Reviewed,
UniProtKB/Swiss-Prot Q55074 (PANCY_SYNY3)
Last modified
November 3, 2009.
Version 60.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Bifunctional pantoate ligase/cytidylate kinase Including the following 2 domains: 1- Recommended name: Pantoate--beta-alanine ligase EC=6.3.2.1 Alternative name(s): Pantothenate synthetase Pantoate-activating enzyme 2- Recommended name: Cytidylate kinase Short name=CK EC=2.7.4.14 Alternative name(s): Cytidine monophosphate kinase Short name=CMP kinase | ||||||
| Gene names |
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| Organism | Synechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1148 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Chroococcales › Synechocystis |
Protein attributes
| Sequence length | 513 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP MF_01349 ATP + (d)CMP = ADP + (d)CDP. HAMAP MF_01349 |
| Pathway | Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP MF_01349 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | In the N-terminal section; belongs to the pantothenate synthetase family. In the C-terminal section; belongs to the cytidylate kinase family. Type 1 subfamily. |
| Sequence caution | The sequence AAA86660.1 differs from that shown. Reason: Frameshift at positions 213, 240, 254 and 258. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pantothenate biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Ligase Transferase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | pantothenate biosynthetic process Inferred from electronic annotation. Source: HAMAP pyrimidine nucleotide metabolic processInferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP cytidylate kinase activityInferred from electronic annotation. Source: HAMAP 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 – 513 | 513 | Bifunctional pantoate ligase/cytidylate kinase HAMAP MF_01349 | PRO_0000131992 | |||||
Regions | |||||||||
| Nucleotide binding | 296 – 304 | 9 | ATP By similarity | ||||||
| Region | 1 – 283 | 283 | Pantoate--beta-alanine ligase HAMAP MF_01349 | ||||||
| Region | 284 – 513 | 230 | Cytidylate kinase HAMAP MF_01349 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning, characterization and expression of carbonic anhydrase from the cyanobacterium Synechocystis PCC6803." So A.K.C., Espie G.S. Plant Mol. Biol. 37:205-215(1998) [PubMed: 9617794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S.DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| U44896 Genomic DNA. Translation: AAA86660.1. Frameshift. U44896 Genomic DNA. Translation: AAA86661.1. BA000022 Genomic DNA. Translation: BAA18165.1. | |
| PIR | S75604. |
| RefSeq | NP_441485.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q55074. 1 interaction. |
| STRING | Q55074. |
Genome annotation databases | |
| GeneID | 954865. |
| GenomeReviews | Gene locus sll1249 in contig BA000022_GR. |
| KEGG | syn:sll1249. |
| NMPDR | fig|1148.1.peg.1586. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q55074. |
| OMA | LGEKDWQ. |
Enzyme and pathway databases | |
| BioCyc | SSP1148:SLL1249-MON. |
Family and domain databases | |
| HAMAP | MF_01349. [Tree] |
| InterPro | IPR003136. Cytidylate_kin. IPR011994. Cytidylate_kin_d. 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 | PF02224. Cytidylate_kin. 1 hit. PF02569. Pantoate_ligase. 1 hit. [Graphical view] |
| ProDom | PD000657. Adenylate_kin. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00017. cmk. 1 hit. TIGR00018. panC. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PANCY_SYNY3 | ||||||||
| Accession | Primary (citable) accession number: Q55074 Secondary accession number(s): P74087, Q55073 | ||||||||
| 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 |
| Synechocystis PCC 6803 Synechocystis (strain PCC 6803): entries and gene names |

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