Q00330 (RFBK_SALMU) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 74.
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 muenchen | ||||
| Taxonomic identifier | 596 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › ![]() |
Protein attributes
| Sequence length | 478 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 C2 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 |
| 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 – 478 | 478 | Phosphomannomutase | PRO_0000147825 | |||||
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
| [1] | "Molecular analysis of the rfb gene cluster of Salmonella serovar muenchen (strain M67): the genetic basis of the polymorphism between groups C2 and B." Brown P.K., Romana L.K., Reeves P.R. Mol. Microbiol. 6:1385-1394(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: M67. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X61917 Genomic DNA. Translation: CAA43916.1. |
| PIR | S22622. |
3D structure databases | |
| ProteinModelPortal | Q00330. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
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_SALMU | ||||||||
| Accession | Primary (citable) accession number: Q00330 | ||||||||
| 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
