Reviewed,
UniProtKB/Swiss-Prot Q81ST2 (PANC_BACAN)
Last modified
February 9, 2010.
Version 45.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names 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 |
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| Organism | Bacillus anthracis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 282 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: 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 – 282 | 282 | Pantothenate synthetase HAMAP MF_00158 | PRO_0000128198 | |||||
Regions | |||||||||
| Nucleotide binding | 30 – 37 | 8 | ATP By similarity | ||||||
| Nucleotide binding | 147 – 150 | 4 | ATP By similarity | ||||||
| Nucleotide binding | 184 – 187 | 4 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 37 | 1 | Proton donor By similarity | ||||||
| Binding site | 61 | 1 | Beta-alanine By similarity | ||||||
| Binding site | 61 | 1 | Pantoate By similarity | ||||||
| Binding site | 153 | 1 | Pantoate By similarity | ||||||
| Binding site | 176 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| [3] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP25499.1. AE017334 Genomic DNA. Translation: AAT30660.1. AE017225 Genomic DNA. Translation: AAT53770.1. |
| RefSeq | NP_844013.1. YP_018185.1. YP_027719.1. |
3D structure databases | |
| SMR | Q81ST2. Positions 1-279. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1086855. 2815431. 2849787. |
| GenomeReviews | Gene locus BA_1563 in contig AE016879_GR. Gene locus BAS1450 in contig AE017225_GR. Gene locus GBAA_1563 in contig AE017334_GR. |
| KEGG | ban:BA1563. bar:GBAA1563. bat:BAS1450. |
| TIGR | BA_1563. GBAA_1563. |
Phylogenomic databases | |
| HOGENOM | HBG428839. |
| OMA | DEAHDAK. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS1450-MONOMER. BANT261594:GBAA1563-MONOMER. |
| BRENDA | 6.3.2.1. 267517. |
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_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81ST2 Secondary accession number(s): Q6I112, Q6KUW6 | ||||||||
| 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
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


