P99148 (ACON_STAAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 66.
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 |
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| Organism | Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 158879 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 901 AA. |
| Sequence status | Complete. |
| 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. |
| Sequence similarities | Belongs to the aconitase/IPM isomerase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Ligand | Iron Iron-sulfur Metal-binding |
| Molecular function | Lyase |
| Technical term | Complete 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)
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. Hiramatsu K.Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315. |
| [2] | "Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: N315. |
| [3] | "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: N315. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000018 Genomic DNA. Translation: BAB42442.1. |
| PIR | F89910. |
| RefSeq | NP_374463.1. NC_002745.2. |
3D structure databases | |
| ProteinModelPortal | P99148. |
| SMR | P99148. Positions 22-901. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 158879.SA1184. |
2D gel databases | |
| SWISS-2DPAGE | P99148. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAB42442; BAB42442; BAB42442. |
| GeneID | 1124021. |
| KEGG | sau:SA1184. |
| PATRIC | 19574614. VBIStaAur116463_1276. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1048. |
| HOGENOM | HOG000025704. |
| KO | K01681. |
| OMA | YSKAQGM. |
| ProtClustDB | PRK09277. |
Enzyme and pathway databases | |
| BioCyc | SAUR158879:GJCB-1249-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_STAAN | ||||||||
| Accession | Primary (citable) accession number: P99148 Secondary accession number(s): Q99UC8 | ||||||||
| 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 |

Clusters with
