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P26405 (RFBK_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphomannomutase

Short name=PMM
EC=5.4.2.8
Gene names
Name:rfbK
Ordered Locus Names:STM2083
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceInferred 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

Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.

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 processLipopolysaccharide biosynthesis
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGDP-mannose biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

O antigen biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphomannomutase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477Phosphomannomutase
PRO_0000147826

Regions

Transmembrane30 – 4617Helical; Potential
Transmembrane265 – 28420Helical; Potential

Sites

Active site1111Phosphoserine intermediate By similarity
Metal binding1111Magnesium; via phosphate group By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity
Metal binding2491Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
P26405 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: BA6BF851AB931915

FASTA47752,086
        10         20         30         40         50         60 
MNVVNNSRDV IYSSGIVFGT SGARGLVKDF TPQVCAAFTV SFVAVMQEHF SFDTVALAID 

        70         80         90        100        110        120 
NRPSSYGMAQ ACAAALADKG VNCIFYGVVP TPALAFQSMS DNMPAIMVTG SHIPFERNGL 

       130        140        150        160        170        180 
KFYRPDGEIT KHDEAAILSV EDTCSHLELK ELIVSEMAAV NYISRYTSLF STPFLKNKRI 

       190        200        210        220        230        240 
GIYEHSSAGR DLYKPLFIAL GAEVVSLGRS DNFVPIDTEA VSKEDREKAR SWAKEFDLDA 

       250        260        270        280        290        300 
IFSTDGDGDR PLIADEAGEW LRGDILGLLC SLALDAEAVA IPVSCNSIIS SGRFFKHVKL 

       310        320        330        340        350        360 
TKIGSPYVIE AFNELSRSYS RIVGFEANGG FLLGSDICIN EQNLHALPTR DAVLPAIMLL 

       370        380        390        400        410        420 
YKSRNTSISA LVNELPTRYT HSDRLQGITT DKSQSLISMG RENLSNLLSY IGLENEGAIS 

       430        440        450        460        470 
TDMTDGMRIT LRDGCIVHLR ASGNAPELRC YAEANLLNRA QDLVNTTLAN IKKRCLL 

« Hide

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. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., 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.
PIRS15313.
RefSeqNP_461028.1. NC_003197.1.

3D structure databases

ProteinModelPortalP26405.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM2083.

Proteomic databases

PaxDbP26405.
PRIDEP26405.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20987; AAL20987; STM2083.
GeneID1253604.
KEGGstm:STM2083.
PATRIC32382749. VBISalEnt20916_2205.

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000066295.
KOK01840.
OMAPVSCNTA.
OrthoDBEOG6TFCNH.
ProtClustDBCLSK894265.

Enzyme and pathway databases

BioCycSENT99287:GCTI-2095-MONOMER.
UniPathwayUPA00126; UER00424.
UPA00281.

Family and domain databases

Gene3D3.30.310.50. 1 hit.
3.40.120.10. 1 hit.
InterProIPR005844. 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]
PfamPF02878. 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]
SUPFAMSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRFBK_SALTY
AccessionPrimary (citable) accession number: P26405
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways