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Q06951 (RFBB_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. 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:rfbB
Ordered Locus Names:VC_0242
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length463 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.

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 Probable.

Sequence similarities

Belongs to the phosphohexose mutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Phosphomannomutase
PRO_0000147827

Sites

Active site1031Phosphoserine intermediate By similarity
Metal binding1031Magnesium; via phosphate group By similarity
Metal binding2481Magnesium By similarity
Metal binding2501Magnesium By similarity
Metal binding2521Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q06951 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 7212EA3A64BFC6BE

FASTA46351,838
        10         20         30         40         50         60 
MKELTCFKAY DIRGQLGSEL DNEIAYRIGR SYGQFLKSEN DADKTVVVGG DVRLTSEALK 

        70         80         90        100        110        120 
QALANGLMDA GINVIDIGVT GTEEIYFATF YLGVDGGIEV TASHNPMDYN GMKLVREGSK 

       130        140        150        160        170        180 
PISGDTGLRE IQALAEKNEF MDVEVKGNYK KVSLLPEYVD HLISYITPAK IKPMKLVINS 

       190        200        210        220        230        240 
GNGAAGHVID ELEKRFIELS IPLEIIKVHH EEDGNFPNGI PNPLLPECRA DTANAVKEHK 

       250        260        270        280        290        300 
ADMGIAFDGD FDRCFLFDEN GDFIEGYYIV GLLAEAFLQK EQGAKIIHDP RLSWNTIDVV 

       310        320        330        340        350        360 
TKSGGVPVMS KTGHAFIKER MRKEDAIYGG EMSAHHYFRD FGYCDSGMIP WLLITELLSL 

       370        380        390        400        410        420 
APDISLSKLI SAKRFLFPCS GEINFKVKQA KLIMEQVYLH YYENSIHFSA IDGISLEFEG 

       430        440        450        460 
WRFNLRDSNT EPLLRLNVES KQNIALMNDK VEELTKLIKK LDI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59554 Genomic DNA. Translation: CAA42135.1.
AE003852 Genomic DNA. Translation: AAF93418.1.
PIRS28469.
RefSeqNP_229899.1. NC_002505.1.

3D structure databases

ProteinModelPortalQ06951.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC0242.

Protocols and materials databases

DNASU2614705.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF93418; AAF93418; VC_0242.
GeneID2614705.
KEGGvch:VC0242.
PATRIC20079528. VBIVibCho83274_0223.

Phylogenomic databases

eggNOGCOG1109.
KOK01840.
OMARDAYIGH.
OrthoDBEOG6W9X55.
ProtClustDBCLSK873915.

Enzyme and pathway databases

BioCycVCHO:VC0242-MONOMER.
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 nameRFBB_VIBCH
AccessionPrimary (citable) accession number: Q06951
Secondary accession number(s): Q9JQ14
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 99 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