B8ZU49 (B8ZU49_MYCLB) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 20.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Pantothenate synthetase HAMAP MF_00158 Short name=PS HAMAP MF_00158 EC=6.3.2.1 HAMAP MF_00158 Alternative name(s): Pantoate--beta-alanine ligase HAMAP MF_00158 Pantoate-activating enzyme HAMAP MF_00158 | ||||
| Gene names |
| ||||
| Organism | Mycobacterium leprae (strain Br4923) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 561304 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 313 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 By similarity 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. HAMAP MF_00158 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pantothenate biosynthesis HAMAP MF_00158 |
| Cellular component | Cytoplasm HAMAP MF_00158 |
| Ligand | ATP-binding HAMAP MF_00158 Nucleotide-binding |
| Molecular function | Ligase HAMAP MF_00158 EMBL CAR70323.1 |
| 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 | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Nucleotide binding | 43 – 50 | 8 | ATP By similarity HAMAP MF_00158 | ||||||
| Nucleotide binding | 161 – 164 | 4 | ATP By similarity HAMAP MF_00158 | ||||||
| Nucleotide binding | 198 – 201 | 4 | ATP By similarity HAMAP MF_00158 | ||||||
Sites | |||||||||
| Active site | 50 | 1 | Proton donor By similarity HAMAP MF_00158 | ||||||
| Binding site | 75 | 1 | Beta-alanine By similarity HAMAP MF_00158 | ||||||
| Binding site | 75 | 1 | Pantoate By similarity HAMAP MF_00158 | ||||||
| Binding site | 167 | 1 | Pantoate By similarity HAMAP MF_00158 | ||||||
| Binding site | 190 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity HAMAP MF_00158 | ||||||
Sequences
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References
| [1] | "Comparative genomic and phylogeographic analysis of Mycobacterium leprae." Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A., Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C., Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H., Vera-Cabrera L. Cole S.T.Nat. Genet. 41:1282-1289(2009) [PubMed: 19881526] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | FM211192 Genomic DNA. Translation: CAR70323.1. |
| RefSeq | YP_002502921.1. NC_011896.1. |
3D structure databases | |
| ProteinModelPortal | B8ZU49. |
| SMR | B8ZU49. Positions 7-294. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B8ZU49. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000085594; EBMYCP00000082062; EBMYCG00000087046. |
| GeneID | 7326323. |
| GenomeReviews | Gene locus MLBr00230 in contig FM211192_GR. |
| PATRIC | 18040248. VBIMycLep121698_0359. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000016962. |
| HOGENOM | HBG428839. |
| OMA | LNMPIQI. |
| ProtClustDB | PRK00380. |
Family and domain databases | |
| HAMAP | MF_00158. PanC. [Tree] |
| InterPro | 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 | TIGR00018. PanC. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | B8ZU49_MYCLB | ||||||||
| Accession | Primary (citable) accession number: B8ZU49 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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