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O80840 (PMM_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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=AtPMM
EC=5.4.2.8
Gene names
Name:PMM
Ordered Locus Names:At2g45790
ORF Names:F4I18.23
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.1 Ref.6

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.

Tissue specificity

Expressed in roots, stems, leaves, flower buds, flowers and immature fruits. Ref.1

Disruption phenotype

The thermosensitive lethality of pmm-12 results from glycosylation defects rather than ascorbic acid depletion. Ref.6

Sequence similarities

Belongs to the eukaryotic PMM family.

Biophysicochemical properties

Kinetic parameters:

Requires glucose-1,6-bisphosphate for activity.

KM=29.7 µM for mannose-1-phosphate Ref.1

KM=65.4 µM for glucose-1-phosphate

Vmax=14.4 µmol/min/mg enzyme with mannose-1-phosphate as substrate

Vmax=1.4 µmol/min/mg enzyme with glucose-1-phosphate as substrate

pH dependence:

Optimum pH is 7.5.

Temperature dependence:

Optimum temperature is 30 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 246246Phosphomannomutase
PRO_0000199700

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

Experimental info

Mutagenesis71G → R in pmm-1; 18% reduction of catalytic activity. In pmm-12/dgr1; 92% reduction of catalytic activity resulting in lethality when grown at restrictive temperature; when associated with Q-37. Ref.6
Mutagenesis371R → Q in pmm-2; 86% reduction of catalytic activity. In pmm-12/dgr1; 92% reduction of catalytic activity resulting in lethality when grown at restrictive temperature; when associated with R-7. Ref.6

Sequences

Sequence LengthMass (Da)Tools
O80840 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 52971A3F1AE08DF9

FASTA24627,762
        10         20         30         40         50         60 
MAAKIPGVIA LFDVDGTLTA PRKEATPELL DFIRELRKVV TIGVVGGSDL SKISEQLGKT 

        70         80         90        100        110        120 
VTNDYDYCFS ENGLVAHKDG KSIGIQSLKL HLGDDKLKEL INFTLHYIAD LDIPIKRGTF 

       130        140        150        160        170        180 
IEFRNGMLNV SPIGRNCSQE ERDEFERYDK VQNIRPKMVA ELRERFAHLN LTFSIGGQIS 

       190        200        210        220        230        240 
FDVFPKGWDK TYCLQYLEDF SEIHFFGDKT YEGGNDYEIY ESPKTIGHSV TSPDDTVAKC 


KALFMS 

« Hide

References

« Hide 'large scale' 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], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"A temperature-sensitive mutation in the Arabidopsis thaliana phosphomannomutase gene disrupts protein glycosylation and triggers cell death."
Hoeberichts F.A., Vaeck E., Kiddle G., Coppens E., van de Cotte B., Adamantidis A., Ormenese S., Foyer C.H., Zabeau M., Inze D., Perilleux C., Van Breusegem F., Vuylsteke M.
J. Biol. Chem. 283:5708-5718(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-7 AND ARG-37, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ442991 mRNA. Translation: ABD97870.1.
AC004665 Genomic DNA. Translation: AAC28545.1.
CP002685 Genomic DNA. Translation: AEC10601.1.
AY050806 mRNA. Translation: AAK92741.1.
AY113964 mRNA. Translation: AAM45012.1.
AY088930 mRNA. Translation: AAM67236.1.
PIRT02468.
RefSeqNP_182103.1. NM_130142.3.
UniGeneAt.20569.
At.48595.

3D structure databases

ProteinModelPortalO80840.
SMRO80840. Positions 6-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO80840. 1 interaction.
STRING3702.AT2G45790.1-P.

Proteomic databases

PaxDbO80840.
PRIDEO80840.

Protocols and materials databases

DNASU819187.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G45790.1; AT2G45790.1; AT2G45790.
GeneID819187.
KEGGath:AT2G45790.

Organism-specific databases

TAIRAT2G45790.

Phylogenomic databases

eggNOGCOG0561.
HOGENOMHOG000181843.
InParanoidO80840.
KOK17497.
OMATYCLQHV.
PhylomeDBO80840.

Enzyme and pathway databases

BioCycARA:AT2G45790-MONOMER.
MetaCyc:AT2G45790-MONOMER.
UniPathwayUPA00126; UER00424.

Gene expression databases

GenevestigatorO80840.

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...

Other

PROO80840.

Entry information

Entry namePMM_ARATH
AccessionPrimary (citable) accession number: O80840
Secondary accession number(s): Q1W379
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1998
Last modified: June 11, 2014
This is version 108 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names