P09339 (ACON_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 108.
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: Aconitate hydratase Short name=Aconitase EC=4.2.1.3 Alternative name(s): Citrate hydro-lyase | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 224308 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 909 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 | Catalyzes the isomerization of citrate to isocitrate via cis-aconitate By similarity. |
| Catalytic activity | Citrate = isocitrate. |
| Cofactor | Binds 1 4Fe-4S cluster per subunit By similarity. |
| Pathway | Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. |
| Subunit structure | Monomer. |
| Induction | By citrate, decoyinine and nutrient depletion. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Ligand | Iron Iron-sulfur Metal-binding |
| Molecular function | Lyase |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: InterPro citrate hydro-lyase (cis-aconitate-forming) activityInferred from electronic annotation. Source: EC isocitrate hydro-lyase (cis-aconitate-forming) activityInferred from electronic annotation. Source: EC 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.4 | ||||||
| Chain | 2 – 909 | 908 | Aconitate hydratase | PRO_0000076655 | |||||
Sites | |||||||||
| Metal binding | 450 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 516 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 519 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 43 – 45 | 3 | SKL → FEA in AAA22316. Ref.4 | ||||||
| Sequence conflict | 119 | 1 | G → V no nucleotide entry Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "New genes in the 170 degrees region of the Bacillus subtilis genome encode DNA gyrase subunits, a thioredoxin, a xylanase and an amino acid transporter." Rose M., Entian K.-D. Microbiology 142:3097-3101(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | Wilde R.J. Thesis (1988), University of Sheffield, United Kingdom Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-141. |
| [4] | "Purification of aconitase from Bacillus subtilis and correlation of its N-terminal amino acid sequence with the sequence of the citB gene." Dingman D.W., Sonenshein A.L. J. Bacteriol. 169:3062-3067(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45, PROTEIN SEQUENCE OF 2-8. |
| [5] | Sonenshein A.L. Submitted (JUL-1987) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z73234 Genomic DNA. Translation: CAA97599.1. AL009126 Genomic DNA. Translation: CAB13684.1. M16776 Genomic DNA. Translation: AAA22316.1. |
| PIR | G69599. |
| RefSeq | NP_389683.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P09339. |
| SMR | P09339. Positions 10-907. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU18000. |
Proteomic databases | |
| PaxDb | P09339. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB13684; CAB13684; BSU18000. |
| GeneID | 938140. |
| KEGG | bsu:BSU18000. |
| PATRIC | 18975429. VBIBacSub10457_1906. |
Organism-specific databases | |
| GenoList | BSU18000. [Micado] |
Phylogenomic databases | |
| eggNOG | COG1048. |
| HOGENOM | HOG000025704. |
| KO | K01681. |
| OMA | DEALYKW. |
| ProtClustDB | PRK09277. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU18000-MONOMER. |
| UniPathway | UPA00223; UER00718. |
Family and domain databases | |
| Gene3D | 3.20.19.10. 1 hit. 3.30.499.10. 3 hits. 3.40.1060.10. 1 hit. |
| InterPro | IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR015937. Acoase/IPM_deHydtase. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015928. Aconitase/3IPM_dehydase_swvl. IPR006249. Aconitase/Fe_reg_prot_2. IPR015934. Aconitase/Fe_reg_prot_2/AcnD. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. IPR000573. AconitaseA/IPMdHydase_ssu_swvl. [Graphical view] |
| PANTHER | PTHR11670. PTHR11670. 1 hit. PTHR11670:SF1. PTHR11670:SF1. 1 hit. |
| Pfam | PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view] |
| PRINTS | PR00415. ACONITASE. |
| SUPFAM | SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. SSF53732. Aconitase_N. 1 hit. |
| TIGRFAMs | TIGR01341. aconitase_1. 1 hit. |
| PROSITE | PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACON_BACSU | ||||||||
| Accession | Primary (citable) accession number: P09339 Secondary accession number(s): Q45059 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |

Clusters with
