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O85343 (MANB_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 93. 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
Ordered Locus Names:Z3194, ECs2835
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [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 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
   Technical termComplete 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

   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_0000147819

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
O85343 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 6845D9D2DD7628B7

FASTA45650,340
        10         20         30         40         50         60 
MKSLTCFKAY DIRGKLGEEL NEDIAWRIGR AYGEFLKPKT IVLGGDVRLT SEALKLALAK 

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

       130        140        150        160        170        180 
TGLRDVQRLA EANDFPPVDE TKRGRYQQIN LRDAYVDHLF GYINVKNLTP LKLVINSGNG 

       190        200        210        220        230        240 
AAGPVVDAIE ARFKALGAPV ELIKVHNTPD GNFPNGIPNP LLPECRDDTR NAVIKHGADM 

       250        260        270        280        290        300 
GIAFDGDFDR CFLFDEKGQF IEGYYIVGLL AEAFLEKNPG AKIIHDPRLS WNTVDVVTAA 

       310        320        330        340        350        360 
GGTPVMSKTG HAFIKERMRK EDAIYGGEMS AHHYFRDFAY CDSGMIPWLL VAELVCLKGK 

       370        380        390        400        410        420 
TLGEMVRDRM AAFPASGEIN SKLAQPVEAI NRVEQHFSRE ALAVDRTDGI SMTFADWRFN 

       430        440        450 
LRSSNTEPVV RLNVESRGDV KLMEKKTKAL LKLLSE 

« Hide

References

« Hide 'large scale' references
[1]"Organization of Escherichia coli O157 O antigen gene cluster and identification of its specific genes."
Wang L., Reeves P.R.
Infect. Immun. 66:3545-3551(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O157:H7 / C664-1992 / EHEC.
[2]"Analysis of the genes responsible for the O-antigen synthesis in enterohaemorrhagic Escherichia coli O157."
Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y.
Microb. Pathog. 26:235-247(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O157:H- / 184 / EHEC.
[3]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[4]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061251 Genomic DNA. Translation: AAC32349.1.
AB008676 Genomic DNA. Translation: BAA77734.1.
AE005174 Genomic DNA. Translation: AAG57090.1.
BA000007 Genomic DNA. Translation: BAB36258.1.
PIRC90983.
F85828.
RefSeqNP_288536.1. NC_002655.2.
NP_310862.1. NC_002695.1.

3D structure databases

ProteinModelPortalO85343.
SMRO85343. Positions 1-456.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z3194.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG57090; AAG57090; Z3194.
BAB36258; BAB36258; BAB36258.
GeneID913941.
962089.
KEGGece:Z3194.
ecs:ECs2835.
PATRIC18355054. VBIEscCol44059_2728.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268679.
KOK01840.
OMARLAIICE.
OrthoDBEOG6W9X55.

Enzyme and pathway databases

BioCycECOL386585:GJFA-2797-MONOMER.
ECOO157:MANB-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 nameMANB_ECO57
AccessionPrimary (citable) accession number: O85343
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: November 1, 1998
Last modified: May 14, 2014
This is version 93 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