Q72HS0 (PANC_THET2) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 47.
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 | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 262724 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus |
Protein attributes
| Sequence length | 276 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 MF_00158 |
| Catalytic activity | ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP MF_00158 |
| Pathway | Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP MF_00158 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00158 |
| Subcellular location | Cytoplasm Potential HAMAP MF_00158. |
| Miscellaneous | The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP 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: UniProtKB-KW |
| 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: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 276 | 276 | Pantothenate synthetase HAMAP MF_00158 | PRO_0000128282 | |||||
Regions | |||||||||
| Nucleotide binding | 25 – 32 | 8 | ATP By similarity | ||||||
| Nucleotide binding | 143 – 146 | 4 | ATP By similarity | ||||||
| Nucleotide binding | 180 – 183 | 4 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 32 | 1 | Proton donor By similarity | ||||||
| Binding site | 56 | 1 | Beta-alanine By similarity | ||||||
| Binding site | 56 | 1 | Pantoate By similarity | ||||||
| Binding site | 149 | 1 | Pantoate By similarity | ||||||
| Binding site | 172 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of the extreme thermophile Thermus thermophilus." Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J. Nat. Biotechnol. 22:547-553(2004) [PubMed: 15064768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB27 / ATCC BAA-163 / DSM 7039. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017221 Genomic DNA. Translation: AAS81758.1. |
| RefSeq | YP_005385.1. NC_005835.1. |
3D structure databases | |
| ProteinModelPortal | Q72HS0. |
| SMR | Q72HS0. Positions 1-276. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q72HS0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2774880. |
| GenomeReviews | Gene locus TT_C1416 in contig AE017221_GR. |
| PATRIC | 23953249. VBITheThe54392_1410. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0414. |
| HOGENOM | HBG428839. |
| OMA | LNMPIQI. |
| PhylomeDB | Q72HS0. |
| ProtClustDB | PRK00380. |
Enzyme and pathway databases | |
| BioCyc | TTHE262724:TT_C1416-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00158. PanC. [Tree] |
| InterPro | IPR004821. Cyt_trans-rel. IPR003721. Pantoate_ligase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. |
| PANTHER | PTHR21299:SF1. Pantoate_ligase. 1 hit. |
| Pfam | PF02569. Pantoate_ligase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00125. Cyt_tran_rel. 1 hit. TIGR00018. PanC. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PANC_THET2 | ||||||||
| Accession | Primary (citable) accession number: Q72HS0 | ||||||||
| 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 |

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