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Q8SVM5 (PMM_ENCCU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphomannomutase
Short name=PMM
EC=5.4.2.8
Gene names
Name:SEC53
Ordered Locus Names:ECU05_0260
OrganismEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) [Reference proteome]
Taxonomic identifier284813 [NCBI]
Taxonomic lineageEukaryota › Fungi › Microsporidia › Unikaryonidae › Encephalitozoon ›

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions By similarity.

Catalytic activity

Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.

Pathway

Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Developmental stage

Expressed in late sporogonial stages.

Sequence similarities

Belongs to the eukaryotic PMM family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGDP-mannose biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

mannose biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphomannomutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 256256Phosphomannomutase
PRO_0000382908

Sites

Active site121Nucleophile By similarity
Active site141 By similarity
Active site471 By similarity
Active site1891 By similarity
Binding site211Substrate By similarity
Binding site1231Substrate By similarity
Binding site1341Substrate By similarity
Binding site1411Substrate By similarity
Binding site1791Substrate By similarity
Binding site1811Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8SVM5 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: DBDEFE2929D73D10

FASTA25629,616
        10         20         30         40         50         60 
MARDEKTIFL FDVDGTLSES RAKMPEKMGK MLESLRRKVR IGFVGGSDLA KQKEQVGDNI 

        70         80         90        100        110        120 
LEIFDYGFPE NGVSFYKNGT LESQEKIIDV LGEEFYKEFA NFVLRYLSDI DLPIKRGNFI 

       130        140        150        160        170        180 
EYRNSMINIS PIGRNCSREE RMKFFELDKK EKFREKMVTA MRDRFKDSCL VFSIGGQISI 

       190        200        210        220        230        240 
DCFPKGWDKT YCLRHIKKEG VENVYFFGDM TMEGGNDYEI YNHKDVHGIS VGNPDDTYRK 

       250 
VDQALKKIGL GGLEEN

« Hide

References

[1]"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi."
Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P.
Nature 414:450-453(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-M1.
[2]"Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi (microsporidia): a reference map for proteins expressed in late sporogonial stages."
Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.
Proteomics 6:3625-3635(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL STAGE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL590445 Genomic DNA. Translation: CAD26542.1.
RefSeqNP_597365.1. NM_001041231.1.

3D structure databases

ProteinModelPortalQ8SVM5.
ModBaseSearch...

Protein-protein interaction databases

STRING6035.ECU05_0260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID859029.
KEGGecu:ECU05_0260.

Organism-specific databases

EuPathDBMicrosporidiaDB:ECU05_0260.

Phylogenomic databases

eggNOGCOG0561.
HOGENOMHOG000181843.
KOK01840.
OMAFDVFPHG.

Enzyme and pathway databases

UniPathwayUPA00126; UER00424.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
InterProIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERPTHR10466. PTHR10466. 1 hit.
PfamPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01484. HAD-SF-IIB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePMM_ENCCU
AccessionPrimary (citable) accession number: Q8SVM5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: June 1, 2002
Last modified: May 29, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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