P52998 (PANC_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 80.
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 | Bacillus subtilis | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 286 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 Reference 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 – 286 | 286 | Pantothenate synthetase HAMAP MF_00158 | PRO_0000128204 | |||||
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
| « Hide 'large scale' references | |
| [1] | "Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome." Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D., Serror P. Microbiology 142:2005-2016(1996) [PubMed: 8760912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501. |
| [2] | "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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L47709 Genomic DNA. Translation: AAB38449.1. AL009126 Genomic DNA. Translation: CAB14158.1. |
| PIR | H69671. |
| RefSeq | NP_390123.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P52998. |
| SMR | P52998. Positions 1-279. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000003278; EBBACP00000003278; EBBACG00000003271. |
| GeneID | 939030. |
| GenomeReviews | Gene locus BSU22420 in contig AL009126_GR. |
| KEGG | bsu:BSU22420. |
| NMPDR | fig|224308.1.peg.2246. |
| PATRIC | 18976293. VBIBacSub10457_2337. |
Organism-specific databases | |
| GenoList | BSU22420. [Micado] |
Phylogenomic databases | |
| GeneTree | EBGT00050000001451. |
| HOGENOM | HBG428839. |
| OMA | LNMPIQI. |
| PhylomeDB | P52998. |
| ProtClustDB | PRK00380. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU22420-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. |
| KO | K01918. |
| 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_BACSU | ||||||||
| Accession | Primary (citable) accession number: P52998 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
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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