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Q1W377 (PMM_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 32. 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
EC=5.4.2.8
Alternative name(s):
LePMM
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum) [Reference proteome]
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in ascorbic acid biosynthesis and 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.

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 – 252252Phosphomannomutase
PRO_0000326494

Sites

Active site131Nucleophile By similarity
Active site151 By similarity
Active site481 By similarity
Active site1901 By similarity
Binding site221Substrate By similarity
Binding site1241Substrate By similarity
Binding site1351Substrate By similarity
Binding site1421Substrate By similarity
Binding site1801Substrate By similarity
Binding site1821Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1W377 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: AE3E701AC82DCC82

FASTA25228,556
        10         20         30         40         50         60 
MAARKAGLIA LFDVDGTLTA PRKESTPQML KFMQELRKVV TVGVVGGSDL VKISEQLGNT 

        70         80         90        100        110        120 
VTNDYDYVFS ENGLVAHKDG KLIGKQSLKS HLGDEKLKEF INFTLHYIAD LDIPIKRGTF 

       130        140        150        160        170        180 
IEFRSGMLNV SPIGRNCSQE ERDEFEKYDK VQKIRETMVS VLREKFAHFN LTFSIGGQIS 

       190        200        210        220        230        240 
FDVFPQGWDK TYCLRYLEEF NEIHFFGDKT YKGGNDHEIY ESERTVGHTV TSPEETLKQC 

       250 
SVLFLGKDNG SS

« Hide

References

[1]"Molecular and functional analysis of phosphomannomutase (PMM) from higher plants and genetic evidence for the involvement of PMM in ascorbic acid biosynthesis in Arabidopsis and Nicotiana benthamiana."
Qian W., Yu C., Qin H., Liu X., Zhang A., Johansen I.E., Wang D.
Plant J. 49:399-413(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ442993 mRNA. Translation: ABD97872.1.
RefSeqNP_001233801.1. NM_001246872.1.
UniGeneLes.5106.

3D structure databases

ProteinModelPortalQ1W377.
SMRQ1W377. Positions 9-244.
ModBaseSearch...

Proteomic databases

PRIDEQ1W377.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID778245.

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_SOLLC
AccessionPrimary (citable) accession number: Q1W377
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 2, 2006
Last modified: March 6, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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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