Reviewed,
UniProtKB/Swiss-Prot P37564 (COAX_BACSU)
Last modified
November 24, 2009.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Type III pantothenate kinase EC=2.7.1.33 Alternative name(s): Pantothenic acid kinase PanK-III | ||||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 258 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Can not utilize a phosphoryl donor other than ATP. Ref.1 Ref.5 |
| Catalytic activity | ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate. HAMAP MF_01274 |
| Cofactor | Monovalent cations. Ammonium or potassium. Ref.5 |
| Enzyme regulation | Not regulated by feedback inhibition by CoA and its thioesters as described for many other pantothenate kinases. Not inhibited by N-pentylpantothenamide (N5-Pan), and this compound can not act as a substrate either. Ref.1 |
| Pathway | Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. HAMAP MF_01274 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the type III pantothenate kinase family. |
| Biophysicochemical properties | Kinetic parameters: KM=168 µM for pantothenate Ref.1 KM=3.0 mM for ATP |
| Sequence caution | The sequence BAA05305.1 differs from that shown. Reason: Frameshift at position 214. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Coenzyme A biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Metal-binding Nucleotide-binding Potassium |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | coenzyme A biosynthetic process Inferred from electronic annotation. Source: HAMAP positive regulation of transcriptionInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP pantothenate kinase activityInferred from electronic annotation. Source: HAMAP potassium ion bindingInferred from electronic annotation. Source: UniProtKB-KW transcription activator activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 258 | 258 | Type III pantothenate kinase HAMAP MF_01274 | PRO_0000049448 | |||||
Regions | |||||||||
| Nucleotide binding | 6 – 13 | 8 | ATP By similarity | ||||||
| Region | 107 – 110 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 109 | 1 | Proton acceptor Potential | ||||||
| Metal binding | 129 | 1 | Monovalent cation Potential | ||||||
| Binding site | 100 | 1 | Substrate By similarity | ||||||
| Binding site | 132 | 1 | ATP Potential | ||||||
| Binding site | 184 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 214 – 215 | 2 | EP → KQ in AAW83041. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of a new pantothenate kinase isoform from Helicobacter pylori." Brand L.A., Strauss E. J. Biol. Chem. 280:20185-20188(2005) [PubMed: 15795230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CHARACTERIZATION, ENZYME REGULATION, KINETIC PARAMETERS. Strain: 168. |
| [2] | "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin." Ogasawara N., Nakai S., Yoshikawa H. DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [3] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [4] | "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO C-TERMINUS. |
| [5] | "Prokaryotic type II and type III pantothenate kinases: the same monomer fold creates dimers with distinct catalytic properties." Hong B.S., Yun M.K., Zhang Y.-M., Chohnan S., Rock C.O., White S.W., Jackowski S., Park H.-W., Leonardi R. Structure 14:1251-1261(2006) [PubMed: 16905099] [Abstract] Cited for: FUNCTION, COFACTOR. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| AY912104 Genomic DNA. Translation: AAW83041.2. D26185 Genomic DNA. Translation: BAA05305.1. Frameshift. AL009126 Genomic DNA. Translation: CAB11846.2. | |
| PIR | S66100. |
| RefSeq | NP_387951.2. |
3D structure databases | |
| SMR | P37564. Positions 1-253. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 936960. |
| GenomeReviews | Gene locus BSU00700 in contig AL009126_GR. |
| KEGG | bsu:BSU00700. |
Organism-specific databases | |
| SubtiList | BG10133. yacB. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P37564. |
Enzyme and pathway databases | |
| BRENDA | 2.7.1.33. 150. |
Family and domain databases | |
| HAMAP | MF_01274. [Tree] |
| InterPro | IPR004619. Baf. [Graphical view] |
| Pfam | PF03309. Bvg_acc_factor. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00671. baf. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | COAX_BACSU | ||||||||
| Accession | Primary (citable) accession number: P37564 Secondary accession number(s): Q5EC36 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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