Reviewed,
UniProtKB/Swiss-Prot Q5P9T3 (PANC_ANAMM)
Last modified
November 3, 2009.
Version 28.
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 | Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 234826 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma |
Protein attributes
| Sequence length | 277 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| 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. |
| Subcellular location | Cytoplasm Potential. |
| Miscellaneous | The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. |
| 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 – 277 | 277 | Pantothenate synthetase HAMAP MF_00158 | PRO_0000305391 | |||||
Regions | |||||||||
| Nucleotide binding | 28 – 35 | 8 | ATP By similarity | ||||||
| Nucleotide binding | 145 – 148 | 4 | ATP By similarity | ||||||
| Nucleotide binding | 182 – 185 | 4 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 35 | 1 | Proton donor By similarity | ||||||
| Binding site | 59 | 1 | Beta-alanine By similarity | ||||||
| Binding site | 59 | 1 | Pantoate By similarity | ||||||
| Binding site | 174 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000030 Genomic DNA. Translation: AAV86947.1. Different initiation. | |
| RefSeq | YP_154202.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5P9T3. |
Genome annotation databases | |
| GeneID | 3171235. |
| GenomeReviews | Gene locus AM1089 in contig CP000030_GR. |
| KEGG | ama:AM1089. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q5P9T3. |
| OMA | ASSKENH. |
Enzyme and pathway databases | |
| BioCyc | AMAR234826:AM1089-MON. |
Family and domain databases | |
| HAMAP | MF_00158. [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_ANAMM | ||||||||
| Accession | Primary (citable) accession number: Q5P9T3 | ||||||||
| 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


