Q3SH82 (PANC_THIDA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 52.
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 |
| ||||
| Organism | Thiobacillus denitrificans (strain ATCC 25259) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 292415 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Hydrogenophilales › Hydrogenophilaceae › Thiobacillus › ![]() |
Protein attributes
| Sequence length | 283 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 – 283 | 283 | Pantothenate synthetase HAMAP-Rule MF_00158 | PRO_0000305568 | |||||
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
| ||||||||||||||||||
References
| [1] | "The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans." Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P. J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25259. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000116 Genomic DNA. Translation: AAZ98007.1. |
| RefSeq | YP_315812.1. NC_007404.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2A7X based on UniProtKB P0A5R0. |
| ProteinModelPortal | Q3SH82. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 292415.Tbd_2054. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAZ98007; AAZ98007; Tbd_2054. |
| GeneID | 3672225. |
| KEGG | tbd:Tbd_2054. |
| PATRIC | 23970283. VBIThiDen82923_2032. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0414. |
| HOGENOM | HOG000175516. |
| KO | K01918. |
| OMA | EDFGSYP. |
| ProtClustDB | PRK00380. |
Enzyme and pathway databases | |
| 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_THIDA | ||||||||
| Accession | Primary (citable) accession number: Q3SH82 | ||||||||
| Entry history |
| ||||||||
| 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
