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Q01411 (MANB_SALMO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 81. 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:rfbL
OrganismSalmonella montevideo
Taxonomic identifier115981 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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 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.

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_0000147821

Sites

Active site981Phosphoserine intermediate By similarity
Metal binding981Magnesium; via phosphate group By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity
Metal binding2491Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01411 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: F2443A7B6CA83460

FASTA45649,900
        10         20         30         40         50         60 
MNNLTCFKAY DIRGRLGEEL NEDIAWRIGR AYGEYLKPKT IVLGGDVRLT SEALKLALAK 

        70         80         90        100        110        120 
GLQDAGVDVL DIGMSGTEEI YFATFHLGVD GGIEVTASHN PMDYNGMKLV REGARPISGD 

       130        140        150        160        170        180 
TGLRDVQRLA EAGDFPPVND AARGSYRQIS LRDAYIDHLL AYISVNNLTP LKLVVNSGNG 

       190        200        210        220        230        240 
AAGPVIDAIE ARLKALGAPV EFIKIHNTPD GTFPNGIPNP LLPECRDDTR KAVIEHGADM 

       250        260        270        280        290        300 
GIAFDGDFDR CFLFDEKGQF IEGYYIVGLL AEAFLEKHPG AKIIHDPRLT WNTEAVVTAA 

       310        320        330        340        350        360 
GGTPVMSKTG HAFIKERMRT EDAIYGGEMS AHHYFRDFAY CDSGMIPWLL VAELVCLKGQ 

       370        380        390        400        410        420 
SLGELVRDRM AAFPASGEIN SRLAEPAAAI ARVEAHFAEE AQAVDRTDGL SMSFADWRFN 

       430        440        450 
LRSSNTEPVV RLNVESRGDI PLMEARTKEI LQLLNS 

« Hide

References

[1]"Sequence and structural analysis of the rfb (O antigen) gene cluster from a group C1 Salmonella enterica strain."
Lee S.J., Romana L.K., Reeves P.R.
J. Gen. Microbiol. 138:1843-1855(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: M40.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84642 Genomic DNA. Translation: AAB49391.1.

3D structure databases

ProteinModelPortalQ01411.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSPR00509. PGMPMM.
SUPFAMSSF53738. SSF53738. 3 hits.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMANB_SALMO
AccessionPrimary (citable) accession number: Q01411
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 16, 2013
This is version 81 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