Q9WZK0 (COAD_THEMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 84.
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: Phosphopantetheine adenylyltransferase EC=2.7.7.3 Alternative name(s): Dephospho-CoA pyrophosphorylase Pantetheine-phosphate adenylyltransferase Short name=PPAT | ||||||
| Gene names |
| ||||||
| Organism | Thermotoga maritima | ||||||
| Taxonomic identifier | 2336 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga |
Protein attributes
| Sequence length | 161 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate By similarity. HAMAP MF_00151 |
| Catalytic activity | ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA. HAMAP MF_00151 |
| Pathway | Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. HAMAP MF_00151 |
| Subunit structure | Homohexamer By similarity. HAMAP MF_00151 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00151. |
| Sequence similarities | Belongs to the bacterial CoaD family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Coenzyme A biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Nucleotidyltransferase Transferase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | coenzyme A 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 pantetheine-phosphate adenylyltransferase 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 – 161 | 161 | Phosphopantetheine adenylyltransferase HAMAP MF_00151 | PRO_0000156296 | ||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||
| Beta strand | 2 – 7 | 6 | ||||||||||||||||||||||||||||||||||
| Helix | 14 – 24 | 11 | ||||||||||||||||||||||||||||||||||
| Beta strand | 28 – 35 | 8 | ||||||||||||||||||||||||||||||||||
| Helix | 46 – 56 | 11 | ||||||||||||||||||||||||||||||||||
| Turn | 57 – 59 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 63 – 68 | 6 | ||||||||||||||||||||||||||||||||||
| Helix | 72 – 79 | 8 | ||||||||||||||||||||||||||||||||||
| Beta strand | 83 – 88 | 6 | ||||||||||||||||||||||||||||||||||
| Helix | 94 – 107 | 14 | ||||||||||||||||||||||||||||||||||
| Beta strand | 112 – 117 | 6 | ||||||||||||||||||||||||||||||||||
| Helix | 120 – 122 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 127 – 135 | 9 | ||||||||||||||||||||||||||||||||||
| Turn | 141 – 143 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 146 – 155 | 10 | ||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. Fraser C.M.Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE000512 Genomic DNA. Translation: AAD35822.1. | ||||||||||||
| PIR | H72339. | ||||||||||||
| RefSeq | NP_228550.1. NC_000853.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q9WZK0. | ||||||||||||
| SMR | Q9WZK0. Positions 1-158. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 898408. | ||||||||||||
| GenomeReviews | Gene locus TM_0741 in contig AE000512_GR. | ||||||||||||
| KEGG | tma:TM0741. | ||||||||||||
| NMPDR | fig|243274.1.peg.734. | ||||||||||||
| PATRIC | 23936402. VBITheMar51294_0754. | ||||||||||||
| TIGR | TM_0741. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG288308. | ||||||||||||
| OMA | AMSDFEY. | ||||||||||||
| PhylomeDB | Q9WZK0. | ||||||||||||
| ProtClustDB | PRK00168. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | TMAR243274:TM_0741-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00151. PPAT_bact. [Tree] | ||||||||||||
| InterPro | IPR004821. Cyt_trans-rel. IPR004820. Cytidylyltransf. IPR001980. LPS_biosynth. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. | ||||||||||||
| KO | K00954. | ||||||||||||
| Pfam | PF01467. CTP_transf_2. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR01020. LPSBIOSNTHSS. | ||||||||||||
| TIGRFAMs | TIGR01510. CoaD_prev_kdtB. 1 hit. TIGR00125. Cyt_tran_rel. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | COAD_THEMA | ||||||||
| Accession | Primary (citable) accession number: Q9WZK0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with