Q2UIM2 (ABFB_ASPOR) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 38.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Alpha-N-arabinofuranosidase B Short name=ABF B Short name=Arabinosidase B EC=3.2.1.55 | ||||
| Gene names |
| ||||
| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome] | ||||
| Taxonomic identifier | 510516 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 506 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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. Ref.1 |
| Catalytic activity | Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. |
| Pathway | |
| Subcellular location | |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Polysaccharide degradation Xylan degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | L-arabinose metabolic process Inferred from electronic annotation. Source: InterPro arabinan metabolic processInferred from electronic annotation. Source: InterPro polysaccharide catabolic processInferred from electronic annotation. Source: UniProtKB-KW xylan catabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from direct assay Ref.1. Source: UniProtKB |
| Molecular function | alpha-N-arabinofuranosidase activity Inferred from direct assay Ref.1. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 26 | 26 | Potential | ||||||||
| Chain | 27 – 506 | 480 | Alpha-N-arabinofuranosidase B | PRO_0000394607 | |||||||
Regions | |||||||||||
| Region | 27 – 343 | 317 | Catalytic By similarity | ||||||||
| Region | 344 – 506 | 163 | ABD By similarity | ||||||||
Sites | |||||||||||
| Active site | 229 | 1 | Nucleophile By similarity | ||||||||
| Active site | 305 | 1 | Proton donor By similarity | ||||||||
| Binding site | 227 | 1 | Substrate By similarity | ||||||||
| Binding site | 230 | 1 | Substrate; via amide nitrogen By similarity | ||||||||
| Binding site | 304 | 1 | Substrate; via amide nitrogen By similarity | ||||||||
| Binding site | 424 | 1 | Substrate By similarity | ||||||||
| Binding site | 426 | 1 | Substrate; via amide nitrogen By similarity | ||||||||
| Binding site | 427 | 1 | Substrate; via amide nitrogen By similarity | ||||||||
| Binding site | 443 | 1 | Substrate By similarity | ||||||||
| Binding site | 471 | 1 | Substrate By similarity | ||||||||
| Binding site | 473 | 1 | Substrate; via amide nitrogen By similarity | ||||||||
| Binding site | 476 | 1 | Substrate; via amide nitrogen By similarity | ||||||||
| Binding site | 496 | 1 | Substrate By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 91 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 29 ↔ 39 | By similarity | |||||||||
| Disulfide bond | 89 ↔ 94 | By similarity | |||||||||
| Disulfide bond | 184 ↔ 185 | Uncommon non-proline cis-peptide bond By similarity | |||||||||
| Disulfide bond | 409 ↔ 447 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 46 | 1 | T → A in BAB71804. Ref.1 | ||||||||
| Sequence conflict | 84 | 1 | I → T in BAB71803. Ref.1 | ||||||||
| Sequence conflict | 167 | 1 | K → E in BAB71803. Ref.1 | ||||||||
| Sequence conflict | 387 | 1 | S → T in BAB71803. Ref.1 | ||||||||
| Sequence conflict | 390 | 1 | T → K in BAB71803. Ref.1 | ||||||||
| Sequence conflict | 393 | 1 | R → K in BAB71803. Ref.1 | ||||||||
| Sequence conflict | 410 | 1 | L → F in BAB71803. Ref.1 | ||||||||
| Sequence conflict | 429 | 1 | L → H in BAB71803. Ref.1 | ||||||||
Sequences
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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: 16233386] [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. Kikuchi H.Nature 438:1157-1161(2005) [PubMed: 16372010] [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. |
| RefSeq | XP_001820595.1. XM_001820543.1. |
3D structure databases | |
| ProteinModelPortal | Q2UIM2. |
| SMR | Q2UIM2. Positions 27-506. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | CADAORAT00007157; CADAORAP00007019; CADAORAG00007157. |
| GeneID | 5993498. |
| GenomeReviews | Gene locus abfB in contig AP007157_GR. |
| KEGG | aor:AOR_1_144. |
Phylogenomic databases | |
| OrthoDB | EOG4N33X5. |
Family and domain databases | |
| InterPro | IPR015289. A-L-arabinofuranosidase_B_cat. IPR007934. AbfB. IPR008985. ConA-like_lec_gl. IPR013320. ConA-like_subgrp. [Graphical view] |
| Gene3D | G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit. |
| Pfam | PF05270. AbfB. 1 hit. PF09206. ArabFuran-catal. 1 hit. [Graphical view] |
| SUPFAM | SSF110221. AbfB. 1 hit. SSF49899. ConA_like_lec_gl. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ABFB_ASPOR | ||||||||
| Accession | Primary (citable) accession number: Q2UIM2 Secondary accession number(s): Q96VA0, Q96VA1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal 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 |

Clusters with