A6QIT5 (THIE_STAAE) 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: Thiamine-phosphate synthase Short name=TP synthase Short name=TPS EC=2.5.1.3 Alternative name(s): Thiamine-phosphate pyrophosphorylase Short name=TMP pyrophosphorylase Short name=TMP-PPase | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain Newman) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 426430 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 213 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP) By similarity. HAMAP-Rule MF_00097 |
| Catalytic activity | 2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate. HAMAP-Rule MF_00097 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Pathway | Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1. HAMAP-Rule MF_00097 |
| Sequence similarities | Belongs to the thiamine-phosphate synthase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Thiamine biosynthesis |
| Ligand | Magnesium Metal-binding |
| Molecular function | Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | thiamine biosynthetic process Inferred from electronic annotation. Source: HAMAP thiamine diphosphate biosynthetic processInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | magnesium ion binding Inferred from electronic annotation. Source: HAMAP thiamine-phosphate diphosphorylase 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 – 213 | 213 | Thiamine-phosphate synthase HAMAP-Rule MF_00097 | PRO_1000071284 | |||||
Regions | |||||||||
| Region | 40 – 44 | 5 | HMP-PP binding By similarity | ||||||
| Region | 139 – 141 | 3 | THZ-P binding By similarity | ||||||
| Region | 191 – 192 | 2 | THZ-P binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 76 | 1 | Magnesium By similarity | ||||||
| Metal binding | 95 | 1 | Magnesium By similarity | ||||||
| Binding site | 75 | 1 | HMP-PP By similarity | ||||||
| Binding site | 113 | 1 | HMP-PP By similarity | ||||||
| Binding site | 142 | 1 | HMP-PP By similarity | ||||||
| Binding site | 171 | 1 | THZ-P; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Staphylococcus aureus strain Newman and comparative analysis of staphylococcal genomes: polymorphism and evolution of two major pathogenicity islands." Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K. J. Bacteriol. 190:300-310(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Newman. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AP009351 Genomic DNA. Translation: BAF68267.1. |
| RefSeq | YP_001333029.1. NC_009641.1. |
3D structure databases | |
| ProteinModelPortal | A6QIT5. |
| SMR | A6QIT5. Positions 4-209. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 426430.NWMN_1995. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAF68267; BAF68267; NWMN_1995. |
| GeneID | 5332232. |
| KEGG | sae:NWMN_1995. |
| PATRIC | 19587794. VBIStaAur133992_2182. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0352. |
| HOGENOM | HOG000155781. |
| KO | K00788. |
| OMA | LFFVNDR. |
| ProtClustDB | PRK00043. |
Enzyme and pathway databases | |
| BioCyc | SAUR426430:GIXC-1996-MONOMER. |
| UniPathway | UPA00060; UER00141. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. |
| HAMAP | MF_00097. TMP_synthase. |
| InterPro | IPR013785. Aldolase_TIM. IPR022998. ThiaminP_synth_SF. IPR003733. TMP_synthase. [Graphical view] |
| Pfam | PF02581. TMP-TENI. 1 hit. [Graphical view] |
| SUPFAM | SSF51391. TMP_synthase. 1 hit. |
| TIGRFAMs | TIGR00693. thiE. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | THIE_STAAE | ||||||||
| Accession | Primary (citable) accession number: A6QIT5 | ||||||||
| 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
