O24035 (PANC_LOTJA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 79.
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: Pantoate--beta-alanine ligase EC=6.3.2.1 Alternative name(s): Pantoate-activating enzyme Pantothenate synthetase | ||
| Gene names |
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| Organism | Lotus japonicus (Lotus corniculatus var. japonicus) | ||
| Taxonomic identifier | 34305 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Loteae › Lotus![]() |
Protein attributes
| Sequence length | 308 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. |
| Pathway | |
| Subunit structure | Homodimer Potential. |
| Subcellular location | Cytoplasm Potential. |
| Tissue specificity | Expressed at low levels in leaf and root. Ref.1 |
| Sequence similarities | Belongs to the pantothenate synthetase family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 7.8. Activity decreases sharply with increasing acidity and is null at pH 7. There is only a slight decrease toward higher pH. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pantothenate biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | pantothenate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| 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)
Sequences
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References
| [1] | "The final step of pantothenate biosynthesis in higher plants: cloning and characterization of pantothenate synthetase from Lotus japonicus and Oryza sativum (rice)." Genschel U., Powell C.A., Abell C., Smith A.G. Biochem. J. 341:669-678(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-17, TISSUE SPECIFICITY. Strain: cv. Gifu / B-129. Tissue: Root nodule. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y10252 mRNA. Translation: CAA71302.1. |
| UniGene | Lja.12058. |
3D structure databases | |
| ProteinModelPortal | O24035. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-9445. |
| BRENDA | 6.3.2.1. 3076. |
| UniPathway | UPA00028; UER00005. |
Family and domain databases | |
| Gene3D | 3.40.50.620. 1 hit. |
| 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_LOTJA | ||||||||
| Accession | Primary (citable) accession number: O24035 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
