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Protein

Phosphomannomutase

Gene

PMM

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Kineticsi

Requires glucose-1,6-bisphosphate for activity.

  1. KM=29.7 µM for mannose-1-phosphate1 Publication
  2. KM=65.4 µM for glucose-1-phosphate1 Publication
  1. Vmax=14.4 µmol/min/mg enzyme with mannose-1-phosphate as substrate1 Publication
  2. Vmax=1.4 µmol/min/mg enzyme with glucose-1-phosphate as substrate1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

Temperature dependencei

Optimum temperature is 30 degrees Celsius.1 Publication

Pathway: GDP-alpha-D-mannose biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Mannose-6-phosphate isomerase 1 (PMI1), Mannose-6-phosphate isomerase 2 (PMI2)
  2. Phosphomannomutase (PMM)
This subpathway is part of the pathway GDP-alpha-D-mannose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate, the pathway GDP-alpha-D-mannose biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei13 – 131NucleophileBy similarity
Active sitei15 – 151Proton donor/acceptorSequence Analysis
Binding sitei22 – 221SubstrateBy similarity
Binding sitei124 – 1241SubstrateBy similarity
Binding sitei135 – 1351SubstrateBy similarity
Binding sitei142 – 1421SubstrateBy similarity
Binding sitei180 – 1801SubstrateBy similarity
Binding sitei182 – 1821SubstrateBy similarity

GO - Molecular functioni

  • phosphomannomutase activity Source: TAIR

GO - Biological processi

  • GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  • L-ascorbic acid biosynthetic process Source: TAIR
  • mannose biosynthetic process Source: InterPro
  • response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciARA:AT2G45790-MONOMER.
MetaCyc:AT2G45790-MONOMER.
BRENDAi5.4.2.8. 399.
ReactomeiREACT_325410. Synthesis of GDP-mannose.
UniPathwayiUPA00126; UER00424.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase (EC:5.4.2.8)
Short name:
AtPMM
Gene namesi
Name:PMM
Ordered Locus Names:At2g45790
ORF Names:F4I18.23
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G45790.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

The thermosensitive lethality of pmm-12 results from glycosylation defects rather than ascorbic acid depletion.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71G → 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. 1 Publication
Mutagenesisi37 – 371R → 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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246PhosphomannomutasePRO_0000199700Add
BLAST

Proteomic databases

PaxDbiO80840.
PRIDEiO80840.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiO80840. 1 interaction.
STRINGi3702.AT2G45790.1.

Structurei

3D structure databases

ProteinModelPortaliO80840.
SMRiO80840. Positions 6-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic PMM family.Curated

Phylogenomic databases

eggNOGiCOG0561.
HOGENOMiHOG000181843.
InParanoidiO80840.
KOiK17497.
OMAiQEERLEF.
PhylomeDBiO80840.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERiPTHR10466. PTHR10466. 1 hit.
PfamiPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.

Sequencei

Sequence statusi: Complete.

O80840-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAKIPGVIA LFDVDGTLTA PRKEATPELL DFIRELRKVV TIGVVGGSDL
60 70 80 90 100
SKISEQLGKT VTNDYDYCFS ENGLVAHKDG KSIGIQSLKL HLGDDKLKEL
110 120 130 140 150
INFTLHYIAD LDIPIKRGTF IEFRNGMLNV SPIGRNCSQE ERDEFERYDK
160 170 180 190 200
VQNIRPKMVA ELRERFAHLN LTFSIGGQIS FDVFPKGWDK TYCLQYLEDF
210 220 230 240
SEIHFFGDKT YEGGNDYEIY ESPKTIGHSV TSPDDTVAKC KALFMS
Length:246
Mass (Da):27,762
Last modified:November 1, 1998 - v1
Checksum:i52971A3F1AE08DF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT02468.
RefSeqiNP_182103.1. NM_130142.3.
UniGeneiAt.20569.
At.48595.

Genome annotation databases

EnsemblPlantsiAT2G45790.1; AT2G45790.1; AT2G45790.
GeneIDi819187.
KEGGiath:AT2G45790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT02468.
RefSeqiNP_182103.1. NM_130142.3.
UniGeneiAt.20569.
At.48595.

3D structure databases

ProteinModelPortaliO80840.
SMRiO80840. Positions 6-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO80840. 1 interaction.
STRINGi3702.AT2G45790.1.

Proteomic databases

PaxDbiO80840.
PRIDEiO80840.

Protocols and materials databases

DNASUi819187.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G45790.1; AT2G45790.1; AT2G45790.
GeneIDi819187.
KEGGiath:AT2G45790.

Organism-specific databases

TAIRiAT2G45790.

Phylogenomic databases

eggNOGiCOG0561.
HOGENOMiHOG000181843.
InParanoidiO80840.
KOiK17497.
OMAiQEERLEF.
PhylomeDBiO80840.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.
BioCyciARA:AT2G45790-MONOMER.
MetaCyc:AT2G45790-MONOMER.
BRENDAi5.4.2.8. 399.
ReactomeiREACT_325410. Synthesis of GDP-mannose.

Miscellaneous databases

PROiO80840.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERiPTHR10466. PTHR10466. 1 hit.
PfamiPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.

Entry informationi

Entry nameiPMM_ARATH
AccessioniPrimary (citable) accession number: O80840
Secondary accession number(s): Q1W379
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1998
Last modified: June 24, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.