H2FR23 (H2FR23_CORPS) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 13.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Acetate kinase HAMAP-Rule MF_00020 EC=2.7.2.1 HAMAP-Rule MF_00020 Alternative name(s): Acetokinase HAMAP-Rule MF_00020 | ||||
| Gene names |
| ||||
| Organism | Corynebacterium pseudotuberculosis 3/99-5 EMBL AEX40333.1 | ||||
| Taxonomic identifier | 1087452 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › ![]() |
Protein attributes
| Sequence length | 400 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction By similarity. HAMAP-Rule MF_00020 |
| Catalytic activity | ATP + acetate = ADP + acetyl phosphate. HAMAP-Rule MF_00020 |
| Cofactor | Mg2+. Can also accept Mn2+ By similarity. HAMAP-Rule MF_00020 |
| Pathway | Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2. HAMAP-Rule MF_00020 |
| Subunit structure | Homodimer By similarity. HAMAP-Rule MF_00020 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00020 SAAS SAAS023865. |
| Sequence similarities | Belongs to the acetokinase family. RuleBase RU003835 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm HAMAP-Rule MF_00020 SAAS SAAS023865 |
| Ligand | ATP-binding HAMAP-Rule MF_00020 SAAS SAAS004372 Magnesium HAMAP-Rule MF_00020 Metal-binding HAMAP-Rule MF_00020 Nucleotide-binding |
| Molecular function | Kinase RuleBase RU003835 HAMAP-Rule MF_00020 SAAS SAAS004372 EMBL AEX40333.1 Transferase |
| Gene Ontology (GO) | |
| Biological_process | acetyl-CoA biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway organic acid metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate kinase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Nucleotide binding | 209 – 213 | 5 | ATP By similarity HAMAP-Rule MF_00020 | ||||||
| Nucleotide binding | 283 – 285 | 3 | ATP By similarity HAMAP-Rule MF_00020 | ||||||
| Nucleotide binding | 331 – 335 | 5 | ATP By similarity HAMAP-Rule MF_00020 | ||||||
Sites | |||||||||
| Active site | 149 | 1 | Proton donor/acceptor By similarity HAMAP-Rule MF_00020 | ||||||
| Metal binding | 8 | 1 | Magnesium By similarity HAMAP-Rule MF_00020 | ||||||
| Metal binding | 385 | 1 | Magnesium By similarity HAMAP-Rule MF_00020 | ||||||
| Binding site | 15 | 1 | ATP By similarity HAMAP-Rule MF_00020 | ||||||
| Binding site | 92 | 1 | Substrate By similarity HAMAP-Rule MF_00020 | ||||||
| Site | 181 | 1 | Transition state stabilizer By similarity HAMAP-Rule MF_00020 | ||||||
| Site | 242 | 1 | Transition state stabilizer By similarity HAMAP-Rule MF_00020 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Complete Genome Sequences of Corynebacterium pseudotuberculosis Strains 3/99-5 and 42/02-A, Isolated from Sheep in Scotland and Australia, Respectively." Pethick F.E., Lainson A.F., Yaga R., Flockhart A., Smith D.G., Donachie W., Cerdeira L.T., Silva A., Bol E., Lopes T.S., Barbosa M.S., Pinto A.C., Dos Santos A.R., Soares S.C., Almeida S.S., Guimaraes L.C., Aburjaile F.F., Abreu V.A. Fontaine M.C.J. Bacteriol. 194:4736-4737(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: 3/99-5 EMBL AEX40333.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP003152 Genomic DNA. Translation: AEX40333.1. |
| RefSeq | YP_005123982.1. NC_016781.1. |
3D structure databases | |
| ProteinModelPortal | H2FR23. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AEX40333; AEX40333; Cp3995_1883. |
| GeneID | 11674761. |
| KEGG | cpl:Cp3995_1883. |
Phylogenomic databases | |
| KO | K00925. |
Enzyme and pathway databases | |
| UniPathway | UPA00340; UER00458. |
Family and domain databases | |
| HAMAP | MF_00020. Acetate_kinase. |
| InterPro | IPR004372. Ac/Proprionate_kinase. IPR000890. Aliphatic_acid_kin_short-chain. IPR023865. Aliphatic_acid_kinase_CS. [Graphical view] |
| PANTHER | PTHR21060. PTHR21060. 1 hit. |
| Pfam | PF00871. Acetate_kinase. 1 hit. [Graphical view] |
| PIRSF | PIRSF000722. Acetate_prop_kin. 1 hit. |
| PRINTS | PR00471. ACETATEKNASE. |
| TIGRFAMs | TIGR00016. ackA. 1 hit. |
| PROSITE | PS01075. ACETATE_KINASE_1. 1 hit. PS01076. ACETATE_KINASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | H2FR23_CORPS | ||||||||
| Accession | Primary (citable) accession number: H2FR23 | ||||||||
| Entry history |
| ||||||||
| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
