P0AGF1 (SUCD_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 45.
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: Succinyl-CoA ligase [ADP-forming] subunit alpha EC=6.2.1.5 Alternative name(s): Succinyl-CoA synthetase subunit alpha Short name=SCS-alpha | ||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 289 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | ATP + succinate + CoA = ADP + phosphate + succinyl-CoA. |
| Subunit structure | Heterotetramer of two alpha and two beta subunits By similarity. |
| Sequence similarities | Belongs to the succinate/malate CoA ligase alpha subunit family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP citrate synthase activityInferred from electronic annotation. Source: InterPro succinate-CoA ligase (ADP-forming) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG55053.1. BA000007 Genomic DNA. Translation: BAB34177.1. |
| PIR | A85574. B90723. |
| RefSeq | NP_286445.1. NC_002655.2. NP_308781.1. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | P0AGF1. |
| SMR | P0AGF1. Positions 2-288. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P0AGF1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000024600; EBESCP00000023493; EBESCG00000023654. EBESCT00000058382; EBESCP00000056210; EBESCG00000057430. |
| GeneID | 917489. 957836. |
| GenomeReviews | Gene locus Z0883 in contig AE005174_GR. Gene locus ECs0754 in contig BA000007_GR. |
| KEGG | ece:Z0883. ecs:ECs0754. |
| PATRIC | 18350530. VBIEscCol44059_0776. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000010106. |
| HOGENOM | HBG615372. |
| OMA | DETTEAI. |
| ProtClustDB | PRK05678. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS0754-MONOMER. |
Family and domain databases | |
| InterPro | IPR017440. Cit_synth/succinyl-CoA_lig_AS. IPR003781. CoA-bd. IPR005810. CoA_lig_alpha. IPR005811. CoA_ligase. IPR016040. NAD(P)-bd_dom. IPR016102. Succinyl-CoA_synth-like. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:3.40.50.261. Succinyl-CoA_synth-like. 1 hit. |
| KO | K01902. |
| Pfam | PF02629. CoA_binding. 1 hit. PF00549. Ligase_CoA. 1 hit. [Graphical view] |
| PIRSF | PIRSF001553. SucCS_alpha. 1 hit. |
| PRINTS | PR01798. SCOASYNTHASE. |
| SMART | SM00881. CoA_binding. 1 hit. [Graphical view] |
| SUPFAM | SSF52210. CoA_ligase. 1 hit. |
| TIGRFAMs | TIGR01019. SucCoAalpha. 1 hit. |
| PROSITE | PS01216. SUCCINYL_COA_LIG_1. 1 hit. PS00399. SUCCINYL_COA_LIG_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SUCD_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0AGF1 Secondary accession number(s): P07459 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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