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Q9C4B1 (ABFB_ASPAW) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable alpha-N-arabinofuranosidase B
Short name=ABF B
Short name=Arabinosidase B
EC=3.2.1.55
Gene names
Name:abfB
OrganismAspergillus awamori (Black koji mold)
Taxonomic identifier105351 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

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-N-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.

Caution

Lacks the conserved Asp residue in position 297 essential for alpha-N-arabinofuranosidase activity. Its enzyme activity is therefore unsure.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 499482Probable alpha-N-arabinofuranosidase B
PRO_0000394602

Regions

Region18 – 335318Catalytic By similarity
Region336 – 499164ABD By similarity

Sites

Active site2211Nucleophile 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

Amino acid modifications

Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Disulfide bond21 ↔ 31 By similarity
Disulfide bond81 ↔ 86 By similarity
Disulfide bond176 ↔ 177Uncommon non-proline cis-peptide bond By similarity
Disulfide bond401 ↔ 439 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9C4B1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 839695CA1D57629F

FASTA49952,646
        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 ILGIGGYNSN 

       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

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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.
Strain: ATCC 38854 / NBRC 4033.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB046701 Genomic DNA. Translation: BAB21567.1.

3D structure databases

ProteinModelPortalQ9C4B1.
SMRQ9C4B1. Positions 19-499.
ModBaseSearch...

Protein family/group databases

CAZyCBM42. Carbohydrate-Binding Module Family 42.
GH54. Glycoside Hydrolase Family 54.
mycoCLAPABF54B_ASPAW.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. AbfB. 1 hit.
SSF49899. ConA_like_lec_gl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameABFB_ASPAW
AccessionPrimary (citable) accession number: Q9C4B1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 1, 2001
Last modified: March 6, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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