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Q1W374 (PMM_WHEAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 32. 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):
TaPMM
OrganismTriticum aestivum (Wheat) [Complete proteome]
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum

Protein attributes

Sequence length249 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
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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Phosphomannomutase
PRO_0000326497

Sites

Active site151Nucleophile By similarity
Active site171Proton donor/acceptor Potential
Binding site241Substrate By similarity
Binding site1261Substrate By similarity
Binding site1371Substrate By similarity
Binding site1441Substrate By similarity
Binding site1821Substrate By similarity
Binding site1841Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1W374 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: AB85F0AB97DCD566

FASTA24928,252
        10         20         30         40         50         60 
MAAARKDAGV LALFDVDGTL TAPRKEVTPE MLEFMKRLRE NVTVGVVGGS DLVKISEQLG 

        70         80         90        100        110        120 
KSVITDYDYV FSENGLVAHK DGKLIGTQSL KTYLGDDQLK EFINFTLHYI ADLDIPIKRG 

       130        140        150        160        170        180 
TFIEFRSGMI NVSPIGRNCS QEERDDFEKY DKVHNVRPKM VSVLREKFAH LNLTFSIGGQ 

       190        200        210        220        230        240 
ISFDVFPQGW DKTYCLRYLE EFKEIHFFGD KTYKGGNDHE IFESDRTVGH TVTSPNDTVQ 


QCKSIFLSE 

« 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
DQ442996 mRNA. Translation: ABD97875.1.
UniGeneTa.3539.

3D structure databases

ProteinModelPortalQ1W374.
SMRQ1W374. Positions 11-246.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ1W374.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneQ1W374.

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

Entry information

Entry namePMM_WHEAT
AccessionPrimary (citable) accession number: Q1W374
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 2, 2006
Last modified: April 16, 2014
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways