P49608 (ACOC_CUCMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 71.
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, cytoplasmic Short name=Aconitase EC=4.2.1.3 Alternative name(s): Citrate hydro-lyase |
| Organism | Cucurbita maxima (Pumpkin) (Winter squash) |
| Taxonomic identifier | 3661 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Cucurbiteae › Cucurbita![]() |
Protein attributes
| Sequence length | 898 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript 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; glyoxylate and dicarboxylate metabolism. |
| Subcellular location | |
| Sequence similarities | Belongs to the aconitase/IPM isomerase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glyoxylate bypass |
| Cellular component | Cytoplasm |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding |
| Molecular function | Lyase |
| Gene Ontology (GO) | |
| Biological_process | glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 898 | 898 | Aconitate hydratase, cytoplasmic | PRO_0000076652 | |||||
Regions | |||||||||
| Region | 209 – 211 | 3 | Substrate binding By similarity | ||||||
| Region | 784 – 785 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 441 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 507 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 510 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Binding site | 90 | 1 | Substrate By similarity | ||||||
| Binding site | 540 | 1 | Substrate By similarity | ||||||
| Binding site | 545 | 1 | Substrate By similarity | ||||||
| Binding site | 703 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Cytosolic aconitase participates in the glyoxylate cycle in etiolated pumpkin cotyledons." Hayashi M., de Bellis L., Alpi A., Nishimura M. Plant Cell Physiol. 36:669-680(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Kurokawa Amakuri Nankin. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D29629 mRNA. Translation: BAA06108.1. |
3D structure databases | |
| ProteinModelPortal | P49608. |
| SMR | P49608. Positions 5-897. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P49608. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| KEGG | dosa:Os03t0136900-01. |
Enzyme and pathway databases | |
| UniPathway | UPA00227. |
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 | ACOC_CUCMA | ||||||||
| Accession | Primary (citable) accession number: P49608 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
