Reviewed,
UniProtKB/Swiss-Prot Q06951 (RFBB_VIBCH)
Last modified
June 16, 2009.
Version 69.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Phosphomannomutase Short name=PMM EC=5.4.2.8 | ||||
| Gene names |
| ||||
| Organism | Vibrio cholerae [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 666 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio |
Protein attributes
| Sequence length | 463 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| 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 Probable. |
| Sequence similarities | Belongs to the phosphohexose mutase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipopolysaccharide biosynthesis |
| Cellular component | Cell membrane Membrane |
| Ligand | Magnesium Metal-binding |
| Molecular function | Isomerase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 463 | 463 | Phosphomannomutase | PRO_0000147827 | |||||
Sites | |||||||||
| Active site | 103 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 103 | 1 | Magnesium; via phosphate group By similarity | ||||||
| Metal binding | 248 | 1 | Magnesium By similarity | ||||||
| Metal binding | 250 | 1 | Magnesium By similarity | ||||||
| Metal binding | 252 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Serotype conversion in Vibrio cholerae O1." Stroeher U.H., Karageorgos L.E., Morona R., Manning P.A. Proc. Natl. Acad. Sci. U.S.A. 89:2566-2570(1992) [PubMed: 1372980] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: El Tor O17 / Serotype O1. |
| [2] | "DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. Fraser C.M.Nature 406:477-483(2000) [PubMed: 10952301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961 / Serotype O1. |
Cross-references
Sequence databases | |
|---|---|
| X59554 Genomic DNA. Translation: CAA42135.1. AE003852 Genomic DNA. Translation: AAF93418.1. | |
| PIR | S28469. |
| RefSeq | NP_229899.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1K2Y based on UniProtKB P26276. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2614705. |
| GenomeReviews | Gene locus VC_0242 in contig AE003852_GR. |
| KEGG | vch:VC0242. |
| TIGR | VC_0242. |
Phylogenomic databases | |
| HOGENOM | Q06951. |
| OMA | Q06951. LENKIFI. |
Enzyme and pathway databases | |
| BRENDA | 5.4.2.8. 19019. |
Family and domain databases | |
| 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. IPR005841. A-D-PHexomutase_N. [Graphical view] |
| Gene3D | G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits. |
| 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] |
| PRINTS | PR00509. PGMPMM. |
| PROSITE | PS00710. PGM_PMM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RFBB_VIBCH | ||||||||
| Accession | Primary (citable) accession number: Q06951 Secondary accession number(s): Q9JQ14 | ||||||||
| 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 |

Clusters with


