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Q1W376 (PMM_SOYBN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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

EC=5.4.2.8
Alternative name(s):
GmPMM
OrganismGlycine max (Soybean) (Glycine hispida) [Reference proteome]
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja

Protein attributes

Sequence length247 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

L-ascorbic acid biosynthetic process

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

mannose biosynthetic process

Inferred from electronic annotation. Source: InterPro

response to salt stress

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentcytosol

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionphosphomannomutase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 247247Phosphomannomutase
PRO_0000326495

Sites

Active site131Nucleophile By similarity
Active site151Proton donor/acceptor Potential
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
Q1W376 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: 7FF516DFA51220A1

FASTA24728,019
        10         20         30         40         50         60 
MAARRPGLIA LFDVDGTLTA PRKVVTPEML TFMQELRKVV TVGVVGGSDL IKISEQLGST 

        70         80         90        100        110        120 
VTNDYDYVFS ENGLVAHKEG KLIGTQSLKS FLGEEKLKEF INFTLHYIAD LDIPIKRGTF 

       130        140        150        160        170        180 
IEFRSGMLNV SPIGRNCSQE ERDEFEKYDK VHNIRPKMVS VLREKFAHLN LTFSIGGQIS 

       190        200        210        220        230        240 
FDVFPQGWDK TYCLRYLDGF NEIHFFGDKT YKGGNDHEIY ESERTVGHTV TSPDDTVKQC 


KSLFLEN 

« 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
DQ442994 mRNA. Translation: ABD97873.1.
RefSeqNP_001237668.1. NM_001250739.1.
XP_006601866.1. XM_006601803.1.
UniGeneGma.3992.

3D structure databases

ProteinModelPortalQ1W376.
SMRQ1W376. Positions 6-244.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ1W376.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsGLYMA18G46390.1; GLYMA18G46390.1; GLYMA18G46390.
GeneID732605.
KEGGgmx:732605.

Phylogenomic databases

KOK17497.
OMATYCLQHV.

Enzyme and pathway databases

UniPathwayUPA00126; UER00424.

Gene expression databases

GenevestigatorQ1W376.

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. SSF56784. 1 hit.
TIGRFAMsTIGR01484. HAD-SF-IIB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePMM_SOYBN
AccessionPrimary (citable) accession number: Q1W376
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 2, 2006
Last modified: May 14, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways