Q65GC0 (ARAA1_BACLD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 50.
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: L-arabinose isomerase 1 EC=5.3.1.4 | ||||
| Gene names |
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| Organism | Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 279010 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 493 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the conversion of L-arabinose to L-ribulose By similarity. HAMAP MF_00519 |
| Catalytic activity | L-arabinose = L-ribulose. HAMAP MF_00519 |
| Cofactor | Binds 1 manganese ion per subunit By similarity. HAMAP MF_00519 |
| Pathway | Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 1/3. HAMAP MF_00519 |
| 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: UniProtKB-KW fucose metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | L-arabinose isomerase activity Inferred from electronic annotation. Source: EC L-fucose isomerase activityInferred from electronic annotation. Source: InterPro metal 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 – 493 | 493 | L-arabinose isomerase 1 HAMAP MF_00519 | PRO_0000259335 | |||||
Sites | |||||||||
| Metal binding | 301 | 1 | Manganese By similarity | ||||||
| Metal binding | 326 | 1 | Manganese By similarity | ||||||
| Metal binding | 343 | 1 | Manganese By similarity | ||||||
| Metal binding | 442 | 1 | Manganese By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580. |
| [2] | "Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. Berka R.M.Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017333 Genomic DNA. Translation: AAU41894.1. CP000002 Genomic DNA. Translation: AAU24535.1. |
| RefSeq | YP_080173.1. NC_006270.3. YP_092587.1. NC_006322.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2AJT based on UniProtKB P08202. |
| ProteinModelPortal | Q65GC0. |
| SMR | Q65GC0. Positions 1-490. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q65GC0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000057641; EBBACP00000056172; EBBACG00000057632. EBBACT00000059576; EBBACP00000058009; EBBACG00000059567. |
| GeneID | 3028672. 3098584. |
| GenomeReviews | Gene locus BLi03028 in contig AE017333_GR. Gene locus BL00352 in contig CP000002_GR. |
| KEGG | bld:BLi03028. bli:BL00352. |
| NMPDR | fig|279010.5.peg.3376. |
| PATRIC | 18951784. VBIBacLic203714_3092. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2160. |
| GeneTree | EBGT00050000001793. |
| HOGENOM | HBG297198. |
| OMA | EVCPTIA. |
| ProtClustDB | PRK02929. |
Enzyme and pathway databases | |
| BioCyc | BLIC279010-1:BLI03028-MONOMER. BLIC279010:BL00352-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00519. Arabinose_Isome. [Tree] |
| InterPro | IPR024664. Ara_Isoase_C. IPR004216. Fuc/Ara_isomerase_C. IPR009015. Fucose_isomerase_N/cen. IPR003762. Lara_isomerase. [Graphical view] |
| KO | K01804. |
| Pfam | PF11762. Arabinose_Iso_C. 1 hit. 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] |
| SUPFAM | SSF50443. Fuc_isomerase_C. 1 hit. SSF53743. Fuc_isomerase_N. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ARAA1_BACLD | ||||||||
| Accession | Primary (citable) accession number: Q65GC0 Secondary accession number(s): Q62RS5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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