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P37742 (RFBK7_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. 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
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length453 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 O7 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.

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 – 453453Phosphomannomutase
PRO_0000147823

Sites

Active site961Phosphoserine intermediate By similarity
Metal binding961Magnesium; via phosphate group By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
P37742 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: F1D1F69F97804391

FASTA45349,932
        10         20         30         40         50         60 
MLTCFKAYDI RGKLGEELNE DIAWRIGRAY GEFLKPKTIV LGGDVRLTSE TLKLALAKGL 

        70         80         90        100        110        120 
QDAGVDVLDI GMSGTEEIYF ATFHLGVDGG IEVTASHNPM DYNGMKLVRE GARPISGDTG 

       130        140        150        160        170        180 
LRDVQRLAEA NDFPPVDETK RGRYQQINLR DAYVDHLFGY INVKNLTPLK LVINSGNGAA 

       190        200        210        220        230        240 
GPVVDAIEAR FKALGAPVEL IKVHNTPDGN FPNGIPNPLL PECRDDTRNA VIKHGADMGI 

       250        260        270        280        290        300 
AFDGDFDRCF LFDEKGQFIE GYYIVGLLAE AFLEKNPGAK IIHDPRLSWN TVDVVTAAGT 

       310        320        330        340        350        360 
PVMSKTGHAF IKERMRKEDA IYGGEMSAHH YFRDFAYCDT GMIPWLLVAE LVCLKGKTLG 

       370        380        390        400        410        420 
ELVRDRMAAF PASGEINSKL AHPVEAINRV EQHFSRDAGG GSHRWHQHDL CRLAALTCAS 

       430        440        450 
SNTEPVVRLN VESRGDVPLM EEKTKLILEL LNK 

« Hide

References

[1]"Identification, expression, and DNA sequence of the GDP-mannose biosynthesis genes encoded by the O7 rfb gene cluster of strain VW187 (Escherichia coli O7:K1)."
Marolda C.L., Valvano M.A.
J. Bacteriol. 175:148-158(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O7:K1 / VW187.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF125322 Genomic DNA. Translation: AAC27539.1. Sequence problems.
PIRD40630.

3D structure databases

ProteinModelPortalP37742.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP37742.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1109.

Enzyme and pathway databases

UniPathwayUPA00126; UER00424.
UPA00281.

Family and domain databases

Gene3D3.40.120.10. 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.
[Graphical view]
PRINTSPR00509. PGMPMM.
SUPFAMSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRFBK7_ECOLX
AccessionPrimary (citable) accession number: P37742
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 74 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