A2SEX7 (PANC_METPP) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 43.
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: Pantothenate synthetase Short name=PS EC=6.3.2.1 Alternative name(s): Pantoate--beta-alanine ligase Pantoate-activating enzyme | ||||
| Gene names |
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| Organism | Methylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 420662 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Methylibium › ![]() |
Protein attributes
| Sequence length | 281 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity. HAMAP-Rule MF_00158 |
| Catalytic activity | ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_00158 |
| Pathway | Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_00158 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm Potential HAMAP-Rule MF_00158. |
| Miscellaneous | The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP-Rule MF_00158 |
| Sequence similarities | Belongs to the pantothenate synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pantothenate biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | pantothenate biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW pantoate-beta-alanine ligase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 281 | 281 | Pantothenate synthetase HAMAP-Rule MF_00158 | PRO_0000305482 | |||||
Regions | |||||||||
| Nucleotide binding | 26 – 33 | 8 | ATP By similarity | ||||||
| Nucleotide binding | 144 – 147 | 4 | ATP By similarity | ||||||
| Nucleotide binding | 181 – 184 | 4 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 33 | 1 | Proton donor By similarity | ||||||
| Binding site | 57 | 1 | Beta-alanine By similarity | ||||||
| Binding site | 57 | 1 | Pantoate By similarity | ||||||
| Binding site | 150 | 1 | Pantoate By similarity | ||||||
| Binding site | 173 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
Sequences
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References
| [1] | "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1." Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R. J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PM1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000555 Genomic DNA. Translation: ABM94116.1. |
| RefSeq | YP_001020351.1. NC_008825.1. |
3D structure databases | |
| ProteinModelPortal | A2SEX7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 420662.Mpe_A1155. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABM94116; ABM94116; Mpe_A1155. |
| GeneID | 4785730. |
| KEGG | mpt:Mpe_A1155. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0414. |
| HOGENOM | HOG000175516. |
| KO | K01918. |
| OMA | HTIVSVF. |
Enzyme and pathway databases | |
| BioCyc | MPET420662:GHBE-1870-MONOMER. |
| UniPathway | UPA00028; UER00005. |
Family and domain databases | |
| Gene3D | 3.40.50.620. 1 hit. |
| HAMAP | MF_00158. PanC. |
| InterPro | IPR003721. Pantoate_ligase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| PANTHER | PTHR21299:SF1. PTHR21299:SF1. 1 hit. |
| Pfam | PF02569. Pantoate_ligase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00018. panC. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PANC_METPP | ||||||||
| Accession | Primary (citable) accession number: A2SEX7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
