Reviewed,
UniProtKB/Swiss-Prot P09339 (ACON_BACSU)
Last modified
November 3, 2009.
Version 80.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names 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 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › 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)
| Catalytic activity | Citrate = isocitrate. |
| Cofactor | Binds 1 4Fe-4S cluster per subunit By similarity. |
| Pathway | |
| 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 |
| Gene Ontology (GO) | |
| Biological process | tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: InterPro aconitate hydratase activityInferred from electronic annotation. Source: EC iron 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 AA sequence Ref.4 | ||||||
| Sequence conflict | 119 | 1 | G → V 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: 8969507] [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: 9384377] [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: 3110133] [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. |
Cross-references
Sequence databases | |
|---|---|
| Z73234 Genomic DNA. Translation: CAA97599.1. AL009126 Genomic DNA. Translation: CAB13684.1. M16776 Genomic DNA. Translation: AAA22316.1. | |
| PIR | G69599. |
| RefSeq | NP_389683.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 938140. |
| GenomeReviews | Gene locus BSU18000 in contig AL009126_GR. |
| KEGG | bsu:BSU18000. |
| NMPDR | fig|224308.1.peg.1804. |
Organism-specific databases | |
| SubtiList | BG10478. citB. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P09339. |
| OMA | RIKNEML. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU1801-MON. |
| BRENDA | 4.2.1.3. 150. |
Family and domain databases | |
| InterPro | IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015937. Aconitase-like_core. 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] |
| Gene3D | G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit. |
| PANTHER | PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF1. Aconitase/Fe_reg_prot_2/AcnD. 1 hit. |
| Pfam | PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view] |
| PRINTS | PR00415. ACONITASE. |
| ProDom | PD000511. Aconitase_N. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| 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 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 |

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