164ABD By similarity

Sites

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

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
A2R511 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: F1F6C21F601419C9

FASTA49952,509
        10         20         30         40         50         60 
MFSRRNLVAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY QLQRGSDDTT 

        70         80         90        100        110        120 
TTISPLTAGG VADASAQDTF CANTTCLITI IYDQSGNGNH LTQAPPGGFD GPDVDGYDNL 

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

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

       250        260        270        280        290        300 
YSFVTAAVKG GADKWAIRGG NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGDNSN 

       310        320        330        340        350        360 
GAQGTFYEGV MTSGYPSDDV ENSVQENIVA AKYVSGSLVS GPSFTSGEVV SLRVTTPGYT 

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

       430        440        450        460        470        480 
LLLNANDGTK QFHEDATFCP QAPLNGEGTS LRSWSYPTRY FRHYDNVLYA ASNGGVQTFD 

       490 
SKTSFNNDVS FEIETAFAS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM270337 Genomic DNA. Translation: CAK42333.1.
RefSeqXP_001396769.1. XM_001396732.2.

3D structure databases

ProteinModelPortalA2R511.
SMRA2R511. Positions 19-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5061.CADANGAP00011686.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANGAT00011909; CADANGAP00011686; CADANGAG00011909.
GeneID4987831.
KEGGang:ANI_1_372134.

Phylogenomic databases

HOGENOMHOG000187007.
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_ASPNC
AccessionPrimary (citable) accession number: A2R511
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 6, 2007
Last modified: April 16, 2014
This is version 50 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