E4TX47 (E4TX47_SULKY) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 17.
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-Rule MF_00158 Short name=PS HAMAP-Rule MF_00158 EC=6.3.2.1 HAMAP-Rule MF_00158 Alternative name(s): Pantoate--beta-alanine ligase HAMAP-Rule MF_00158 Pantoate-activating enzyme HAMAP-Rule MF_00158 | ||||
| Gene names |
| ||||
| Organism | Sulfuricurvum kujiense (strain ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1) [Complete proteome] [HAMAP] EMBL ADR34913.1 | ||||
| Taxonomic identifier | 709032 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Sulfuricurvum › ![]() |
Protein attributes
| Sequence length | 273 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 SAAS SAAS003721 |
| Pathway | Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_00158 SAAS SAAS003721 |
| Subunit structure | Homodimer By similarity. HAMAP-Rule MF_00158 |
| Subcellular location | Cytoplasm By similarity 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. HAMAP-Rule MF_00158 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pantothenate biosynthesis HAMAP-Rule MF_00158 SAAS SAAS003721 |
| Cellular component | Cytoplasm HAMAP-Rule MF_00158 SAAS SAAS003721 |
| Ligand | ATP-binding HAMAP-Rule MF_00158 SAAS SAAS003721 Nucleotide-binding |
| Molecular function | Ligase HAMAP-Rule MF_00158 SAAS SAAS003721 EMBL ADR34913.1 |
| 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 | 27 – 34 | 8 | ATP By similarity HAMAP-Rule MF_00158 | ||||||
| Nucleotide binding | 144 – 147 | 4 | ATP By similarity HAMAP-Rule MF_00158 | ||||||
| Nucleotide binding | 181 – 184 | 4 | ATP By similarity HAMAP-Rule MF_00158 | ||||||
Sites | |||||||||
| Active site | 34 | 1 | Proton donor By similarity HAMAP-Rule MF_00158 | ||||||
| Binding site | 58 | 1 | Beta-alanine By similarity HAMAP-Rule MF_00158 | ||||||
| Binding site | 58 | 1 | Pantoate By similarity HAMAP-Rule MF_00158 | ||||||
| Binding site | 150 | 1 | Pantoate By similarity HAMAP-Rule MF_00158 | ||||||
| Binding site | 173 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity HAMAP-Rule MF_00158 | ||||||
Sequences
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References
| [1] | "Complete genome sequence of the sulfur compounds oxidizing chemolithoautotroph Sulfuricurvum kujiense type strain (YK-1(T))." Han C., Kotsyurbenko O., Chertkov O., Held B., Lapidus A., Nolan M., Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Mikhailova N. Detter J.C.Stand. Genomic Sci. 6:94-103(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP002355 Genomic DNA. Translation: ADR34913.1. |
| RefSeq | YP_004061113.1. NC_014762.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ADR34913; ADR34913; Sulku_2253. |
| GeneID | 10019436. |
| KEGG | sku:Sulku_2253. |
| PATRIC | 45373303. VBISulKuj150841_2491. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000175517. |
| KO | K01918. |
Enzyme and pathway databases | |
| BioCyc | SKUJ709032:GHTQ-2303-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 | E4TX47_SULKY | ||||||||
| Accession | Primary (citable) accession number: E4TX47 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
