O93988 (ACL1_SORMK) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 67.
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: ATP-citrate synthase subunit 1 EC=2.3.3.8 Alternative name(s): ATP-citrate (pro-S-)-lyase 1 Citrate cleavage enzyme subunit 1 | ||||||
| Gene names |
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| Organism | Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell) [Complete proteome] | ||||||
| Taxonomic identifier | 771870 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Sordaria |
Protein attributes
| Sequence length | 674 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the formation of cytosolic acetyl-CoA, which is mainly used for the biosynthesis of fatty acids and sterols. |
| Catalytic activity | ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA. |
| Subunit structure | Composed of two subunits. |
| Subcellular location | |
| Sequence similarities | 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 |
| 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 – 674 | 674 | ATP-citrate synthase subunit 1 | PRO_0000102787 | |||||
Regions | |||||||||
| Nucleotide binding | 261 – 281 | 21 | ATP By similarity | ||||||
| Nucleotide binding | 312 – 338 | 27 | ATP By similarity | ||||||
| Region | 339 – 349 | 11 | CoA-binding Potential | ||||||
Sites | |||||||||
| Active site | 320 | 1 | Tele-phosphohistidine intermediate By similarity | ||||||
| Metal binding | 278 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cell differentiation during sexual development of the fungus Sordaria macrospora requires ATP citrate lyase activity." Nowrousian M., Masloff S., Poeggeler S., Kueck U. Mol. Cell. Biol. 19:450-460(1999) [PubMed: 9858569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC MYA-333 / DSM 997 / K(L3346) / K-hell. |
| [2] | "The fungal acl1 and acl2 genes encode two polypeptides with homology to the N- and C-terminal parts of the animal ATP citrate lyase polypeptide." Nowrousian M., Kueck U., Loser K., Weltring K.-M. Curr. Genet. 37:189-193(2000) [PubMed: 10794176] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC MYA-333 / DSM 997 / K(L3346) / K-hell. |
| [3] | "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads: Sordaria macrospora, a model organism for fungal morphogenesis." Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K., Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S., Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M. PLoS Genet. 6:E1000891-E1000891(2010) [PubMed: 20386741] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-333 / DSM 997 / K(L3346) / K-hell. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ224922 Genomic DNA. Translation: CAA12224.1. AJ243817 Genomic DNA. Translation: CAB76165.1. CABT02000003 Genomic DNA. Translation: CCC07573.1. |
| RefSeq | XP_003344998.1. XM_003344950.1. |
3D structure databases | |
| ProteinModelPortal | O93988. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 10802343. |
| KEGG | smp:SMAC_06775. |
Family and domain databases | |
| InterPro | 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: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. 1 hit. |
| KO | K01648. |
| Pfam | PF00285. Citrate_synt. 1 hit. PF02629. CoA_binding. 1 hit. PF00549. Ligase_CoA. 1 hit. [Graphical view] |
| PRINTS | PR01798. SCOASYNTHASE. |
| SUPFAM | SSF48256. Citrate_synthase_core. 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... |
Entry information
| Entry name | ACL1_SORMK | ||||||||
| Accession | Primary (citable) accession number: O93988 Secondary accession number(s): D1ZRT9, F7VPZ5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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