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A1CGD1 (ABFB_ASPCL) 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:ACLA_066470
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [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_0000394603

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

Amino acid modifications

Glycosylation2851N-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
A1CGD1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: CDEB3D1906F35DD2

FASTA50651,886
        10         20         30         40         50         60 
MLSQPSRERA FVLALGLVVS SSLAAAAPCD IYSSGGTPCV AAHSTTRALY SAYSGPLYQV 

        70         80         90        100        110        120 
KRGSDGATTN IAPRSAGGVA NAAAQDTFCA SMTCLITVIY DQSGRGNHLT QAPPGGFKGP 

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

       190        200        210        220        230        240 
NGGCCFDYGN AETSSLDTGN GHMEAIYFGT NTVWGSGSGS GPWIMADLEN GLFSGSSPAN 

       250        260        270        280        290        300 
NAGDPSVSYR FLTAAIKGGP NRWAIRGANA ASGSLATYYS GARPNASGYN PMSKEGAIIL 

       310        320        330        340        350        360 
GIGGDNSNGA QGTFYEGVMT SGYPSDATEN AVQADIVAAN YAVTSLTSGP ALTVGSAISL 

       370        380        390        400        410        420 
RATTSCCTTR YLAHTGSTIN TQVVSSASAT TLKQQATWTV RTGLANSGCF SFESKDTPGS 

       430        440        450        460        470        480 
FIRHSNFALV LNGNDGTKQF KEDATFCPQA GLNGQGSSIR SWSFPTRYFR HYSNVLYAAS 

       490        500 
NGGVHTFDAA GSFNDDVSWV ISSGFA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027053 Genomic DNA. Translation: EAW11011.1.
RefSeqXP_001272437.1. XM_001272436.1.

3D structure databases

ProteinModelPortalA1CGD1.
SMRA1CGD1. Positions 27-506.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5057.CADACLAP00006216.

Proteomic databases

PRIDEA1CGD1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00006371; CADACLAP00006216; CADACLAG00006371.
GeneID4704554.
KEGGact:ACLA_066470.

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_ASPCL
AccessionPrimary (citable) accession number: A1CGD1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 23, 2007
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