P53585 (ACLY_CAEEL) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 91.
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: Probable ATP-citrate synthase EC=2.3.3.8 Alternative name(s): ATP-citrate (pro-S-)-lyase Citrate cleavage enzyme | ||
| Gene names |
| ||
| Organism | Caenorhabditis elegans | ||
| Taxonomic identifier | 6239 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis |
Protein attributes
| Sequence length | 1106 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | ATP-citrate synthase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues By similarity. |
| Catalytic activity | ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family. In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid synthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Transferase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro lipid biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP citrate synthase activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW succinate-CoA ligase (ADP-forming) activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1106 | 1106 | Probable ATP-citrate synthase | PRO_0000102784 | |||||
Regions | |||||||||
| Nucleotide binding | 701 – 721 | 21 | ATP By similarity | ||||||
| Nucleotide binding | 752 – 778 | 27 | ATP By similarity | ||||||
| Region | 779 – 789 | 11 | CoA-binding Potential | ||||||
Sites | |||||||||
| Active site | 760 | 1 | Tele-phosphohistidine intermediate By similarity | ||||||
| Metal binding | 718 | 1 | Magnesium By similarity | ||||||
| Binding site | 358 | 1 | Citrate; via amide nitrogen By similarity | ||||||
| Binding site | 360 | 1 | Citrate By similarity | ||||||
| Binding site | 391 | 1 | Citrate By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | FO080989 Genomic DNA. Translation: CCD68276.1. |
| PIR | T29496. |
| RefSeq | NP_508280.1. NM_075879.3. |
| UniGene | Cel.17436. |
3D structure databases | |
| ProteinModelPortal | P53585. |
| SMR | P53585. Positions 2-437, 492-819, 875-1100. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-26861N. |
| IntAct | P53585. 5 interactions. |
| MINT | MINT-213164. |
| STRING | P53585. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | D1005.1.1; D1005.1.1; D1005.1. D1005.1.2; D1005.1.2; D1005.1. |
| GeneID | 180485. |
| KEGG | cel:D1005.1. |
| NMPDR | fig|6239.3.peg.22493. |
| UCSC | D1005.1. c. elegans. |
Organism-specific databases | |
| CTD | 180485. |
| WormBase | D1005.1; CE06997; WBGene00016995. |
Phylogenomic databases | |
| eggNOG | meNOG06139. |
| HOGENOM | HBG356295. |
| InParanoid | P53585. |
| OMA | MDAHTAN. |
| PhylomeDB | P53585. |
Gene expression databases | |
| ArrayExpress | P53585. |
Family and domain databases | |
| InterPro | IPR014608. ATP-citrate_synthase. IPR013650. ATP-grasp_succ-CoA_synth-type. IPR013816. ATP_grasp_subdomain_2. IPR017440. Cit_synth/succinyl-CoA_lig_AS. IPR016142. Citrate_synth-like_lrg_a-sub. IPR016143. Citrate_synth-like_sm_a-sub. IPR002020. Citrate_synthase-like. IPR016141. Citrate_synthase-like_core. IPR003781. CoA-bd. IPR005810. CoA_lig_alpha. IPR005811. CoA_ligase. IPR016040. NAD(P)-bd_dom. IPR017866. Succ-CoA_synthase_bsu_CS. IPR016102. Succinyl-CoA_synth-like. [Graphical view] |
| Gene3D | G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:1.10.580.10. Citrate_synthase_lrg_a-sub. 1 hit. G3DSA:1.10.230.10. Citrate_synthase_sm_a-sub. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:3.40.50.261. Succinyl-CoA_synth-like. 2 hits. |
| KO | K01648. |
| Pfam | PF08442. ATP-grasp_2. 1 hit. PF00285. Citrate_synt. 1 hit. PF02629. CoA_binding. 1 hit. PF00549. Ligase_CoA. 1 hit. [Graphical view] |
| PIRSF | PIRSF036511. ATP_citrt_syn. 1 hit. |
| SUPFAM | SSF48256. Citrate_synthase_core. 1 hit. SSF52210. CoA_ligase. 1 hit. |
| PROSITE | PS01216. SUCCINYL_COA_LIG_1. 1 hit. PS00399. SUCCINYL_COA_LIG_2. 1 hit. PS01217. SUCCINYL_COA_LIG_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 909586. |
Entry information
| Entry name | ACLY_CAEEL | ||||||||
| Accession | Primary (citable) accession number: P53585 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Caenorhabditis annotation project | ||||||||
Relevant documents
| Caenorhabditis elegans Caenorhabditis elegans: entries, gene names and cross-references to WormPep |
| SIMILARITY comments Index of protein domains and families |

Clusters with