A0QA93 (PANC_MYCA1) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 44.
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 |
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| Organism | Mycobacterium avium (strain 104) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 243243 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium avium complex (MAC) › ![]() |
Protein attributes
| Sequence length | 308 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-Rule MF_00158 |
| Catalytic activity | ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_00158 |
| Pathway | Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_00158 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm Potential HAMAP-Rule MF_00158. |
| Miscellaneous | The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP-Rule 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 – 308 | 308 | Pantothenate synthetase HAMAP-Rule MF_00158 | PRO_0000305485 | |||||
Regions | |||||||||
| Nucleotide binding | 39 – 46 | 8 | ATP By similarity | ||||||
| Nucleotide binding | 157 – 160 | 4 | ATP By similarity | ||||||
| Nucleotide binding | 194 – 197 | 4 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 46 | 1 | Proton donor By similarity | ||||||
| Binding site | 71 | 1 | Beta-alanine By similarity | ||||||
| Binding site | 71 | 1 | Pantoate By similarity | ||||||
| Binding site | 163 | 1 | Pantoate By similarity | ||||||
| Binding site | 186 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
Sequences
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References
| [1] | Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 104. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000479 Genomic DNA. Translation: ABK64754.1. |
| RefSeq | YP_879831.1. NC_008595.1. |
3D structure databases | |
| ProteinModelPortal | A0QA93. |
| SMR | A0QA93. Positions 3-288. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 243243.MAV_0551. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABK64754; ABK64754; MAV_0551. |
| GeneID | 4528629. |
| KEGG | mav:MAV_0551. |
| PATRIC | 17982838. VBIMycAvi38287_0532. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0414. |
| HOGENOM | HOG000175516. |
| KO | K01918. |
| OMA | EDFGSYP. |
| ProtClustDB | PRK00380. |
Enzyme and pathway databases | |
| BioCyc | MAVI243243:GH3Y-590-MONOMER. |
| UniPathway | UPA00028; UER00005. |
Family and domain databases | |
| Gene3D | 3.40.50.620. 1 hit. |
| HAMAP | MF_00158. PanC. |
| InterPro | IPR003721. Pantoate_ligase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| PANTHER | PTHR21299:SF1. PTHR21299:SF1. 1 hit. |
| Pfam | PF02569. Pantoate_ligase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00018. panC. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PANC_MYCA1 | ||||||||
| Accession | Primary (citable) accession number: A0QA93 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
