Reviewed,
UniProtKB/Swiss-Prot Q9X713 (PANC_CORGL)
Last modified
February 9, 2010.
Version 60.
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 |
| ||||
| Organism | Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1718 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium |
Protein attributes
| Sequence length | 279 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Ref.1 |
| Catalytic activity | ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. Ref.1 |
| 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 Potential 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. |
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 – 279 | 279 | Pantothenate synthetase HAMAP MF_00158 | PRO_0000128224 | |||||
Regions | |||||||||
| Nucleotide binding | 26 – 33 | 8 | ATP By similarity | ||||||
| Nucleotide binding | 147 – 150 | 4 | ATP By similarity | ||||||
| Nucleotide binding | 184 – 187 | 4 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 33 | 1 | Proton donor By similarity | ||||||
| Binding site | 57 | 1 | Beta-alanine By similarity | ||||||
| Binding site | 57 | 1 | Pantoate By similarity | ||||||
| Binding site | 153 | 1 | Pantoate By similarity | ||||||
| Binding site | 176 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "D-pantothenate synthesis in Corynebacterium glutamicum and use of panBC and genes encoding L-valine synthesis for D-pantothenate overproduction." Eggeling L., Sahm H. Appl. Environ. Microbiol. 65:1973-1979(1999) [PubMed: 10223988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [2] | "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [3] | "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. Tauch A.J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X96580 Genomic DNA. Translation: CAA65398.1. BA000036 Genomic DNA. Translation: BAB97506.1. BX927148 Genomic DNA. Translation: CAF18681.1. |
| PIR | T47120. |
| RefSeq | NP_599366.1. YP_224410.1. |
3D structure databases | |
| SMR | Q9X713. Positions 1-279. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1021074. 3343643. |
| GenomeReviews | Gene locus Cgl0113 in contig BA000036_GR. |
| KEGG | cgb:cg0148. cgl:NCgl0112. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG428839. |
| OMA | MPIQIIG. |
| PhylomeDB | Q9X713. |
Enzyme and pathway databases | |
| BioCyc | CGLU196627:CG0148-MONOMER. |
| BRENDA | 6.3.2.1. 812. |
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 | PANC_CORGL | ||||||||
| Accession | Primary (citable) accession number: Q9X713 | ||||||||
| 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 |

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