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O80840

- PMM_ARATH

UniProt

O80840 - PMM_ARATH

Protein

Phosphomannomutase

Gene

PMM

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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

    Vmax=14.4 µmol/min/mg enzyme with mannose-1-phosphate as substrate1 Publication

    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

    Pathwayi

    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

    1. phosphomannomutase activity Source: TAIR
    2. protein binding Source: TAIR

    GO - Biological processi

    1. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
    2. L-ascorbic acid biosynthetic process Source: TAIR
    3. mannose biosynthetic process Source: InterPro
    4. response to salt stress Source: TAIR

    Keywords - Molecular functioni

    Isomerase

    Enzyme and pathway databases

    BioCyciARA:AT2G45790-MONOMER.
    MetaCyc:AT2G45790-MONOMER.
    ReactomeiREACT_190862. 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: Chromosome 2

    Organism-specific databases

    TAIRiAT2G45790.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: TAIR

    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

    Gene expression databases

    GenevestigatoriO80840.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiO80840. 1 interaction.
    STRINGi3702.AT2G45790.1-P.

    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.
    OMAiTYCLQHV.
    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

    MAAKIPGVIA LFDVDGTLTA PRKEATPELL DFIRELRKVV TIGVVGGSDL    50
    SKISEQLGKT VTNDYDYCFS ENGLVAHKDG KSIGIQSLKL HLGDDKLKEL 100
    INFTLHYIAD LDIPIKRGTF IEFRNGMLNV SPIGRNCSQE ERDEFERYDK 150
    VQNIRPKMVA ELRERFAHLN LTFSIGGQIS FDVFPKGWDK TYCLQYLEDF 200
    SEIHFFGDKT YEGGNDYEIY ESPKTIGHSV TSPDDTVAKC KALFMS 246
    Length:246
    Mass (Da):27,762
    Last modified:November 1, 1998 - v1
    Checksum:i52971A3F1AE08DF9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi T02468.
    RefSeqi NP_182103.1. NM_130142.3.
    UniGenei At.20569.
    At.48595.

    3D structure databases

    ProteinModelPortali O80840.
    SMRi O80840. Positions 6-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O80840. 1 interaction.
    STRINGi 3702.AT2G45790.1-P.

    Proteomic databases

    PaxDbi O80840.
    PRIDEi O80840.

    Protocols and materials databases

    DNASUi 819187.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G45790.1 ; AT2G45790.1 ; AT2G45790 .
    GeneIDi 819187.
    KEGGi ath:AT2G45790.

    Organism-specific databases

    TAIRi AT2G45790.

    Phylogenomic databases

    eggNOGi COG0561.
    HOGENOMi HOG000181843.
    InParanoidi O80840.
    KOi K17497.
    OMAi TYCLQHV.
    PhylomeDBi O80840.

    Enzyme and pathway databases

    UniPathwayi UPA00126 ; UER00424 .
    BioCyci ARA:AT2G45790-MONOMER.
    MetaCyc:AT2G45790-MONOMER.
    Reactomei REACT_190862. Synthesis of GDP-mannose.

    Miscellaneous databases

    PROi O80840.

    Gene expression databases

    Genevestigatori O80840.

    Family and domain databases

    Gene3Di 3.40.50.1000. 2 hits.
    InterProi IPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR005002. PMM.
    [Graphical view ]
    PANTHERi PTHR10466. PTHR10466. 1 hit.
    Pfami PF03332. PMM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR01484. HAD-SF-IIB. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 110 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