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P37755 (RFBK9_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. 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:manB
Synonyms:rfbK, rfbK2
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length456 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 O9 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.

Miscellaneous

There are two duplicated genes for manB and manC in this E.coli strain.

Sequence similarities

Belongs to the phosphohexose mutase family.

Ontologies

Keywords
   Biological processLipopolysaccharide biosynthesis
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
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

   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 – 456456Phosphomannomutase
PRO_0000147824

Sites

Active site981Phosphoserine intermediate By similarity
Metal binding981Magnesium; via phosphate group By similarity
Metal binding2461Magnesium By similarity
Metal binding2481Magnesium By similarity
Metal binding2501Magnesium By similarity

Natural variations

Natural variant3921A → R.
Natural variant4411T → V.
Natural variant4461A → E.
Natural variant449 – 4535EEILA → TELLN.
Natural variant4561K → KEELL.

Sequences

Sequence LengthMass (Da)Tools
P37755 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 40100B6075791BF3

FASTA45650,423
        10         20         30         40         50         60 
MTQLTCFKAY DIRGELGEEL NEDIAYRIGR AYGEFLKPGK IVVGGDVRLT SESLKLALAR 

        70         80         90        100        110        120 
GLMDAGTDVL DIGLSGTEEI YFATFHLGVD GGIEVTASHN PMNYNGMKLV RENAKPISGD 

       130        140        150        160        170        180 
TGLRDIQRLA EENQFPPVDP ARRGTLRQIS VLKEYVDHLM GYVDLANFTR PLKLVVNSGN 

       190        200        210        220        230        240 
GAAGHVIDEV EKRFAAAGVP VTFIKVHHQP DGHFPNGIPN PLLPECRQDT ADAVREHQAD 

       250        260        270        280        290        300 
MGIAFDGDFD RCFLFDDEAS FIEGYYIVGL LAEAFLQKQP GAKIIHDPRL TWNTVDIVTR 

       310        320        330        340        350        360 
NGGQPVMSKT GHAFIKERMR QEDAIYGGEM SAHHYFRDFA YCDSGMIPWL LVAELLCLKN 

       370        380        390        400        410        420 
SSLKSLVADR QAAFPASGEI NRKLGNAAEA IARIRAQYEP AAAHIDTTDG ISIEYPEWRF 

       430        440        450 
NLRTSNTEPV VRLNVESRAD TALMNAKTEE ILALLK 

« Hide

References

[1]"Cloning and analysis of duplicated rfbM and rfbK genes involved in the formation of GDP-mannose in Escherichia coli O9:K30 and participation of rfb genes in the synthesis of the group I K30 capsular polysaccharide."
Jayaratne P., Bronner D., Maclachlan R.P., Dodgson C., Kido N., Whitfield C.
J. Bacteriol. 176:3126-3139(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O9:K30:H12 / E69.
[2]"Bacterial polysaccharide synthesis and gene nomenclature."
Reeves P.R., Hobbs M., Valvano M.A., Skurnik M., Whitfield C., Coplin D., Kido N., Klena J., Maskell D., Raetz C.R.H., Rick P.D.
Trends Microbiol. 4:495-503(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE NAME.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L27646 Genomic DNA. Translation: AAA21138.1.
L27632 Genomic DNA. Translation: AAA21140.1.

3D structure databases

ProteinModelPortalP37755.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP37755.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00126; UER00424.
UPA00281.

Family and domain databases

Gene3D3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
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.
IPR005841. Alpha-D-phosphohexomutase_SF.
[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]
PRINTSPR00509. PGMPMM.
SUPFAMSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRFBK9_ECOLX
AccessionPrimary (citable) accession number: P37755
Secondary accession number(s): P82275
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 72 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