Reviewed,
UniProtKB/Swiss-Prot P94523 (ARAA_BACSU)
Last modified
November 4, 2008.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: L-arabinose isomerase EC=5.3.1.4 | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 496 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Catalyzes the conversion of L-arabinose to L-ribulose By similarity. |
| Catalytic activity | L-arabinose = L-ribulose. |
| Cofactor | Binds 1 manganese ion per subunit By similarity. |
| Pathway | |
| Induction | Transcription is repressed by glucose and by the binding of araR to the operon promoter. L-arabinose acts as an inducer by inhibiting the binding of araR to the DNA, thus allowing expression of the gene. |
| Sequence similarities | Belongs to the arabinose isomerase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Arabinose catabolism Carbohydrate metabolism |
| Ligand | Manganese Metal-binding |
| Molecular function | Isomerase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | arabinose catabolic process Inferred from electronic annotation. Source: HAMAP |
| Molecular function | L-arabinose isomerase activity Inferred from electronic annotation. Source: HAMAP manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 496 | 496 | L-arabinose isomerase | PRO_0000198382 | |||||
Sites | |||||||||
| Metal binding | 305 | 1 | Manganese By similarity | ||||||
| Metal binding | 330 | 1 | Manganese By similarity | ||||||
| Metal binding | 347 | 1 | Manganese By similarity | ||||||
| Metal binding | 446 | 1 | Manganese By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 85 – 94 | 10 | AKMWIEGLSS → SQKLWKRRPFPP Ref.2 Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression." Sa-Nogueira I.M.G., Nogueira T.V., Soares S., de Lencastre H. Microbiology 143:957-969(1997) [PubMed: 9084180] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism." Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R. Microbiology 142:3067-3078(1996) [PubMed: 8969504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [3] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [4] | "Mode of action of AraR, the key regulator of L-arabinose metabolism in Bacillus subtilis." Mota L.J., Tavares P., Sa-Nogueira I.M.G. Mol. Microbiol. 33:476-489(1999) [PubMed: 10417639] [Abstract] Cited for: TRANSCRIPTIONAL REGULATION. |
Cross-references
Sequence databases | |
|---|---|
| X89408 Genomic DNA. Translation: CAA61585.1. Z75208 Genomic DNA. Translation: CAA99587.1. Z99118 Genomic DNA. Translation: CAB14840.1. | |
| PIR | C69587. |
| RefSeq | NP_390758.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 936764. |
| GenomeReviews | Gene locus BSU28800 in contig AL009126_GR. |
| KEGG | bsu:BSU28800. |
Organism-specific databases | |
| SubtiList | BG11904. araA. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P94523. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU2876-MON. |
Family and domain databases | |
| HAMAP | MF_00519. [Tree] |
| InterPro | IPR003762. Lara_isomerase. [Graphical view] |
| Pfam | PF02610. Arabinose_Isome. 1 hit. [Graphical view] |
| PIRSF | PIRSF001478. L-ara_isomerase. 1 hit. |
| ProDom | PD018364. Lara_isomerase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| BLOCKS | Search... |
| ProtoNet | Search... |
Entry information
| Entry name | ARAA_BACSU | ||||||||
| Accession | Primary (citable) accession number: P94523 Secondary accession number(s): O05184 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

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