P26405 (RFBK_SALTY) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 102.
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: Phosphomannomutase Short name=PMM EC=5.4.2.8 | ||||
| Gene names |
| ||||
| Organism | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 99287 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › ![]() |
Protein attributes
| Sequence length | 477 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS group B O antigen. |
| Catalytic activity | Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate. |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Pathway | Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis. |
| Subcellular location | Cell membrane; Multi-pass membrane protein Potential. |
| Sequence similarities | Belongs to the phosphohexose mutase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipopolysaccharide biosynthesis |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | Magnesium Metal-binding |
| Molecular function | Isomerase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | GDP-mannose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway O antigen biosynthetic processInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphomannomutase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 477 | 477 | Phosphomannomutase | PRO_0000147826 | |||||
Regions | |||||||||
| Transmembrane | 30 – 46 | 17 | Helical; Potential | ||||||
| Transmembrane | 265 – 284 | 20 | Helical; Potential | ||||||
Sites | |||||||||
| Active site | 111 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 111 | 1 | Magnesium; via phosphate group By similarity | ||||||
| Metal binding | 245 | 1 | Magnesium By similarity | ||||||
| Metal binding | 247 | 1 | Magnesium By similarity | ||||||
| Metal binding | 249 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Structure and sequence of the rfb (O antigen) gene cluster of Salmonella serovar typhimurium (strain LT2)." Jiang X.-M., Neal B., Santiago F., Lee S.J., Romana L.K., Reeves P.R. Mol. Microbiol. 5:695-713(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LT2. |
| [2] | "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K.Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X56793 Genomic DNA. Translation: CAA40129.1. AE006468 Genomic DNA. Translation: AAL20987.1. |
| PIR | S15313. |
| RefSeq | NP_461028.1. NC_003197.1. |
3D structure databases | |
| ProteinModelPortal | P26405. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 99287.STM2083. |
Proteomic databases | |
| PaxDb | P26405. |
| PRIDE | P26405. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAL20987; AAL20987; STM2083. |
| GeneID | 1253604. |
| KEGG | stm:STM2083. |
| PATRIC | 32382749. VBISalEnt20916_2205. |
Phylogenomic databases | |
| eggNOG | COG1109. |
| HOGENOM | HOG000066295. |
| KO | K01840. |
| OMA | RPSSYAM. |
| ProtClustDB | CLSK894265. |
Enzyme and pathway databases | |
| UniPathway | UPA00126; UER00424. UPA00281. |
Family and domain databases | |
| Gene3D | 3.40.120.10. 1 hit. |
| InterPro | IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. [Graphical view] |
| Pfam | PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view] |
| SUPFAM | SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits. |
| PROSITE | PS00710. PGM_PMM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RFBK_SALTY | ||||||||
| Accession | Primary (citable) accession number: P26405 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
